Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 21:11, 15 December 2007 (UTC)
[edit]Proteins without matches (20)
[edit]Proteins with a High Potential Match (1)
[edit]Redirected Proteins (4)
[edit]Manual Inspection (Page not found) (20)
[edit]Updated with Warning (1)
[edit]
Protein Status Grid - Date: 21:11, 15 December 2007 (UTC)
[edit]Vebose Log - Date: 21:11, 15 December 2007 (UTC)
[edit]- INFO: Beginning work on APAF1... {December 15, 2007 12:48:22 PM PST}
- REDIRECT: Page directory gave bad page (APAF1). Continuing with search.. Please correct entry: <317,APAF1>. {December 15, 2007 12:48:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 12:48:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_APAF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c15.
| PDB = {{PDB2|1c15}}, {{PDB2|1cww}}, {{PDB2|1cy5}}, {{PDB2|1z6t}}, {{PDB2|2p1h}}, {{PDB2|2ygs}}, {{PDB2|3ygs}}
| Name = Apoptotic peptidase activating factor 1
| HGNCid = 576
| Symbol = APAF1
| AltSymbols =; CED4
| OMIM = 602233
| ECnumber =
| Homologene = 7626
| MGIid = 1306796
| GeneAtlas_image1 = PBB_GE_APAF1_204859_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_APAF1_211553_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_APAF1_211554_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008656 |text = caspase activator activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0001843 |text = neural tube closure}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0008635 |text = caspase activation via cytochrome c}} {{GNF_GO|id=GO:0030900 |text = forebrain development}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 317
| Hs_Ensembl = ENSG00000120868
| Hs_RefseqProtein = NP_001151
| Hs_RefseqmRNA = NM_001160
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 97563209
| Hs_GenLoc_end = 97653335
| Hs_Uniprot = O14727
| Mm_EntrezGene = 11783
| Mm_Ensembl = ENSMUSG00000019979
| Mm_RefseqmRNA = NM_001042558
| Mm_RefseqProtein = NP_001036023
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 90419117
| Mm_GenLoc_end = 90512538
| Mm_Uniprot = Q4VZG8
}}
}}
'''Apoptotic peptidase activating factor 1''', also known as '''APAF1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: APAF1 apoptotic peptidase activating factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=317| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a cytoplasmic protein that initiates apoptosis. This protein contains several copies of the WD-40 domain, a caspase recruitment domain (CARD), and an ATPase domain (NB-ARC). Upon binding cytochrome c and dATP, this protein forms an oligomeric apoptosome. The apoptosome binds and cleaves caspase 9 preproprotein, releasing its mature, activated form. Activated caspase 9 stimulates the subsequent caspase cascade that commits the cell to apoptosis. Alternative splicing results in several transcript variants encoding different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: APAF1 apoptotic peptidase activating factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=317| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Smith TF, Gaitatzes C, Saxena K, Neer EJ |title=The WD repeat: a common architecture for diverse functions. |journal=Trends Biochem. Sci. |volume=24 |issue= 5 |pages= 181-5 |year= 1999 |pmid= 10322433 |doi= }}
*{{cite journal | author=van Oirschot JT |title=Diva vaccines that reduce virus transmission. |journal=J. Biotechnol. |volume=73 |issue= 2-3 |pages= 195-205 |year= 1999 |pmid= 10486928 |doi= }}
*{{cite journal | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi= }}
*{{cite journal | author=Campioni M, Santini D, Tonini G, ''et al.'' |title=Role of Apaf-1, a key regulator of apoptosis, in melanoma progression and chemoresistance. |journal=Exp. Dermatol. |volume=14 |issue= 11 |pages= 811-8 |year= 2006 |pmid= 16232302 |doi= 10.1111/j.1600-0625.2005.00360.x }}
*{{cite journal | author=Zou H, Henzel WJ, Liu X, ''et al.'' |title=Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. |journal=Cell |volume=90 |issue= 3 |pages= 405-13 |year= 1997 |pmid= 9267021 |doi= }}
*{{cite journal | author=Li P, Nijhawan D, Budihardjo I, ''et al.'' |title=Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. |journal=Cell |volume=91 |issue= 4 |pages= 479-89 |year= 1997 |pmid= 9390557 |doi= }}
*{{cite journal | author=Ishikawa K, Nagase T, Nakajima D, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=4 |issue= 5 |pages= 307-13 |year= 1998 |pmid= 9455477 |doi= }}
*{{cite journal | author=Pan G, O'Rourke K, Dixit VM |title=Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex. |journal=J. Biol. Chem. |volume=273 |issue= 10 |pages= 5841-5 |year= 1998 |pmid= 9488720 |doi= }}
*{{cite journal | author=Hu Y, Benedict MA, Wu D, ''et al.'' |title=Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 8 |pages= 4386-91 |year= 1998 |pmid= 9539746 |doi= }}
*{{cite journal | author=Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES |title=Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. |journal=Mol. Cell |volume=1 |issue= 7 |pages= 949-57 |year= 1998 |pmid= 9651578 |doi= }}
*{{cite journal | author=Cecconi F, Alvarez-Bolado G, Meyer BI, ''et al.'' |title=Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. |journal=Cell |volume=94 |issue= 6 |pages= 727-37 |year= 1998 |pmid= 9753320 |doi= }}
*{{cite journal | author=Inohara N, Gourley TS, Carrio R, ''et al.'' |title=Diva, a Bcl-2 homologue that binds directly to Apaf-1 and induces BH3-independent cell death. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32479-86 |year= 1999 |pmid= 9829980 |doi= }}
*{{cite journal | author=Hu Y, Ding L, Spencer DM, Núñez G |title=WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation. |journal=J. Biol. Chem. |volume=273 |issue= 50 |pages= 33489-94 |year= 1999 |pmid= 9837928 |doi= }}
*{{cite journal | author=Song Q, Kuang Y, Dixit VM, Vincenz C |title=Boo, a novel negative regulator of cell death, interacts with Apaf-1. |journal=EMBO J. |volume=18 |issue= 1 |pages= 167-78 |year= 1999 |pmid= 9878060 |doi= 10.1093/emboj/18.1.167 }}
*{{cite journal | author=Slee EA, Harte MT, Kluck RM, ''et al.'' |title=Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner. |journal=J. Cell Biol. |volume=144 |issue= 2 |pages= 281-92 |year= 1999 |pmid= 9922454 |doi= }}
*{{cite journal | author=Zou H, Li Y, Liu X, Wang X |title=An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. |journal=J. Biol. Chem. |volume=274 |issue= 17 |pages= 11549-56 |year= 1999 |pmid= 10206961 |doi= }}
*{{cite journal | author=Saleh A, Srinivasula SM, Acharya S, ''et al.'' |title=Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation. |journal=J. Biol. Chem. |volume=274 |issue= 25 |pages= 17941-5 |year= 1999 |pmid= 10364241 |doi= }}
*{{cite journal | author=Qin H, Srinivasula SM, Wu G, ''et al.'' |title=Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1. |journal=Nature |volume=399 |issue= 6736 |pages= 549-57 |year= 1999 |pmid= 10376594 |doi= 10.1038/21124 }}
*{{cite journal | author=Drosopoulos NE, Walsh FS, Doherty P |title=A soluble version of the receptor-like protein tyrosine phosphatase kappa stimulates neurite outgrowth via a Grb2/MEK1-dependent signaling cascade. |journal=Mol. Cell. Neurosci. |volume=13 |issue= 6 |pages= 441-9 |year= 1999 |pmid= 10383829 |doi= 10.1006/mcne.1999.0758 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ATF2... {December 15, 2007 12:51:51 PM PST}
- REDIRECT: Page directory gave bad page (ATF2 (gene)). Continuing with search.. Please correct entry: <1386,ATF2 (gene)>. {December 15, 2007 12:52:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 12:52:44 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ATF2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bhi.
| PDB = {{PDB2|1bhi}}, {{PDB2|1t2k}}
| Name = Activating transcription factor 2
| HGNCid = 784
| Symbol = ATF2
| AltSymbols =; CREB2; CRE-BP1; HB16; MGC111558; TREB7
| OMIM = 123811
| ECnumber =
| Homologene = 31061
| MGIid = 109349
| GeneAtlas_image1 = PBB_GE_ATF2_205446_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ATF2_212984_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0046983 |text = protein dimerization activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1386
| Hs_Ensembl = ENSG00000115966
| Hs_RefseqProtein = NP_001871
| Hs_RefseqmRNA = NM_001880
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 175645228
| Hs_GenLoc_end = 175741161
| Hs_Uniprot = P15336
| Mm_EntrezGene = 11909
| Mm_Ensembl = ENSMUSG00000027104
| Mm_RefseqmRNA = NM_001025093
| Mm_RefseqProtein = NP_001020264
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 73617360
| Mm_GenLoc_end = 73664083
| Mm_Uniprot = P70299
}}
}}
'''Activating transcription factor 2''', also known as '''ATF2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATF2 activating transcription factor 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1386| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a transcription factor that is a member of the leucine zipper family of DNA binding proteins. This protein binds to the cAMP-responsive element (CRE), an octameric palindrome. The protein forms a homodimer or heterodimer with c-Jun and stimulates CRE-dependent transcription. The protein is also a histone acetyltransferase (HAT) that specifically acetylates histones H2B and H4 in vitro; thus it may represent a class of sequence-specific factors that activate transcription by direct effects on chromatin components. Additional transcript variants have been identified but their biological validity has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: ATF2 activating transcription factor 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1386| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Denys H, Desmet R, Stragier M, ''et al.'' |title=Cystitis emphysematosa. |journal=Acta urologica Belgica |volume=45 |issue= 4 |pages= 327-31 |year= 1978 |pmid= 602896 |doi= }}
*{{cite journal | author=Kim SJ, Wagner S, Liu F, ''et al.'' |title=Retinoblastoma gene product activates expression of the human TGF-beta 2 gene through transcription factor ATF-2. |journal=Nature |volume=358 |issue= 6384 |pages= 331-4 |year= 1992 |pmid= 1641004 |doi= 10.1038/358331a0 }}
*{{cite journal | author=Hai T, Curran T |title=Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 9 |pages= 3720-4 |year= 1991 |pmid= 1827203 |doi= }}
*{{cite journal | author=Hoeffler JP, Lustbader JW, Chen CY |title=Identification of multiple nuclear factors that interact with cyclic adenosine 3',5'-monophosphate response element-binding protein and activating transcription factor-2 by protein-protein interactions. |journal=Mol. Endocrinol. |volume=5 |issue= 2 |pages= 256-66 |year= 1991 |pmid= 1828107 |doi= }}
*{{cite journal | author=Ozawa K, Sudo T, Soeda E, ''et al.'' |title=Assignment of the human CREB2 (CRE-BP1) gene to 2q32. |journal=Genomics |volume=10 |issue= 4 |pages= 1103-4 |year= 1991 |pmid= 1833307 |doi= }}
*{{cite journal | author=Diep A, Li C, Klisak I, ''et al.'' |title=Assignment of the gene for cyclic AMP-response element binding protein 2 (CREB2) to human chromosome 2q24.1-q32. |journal=Genomics |volume=11 |issue= 4 |pages= 1161-3 |year= 1992 |pmid= 1838349 |doi= }}
*{{cite journal | author=Kara CJ, Liou HC, Ivashkiv LB, Glimcher LH |title=A cDNA for a human cyclic AMP response element-binding protein which is distinct from CREB and expressed preferentially in brain. |journal=Mol. Cell. Biol. |volume=10 |issue= 4 |pages= 1347-57 |year= 1990 |pmid= 2320002 |doi= }}
*{{cite journal | author=Gonzalez GA, Yamamoto KK, Fischer WH, ''et al.'' |title=A cluster of phosphorylation sites on the cyclic AMP-regulated nuclear factor CREB predicted by its sequence. |journal=Nature |volume=337 |issue= 6209 |pages= 749-52 |year= 1989 |pmid= 2521922 |doi= 10.1038/337749a0 }}
*{{cite journal | author=Maekawa T, Sakura H, Kanei-Ishii C, ''et al.'' |title=Leucine zipper structure of the protein CRE-BP1 binding to the cyclic AMP response element in brain. |journal=EMBO J. |volume=8 |issue= 7 |pages= 2023-8 |year= 1989 |pmid= 2529117 |doi= }}
*{{cite journal | author=Raingeaud J, Gupta S, Rogers JS, ''et al.'' |title=Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7420-6 |year= 1995 |pmid= 7535770 |doi= }}
*{{cite journal | author=Livingstone C, Patel G, Jones N |title=ATF-2 contains a phosphorylation-dependent transcriptional activation domain. |journal=EMBO J. |volume=14 |issue= 8 |pages= 1785-97 |year= 1995 |pmid= 7737129 |doi= }}
*{{cite journal | author=van Dam H, Wilhelm D, Herr I, ''et al.'' |title=ATF-2 is preferentially activated by stress-activated protein kinases to mediate c-jun induction in response to genotoxic agents. |journal=EMBO J. |volume=14 |issue= 8 |pages= 1798-811 |year= 1995 |pmid= 7737130 |doi= }}
*{{cite journal | author=Zhou Q, Gedrich RW, Engel DA |title=Transcriptional repression of the c-fos gene by YY1 is mediated by a direct interaction with ATF/CREB. |journal=J. Virol. |volume=69 |issue= 7 |pages= 4323-30 |year= 1995 |pmid= 7769693 |doi= }}
*{{cite journal | author=Newell CL, Deisseroth AB, Lopez-Berestein G |title=Interaction of nuclear proteins with an AP-1/CRE-like promoter sequence in the human TNF-alpha gene. |journal=J. Leukoc. Biol. |volume=56 |issue= 1 |pages= 27-35 |year= 1994 |pmid= 8027667 |doi= }}
*{{cite journal | author=Nomura N, Zu YL, Maekawa T, ''et al.'' |title=Isolation and characterization of a novel member of the gene family encoding the cAMP response element-binding protein CRE-BP1. |journal=J. Biol. Chem. |volume=268 |issue= 6 |pages= 4259-66 |year= 1993 |pmid= 8440710 |doi= }}
*{{cite journal | author=Martin ML, Lieberman PM, Curran T |title=Fos-Jun dimerization promotes interaction of the basic region with TFIIE-34 and TFIIF. |journal=Mol. Cell. Biol. |volume=16 |issue= 5 |pages= 2110-8 |year= 1996 |pmid= 8628277 |doi= }}
*{{cite journal | author=Yang L, Lanier ER, Kraig E |title=Identification of a novel, spliced variant of CREB that is preferentially expressed in the thymus. |journal=J. Immunol. |volume=158 |issue= 6 |pages= 2522-5 |year= 1997 |pmid= 9058782 |doi= }}
*{{cite journal | author=Shuman JD, Cheong J, Coligan JE |title=ATF-2 and C/EBPalpha can form a heterodimeric DNA binding complex in vitro. Functional implications for transcriptional regulation. |journal=J. Biol. Chem. |volume=272 |issue= 19 |pages= 12793-800 |year= 1997 |pmid= 9139739 |doi= }}
*{{cite journal | author=Fukunaga R, Hunter T |title=MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. |journal=EMBO J. |volume=16 |issue= 8 |pages= 1921-33 |year= 1997 |pmid= 9155018 |doi= 10.1093/emboj/16.8.1921 }}
*{{cite journal | author=Kumar S, McDonnell PC, Gum RJ, ''et al.'' |title=Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles. |journal=Biochem. Biophys. Res. Commun. |volume=235 |issue= 3 |pages= 533-8 |year= 1997 |pmid= 9207191 |doi= 10.1006/bbrc.1997.6849 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD81... {December 15, 2007 12:49:45 PM PST}
- REDIRECT: Page directory gave bad page (CD81 (gene)). Continuing with search.. Please correct entry: <975,CD81 (gene)>. {December 15, 2007 12:50:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 12:50:18 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CD81_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1g8q.
| PDB = {{PDB2|1g8q}}, {{PDB2|1iv5}}
| Name = CD81 molecule
| HGNCid = 1701
| Symbol = CD81
| AltSymbols =; S5.7; TAPA1; TSPAN28
| OMIM = 186845
| ECnumber =
| Homologene = 20915
| MGIid = 1096398
| GeneAtlas_image1 = PBB_GE_CD81_200675_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0000187 |text = activation of MAPK activity}} {{GNF_GO|id=GO:0006661 |text = phosphatidylinositol biosynthetic process}} {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0008104 |text = protein localization}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0030384 |text = phosphoinositide metabolic process}} {{GNF_GO|id=GO:0030890 |text = positive regulation of B cell proliferation}} {{GNF_GO|id=GO:0043128 |text = positive regulation of 1-phosphatidylinositol 4-kinase activity}} {{GNF_GO|id=GO:0046718 |text = entry of virus into host cell}} {{GNF_GO|id=GO:0046813 |text = virion attachment, binding of host cell surface receptor}} {{GNF_GO|id=GO:0050731 |text = positive regulation of peptidyl-tyrosine phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 975
| Hs_Ensembl = ENSG00000110651
| Hs_RefseqProtein = NP_004347
| Hs_RefseqmRNA = NM_004356
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 2355096
| Hs_GenLoc_end = 2375225
| Hs_Uniprot = P60033
| Mm_EntrezGene = 12520
| Mm_Ensembl = ENSMUSG00000037706
| Mm_RefseqmRNA = XM_993688
| Mm_RefseqProtein = XP_998782
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 142862185
| Mm_GenLoc_end = 142877314
| Mm_Uniprot = Q3UWG5
}}
}}
'''CD81 molecule''', also known as '''CD81''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD81 CD81 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=975| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is a cell surface glycoprotein that is known to complex with integrins. This protein appears to promote muscle cell fusion and support myotube maintenance. Also it may be involved in signal transduction. This gene is localized in the tumor-suppressor gene region and thus it is a candidate gene for malignancies.<ref name="entrez">{{cite web | title = Entrez Gene: CD81 CD81 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=975| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Berditchevski F |title=Complexes of tetraspanins with integrins: more than meets the eye. |journal=J. Cell. Sci. |volume=114 |issue= Pt 23 |pages= 4143-51 |year= 2002 |pmid= 11739647 |doi= }}
*{{cite journal | author=Ye J |title=Reliance of host cholesterol metabolic pathways for the life cycle of hepatitis C virus. |journal=PLoS Pathog. |volume=3 |issue= 8 |pages= e108 |year= 2007 |pmid= 17784784 |doi= 10.1371/journal.ppat.0030108 }}
*{{cite journal | author=Bradbury LE, Kansas GS, Levy S, ''et al.'' |title=The CD19/CD21 signal transducing complex of human B lymphocytes includes the target of antiproliferative antibody-1 and Leu-13 molecules. |journal=J. Immunol. |volume=149 |issue= 9 |pages= 2841-50 |year= 1992 |pmid= 1383329 |doi= }}
*{{cite journal | author=Andria ML, Hsieh CL, Oren R, ''et al.'' |title=Genomic organization and chromosomal localization of the TAPA-1 gene. |journal=J. Immunol. |volume=147 |issue= 3 |pages= 1030-6 |year= 1991 |pmid= 1650385 |doi= }}
*{{cite journal | author=Oren R, Takahashi S, Doss C, ''et al.'' |title=TAPA-1, the target of an antiproliferative antibody, defines a new family of transmembrane proteins. |journal=Mol. Cell. Biol. |volume=10 |issue= 8 |pages= 4007-15 |year= 1990 |pmid= 1695320 |doi= }}
*{{cite journal | author=Levy S, Nguyen VQ, Andria ML, Takahashi S |title=Structure and membrane topology of TAPA-1. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14597-602 |year= 1991 |pmid= 1860863 |doi= }}
*{{cite journal | author=Takahashi S, Doss C, Levy S, Levy R |title=TAPA-1, the target of an antiproliferative antibody, is associated on the cell surface with the Leu-13 antigen. |journal=J. Immunol. |volume=145 |issue= 7 |pages= 2207-13 |year= 1990 |pmid= 2398277 |doi= }}
*{{cite journal | author=Matsumoto AK, Martin DR, Carter RH, ''et al.'' |title=Functional dissection of the CD21/CD19/TAPA-1/Leu-13 complex of B lymphocytes. |journal=J. Exp. Med. |volume=178 |issue= 4 |pages= 1407-17 |year= 1993 |pmid= 7690834 |doi= }}
*{{cite journal | author=Nagira M, Imai T, Ishikawa I, ''et al.'' |title=Mouse homologue of C33 antigen (CD82), a member of the transmembrane 4 superfamily: complementary DNA, genomic structure, and expression. |journal=Cell. Immunol. |volume=157 |issue= 1 |pages= 144-57 |year= 1994 |pmid= 8039242 |doi= 10.1006/cimm.1994.1212 }}
*{{cite journal | author=Virtaneva KI, Emi N, Marken JS, ''et al.'' |title=Chromosomal localization of three human genes coding for A15, L6, and S5.7 (TAPA1): all members of the transmembrane 4 superfamily of proteins. |journal=Immunogenetics |volume=39 |issue= 5 |pages= 329-34 |year= 1994 |pmid= 8168850 |doi= }}
*{{cite journal | author=Radford KJ, Thorne RF, Hersey P |title=CD63 associates with transmembrane 4 superfamily members, CD9 and CD81, and with beta 1 integrins in human melanoma. |journal=Biochem. Biophys. Res. Commun. |volume=222 |issue= 1 |pages= 13-8 |year= 1996 |pmid= 8630057 |doi= 10.1006/bbrc.1996.0690 }}
*{{cite journal | author=Szöllósi J, Horejsí V, Bene L, ''et al.'' |title=Supramolecular complexes of MHC class I, MHC class II, CD20, and tetraspan molecules (CD53, CD81, and CD82) at the surface of a B cell line JY. |journal=J. Immunol. |volume=157 |issue= 7 |pages= 2939-46 |year= 1996 |pmid= 8816400 |doi= }}
*{{cite journal | author=Berditchevski F, Tolias KF, Wong K, ''et al.'' |title=A novel link between integrins, transmembrane-4 superfamily proteins (CD63 and CD81), and phosphatidylinositol 4-kinase. |journal=J. Biol. Chem. |volume=272 |issue= 5 |pages= 2595-8 |year= 1997 |pmid= 9006891 |doi= }}
*{{cite journal | author=Berditchevski F, Chang S, Bodorova J, Hemler ME |title=Generation of monoclonal antibodies to integrin-associated proteins. Evidence that alpha3beta1 complexes with EMMPRIN/basigin/OX47/M6. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29174-80 |year= 1997 |pmid= 9360995 |doi= }}
*{{cite journal | author=Tachibana I, Bodorova J, Berditchevski F, ''et al.'' |title=NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29181-9 |year= 1997 |pmid= 9360996 |doi= }}
*{{cite journal | author=Hu RJ, Lee MP, Connors TD, ''et al.'' |title=A 2.5-Mb transcript map of a tumor-suppressing subchromosomal transferable fragment from 11p15.5, and isolation and sequence analysis of three novel genes. |journal=Genomics |volume=46 |issue= 1 |pages= 9-17 |year= 1998 |pmid= 9403053 |doi= 10.1006/geno.1997.4981 }}
*{{cite journal | author=Pileri P, Uematsu Y, Campagnoli S, ''et al.'' |title=Binding of hepatitis C virus to CD81. |journal=Science |volume=282 |issue= 5390 |pages= 938-41 |year= 1998 |pmid= 9794763 |doi= }}
*{{cite journal | author=Serru V, Le Naour F, Billard M, ''et al.'' |title=Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions. |journal=Biochem. J. |volume=340 ( Pt 1) |issue= |pages= 103-11 |year= 1999 |pmid= 10229664 |doi= }}
*{{cite journal | author=Tachibana I, Hemler ME |title=Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance. |journal=J. Cell Biol. |volume=146 |issue= 4 |pages= 893-904 |year= 1999 |pmid= 10459022 |doi= }}
*{{cite journal | author=Higginbottom A, Quinn ER, Kuo CC, ''et al.'' |title=Identification of amino acid residues in CD81 critical for interaction with hepatitis C virus envelope glycoprotein E2. |journal=J. Virol. |volume=74 |issue= 8 |pages= 3642-9 |year= 2000 |pmid= 10729140 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CEACAM1... {December 15, 2007 12:48:58 PM PST}
- REDIRECT: Page directory gave bad page (CEACAM1). Continuing with search.. Please correct entry: <634,CEACAM1>. {December 15, 2007 12:49:29 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 12:49:45 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CEACAM1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2gk2.
| PDB = {{PDB2|2gk2}}
| Name = Carcinoembryonic antigen-related cell adhesion molecule 1 (biliary glycoprotein)
| HGNCid = 1814
| Symbol = CEACAM1
| AltSymbols =; BGP; BGP1; BGPI
| OMIM = 109770
| ECnumber =
| Homologene = 86044
| MGIid = 1347245
| GeneAtlas_image1 = PBB_GE_CEACAM1_206576_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CEACAM1_209498_at_tn.png
| GeneAtlas_image3 = PBB_GE_CEACAM1_211883_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0007156 |text = homophilic cell adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007565 |text = female pregnancy}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0016477 |text = cell migration}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 634
| Hs_Ensembl = ENSG00000079385
| Hs_RefseqProtein = NP_001020083
| Hs_RefseqmRNA = NM_001024912
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 47703298
| Hs_GenLoc_end = 47724479
| Hs_Uniprot = P13688
| Mm_EntrezGene = 26365
| Mm_Ensembl = ENSMUSG00000074272
| Mm_RefseqmRNA = XM_989614
| Mm_RefseqProtein = XP_994708
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 24990200
| Mm_GenLoc_end = 25186385
| Mm_Uniprot = Q3LFS7
}}
}}
'''Carcinoembryonic antigen-related cell adhesion molecule 1 (biliary glycoprotein)''', also known as '''CEACAM1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CEACAM1 carcinoembryonic antigen-related cell adhesion molecule 1 (biliary glycoprotein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=634| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the carcinoembryonic antigen (CEA) gene family, which belongs to the immunoglobulin superfamily. Two subgroups of the CEA family, the CEA cell adhesion molecules and the pregnancy-specific glycoproteins, are located within a 1.2 Mb cluster on the long arm of chromosome 19. Eleven pseudogenes of the CEA cell adhesion molecule subgroup are also found in the cluster. The encoded protein was originally described in bile ducts of liver as biliary glycoprotein. Subsequently, it was found to be a cell-cell adhesion molecule detected on leukocytes, epithelia, and endothelia. The encoded protein mediates cell adhesion via homophilic as well as heterophilic binding to other proteins of the subgroup. Multiple cellular activities have been attributed to the encoded protein, including roles in the differentiation and arrangement of tissue three-dimensional structure, angiogenesis, apoptosis, tumor suppression, metastasis, and the modulation of innate and adaptive immune responses. Multiple transcript variants encoding different isoforms have been reported, but the full-length nature of only two has been determined.<ref name="entrez">{{cite web | title = Entrez Gene: CEACAM1 carcinoembryonic antigen-related cell adhesion molecule 1 (biliary glycoprotein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=634| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gray-Owen SD, Blumberg RS |title=CEACAM1: contact-dependent control of immunity. |journal=Nat. Rev. Immunol. |volume=6 |issue= 6 |pages= 433-46 |year= 2006 |pmid= 16724098 |doi= 10.1038/nri1864 }}
*{{cite journal | author=Svenberg T, Hammarström S, Zeromski J |title=Immunofluorescence studies on the occurrence and localization of the CEA-related biliary glycoprotein I (BGP I) in normal human gastrointestinal tissues. |journal=Clin. Exp. Immunol. |volume=36 |issue= 3 |pages= 436-41 |year= 1979 |pmid= 385181 |doi= }}
*{{cite journal | author=Thompson J, Zimmermann W, Osthus-Bugat P, ''et al.'' |title=Long-range chromosomal mapping of the carcinoembryonic antigen (CEA) gene family cluster. |journal=Genomics |volume=12 |issue= 4 |pages= 761-72 |year= 1992 |pmid= 1572649 |doi= }}
*{{cite journal | author=Kuroki M, Arakawa F, Matsuo Y, ''et al.'' |title=Three novel molecular forms of biliary glycoprotein deduced from cDNA clones from a human leukocyte library. |journal=Biochem. Biophys. Res. Commun. |volume=176 |issue= 2 |pages= 578-85 |year= 1991 |pmid= 2025273 |doi= }}
*{{cite journal | author=Hinoda Y, Neumaier M, Hefta SA, ''et al.'' |title=Molecular cloning of a cDNA coding biliary glycoprotein I: primary structure of a glycoprotein immunologically crossreactive with carcinoembryonic antigen. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 18 |pages= 6959-63 |year= 1988 |pmid= 2457922 |doi= }}
*{{cite journal | author=Barnett TR, Kretschmer A, Austen DA, ''et al.'' |title=Carcinoembryonic antigens: alternative splicing accounts for the multiple mRNAs that code for novel members of the carcinoembryonic antigen family. |journal=J. Cell Biol. |volume=108 |issue= 2 |pages= 267-76 |year= 1989 |pmid= 2537311 |doi= }}
*{{cite journal | author=Neumaier M, Paululat S, Chan A, ''et al.'' |title=Biliary glycoprotein, a potential human cell adhesion molecule, is down-regulated in colorectal carcinomas. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 22 |pages= 10744-8 |year= 1993 |pmid= 7504281 |doi= }}
*{{cite journal | author=Formisano P, Najjar SM, Gross CN, ''et al.'' |title=Receptor-mediated internalization of insulin. Potential role of pp120/HA4, a substrate of the insulin receptor kinase. |journal=J. Biol. Chem. |volume=270 |issue= 41 |pages= 24073-7 |year= 1995 |pmid= 7592607 |doi= }}
*{{cite journal | author=Frängsmyr L, Baranov V, Prall F, ''et al.'' |title=Cell- and region-specific expression of biliary glycoprotein and its messenger RNA in normal human colonic mucosa. |journal=Cancer Res. |volume=55 |issue= 14 |pages= 2963-7 |year= 1995 |pmid= 7606710 |doi= }}
*{{cite journal | author=Najjar SM, Philippe N, Suzuki Y, ''et al.'' |title=Insulin-stimulated phosphorylation of recombinant pp120/HA4, an endogenous substrate of the insulin receptor tyrosine kinase. |journal=Biochemistry |volume=34 |issue= 29 |pages= 9341-9 |year= 1995 |pmid= 7626603 |doi= }}
*{{cite journal | author=Nédellec P, Turbide C, Beauchemin N |title=Characterization and transcriptional activity of the mouse biliary glycoprotein 1 gene, a carcinoembryonic antigen-related gene. |journal=Eur. J. Biochem. |volume=231 |issue= 1 |pages= 104-14 |year= 1995 |pmid= 7628460 |doi= }}
*{{cite journal | author=Watt SM, Fawcett J, Murdoch SJ, ''et al.'' |title=CD66 identifies the biliary glycoprotein (BGP) adhesion molecule: cloning, expression, and adhesion functions of the BGPc splice variant. |journal=Blood |volume=84 |issue= 1 |pages= 200-10 |year= 1994 |pmid= 8018919 |doi= }}
*{{cite journal | author=Hauck W, Nédellec P, Turbide C, ''et al.'' |title=Transcriptional control of the human biliary glycoprotein gene, a CEA gene family member down-regulated in colorectal carcinomas. |journal=Eur. J. Biochem. |volume=223 |issue= 2 |pages= 529-41 |year= 1994 |pmid= 8055923 |doi= }}
*{{cite journal | author=Barnett TR, Drake L, Pickle W |title=Human biliary glycoprotein gene: characterization of a family of novel alternatively spliced RNAs and their expressed proteins. |journal=Mol. Cell. Biol. |volume=13 |issue= 2 |pages= 1273-82 |year= 1993 |pmid= 8423792 |doi= }}
*{{cite journal | author=Kuroki M, Yamanaka T, Matsuo Y, ''et al.'' |title=Immunochemical analysis of carcinoembryonic antigen (CEA)-related antigens differentially localized in intracellular granules of human neutrophils. |journal=Immunol. Invest. |volume=24 |issue= 5 |pages= 829-43 |year= 1996 |pmid= 8543346 |doi= }}
*{{cite journal | author=Huber M, Izzi L, Grondin P, ''et al.'' |title=The carboxyl-terminal region of biliary glycoprotein controls its tyrosine phosphorylation and association with protein-tyrosine phosphatases SHP-1 and SHP-2 in epithelial cells. |journal=J. Biol. Chem. |volume=274 |issue= 1 |pages= 335-44 |year= 1999 |pmid= 9867848 |doi= }}
*{{cite journal | author=Feuk-Lagerstedt E, Jordan ET, Leffler H, ''et al.'' |title=Identification of CD66a and CD66b as the major galectin-3 receptor candidates in human neutrophils. |journal=J. Immunol. |volume=163 |issue= 10 |pages= 5592-8 |year= 1999 |pmid= 10553088 |doi= }}
*{{cite journal | author=Soni P, Lakkis M, Poy MN, ''et al.'' |title=The differential effects of pp120 (Ceacam 1) on the mitogenic action of insulin and insulin-like growth factor 1 are regulated by the nonconserved tyrosine 1316 in the insulin receptor. |journal=Mol. Cell. Biol. |volume=20 |issue= 11 |pages= 3896-905 |year= 2000 |pmid= 10805733 |doi= }}
*{{cite journal | author=Ergün S, Kilik N, Ziegeler G, ''et al.'' |title=CEA-related cell adhesion molecule 1: a potent angiogenic factor and a major effector of vascular endothelial growth factor. |journal=Mol. Cell |volume=5 |issue= 2 |pages= 311-20 |year= 2000 |pmid= 10882072 |doi= }}
*{{cite journal | author=Wang L, Lin SH, Wu WG, ''et al.'' |title=C-CAM1, a candidate tumor suppressor gene, is abnormally expressed in primary lung cancers. |journal=Clin. Cancer Res. |volume=6 |issue= 8 |pages= 2988-93 |year= 2000 |pmid= 10955775 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on COL4A1... {December 15, 2007 12:50:18 PM PST}
- REDIRECT: Page directory gave bad page (COL4A1 (gene)). Continuing with search.. Please correct entry: <1282,COL4A1 (gene)>. {December 15, 2007 12:50:52 PM PST}
- SEARCH REDIRECT: Control Box Found: COL4A1 {December 15, 2007 12:50:57 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {December 15, 2007 12:51:00 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {December 15, 2007 12:51:00 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {December 15, 2007 12:51:00 PM PST}
- UPDATED: Updated protein page: COL4A1 {December 15, 2007 12:51:07 PM PST}
- INFO: Beginning work on COL4A3... {December 15, 2007 12:51:07 PM PST}
- REDIRECT: Page directory gave bad page (COL4A3 (gene)). Continuing with search.. Please correct entry: <1285,COL4A3 (gene)>. {December 15, 2007 12:51:47 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 12:51:51 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Collagen, type IV, alpha 3 (Goodpasture antigen)
| HGNCid = 2204
| Symbol = COL4A3
| AltSymbols =;
| OMIM = 120070
| ECnumber =
| Homologene = 68033
| MGIid = 104688
| GeneAtlas_image1 = PBB_GE_COL4A3_214641_at_tn.png
| GeneAtlas_image2 = PBB_GE_COL4A3_216893_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_COL4A3_222073_at_tn.png
| Function = {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008191 |text = metalloendopeptidase inhibitor activity}}
| Component = {{GNF_GO|id=GO:0005581 |text = collagen}} {{GNF_GO|id=GO:0005587 |text = collagen type IV}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006919 |text = caspase activation}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0008015 |text = circulation}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0016525 |text = negative regulation of angiogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1285
| Hs_Ensembl = ENSG00000169031
| Hs_RefseqProtein = NP_000082
| Hs_RefseqmRNA = NM_000091
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 227810928
| Hs_GenLoc_end = 227884953
| Hs_Uniprot = Q01955
| Mm_EntrezGene = 12828
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_007734
| Mm_RefseqProtein = NP_031760
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Collagen, type IV, alpha 3 (Goodpasture antigen)''', also known as '''COL4A3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COL4A3 collagen, type IV, alpha 3 (Goodpasture antigen)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1285| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Type IV collagen, the major structural component of basement membranes, is a multimeric protein composed of 3 alpha subunits. These subunits are encoded by 6 different genes, alpha 1 through alpha 6, each of which can form a triple helix structure with 2 other subunits to form type IV collagen. This gene encodes alpha 3. In the Goodpasture syndrome, autoantibodies bind to the collagen molecules in the basement membranes of alveoli and glomeruli. The epitopes that elicit these autoantibodies are localized largely to the non-collagenous C-terminal domain of the protein. A specific kinase phosphorylates amino acids in this same C-terminal region and the expression of this kinase is upregulated during pathogenesis. There are multiple alternate transcripts that appear to be unique to this human alpha 3 gene and alternate splicing is restricted to the six exons that encode this C-terminal domain. This gene is also linked to an autosomal recessive form of Alport syndrome. The mutations contributing to this syndrome are also located within the exons that encode this C-terminal region. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. Some exons of this gene are interspersed with exons of an uncharacterized gene which is on the opposite strand.<ref name="entrez">{{cite web | title = Entrez Gene: COL4A3 collagen, type IV, alpha 3 (Goodpasture antigen)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1285| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hinek A |title=Nature and the multiple functions of the 67-kD elastin-/laminin binding protein. |journal=Cell Adhes. Commun. |volume=2 |issue= 3 |pages= 185-93 |year= 1995 |pmid= 7827955 |doi= }}
*{{cite journal | author=Ständer M, Naumann U, Wick W, Weller M |title=Transforming growth factor-beta and p-21: multiple molecular targets of decorin-mediated suppression of neoplastic growth. |journal=Cell Tissue Res. |volume=296 |issue= 2 |pages= 221-7 |year= 1999 |pmid= 10382266 |doi= }}
*{{cite journal | author=Kurpakus Wheater M, Kernacki KA, Hazlett LD |title=Corneal cell proteins and ocular surface pathology. |journal=Biotechnic & histochemistry : official publication of the Biological Stain Commission |volume=74 |issue= 3 |pages= 146-59 |year= 1999 |pmid= 10416788 |doi= }}
*{{cite journal | author=Pescucci C, Longo I, Bruttini M, ''et al.'' |title=Type-IV collagen related diseases. |journal=J. Nephrol. |volume=16 |issue= 2 |pages= 314-6 |year= 2003 |pmid= 12768082 |doi= }}
*{{cite journal | author=Torra R, Tazón-Vega B, Ars E, Ballarín J |title=Collagen type IV (alpha3-alpha4) nephropathy: from isolated haematuria to renal failure. |journal=Nephrol. Dial. Transplant. |volume=19 |issue= 10 |pages= 2429-32 |year= 2005 |pmid= 15280517 |doi= 10.1093/ndt/gfh435 }}
*{{cite journal | author=Rana K, Wang YY, Buzza M, ''et al.'' |title=The genetics of thin basement membrane nephropathy. |journal=Semin. Nephrol. |volume=25 |issue= 3 |pages= 163-70 |year= 2005 |pmid= 15880327 |doi= }}
*{{cite journal | author=Maziers N, Dahan K, Pirson Y |title=[From Alport syndrome to benign familial hematuria: clinical and genetic aspect] |journal=Nephrol. Ther. |volume=1 |issue= 2 |pages= 90-100 |year= 2006 |pmid= 16895672 |doi= 10.1016/j.nephro.2005.03.005 }}
*{{cite journal | author=Ghebrehiwet B, Peerschke EI, Hong Y, ''et al.'' |title=Short amino acid sequences derived from C1q receptor (C1q-R) show homology with the alpha chains of fibronectin and vitronectin receptors and collagen type IV. |journal=J. Leukoc. Biol. |volume=51 |issue= 6 |pages= 546-56 |year= 1992 |pmid= 1377218 |doi= }}
*{{cite journal | author=Quinones S, Bernal D, García-Sogo M, ''et al.'' |title=Exon/intron structure of the human alpha 3(IV) gene encompassing the Goodpasture antigen (alpha 3(IV)NC1). Identification of a potentially antigenic region at the triple helix/NC1 domain junction. |journal=J. Biol. Chem. |volume=267 |issue= 28 |pages= 19780-4 |year= 1992 |pmid= 1400291 |doi= }}
*{{cite journal | author=Gupta S, Batchu RB, Datta K |title=Purification, partial characterization of rat kidney hyaluronic acid binding protein and its localization on the cell surface. |journal=Eur. J. Cell Biol. |volume=56 |issue= 1 |pages= 58-67 |year= 1992 |pmid= 1724753 |doi= }}
*{{cite journal | author=Turner N, Mason PJ, Brown R, ''et al.'' |title=Molecular cloning of the human Goodpasture antigen demonstrates it to be the alpha 3 chain of type IV collagen. |journal=J. Clin. Invest. |volume=89 |issue= 2 |pages= 592-601 |year= 1992 |pmid= 1737849 |doi= }}
*{{cite journal | author=Morrison KE, Mariyama M, Yang-Feng TL, Reeders ST |title=Sequence and localization of a partial cDNA encoding the human alpha 3 chain of type IV collagen. |journal=Am. J. Hum. Genet. |volume=49 |issue= 3 |pages= 545-54 |year= 1991 |pmid= 1882840 |doi= }}
*{{cite journal | author=Hernandez MR, Igoe F, Neufeld AH |title=Extracellular matrix of the human optic nerve head. |journal=Am. J. Ophthalmol. |volume=102 |issue= 2 |pages= 139-48 |year= 1986 |pmid= 2426947 |doi= }}
*{{cite journal | author=Griffin CA, Emanuel BS, Hansen JR, ''et al.'' |title=Human collagen genes encoding basement membrane alpha 1 (IV) and alpha 2 (IV) chains map to the distal long arm of chromosome 13. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 2 |pages= 512-6 |year= 1987 |pmid= 3025878 |doi= }}
*{{cite journal | author=Murata K, Motayama T, Kotake C |title=Collagen types in various layers of the human aorta and their changes with the atherosclerotic process. |journal=Atherosclerosis |volume=60 |issue= 3 |pages= 251-62 |year= 1986 |pmid= 3089234 |doi= }}
*{{cite journal | author=Glant TT, Hadházy C, Mikecz K, Sipos A |title=Appearance and persistence of fibronectin in cartilage. Specific interaction of fibronectin with collagen type II. |journal=Histochemistry |volume=82 |issue= 2 |pages= 149-58 |year= 1985 |pmid= 3997552 |doi= }}
*{{cite journal | author=Uscanga L, Kennedy RH, Stocker S, ''et al.'' |title=Immunolocalization of collagen types, laminin and fibronectin in the normal human pancreas. |journal=Digestion |volume=30 |issue= 3 |pages= 158-64 |year= 1984 |pmid= 6389236 |doi= }}
*{{cite journal | author=Sundarraj N, Willson J |title=Monoclonal antibody to human basement membrane collagen type IV. |journal=Immunology |volume=47 |issue= 1 |pages= 133-40 |year= 1982 |pmid= 6811420 |doi= }}
*{{cite journal | author=Hahn E, Wick G, Pencev D, Timpl R |title=Distribution of basement membrane proteins in normal and fibrotic human liver: collagen type IV, laminin, and fibronectin. |journal=Gut |volume=21 |issue= 1 |pages= 63-71 |year= 1980 |pmid= 6988303 |doi= }}
*{{cite journal | author=Singhal PC, Sharma P, Garg P |title=HIV-1 gp160 protein-macrophage interactions modulate mesangial cell proliferation and matrix synthesis. |journal=Am. J. Pathol. |volume=147 |issue= 6 |pages= 1780-9 |year= 1996 |pmid= 7495302 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CTSD... {December 15, 2007 12:52:44 PM PST}
- REDIRECT: Page directory gave bad page (CTSD). Continuing with search.. Please correct entry: <1509,CTSD>. {December 15, 2007 12:53:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 12:53:23 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CTSD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1lya.
| PDB = {{PDB2|1lya}}, {{PDB2|1lyb}}, {{PDB2|1lyw}}
| Name = Cathepsin D
| HGNCid = 2529
| Symbol = CTSD
| AltSymbols =; CLN10; CPSD; MGC2311
| OMIM = 116840
| ECnumber =
| Homologene = 55616
| MGIid = 88562
| GeneAtlas_image1 = PBB_GE_CTSD_200766_at_tn.png
| GeneAtlas_image2 = PBB_GE_CTSD_gnf1h05436_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004192 |text = cathepsin D activity}} {{GNF_GO|id=GO:0004194 |text = pepsin A activity}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1509
| Hs_Ensembl = ENSG00000117984
| Hs_RefseqProtein = NP_001900
| Hs_RefseqmRNA = NM_001909
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 1730558
| Hs_GenLoc_end = 1741798
| Hs_Uniprot = P07339
| Mm_EntrezGene = 13033
| Mm_Ensembl = ENSMUSG00000007891
| Mm_RefseqmRNA = NM_009983
| Mm_RefseqProtein = NP_034113
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 142185307
| Mm_GenLoc_end = 142197290
| Mm_Uniprot = Q05BF3
}}
}}
'''Cathepsin D''', also known as '''CTSD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CTSD cathepsin D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1509| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a lysosomal aspartyl protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. This proteinase, which is a member of the peptidase C1 family, has a specificity similar to but narrower than that of pepsin A. Transcription of this gene is initiated from several sites, including one which is a start site for an estrogen-regulated transcript. Mutations in this gene are involved in the pathogenesis of several diseases, including breast cancer and possibly Alzheimer disease.<ref name="entrez">{{cite web | title = Entrez Gene: CTSD cathepsin D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1509| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Chao J, Miao RQ, Chen V, ''et al.'' |title=Novel roles of kallistatin, a specific tissue kallikrein inhibitor, in vascular remodeling. |journal=Biol. Chem. |volume=382 |issue= 1 |pages= 15-21 |year= 2001 |pmid= 11258665 |doi= }}
*{{cite journal | author=Leto G, Tumminello FM, Crescimanno M, ''et al.'' |title=Cathepsin D expression levels in nongynecological solid tumors: clinical and therapeutic implications. |journal=Clin. Exp. Metastasis |volume=21 |issue= 2 |pages= 91-106 |year= 2004 |pmid= 15168727 |doi= }}
*{{cite journal | author=Liaudet-Coopman E, Beaujouin M, Derocq D, ''et al.'' |title=Cathepsin D: newly discovered functions of a long-standing aspartic protease in cancer and apoptosis. |journal=Cancer Lett. |volume=237 |issue= 2 |pages= 167-79 |year= 2006 |pmid= 16046058 |doi= 10.1016/j.canlet.2005.06.007 }}
*{{cite journal | author=Knight CG, Barrett AJ |title=Interaction of human cathepsin D with the inhibitor pepstatin. |journal=Biochem. J. |volume=155 |issue= 1 |pages= 117-25 |year= 1976 |pmid= 938470 |doi= }}
*{{cite journal | author=Gulnik S, Baldwin ET, Tarasova N, Erickson J |title=Human liver cathepsin D. Purification, crystallization and preliminary X-ray diffraction analysis of a lysosomal enzyme. |journal=J. Mol. Biol. |volume=227 |issue= 1 |pages= 265-70 |year= 1992 |pmid= 1522590 |doi= }}
*{{cite journal | author=Conner GE, Richo G |title=Isolation and characterization of a stable activation intermediate of the lysosomal aspartyl protease cathepsin D. |journal=Biochemistry |volume=31 |issue= 4 |pages= 1142-7 |year= 1992 |pmid= 1734961 |doi= }}
*{{cite journal | author=Fujita H, Tanaka Y, Noguchi Y, ''et al.'' |title=Isolation and sequencing of a cDNA clone encoding rat liver lysosomal cathepsin D and the structure of three forms of mature enzymes. |journal=Biochem. Biophys. Res. Commun. |volume=179 |issue= 1 |pages= 190-6 |year= 1991 |pmid= 1883350 |doi= }}
*{{cite journal | author=Dunn AD, Crutchfield HE, Dunn JT |title=Thyroglobulin processing by thyroidal proteases. Major sites of cleavage by cathepsins B, D, and L. |journal=J. Biol. Chem. |volume=266 |issue= 30 |pages= 20198-204 |year= 1991 |pmid= 1939080 |doi= }}
*{{cite journal | author=Lenarcic B, Krasovec M, Ritonja A, ''et al.'' |title=Inactivation of human cystatin C and kininogen by human cathepsin D. |journal=FEBS Lett. |volume=280 |issue= 2 |pages= 211-5 |year= 1991 |pmid= 2013314 |doi= }}
*{{cite journal | author=Redecker B, Heckendorf B, Grosch HW, ''et al.'' |title=Molecular organization of the human cathepsin D gene. |journal=DNA Cell Biol. |volume=10 |issue= 6 |pages= 423-31 |year= 1991 |pmid= 2069717 |doi= }}
*{{cite journal | author=Conner GE, Udey JA |title=Expression and refolding of recombinant human fibroblast procathepsin D. |journal=DNA Cell Biol. |volume=9 |issue= 1 |pages= 1-9 |year= 1990 |pmid= 2180427 |doi= }}
*{{cite journal | author=Capony F, Rougeot C, Montcourrier P, ''et al.'' |title=Increased secretion, altered processing, and glycosylation of pro-cathepsin D in human mammary cancer cells. |journal=Cancer Res. |volume=49 |issue= 14 |pages= 3904-9 |year= 1989 |pmid= 2736531 |doi= }}
*{{cite journal | author=Lenarcic B, Kos J, Dolenc I, ''et al.'' |title=Cathepsin D inactivates cysteine proteinase inhibitors, cystatins. |journal=Biochem. Biophys. Res. Commun. |volume=154 |issue= 2 |pages= 765-72 |year= 1988 |pmid= 3261170 |doi= }}
*{{cite journal | author=Westley BR, May FE |title=Oestrogen regulates cathepsin D mRNA levels in oestrogen responsive human breast cancer cells. |journal=Nucleic Acids Res. |volume=15 |issue= 9 |pages= 3773-86 |year= 1987 |pmid= 3588310 |doi= }}
*{{cite journal | author=Terayama H, Fukuzumi R |title=Ubiquitous presence of calciferin-like and cathepsin D-like activities in the sera (vertebrates) and humoral fluids (invertebrates). |journal=Comp. Biochem. Physiol., B |volume=87 |issue= 4 |pages= 675-9 |year= 1987 |pmid= 3665421 |doi= }}
*{{cite journal | author=Faust PL, Kornfeld S, Chirgwin JM |title=Cloning and sequence analysis of cDNA for human cathepsin D. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 15 |pages= 4910-4 |year= 1985 |pmid= 3927292 |doi= }}
*{{cite journal | author=Sekiguchi K, Siri A, Zardi L, Hakomori S |title=Differences in domain structure between human fibronectins isolated from plasma and from culture supernatants of normal and transformed fibroblasts. Studies with domain-specific antibodies. |journal=J. Biol. Chem. |volume=260 |issue= 8 |pages= 5105-14 |year= 1985 |pmid= 3988746 |doi= }}
*{{cite journal | author=Lemansky P, Gieselmann V, Hasilik A, von Figura K |title=Cathepsin D and beta-hexosaminidase synthesized in the presence of 1-deoxynojirimycin accumulate in the endoplasmic reticulum. |journal=J. Biol. Chem. |volume=259 |issue= 16 |pages= 10129-35 |year= 1984 |pmid= 6236213 |doi= }}
*{{cite journal | author=Dreyer RN, Bausch KM, Fracasso P, ''et al.'' |title=Processing of the pre-beta-amyloid protein by cathepsin D is enhanced by a familial Alzheimer's disease mutation. |journal=Eur. J. Biochem. |volume=224 |issue= 2 |pages= 265-71 |year= 1994 |pmid= 7523115 |doi= }}
*{{cite journal | author=Atkins KB, Troen BR |title=Regulation of cathepsin D gene expression in HL-60 cells by retinoic acid and calcitriol. |journal=Cell Growth Differ. |volume=6 |issue= 7 |pages= 871-7 |year= 1995 |pmid= 7547509 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CTSL1... {December 15, 2007 12:53:23 PM PST}
- REDIRECT: Page directory gave bad page (CTSL1). Continuing with search.. Please correct entry: <1514,CTSL1>. {December 15, 2007 12:53:43 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 12:53:59 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CTSL1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cjl.
| PDB = {{PDB2|1cjl}}, {{PDB2|1cs8}}, {{PDB2|1icf}}, {{PDB2|1mhw}}
| Name = Cathepsin L1
| HGNCid = 2537
| Symbol = CTSL1
| AltSymbols =; CATL; CTSL; FLJ31037; MEP
| OMIM = 116880
| ECnumber =
| Homologene = 76699
| MGIid =
| GeneAtlas_image1 = PBB_GE_CTSL1_202087_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004197 |text = cysteine-type endopeptidase activity}} {{GNF_GO|id=GO:0004217 |text = cathepsin L activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1514
| Hs_Ensembl = ENSG00000135047
| Hs_RefseqProtein = NP_001903
| Hs_RefseqmRNA = NM_001912
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 89530254
| Hs_GenLoc_end = 89536127
| Hs_Uniprot = P07711
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Cathepsin L1''', also known as '''CTSL1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CTSL1 cathepsin L1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1514| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a lysosomal cysteine proteinase that plays a major role in intracellular protein catabolism. Its substrates include collagen and elastin, as well as alpha-1 protease inhibitor, a major controlling element of neutrophil elastase activity. The encoded protein has been implicated in several pathologic processes, including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. This protein, which is a member of the peptidase C1 family, is a dimer composed of disulfide-linked heavy and light chains, both produced from a single protein precursor. At least two transcript variants encoding the same protein have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CTSL1 cathepsin L1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1514| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Smith CG, Smith MT, Besch NF, ''et al.'' |title=Effect of delta 9-tetrahydrocannabinol (THC) on female reproductive function. |journal=Advances in the biosciences |volume=22-23 |issue= |pages= 449-67 |year= 1980 |pmid= 116880 |doi= }}
*{{cite journal | author=Goretzki L, Schmitt M, Mann K, ''et al.'' |title=Effective activation of the proenzyme form of the urokinase-type plasminogen activator (pro-uPA) by the cysteine protease cathepsin L. |journal=FEBS Lett. |volume=297 |issue= 1-2 |pages= 112-8 |year= 1992 |pmid= 1551416 |doi= }}
*{{cite journal | author=Dunn AD, Crutchfield HE, Dunn JT |title=Thyroglobulin processing by thyroidal proteases. Major sites of cleavage by cathepsins B, D, and L. |journal=J. Biol. Chem. |volume=266 |issue= 30 |pages= 20198-204 |year= 1991 |pmid= 1939080 |doi= }}
*{{cite journal | author=Stearns NA, Dong JM, Pan JX, ''et al.'' |title=Comparison of cathepsin L synthesized by normal and transformed cells at the gene, message, protein, and oligosaccharide levels. |journal=Arch. Biochem. Biophys. |volume=283 |issue= 2 |pages= 447-57 |year= 1991 |pmid= 2275556 |doi= }}
*{{cite journal | author=Joseph LJ, Chang LC, Stamenkovich D, Sukhatme VP |title=Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts. |journal=J. Clin. Invest. |volume=81 |issue= 5 |pages= 1621-9 |year= 1988 |pmid= 2835398 |doi= }}
*{{cite journal | author=Ritonja A, Popović T, Kotnik M, ''et al.'' |title=Amino acid sequences of the human kidney cathepsins H and L. |journal=FEBS Lett. |volume=228 |issue= 2 |pages= 341-5 |year= 1988 |pmid= 3342889 |doi= }}
*{{cite journal | author=Gal S, Gottesman MM |title=Isolation and sequence of a cDNA for human pro-(cathepsin L). |journal=Biochem. J. |volume=253 |issue= 1 |pages= 303-6 |year= 1988 |pmid= 3421948 |doi= }}
*{{cite journal | author=Johnson DA, Barrett AJ, Mason RW |title=Cathepsin L inactivates alpha 1-proteinase inhibitor by cleavage in the reactive site region. |journal=J. Biol. Chem. |volume=261 |issue= 31 |pages= 14748-51 |year= 1986 |pmid= 3490478 |doi= }}
*{{cite journal | author=Mason RW, Walker JE, Northrop FD |title=The N-terminal amino acid sequences of the heavy and light chains of human cathepsin L. Relationship to a cDNA clone for a major cysteine proteinase from a mouse macrophage cell line. |journal=Biochem. J. |volume=240 |issue= 2 |pages= 373-7 |year= 1987 |pmid= 3545185 |doi= }}
*{{cite journal | author=Joseph L, Lapid S, Sukhatme V |title=The major ras induced protein in NIH3T3 cells is cathepsin L. |journal=Nucleic Acids Res. |volume=15 |issue= 7 |pages= 3186 |year= 1987 |pmid= 3550705 |doi= }}
*{{cite journal | author=Kärgel HJ, Dettmer R, Etzold G, ''et al.'' |title=Action of rat liver cathepsin L on glucagon. |journal=Acta Biol. Med. Ger. |volume=40 |issue= 9 |pages= 1139-43 |year= 1982 |pmid= 7340337 |doi= }}
*{{cite journal | author=Chauhan SS, Popescu NC, Ray D, ''et al.'' |title=Cloning, genomic organization, and chromosomal localization of human cathepsin L. |journal=J. Biol. Chem. |volume=268 |issue= 2 |pages= 1039-45 |year= 1993 |pmid= 8419312 |doi= }}
*{{cite journal | author=Bevec T, Stoka V, Pungercic G, ''et al.'' |title=Major histocompatibility complex class II-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L. |journal=J. Exp. Med. |volume=183 |issue= 4 |pages= 1331-8 |year= 1996 |pmid= 8666891 |doi= }}
*{{cite journal | author=Coulombe R, Grochulski P, Sivaraman J, ''et al.'' |title=Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. |journal=EMBO J. |volume=15 |issue= 20 |pages= 5492-503 |year= 1996 |pmid= 8896443 |doi= }}
*{{cite journal | author=Baumgrass R, Williamson MK, Price PA |title=Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B, D, L, H, and S. |journal=J. Bone Miner. Res. |volume=12 |issue= 3 |pages= 447-55 |year= 1997 |pmid= 9076588 |doi= }}
*{{cite journal | author=Fujishima A, Imai Y, Nomura T, ''et al.'' |title=The crystal structure of human cathepsin L complexed with E-64. |journal=FEBS Lett. |volume=407 |issue= 1 |pages= 47-50 |year= 1997 |pmid= 9141479 |doi= }}
*{{cite journal | author=Ménard R, Carmona E, Takebe S, ''et al.'' |title=Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro. |journal=J. Biol. Chem. |volume=273 |issue= 8 |pages= 4478-84 |year= 1998 |pmid= 9468501 |doi= }}
*{{cite journal | author=Schick C, Pemberton PA, Shi GP, ''et al.'' |title=Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: a kinetic analysis. |journal=Biochemistry |volume=37 |issue= 15 |pages= 5258-66 |year= 1998 |pmid= 9548757 |doi= 10.1021/bi972521d }}
*{{cite journal | author=Estrada S, Nycander M, Hill NJ, ''et al.'' |title=The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L. |journal=Biochemistry |volume=37 |issue= 20 |pages= 7551-60 |year= 1998 |pmid= 9585570 |doi= 10.1021/bi980026r }}
*{{cite journal | author=Halfon S, Ford J, Foster J, ''et al.'' |title=Leukocystatin, a new Class II cystatin expressed selectively by hematopoietic cells. |journal=J. Biol. Chem. |volume=273 |issue= 26 |pages= 16400-8 |year= 1998 |pmid= 9632704 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GRIN1... {December 15, 2007 12:53:59 PM PST}
- REDIRECT: Page directory gave bad page (GRIN1). Continuing with search.. Please correct entry: <2902,GRIN1>. {December 15, 2007 12:54:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 12:54:48 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Glutamate receptor, ionotropic, N-methyl D-aspartate 1
| HGNCid = 4584
| Symbol = GRIN1
| AltSymbols =; NMDA1; NMDAR1; NR1
| OMIM = 138249
| ECnumber =
| Homologene = 7187
| MGIid = 95819
| GeneAtlas_image1 = PBB_GE_GRIN1_205914_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_GRIN1_205915_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_GRIN1_210781_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003774 |text = motor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004970 |text = ionotropic glutamate receptor activity}} {{GNF_GO|id=GO:0004972 |text = N-methyl-D-aspartate selective glutamate receptor activity}} {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005234 |text = extracellular-glutamate-gated ion channel activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016594 |text = glycine binding}} {{GNF_GO|id=GO:0016595 |text = glutamate binding}} {{GNF_GO|id=GO:0016933 |text = extracellular-glycine-gated ion channel activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0017146 |text = N-methyl-D-aspartate selective glutamate receptor complex}} {{GNF_GO|id=GO:0030425 |text = dendrite}} {{GNF_GO|id=GO:0030426 |text = growth cone}} {{GNF_GO|id=GO:0045211 |text = postsynaptic membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006812 |text = cation transport}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0007215 |text = glutamate signaling pathway}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007611 |text = learning and/or memory}} {{GNF_GO|id=GO:0045471 |text = response to ethanol}} {{GNF_GO|id=GO:0048167 |text = regulation of synaptic plasticity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2902
| Hs_Ensembl = ENSG00000176884
| Hs_RefseqProtein = NP_000823
| Hs_RefseqmRNA = NM_000832
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 139152663
| Hs_GenLoc_end = 139183028
| Hs_Uniprot = Q05586
| Mm_EntrezGene = 14810
| Mm_Ensembl = ENSMUSG00000026959
| Mm_RefseqmRNA = NM_008169
| Mm_RefseqProtein = NP_032195
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 25114256
| Mm_GenLoc_end = 25140988
| Mm_Uniprot = Q3TZ31
}}
}}
'''Glutamate receptor, ionotropic, N-methyl D-aspartate 1''', also known as '''GRIN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GRIN1 glutamate receptor, ionotropic, N-methyl D-aspartate 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2902| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a critical subunit of N-methyl-D-aspartate receptors, members of the glutamate receptor channel superfamily which are heteromeric protein complexes with multiple subunits arranged to form a ligand-gated ion channel. These subunits play a key role in the plasticity of synapses, which is believed to underlie memory and learning. The gene consists of 21 exons and is alternatively spliced, producing transcript variants differing in the C-terminus. Although the sequence of exon 5 is identical in human and rat, the alternative exon 5 splicing in rat has yet to be demonstrated in human. Cell-specific factors are thought to control expression of different isoforms, possibly contributing to the functional diversity of the subunits.<ref name="entrez">{{cite web | title = Entrez Gene: GRIN1 glutamate receptor, ionotropic, N-methyl D-aspartate 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2902| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lin JW, Wyszynski M, Madhavan R, ''et al.'' |title=Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1. |journal=J. Neurosci. |volume=18 |issue= 6 |pages= 2017-27 |year= 1998 |pmid= 9482789 |doi= }}
*{{cite journal | author=Schröder HC, Perovic S, Kavsan V, ''et al.'' |title=Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death. |journal=Neurotoxicology |volume=19 |issue= 4-5 |pages= 683-8 |year= 1998 |pmid= 9745929 |doi= }}
*{{cite journal | author=Adriani W, Felici A, Sargolini F, ''et al.'' |title=N-methyl-D-aspartate and dopamine receptor involvement in the modulation of locomotor activity and memory processes. |journal=Experimental brain research. Experimentelle Hirnforschung. Expérimentation cérébrale |volume=123 |issue= 1-2 |pages= 52-9 |year= 1999 |pmid= 9835392 |doi= }}
*{{cite journal | author=Dingledine R, Borges K, Bowie D, Traynelis SF |title=The glutamate receptor ion channels. |journal=Pharmacol. Rev. |volume=51 |issue= 1 |pages= 7-61 |year= 1999 |pmid= 10049997 |doi= }}
*{{cite journal | author=King JE, Eugenin EA, Buckner CM, Berman JW |title=HIV tat and neurotoxicity. |journal=Microbes Infect. |volume=8 |issue= 5 |pages= 1347-57 |year= 2006 |pmid= 16697675 |doi= 10.1016/j.micinf.2005.11.014 }}
*{{cite journal | author=Monyer H, Sprengel R, Schoepfer R, ''et al.'' |title=Heteromeric NMDA receptors: molecular and functional distinction of subtypes. |journal=Science |volume=256 |issue= 5060 |pages= 1217-21 |year= 1992 |pmid= 1350383 |doi= }}
*{{cite journal | author=Zimmer M, Fink TM, Franke Y, ''et al.'' |title=Cloning and structure of the gene encoding the human N-methyl-D-aspartate receptor (NMDAR1). |journal=Gene |volume=159 |issue= 2 |pages= 219-23 |year= 1995 |pmid= 7622053 |doi= }}
*{{cite journal | author=Karp SJ, Masu M, Eki T, ''et al.'' |title=Molecular cloning and chromosomal localization of the key subunit of the human N-methyl-D-aspartate receptor. |journal=J. Biol. Chem. |volume=268 |issue= 5 |pages= 3728-33 |year= 1993 |pmid= 7679115 |doi= }}
*{{cite journal | author=Younkin DP, Tang CM, Hardy M, ''et al.'' |title=Inducible expression of neuronal glutamate receptor channels in the NT2 human cell line. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 6 |pages= 2174-8 |year= 1993 |pmid= 7681588 |doi= }}
*{{cite journal | author=Planells-Cases R, Sun W, Ferrer-Montiel AV, Montal M |title=Molecular cloning, functional expression, and pharmacological characterization of an N-methyl-D-aspartate receptor subunit from human brain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 11 |pages= 5057-61 |year= 1993 |pmid= 7685113 |doi= }}
*{{cite journal | author=Magnuson DS, Knudsen BE, Geiger JD, ''et al.'' |title=Human immunodeficiency virus type 1 tat activates non-N-methyl-D-aspartate excitatory amino acid receptors and causes neurotoxicity. |journal=Ann. Neurol. |volume=37 |issue= 3 |pages= 373-80 |year= 1995 |pmid= 7695237 |doi= 10.1002/ana.410370314 }}
*{{cite journal | author=Foldes RL, Rampersad V, Kamboj RK |title=Cloning and sequence analysis of additional splice variants encoding human N-methyl-D-aspartate receptor (hNR1) subunits. |journal=Gene |volume=147 |issue= 2 |pages= 303-4 |year= 1994 |pmid= 7926821 |doi= }}
*{{cite journal | author=Sheng M, Cummings J, Roldan LA, ''et al.'' |title=Changing subunit composition of heteromeric NMDA receptors during development of rat cortex. |journal=Nature |volume=368 |issue= 6467 |pages= 144-7 |year= 1994 |pmid= 8139656 |doi= 10.1038/368144a0 }}
*{{cite journal | author=Tingley WG, Roche KW, Thompson AK, Huganir RL |title=Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain. |journal=Nature |volume=364 |issue= 6432 |pages= 70-3 |year= 1993 |pmid= 8316301 |doi= 10.1038/364070a0 }}
*{{cite journal | author=Foldes RL, Rampersad V, Kamboj RK |title=Cloning and sequence analysis of cDNAs encoding human hippocampus N-methyl-D-aspartate receptor subunits: evidence for alternative RNA splicing. |journal=Gene |volume=131 |issue= 2 |pages= 293-8 |year= 1993 |pmid= 8406025 |doi= }}
*{{cite journal | author=Collins C, Duff C, Duncan AM, ''et al.'' |title=Mapping of the human NMDA receptor subunit (NMDAR1) and the proposed NMDA receptor glutamate-binding subunit (NMDARA1) to chromosomes 9q34.3 and chromosome 8, respectively. |journal=Genomics |volume=17 |issue= 1 |pages= 237-9 |year= 1993 |pmid= 8406459 |doi= 10.1006/geno.1993.1311 }}
*{{cite journal | author=Lannuzel A, Lledo PM, Lamghitnia HO, ''et al.'' |title=HIV-1 envelope proteins gp120 and gp160 potentiate NMDA-induced [Ca2+]i increase, alter [Ca2+]i homeostasis and induce neurotoxicity in human embryonic neurons. |journal=Eur. J. Neurosci. |volume=7 |issue= 11 |pages= 2285-93 |year= 1996 |pmid= 8563977 |doi= }}
*{{cite journal | author=Corasaniti MT, Melino G, Navarra M, ''et al.'' |title=Death of cultured human neuroblastoma cells induced by HIV-1 gp120 is prevented by NMDA receptor antagonists and inhibitors of nitric oxide and cyclooxygenase. |journal=Neurodegeneration : a journal for neurodegenerative disorders, neuroprotection, and neuroregeneration |volume=4 |issue= 3 |pages= 315-21 |year= 1996 |pmid= 8581564 |doi= }}
*{{cite journal | author=Ehlers MD, Zhang S, Bernhadt JP, Huganir RL |title=Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit. |journal=Cell |volume=84 |issue= 5 |pages= 745-55 |year= 1996 |pmid= 8625412 |doi= }}
*{{cite journal | author=Pittaluga A, Pattarini R, Severi P, Raiteri M |title=Human brain N-methyl-D-aspartate receptors regulating noradrenaline release are positively modulated by HIV-1 coat protein gp120. |journal=AIDS |volume=10 |issue= 5 |pages= 463-8 |year= 1996 |pmid= 8724036 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HLA-DRB4... {December 15, 2007 12:54:48 PM PST}
- REDIRECT: Page directory gave bad page (HLA-DRB4 (gene)). Continuing with search.. Please correct entry: <3126,HLA-DRB4 (gene)>. {December 15, 2007 12:55:06 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 12:55:21 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Major histocompatibility complex, class II, DR beta 4
| HGNCid = 4952
| Symbol = HLA-DRB4
| AltSymbols =; HLA DRB1; DRB4; HLA-DR4B
| OMIM =
| ECnumber =
| Homologene =
| MGIid =
| Function = {{GNF_GO|id=GO:0032395 |text = MHC class II receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042613 |text = MHC class II protein complex}}
| Process = {{GNF_GO|id=GO:0002504 |text = antigen processing and presentation of peptide or polysaccharide antigen via MHC class II}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0009405 |text = pathogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3126
| Hs_Ensembl =
| Hs_RefseqProtein = XP_945196
| Hs_RefseqmRNA = XM_940103
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Major histocompatibility complex, class II, DR beta 4''', also known as '''HLA-DRB4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HLA-DRB4 major histocompatibility complex, class II, DR beta 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3126| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = HLA-DRB4 belongs to the HLA class II beta chain paralogues. This class II molecule is a heterodimer consisting of an alpha (DRA) and a beta (DRB) chain, both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa and its gene contains 6 exons. Exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail. Within the DR molecule the beta chain contains all the polymorphisms specifying the peptide binding specificities. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. DRB1 is expressed at a level five times higher than its paralogues DRB3, DRB4 and DRB5. The presence of DRB4 is linked with allelic variants of DRB1, otherwise it is omitted. There are 4 related pseudogenes: DRB2, DRB6, DRB7, DRB8 and DRB9.<ref name="entrez">{{cite web | title = Entrez Gene: HLA-DRB4 major histocompatibility complex, class II, DR beta 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3126| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Germain RN |title=Binding domain regulation of MHC class II molecule assembly, trafficking, fate, and function. |journal=Semin. Immunol. |volume=7 |issue= 6 |pages= 361-72 |year= 1996 |pmid= 8775462 |doi= 10.1006/smim.1995.0041 }}
*{{cite journal | author=O'Brien RM, Cram DS, Russ GR, ''et al.'' |title=Nucleotide sequences of the HLA-DRw12 and DRw8 B1 chains from an Australian aborigine. |journal=Hum. Immunol. |volume=34 |issue= 2 |pages= 147-51 |year= 1992 |pmid= 1358866 |doi= }}
*{{cite journal | author=Kenter M, Otting N, Anholts J, ''et al.'' |title=Mhc-DRB diversity of the chimpanzee (Pan troglodytes). |journal=Immunogenetics |volume=37 |issue= 1 |pages= 1-11 |year= 1992 |pmid= 1428007 |doi= }}
*{{cite journal | author=Dong RP, Kimura A, Sasazuki T |title=Sequence analysis of three novel DRw14-DRB1 alleles. |journal=Immunogenetics |volume=36 |issue= 2 |pages= 130-3 |year= 1992 |pmid= 1612646 |doi= }}
*{{cite journal | author=Piatier-Tonneau D, Gastinel LN, Amblard F, ''et al.'' |title=Interaction of CD4 with HLA class II antigens and HIV gp120. |journal=Immunogenetics |volume=34 |issue= 2 |pages= 121-8 |year= 1991 |pmid= 1869305 |doi= }}
*{{cite journal | author=Nong Y, Kandil O, Tobin EH, ''et al.'' |title=The HIV core protein p24 inhibits interferon-gamma-induced increase of HLA-DR and cytochrome b heavy chain mRNA levels in the human monocyte-like cell line THP1. |journal=Cell. Immunol. |volume=132 |issue= 1 |pages= 10-6 |year= 1991 |pmid= 1905983 |doi= }}
*{{cite journal | author=Rosenstein Y, Burakoff SJ, Herrmann SH |title=HIV-gp120 can block CD4-class II MHC-mediated adhesion. |journal=J. Immunol. |volume=144 |issue= 2 |pages= 526-31 |year= 1990 |pmid= 1967269 |doi= }}
*{{cite journal | author=Callahan KM, Fort MM, Obah EA, ''et al.'' |title=Genetic variability in HIV-1 gp120 affects interactions with HLA molecules and T cell receptor. |journal=J. Immunol. |volume=144 |issue= 9 |pages= 3341-6 |year= 1990 |pmid= 1970352 |doi= }}
*{{cite journal | author=Bowman MR, MacFerrin KD, Schreiber SL, Burakoff SJ |title=Identification and structural analysis of residues in the V1 region of CD4 involved in interaction with human immunodeficiency virus envelope glycoprotein gp120 and class II major histocompatibility complex molecules. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 22 |pages= 9052-6 |year= 1991 |pmid= 1978941 |doi= }}
*{{cite journal | author=Gyllensten UB, Sundvall M, Erlich HA |title=Allelic diversity is generated by intraexon sequence exchange at the DRB1 locus of primates. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 9 |pages= 3686-90 |year= 1991 |pmid= 2023919 |doi= }}
*{{cite journal | author=Lee KW, Johnson AH, Hurley CK |title=Two divergent routes of evolution gave rise to the DRw13 haplotypes. |journal=J. Immunol. |volume=145 |issue= 9 |pages= 3119-25 |year= 1990 |pmid= 2212675 |doi= }}
*{{cite journal | author=Gorski J |title=First domain sequence of the HLA-DRB1 chain from two HLA-DRw14 homozygous typing cell lines: TEM (Dw9) and AMALA (Dw16). |journal=Hum. Immunol. |volume=24 |issue= 2 |pages= 145-9 |year= 1989 |pmid= 2466818 |doi= }}
*{{cite journal | author=Fan WM, Kasahara M, Gutknecht J, ''et al.'' |title=Shared class II MHC polymorphisms between humans and chimpanzees. |journal=Hum. Immunol. |volume=26 |issue= 2 |pages= 107-21 |year= 1990 |pmid= 2511168 |doi= }}
*{{cite journal | author=Clayton LK, Sieh M, Pious DA, Reinherz EL |title=Identification of human CD4 residues affecting class II MHC versus HIV-1 gp120 binding. |journal=Nature |volume=339 |issue= 6225 |pages= 548-51 |year= 1989 |pmid= 2543930 |doi= 10.1038/339548a0 }}
*{{cite journal | author=Abe A, Ito I, Ohkubo M, ''et al.'' |title=Two distinct subtypes of the HLA-DRw12 haplotypes in the Japanese population detected by nucleotide sequence analysis and oligonucleotide genotyping. |journal=Immunogenetics |volume=30 |issue= 6 |pages= 422-6 |year= 1990 |pmid= 2592019 |doi= }}
*{{cite journal | author=Diamond DC, Sleckman BP, Gregory T, ''et al.'' |title=Inhibition of CD4+ T cell function by the HIV envelope protein, gp120. |journal=J. Immunol. |volume=141 |issue= 11 |pages= 3715-7 |year= 1988 |pmid= 2846691 |doi= }}
*{{cite journal | author=Owerbach D, Rich C, Taneja K |title=Characterization of three HLA-DR beta genes isolated from an HLA-DR 3/4 insulin-dependent diabetic patient. |journal=Immunogenetics |volume=24 |issue= 1 |pages= 41-6 |year= 1986 |pmid= 3015788 |doi= }}
*{{cite journal | author=Karr RW, Gregersen PK, Obata F, ''et al.'' |title=Analysis of DR beta and DQ beta chain cDNA clones from a DR7 haplotype. |journal=J. Immunol. |volume=137 |issue= 9 |pages= 2886-90 |year= 1986 |pmid= 3020127 |doi= }}
*{{cite journal | author=Andersson G, Larhammar D, Widmark E, ''et al.'' |title=Class II genes of the human major histocompatibility complex. Organization and evolutionary relationship of the DR beta genes. |journal=J. Biol. Chem. |volume=262 |issue= 18 |pages= 8748-58 |year= 1987 |pmid= 3036826 |doi= }}
*{{cite journal | author=Wu S, Saunders TL, Bach FH |title=Polymorphism of human Ia antigens generated by reciprocal intergenic exchange between two DR beta loci. |journal=Nature |volume=324 |issue= 6098 |pages= 676-9 |year= 1987 |pmid= 3099214 |doi= 10.1038/324676a0 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IFNA1... {December 15, 2007 12:55:21 PM PST}
- REDIRECT: Page directory gave bad page (IFNA1). Continuing with search.. Please correct entry: <3439,IFNA1>. {December 15, 2007 12:55:43 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 12:56:10 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Interferon, alpha 1
| HGNCid = 5417
| Symbol = IFNA1
| AltSymbols =; IFL; IFN; IFN-ALPHA; IFNA13; IFNA@; MGC138207; MGC138505; MGC138507
| OMIM = 147660
| ECnumber =
| Homologene = 88748
| MGIid =
| GeneAtlas_image1 = PBB_GE_IFNA1_208344_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_IFNA1_208375_at_tn.png
| Function = {{GNF_GO|id=GO:0005126 |text = hematopoietin/interferon-class (D200-domain) cytokine receptor binding}} {{GNF_GO|id=GO:0005132 |text = interferon-alpha/beta receptor binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0009615 |text = response to virus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3439
| Hs_Ensembl = ENSG00000197919
| Hs_RefseqProtein = NP_076918
| Hs_RefseqmRNA = NM_024013
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 21430440
| Hs_GenLoc_end = 21431315
| Hs_Uniprot = P01562
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Interferon, alpha 1''', also known as '''IFNA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IFNA1 interferon, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3439| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Leukocyte interferon is produced predominantly by B lymphocytes. Immune interferon (IFN-gamma; MIM 147570) is produced by mitogen- or antigen-stimulated T lymphocytes.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: IFNA1 interferon, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3439| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Conti L, Fantuzzi L, Del Cornò M, ''et al.'' |title=Immunomodulatory effects of the HIV-1 gp120 protein on antigen presenting cells: implications for AIDS pathogenesis. |journal=Immunobiology |volume=209 |issue= 1-2 |pages= 99-115 |year= 2005 |pmid= 15481145 |doi= }}
*{{cite journal | author=Bekisz J, Schmeisser H, Hernandez J, ''et al.'' |title=Human interferons alpha, beta and omega. |journal=Growth Factors |volume=22 |issue= 4 |pages= 243-51 |year= 2005 |pmid= 15621727 |doi= 10.1080/08977190400000833 }}
*{{cite journal | author=Copeland KF |title=Modulation of HIV-1 transcription by cytokines and chemokines. |journal=Mini reviews in medicinal chemistry |volume=5 |issue= 12 |pages= 1093-101 |year= 2006 |pmid= 16375755 |doi= }}
*{{cite journal | author=Capobianchi MR, Ankel H, Ameglio F, ''et al.'' |title=Recombinant glycoprotein 120 of human immunodeficiency virus is a potent interferon inducer. |journal=AIDS Res. Hum. Retroviruses |volume=8 |issue= 5 |pages= 575-9 |year= 1992 |pmid= 1381203 |doi= }}
*{{cite journal | author=Olopade OI, Bohlander SK, Pomykala H, ''et al.'' |title=Mapping of the shortest region of overlap of deletions of the short arm of chromosome 9 associated with human neoplasia. |journal=Genomics |volume=14 |issue= 2 |pages= 437-43 |year= 1992 |pmid= 1385305 |doi= }}
*{{cite journal | author=Silverman RH, Sengupta DN |title=Translational regulation by HIV leader RNA, TAT, and interferon-inducible enzymes. |journal=J. Exp. Pathol. |volume=5 |issue= 2 |pages= 69-77 |year= 1991 |pmid= 1708818 |doi= }}
*{{cite journal | author=Delcayre AX, Salas F, Mathur S, ''et al.'' |title=Epstein Barr virus/complement C3d receptor is an interferon alpha receptor. |journal=EMBO J. |volume=10 |issue= 4 |pages= 919-26 |year= 1991 |pmid= 1849076 |doi= }}
*{{cite journal | author=Tyring SK, Cauda R, Tumbarello M, ''et al.'' |title=Synthetic peptides corresponding to sequences in HIV envelope gp41 and gp120 enhance in vitro production of interleukin-1 and tumor necrosis factor but depress production of interferon-alpha, interferon-gamma and interleukin-2. |journal=Viral Immunol. |volume=4 |issue= 1 |pages= 33-42 |year= 1991 |pmid= 1905933 |doi= }}
*{{cite journal | author=Göttlinger HG, Dorfman T, Sodroski JG, Haseltine WA |title=Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 8 |pages= 3195-9 |year= 1991 |pmid= 2014240 |doi= }}
*{{cite journal | author=Stine KC, Bolognesi D, Weinhold KJ |title=Cytokine augmentation of human immunodeficiency virus type 1 (HIV-1) gp120-specific cellular cytotoxicity. |journal=Journal of biological response modifiers |volume=8 |issue= 5 |pages= 501-10 |year= 1989 |pmid= 2552026 |doi= }}
*{{cite journal | author=Capon DJ, Shepard HM, Goeddel DV |title=Two distinct families of human and bovine interferon-alpha genes are coordinately expressed and encode functional polypeptides. |journal=Mol. Cell. Biol. |volume=5 |issue= 4 |pages= 768-79 |year= 1985 |pmid= 2985969 |doi= }}
*{{cite journal | author=Delfraissy JF, Wallon C, Galanaud P |title=Interferon-alpha can synergize with interleukin 2 for human in vitro antibody response. |journal=Eur. J. Immunol. |volume=18 |issue= 9 |pages= 1379-84 |year= 1988 |pmid= 3262520 |doi= }}
*{{cite journal | author=Henco K, Brosius J, Fujisawa A, ''et al.'' |title=Structural relationship of human interferon alpha genes and pseudogenes. |journal=J. Mol. Biol. |volume=185 |issue= 2 |pages= 227-60 |year= 1985 |pmid= 4057246 |doi= }}
*{{cite journal | author=Taniguchi T, Mantei N, Schwarzstein M, ''et al.'' |title=Human leukocyte and fibroblast interferons are structurally related. |journal=Nature |volume=285 |issue= 5766 |pages= 547-9 |year= 1980 |pmid= 6157095 |doi= }}
*{{cite journal | author=Mantei N, Schwarzstein M, Streuli M, ''et al.'' |title=The nucleotide sequence of a cloned human leukocyte interferon cDNA. |journal=Gene |volume=10 |issue= 1 |pages= 1-10 |year= 1980 |pmid= 6157600 |doi= }}
*{{cite journal | author=Nagata S, Mantei N, Weissmann C |title=The structure of one of the eight or more distinct chromosomal genes for human interferon-alpha. |journal=Nature |volume=287 |issue= 5781 |pages= 401-8 |year= 1981 |pmid= 6159536 |doi= }}
*{{cite journal | author=Goeddel DV, Leung DW, Dull TJ, ''et al.'' |title=The structure of eight distinct cloned human leukocyte interferon cDNAs. |journal=Nature |volume=290 |issue= 5801 |pages= 20-6 |year= 1981 |pmid= 6163083 |doi= }}
*{{cite journal | author=Weber H, Weissmann C |title=Formation of genes coding for hybrid proteins by recombination between related, cloned genes in E. coli. |journal=Nucleic Acids Res. |volume=11 |issue= 16 |pages= 5661-9 |year= 1983 |pmid= 6310510 |doi= }}
*{{cite journal | author=Todokoro K, Kioussis D, Weissmann C |title=Two non-allelic human interferon alpha genes with identical coding regions. |journal=EMBO J. |volume=3 |issue= 8 |pages= 1809-12 |year= 1984 |pmid= 6479148 |doi= }}
*{{cite journal | author=Ameglio F, Capobianchi MR, Castilletti C, ''et al.'' |title=Recombinant gp120 induces IL-10 in resting peripheral blood mononuclear cells; correlation with the induction of other cytokines. |journal=Clin. Exp. Immunol. |volume=95 |issue= 3 |pages= 455-8 |year= 1994 |pmid= 7511078 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IFNB1... {December 15, 2007 12:56:10 PM PST}
- REDIRECT: Page directory gave bad page (IFNB1). Continuing with search.. Please correct entry: <3456,IFNB1>. {December 15, 2007 12:57:05 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 12:57:25 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IFNB1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1au1.
| PDB = {{PDB2|1au1}}
| Name = Interferon, beta 1, fibroblast
| HGNCid = 5434
| Symbol = IFNB1
| AltSymbols =; IFB; IFF; IFNB; MGC96956
| OMIM = 147640
| ECnumber =
| Homologene = 1640
| MGIid = 107657
| GeneAtlas_image1 = PBB_GE_IFNB1_208173_at_tn.png
| Function = {{GNF_GO|id=GO:0005132 |text = interferon-alpha/beta receptor binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006919 |text = caspase activation}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0009615 |text = response to virus}} {{GNF_GO|id=GO:0030101 |text = natural killer cell activation}} {{GNF_GO|id=GO:0042100 |text = B cell proliferation}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}} {{GNF_GO|id=GO:0045089 |text = positive regulation of innate immune response}} {{GNF_GO|id=GO:0045343 |text = regulation of MHC class I biosynthetic process}} {{GNF_GO|id=GO:0046597 |text = negative regulation of virion penetration into host}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3456
| Hs_Ensembl = ENSG00000171855
| Hs_RefseqProtein = NP_002167
| Hs_RefseqmRNA = NM_002176
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 21067104
| Hs_GenLoc_end = 21067962
| Hs_Uniprot = P01574
| Mm_EntrezGene = 15977
| Mm_Ensembl = ENSMUSG00000048806
| Mm_RefseqmRNA = NM_010510
| Mm_RefseqProtein = NP_034640
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 87993457
| Mm_GenLoc_end = 87994005
| Mm_Uniprot = Q0VE17
}}
}}
'''Interferon, beta 1, fibroblast''', also known as '''IFNB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IFNB1 interferon, beta 1, fibroblast| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3456| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Biron CA, Nguyen KB, Pien GC |title=Innate immune responses to LCMV infections: natural killer cells and cytokines. |journal=Curr. Top. Microbiol. Immunol. |volume=263 |issue= |pages= 7-27 |year= 2002 |pmid= 11987821 |doi= }}
*{{cite journal | author=Conti L, Fantuzzi L, Del Cornò M, ''et al.'' |title=Immunomodulatory effects of the HIV-1 gp120 protein on antigen presenting cells: implications for AIDS pathogenesis. |journal=Immunobiology |volume=209 |issue= 1-2 |pages= 99-115 |year= 2005 |pmid= 15481145 |doi= }}
*{{cite journal | author=Bekisz J, Schmeisser H, Hernandez J, ''et al.'' |title=Human interferons alpha, beta and omega. |journal=Growth Factors |volume=22 |issue= 4 |pages= 243-51 |year= 2005 |pmid= 15621727 |doi= 10.1080/08977190400000833 }}
*{{cite journal | author=Copeland KF |title=Modulation of HIV-1 transcription by cytokines and chemokines. |journal=Mini reviews in medicinal chemistry |volume=5 |issue= 12 |pages= 1093-101 |year= 2006 |pmid= 16375755 |doi= }}
*{{cite journal | author=Silverman RH, Sengupta DN |title=Translational regulation by HIV leader RNA, TAT, and interferon-inducible enzymes. |journal=J. Exp. Pathol. |volume=5 |issue= 2 |pages= 69-77 |year= 1991 |pmid= 1708818 |doi= }}
*{{cite journal | author=Flores I, Mariano TM, Pestka S |title=Human interferon omega (omega) binds to the alpha/beta receptor. |journal=J. Biol. Chem. |volume=266 |issue= 30 |pages= 19875-7 |year= 1991 |pmid= 1834641 |doi= }}
*{{cite journal | author=May LT, Sehgal PB |title=On the relationship between human interferon alpha 1 and beta 1 genes. |journal=J. Interferon Res. |volume=5 |issue= 3 |pages= 521-6 |year= 1985 |pmid= 2414376 |doi= }}
*{{cite journal | author=Francois DT, Katona IM, June CH, ''et al.'' |title=Examination of the inhibitory and stimulatory effects of IFN-alpha, -beta, and -gamma on human B-cell proliferation induced by various B-cell mitogens. |journal=Clin. Immunol. Immunopathol. |volume=48 |issue= 3 |pages= 297-306 |year= 1988 |pmid= 3135963 |doi= }}
*{{cite journal | author=Conradt HS, Egge H, Peter-Katalinic J, ''et al.'' |title=Structure of the carbohydrate moiety of human interferon-beta secreted by a recombinant Chinese hamster ovary cell line. |journal=J. Biol. Chem. |volume=262 |issue= 30 |pages= 14600-5 |year= 1987 |pmid= 3667593 |doi= }}
*{{cite journal | author=Blank KJ, McKernan LN, Murasko DM |title=Poly I:C or IFN-alpha/beta treatment inhibits macrophage induced T cell proliferation. |journal=J. Interferon Res. |volume=5 |issue= 1 |pages= 215-21 |year= 1985 |pmid= 3872918 |doi= }}
*{{cite journal | author=Derynck R, Content J, DeClercq E, ''et al.'' |title=Isolation and structure of a human fibroblast interferon gene. |journal=Nature |volume=285 |issue= 5766 |pages= 542-7 |year= 1980 |pmid= 6157094 |doi= }}
*{{cite journal | author=Taniguchi T, Ohno S, Fujii-Kuriyama Y, Muramatsu M |title=The nucleotide sequence of human fibroblast interferon cDNA. |journal=Gene |volume=10 |issue= 1 |pages= 11-5 |year= 1980 |pmid= 6157601 |doi= }}
*{{cite journal | author=Houghton M, Easton MA, Stewart AG, ''et al.'' |title=The complete amino acid sequence of human fibroblast interferon as deduced using synthetic oligodeoxyribonucleotide primers of reverse transcriptase. |journal=Nucleic Acids Res. |volume=8 |issue= 13 |pages= 2885-94 |year= 1981 |pmid= 6159580 |doi= }}
*{{cite journal | author=Goeddel DV, Shepard HM, Yelverton E, ''et al.'' |title=Synthesis of human fibroblast interferon by E. coli. |journal=Nucleic Acids Res. |volume=8 |issue= 18 |pages= 4057-74 |year= 1981 |pmid= 6159584 |doi= }}
*{{cite journal | author=Houghton M, Stewart AG, Doel SM, ''et al.'' |title=The amino-terminal sequence of human fibroblast interferon as deduced from reverse transcripts obtained using synthetic oligonucleotide primers. |journal=Nucleic Acids Res. |volume=8 |issue= 9 |pages= 1913-31 |year= 1981 |pmid= 6159597 |doi= }}
*{{cite journal | author=Wetzel R |title=Assignment of the disulphide bonds of leukocyte interferon. |journal=Nature |volume=289 |issue= 5798 |pages= 606-7 |year= 1981 |pmid= 6162107 |doi= }}
*{{cite journal | author=Lawn RM, Adelman J, Franke AE, ''et al.'' |title=Human fibroblast interferon gene lacks introns. |journal=Nucleic Acids Res. |volume=9 |issue= 5 |pages= 1045-52 |year= 1981 |pmid= 6164984 |doi= }}
*{{cite journal | author=Shepard HM, Leung D, Stebbing N, Goeddel DV |title=A single amino acid change in IFN-beta1 abolishes its antiviral activity. |journal=Nature |volume=294 |issue= 5841 |pages= 563-5 |year= 1982 |pmid= 6171735 |doi= }}
*{{cite journal | author=Content J, De Wit L, Pierard D, ''et al.'' |title=Secretory proteins induced in human fibroblasts under conditions used for the production of interferon beta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=79 |issue= 9 |pages= 2768-72 |year= 1982 |pmid= 6178110 |doi= }}
*{{cite journal | author=Fiers W, Remaut E, Devos R, ''et al.'' |title=The human fibroblast and human immune interferon genes and their expression in homologous and heterologous cells. |journal=Philos. Trans. R. Soc. Lond., B, Biol. Sci. |volume=299 |issue= 1094 |pages= 29-38 |year= 1983 |pmid= 6183692 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IGFBP1... {December 15, 2007 12:57:25 PM PST}
- REDIRECT: Page directory gave bad page (IGFBP1). Continuing with search.. Please correct entry: <3484,IGFBP1>. {December 15, 2007 12:57:47 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 12:58:14 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IGFBP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1zt3.
| PDB = {{PDB2|1zt3}}, {{PDB2|1zt5}}, {{PDB2|2dsq}}
| Name = Insulin-like growth factor binding protein 1
| HGNCid = 5469
| Symbol = IGFBP1
| AltSymbols =; IBP1; AFBP; IGF-BP25; PP12; hIGFBP-1
| OMIM = 146730
| ECnumber =
| Homologene = 498
| MGIid = 96436
| GeneAtlas_image1 = PBB_GE_IGFBP1_205302_at_tn.png
| Function = {{GNF_GO|id=GO:0005520 |text = insulin-like growth factor binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001558 |text = regulation of cell growth}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3484
| Hs_Ensembl = ENSG00000146678
| Hs_RefseqProtein = NP_000587
| Hs_RefseqmRNA = NM_000596
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 45894484
| Hs_GenLoc_end = 45899791
| Hs_Uniprot = P08833
| Mm_EntrezGene = 16006
| Mm_Ensembl = ENSMUSG00000020429
| Mm_RefseqmRNA = NM_008341
| Mm_RefseqProtein = NP_032367
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 7097782
| Mm_GenLoc_end = 7102541
| Mm_Uniprot = Q5SVY8
}}
}}
'''Insulin-like growth factor binding protein 1''', also known as '''IGFBP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IGFBP1 insulin-like growth factor binding protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3484| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. Binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: IGFBP1 insulin-like growth factor binding protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3484| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rajaram S, Baylink DJ, Mohan S |title=Insulin-like growth factor-binding proteins in serum and other biological fluids: regulation and functions. |journal=Endocr. Rev. |volume=18 |issue= 6 |pages= 801-31 |year= 1998 |pmid= 9408744 |doi= }}
*{{cite journal | author=Ferry RJ, Cerri RW, Cohen P |title=Insulin-like growth factor binding proteins: new proteins, new functions. |journal=Horm. Res. |volume=51 |issue= 2 |pages= 53-67 |year= 1999 |pmid= 10352394 |doi= }}
*{{cite journal | author=Firth SM, Baxter RC |title=Cellular actions of the insulin-like growth factor binding proteins. |journal=Endocr. Rev. |volume=23 |issue= 6 |pages= 824-54 |year= 2003 |pmid= 12466191 |doi= }}
*{{cite journal | author=Wood AW, Duan C, Bern HA |title=Insulin-like growth factor signaling in fish. |journal=Int. Rev. Cytol. |volume=243 |issue= |pages= 215-85 |year= 2005 |pmid= 15797461 |doi= 10.1016/S0074-7696(05)43004-1 }}
*{{cite journal | author=Ehrenborg E, Larsson C, Stern I, ''et al.'' |title=Contiguous localization of the genes encoding human insulin-like growth factor binding proteins 1 (IGBP1) and 3 (IGBP3) on chromosome 7. |journal=Genomics |volume=12 |issue= 3 |pages= 497-502 |year= 1992 |pmid= 1373120 |doi= }}
*{{cite journal | author=Ekstrand J, Ehrenborg E, Stern I, ''et al.'' |title=The gene for insulin-like growth factor-binding protein-1 is localized to human chromosomal region 7p14-p12. |journal=Genomics |volume=6 |issue= 3 |pages= 413-8 |year= 1990 |pmid= 1691735 |doi= }}
*{{cite journal | author=Suwanichkul A, Cubbage ML, Powell DR |title=The promoter of the human gene for insulin-like growth factor binding protein-1. Basal promoter activity in HEP G2 cells depends upon liver factor B1. |journal=J. Biol. Chem. |volume=265 |issue= 34 |pages= 21185-93 |year= 1991 |pmid= 1701175 |doi= }}
*{{cite journal | author=Brinkman A, Kortleve DJ, Schuller AG, ''et al.'' |title=Site-directed mutagenesis of the N-terminal region of IGF binding protein 1; analysis of IGF binding capability. |journal=FEBS Lett. |volume=291 |issue= 2 |pages= 264-8 |year= 1991 |pmid= 1718783 |doi= }}
*{{cite journal | author=Brewer MT, Stetler GL, Squires CH, ''et al.'' |title=Cloning, characterization, and expression of a human insulin-like growth factor binding protein. |journal=Biochem. Biophys. Res. Commun. |volume=152 |issue= 3 |pages= 1289-97 |year= 1988 |pmid= 2454104 |doi= }}
*{{cite journal | author=Julkunen M, Koistinen R, Aalto-Setälä K, ''et al.'' |title=Primary structure of human insulin-like growth factor-binding protein/placental protein 12 and tissue-specific expression of its mRNA. |journal=FEBS Lett. |volume=236 |issue= 2 |pages= 295-302 |year= 1988 |pmid= 2457513 |doi= }}
*{{cite journal | author=Lee YL, Hintz RL, James PM, ''et al.'' |title=Insulin-like growth factor (IGF) binding protein complementary deoxyribonucleic acid from human HEP G2 hepatoma cells: predicted protein sequence suggests an IGF binding domain different from those of the IGF-I and IGF-II receptors. |journal=Mol. Endocrinol. |volume=2 |issue= 5 |pages= 404-11 |year= 1988 |pmid= 2458522 |doi= }}
*{{cite journal | author=Brinkman A, Groffen C, Kortleve DJ, ''et al.'' |title=Isolation and characterization of a cDNA encoding the low molecular weight insulin-like growth factor binding protein (IBP-1). |journal=EMBO J. |volume=7 |issue= 8 |pages= 2417-23 |year= 1989 |pmid= 2461294 |doi= }}
*{{cite journal | author=Luthman H, Söderling-Barros J, Persson B, ''et al.'' |title=Human insulin-like growth-factor-binding protein. Low-molecular-mass form: protein sequence and cDNA cloning. |journal=Eur. J. Biochem. |volume=180 |issue= 2 |pages= 259-65 |year= 1989 |pmid= 2466665 |doi= }}
*{{cite journal | author=Cubbage ML, Suwanichkul A, Powell DR |title=Structure of the human chromosomal gene for the 25 kilodalton insulin-like growth factor binding protein. |journal=Mol. Endocrinol. |volume=3 |issue= 5 |pages= 846-51 |year= 1989 |pmid= 2474129 |doi= }}
*{{cite journal | author=Alitalo T, Kontula K, Koistinen R, ''et al.'' |title=The gene encoding human low-molecular weight insulin-like growth-factor binding protein (IGF-BP25): regional localization to 7p12-p13 and description of a DNA polymorphism. |journal=Hum. Genet. |volume=83 |issue= 4 |pages= 335-8 |year= 1989 |pmid= 2478445 |doi= }}
*{{cite journal | author=Brinkman A, Groffen CA, Kortleve DJ, Drop SL |title=Organization of the gene encoding the insulin-like growth factor binding protein IBP-1. |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 3 |pages= 898-907 |year= 1989 |pmid= 2849945 |doi= }}
*{{cite journal | author=Busby WH, Klapper DG, Clemmons DR |title=Purification of a 31,000-dalton insulin-like growth factor binding protein from human amniotic fluid. Isolation of two forms with different biologic actions. |journal=J. Biol. Chem. |volume=263 |issue= 28 |pages= 14203-10 |year= 1988 |pmid= 2971653 |doi= }}
*{{cite journal | author=Grundmann U, Nerlich C, Bohn H, Rein T |title=Cloning of cDNA encoding human placental protein 12 (PP12): binding protein for IGF I and somatomedin. |journal=Nucleic Acids Res. |volume=16 |issue= 17 |pages= 8711 |year= 1988 |pmid= 3419931 |doi= }}
*{{cite journal | author=Jones JI, Gockerman A, Busby WH, ''et al.'' |title=Insulin-like growth factor binding protein 1 stimulates cell migration and binds to the alpha 5 beta 1 integrin by means of its Arg-Gly-Asp sequence. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 22 |pages= 10553-7 |year= 1993 |pmid= 7504269 |doi= }}
*{{cite journal | author=Jones JI, Busby WH, Wright G, ''et al.'' |title=Identification of the sites of phosphorylation in insulin-like growth factor binding protein-1. Regulation of its affinity by phosphorylation of serine 101. |journal=J. Biol. Chem. |volume=268 |issue= 2 |pages= 1125-31 |year= 1993 |pmid= 7678248 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ITGB4... {December 15, 2007 12:58:14 PM PST}
- REDIRECT: Page directory gave bad page (ITGB4). Continuing with search.. Please correct entry: <3691,ITGB4>. {December 15, 2007 12:58:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 12:59:05 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ITGB4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1qg3.
| PDB = {{PDB2|1qg3}}
| Name = Integrin, beta 4
| HGNCid = 6158
| Symbol = ITGB4
| AltSymbols =; CD104
| OMIM = 147557
| ECnumber =
| Homologene = 179
| MGIid = 96613
| GeneAtlas_image1 = PBB_GE_ITGB4_204990_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ITGB4_204989_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ITGB4_211905_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007154 |text = cell communication}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3691
| Hs_Ensembl = ENSG00000132470
| Hs_RefseqProtein = NP_000204
| Hs_RefseqmRNA = NM_000213
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 71229111
| Hs_GenLoc_end = 71265493
| Hs_Uniprot = P16144
| Mm_EntrezGene = 192897
| Mm_Ensembl = ENSMUSG00000020758
| Mm_RefseqmRNA = NM_001005607
| Mm_RefseqProtein = NP_001005607
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 115791069
| Mm_GenLoc_end = 115824502
| Mm_Uniprot =
}}
}}
'''Integrin, beta 4''', also known as '''ITGB4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ITGB4 integrin, beta 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3691| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Integrins are heterodimers comprised of alpha and beta subunits, that are noncovalently associated transmembrane glycoprotein receptors. Different combinations of alpha and beta polypeptides form complexes that vary in their ligand-binding specificities. Integrins mediate cell-matrix or cell-cell adhesion, and transduced signals that regulate gene expression and cell growth. This gene encodes the integrin beta 4 subunit, a receptor for the laminins. This subunit tends to associate with alpha 6 subunit and is likely to play a pivotal role in the biology of invasive carcinoma. Mutations in this gene are associated with epidermolysis bullosa with pyloric atresia. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ITGB4 integrin, beta 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3691| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lipscomb EA, Mercurio AM |title=Mobilization and activation of a signaling competent alpha6beta4integrin underlies its contribution to carcinoma progression. |journal=Cancer Metastasis Rev. |volume=24 |issue= 3 |pages= 413-23 |year= 2006 |pmid= 16258729 |doi= 10.1007/s10555-005-5133-4 }}
*{{cite journal | author=Sonnenberg A, Linders CJ, Modderman PW, ''et al.'' |title=Integrin recognition of different cell-binding fragments of laminin (P1, E3, E8) and evidence that alpha 6 beta 1 but not alpha 6 beta 4 functions as a major receptor for fragment E8. |journal=J. Cell Biol. |volume=110 |issue= 6 |pages= 2145-55 |year= 1990 |pmid= 1693624 |doi= }}
*{{cite journal | author=Tamura RN, Rozzo C, Starr L, ''et al.'' |title=Epithelial integrin alpha 6 beta 4: complete primary structure of alpha 6 and variant forms of beta 4. |journal=J. Cell Biol. |volume=111 |issue= 4 |pages= 1593-604 |year= 1990 |pmid= 1976638 |doi= }}
*{{cite journal | author=Hogervorst F, Kuikman I, van Kessel AG, Sonnenberg A |title=Molecular cloning of the human alpha 6 integrin subunit. Alternative splicing of alpha 6 mRNA and chromosomal localization of the alpha 6 and beta 4 genes. |journal=Eur. J. Biochem. |volume=199 |issue= 2 |pages= 425-33 |year= 1991 |pmid= 2070796 |doi= }}
*{{cite journal | author=Vogel BE, Tarone G, Giancotti FG, ''et al.'' |title=A novel fibronectin receptor with an unexpected subunit composition (alpha v beta 1). |journal=J. Biol. Chem. |volume=265 |issue= 11 |pages= 5934-7 |year= 1990 |pmid= 2138612 |doi= }}
*{{cite journal | author=Suzuki S, Naitoh Y |title=Amino acid sequence of a novel integrin beta 4 subunit and primary expression of the mRNA in epithelial cells. |journal=EMBO J. |volume=9 |issue= 3 |pages= 757-63 |year= 1990 |pmid= 2311577 |doi= }}
*{{cite journal | author=Hogervorst F, Kuikman I, von dem Borne AE, Sonnenberg A |title=Cloning and sequence analysis of beta-4 cDNA: an integrin subunit that contains a unique 118 kd cytoplasmic domain. |journal=EMBO J. |volume=9 |issue= 3 |pages= 765-70 |year= 1990 |pmid= 2311578 |doi= }}
*{{cite journal | author=Kajiji S, Tamura RN, Quaranta V |title=A novel integrin (alpha E beta 4) from human epithelial cells suggests a fourth family of integrin adhesion receptors. |journal=EMBO J. |volume=8 |issue= 3 |pages= 673-80 |year= 1989 |pmid= 2542022 |doi= }}
*{{cite journal | author=Hemler ME, Crouse C, Sonnenberg A |title=Association of the VLA alpha 6 subunit with a novel protein. A possible alternative to the common VLA beta 1 subunit on certain cell lines. |journal=J. Biol. Chem. |volume=264 |issue= 11 |pages= 6529-35 |year= 1989 |pmid= 2649503 |doi= }}
*{{cite journal | author=Vidal F, Aberdam D, Miquel C, ''et al.'' |title=Integrin beta 4 mutations associated with junctional epidermolysis bullosa with pyloric atresia. |journal=Nat. Genet. |volume=10 |issue= 2 |pages= 229-34 |year= 1995 |pmid= 7545057 |doi= 10.1038/ng0695-229 }}
*{{cite journal | author=Mainiero F, Pepe A, Wary KK, ''et al.'' |title=Signal transduction by the alpha 6 beta 4 integrin: distinct beta 4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes. |journal=EMBO J. |volume=14 |issue= 18 |pages= 4470-81 |year= 1995 |pmid= 7556090 |doi= }}
*{{cite journal | author=Clarke AS, Lotz MM, Mercurio AM |title=A novel structural variant of the human beta 4 integrin cDNA. |journal=Cell Adhes. Commun. |volume=2 |issue= 1 |pages= 1-6 |year= 1995 |pmid= 7982032 |doi= }}
*{{cite journal | author=Weeks BS, Desai K, Loewenstein PM, ''et al.'' |title=Identification of a novel cell attachment domain in the HIV-1 Tat protein and its 90-kDa cell surface binding protein. |journal=J. Biol. Chem. |volume=268 |issue= 7 |pages= 5279-84 |year= 1993 |pmid= 8444901 |doi= }}
*{{cite journal | author=Iacovacci S, Gagnoux-Palacios L, Zambruno G, ''et al.'' |title=Genomic organization of the human integrin beta4 gene. |journal=Mamm. Genome |volume=8 |issue= 6 |pages= 448-50 |year= 1997 |pmid= 9166594 |doi= }}
*{{cite journal | author=Mainiero F, Murgia C, Wary KK, ''et al.'' |title=The coupling of alpha6beta4 integrin to Ras-MAP kinase pathways mediated by Shc controls keratinocyte proliferation. |journal=EMBO J. |volume=16 |issue= 9 |pages= 2365-75 |year= 1997 |pmid= 9171350 |doi= 10.1093/emboj/16.9.2365 }}
*{{cite journal | author=Pulkkinen L, Kurtz K, Xu Y, ''et al.'' |title=Genomic organization of the integrin beta 4 gene (ITGB4): a homozygous splice-site mutation in a patient with junctional epidermolysis bullosa associated with pyloric atresia. |journal=Lab. Invest. |volume=76 |issue= 6 |pages= 823-33 |year= 1997 |pmid= 9194858 |doi= }}
*{{cite journal | author=van Leusden MR, Kuikman I, Sonnenberg A |title=The unique cytoplasmic domain of the human integrin variant beta4E is produced by partial retention of intronic sequences. |journal=Biochem. Biophys. Res. Commun. |volume=235 |issue= 3 |pages= 826-30 |year= 1997 |pmid= 9207246 |doi= 10.1006/bbrc.1997.6892 }}
*{{cite journal | author=von Bredow DC, Nagle RB, Bowden GT, Cress AE |title=Cleavage of beta 4 integrin by matrilysin. |journal=Exp. Cell Res. |volume=236 |issue= 1 |pages= 341-5 |year= 1997 |pmid= 9344615 |doi= 10.1006/excr.1997.3711 }}
*{{cite journal | author=Biffo S, Sanvito F, Costa S, ''et al.'' |title=Isolation of a novel beta4 integrin-binding protein (p27(BBP)) highly expressed in epithelial cells. |journal=J. Biol. Chem. |volume=272 |issue= 48 |pages= 30314-21 |year= 1997 |pmid= 9374518 |doi= }}
*{{cite journal | author=Pulkkinen L, Kim DU, Uitto J |title=Epidermolysis bullosa with pyloric atresia: novel mutations in the beta4 integrin gene (ITGB4). |journal=Am. J. Pathol. |volume=152 |issue= 1 |pages= 157-66 |year= 1998 |pmid= 9422533 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NEWENTRY... {December 15, 2007 1:09:23 PM PST}
- REDIRECT: Page directory gave bad page (NEWENTRY). Continuing with search.. Please correct entry: <192343,NEWENTRY>. {December 15, 2007 1:09:41 PM PST}
- CREATE: Found no pages, creating new page. {December 15, 2007 1:09:44 PM PST}
- CREATED: Created new protein page: NEWENTRY {December 15, 2007 1:09:55 PM PST}
- INFO: Beginning work on RBL1... {December 15, 2007 12:59:05 PM PST}
- REDIRECT: Page directory gave bad page (RBL1 (gene)). Continuing with search.. Please correct entry: <5933,RBL1 (gene)>. {December 15, 2007 12:59:43 PM PST}
- SEARCH REDIRECT: Control Box Found: Retinoblastoma-like protein 1 {December 15, 2007 12:59:58 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {December 15, 2007 1:00:04 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {December 15, 2007 1:00:04 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {December 15, 2007 1:00:04 PM PST}
- UPDATED: Updated protein page: Retinoblastoma-like protein 1 {December 15, 2007 1:00:10 PM PST}
- INFO: Beginning work on RPGR... {December 15, 2007 1:00:10 PM PST}
- REDIRECT: Page directory gave bad page (RPGR). Continuing with search.. Please correct entry: <6103,RPGR>. {December 15, 2007 1:00:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:01:04 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Retinitis pigmentosa GTPase regulator
| HGNCid = 10295
| Symbol = RPGR
| AltSymbols =; CRD; COD1; CORDX1; PCDX; RP15; RP3; XLRP3; orf15
| OMIM = 312610
| ECnumber =
| Homologene = 55455
| MGIid = 1344037
| GeneAtlas_image1 = PBB_GE_RPGR_207624_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005085 |text = guanyl-nucleotide exchange factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}}
| Process = {{GNF_GO|id=GO:0006886 |text = intracellular protein transport}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6103
| Hs_Ensembl = ENSG00000156313
| Hs_RefseqProtein = NP_000319
| Hs_RefseqmRNA = NM_000328
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 38013368
| Hs_GenLoc_end = 38071732
| Hs_Uniprot = Q92834
| Mm_EntrezGene = 19893
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_011285
| Mm_RefseqProtein = NP_035415
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Retinitis pigmentosa GTPase regulator''', also known as '''RPGR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RPGR retinitis pigmentosa GTPase regulator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6103| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein with a series of six RCC1-like domains (RLDs), characteristic of the highly conserved guanine nucleotide exchange factors. Mutations in this gene have been associated with X-linked retinitis pigmentosa (XLRP). Multiple alternatively spliced transcript variants that encode different isoforms of this gene have been reported, but the full-length natures of only some have been determined.<ref name="entrez">{{cite web | title = Entrez Gene: RPGR retinitis pigmentosa GTPase regulator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6103| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Jin ZB, Hayakawa M, Murakami A, Nao-i N |title=RCC1-like domain and ORF15: essentials in RPGR gene. |journal=Adv. Exp. Med. Biol. |volume=572 |issue= |pages= 29-33 |year= 2007 |pmid= 17249551 |doi= }}
*{{cite journal | author=Ott J, Bhattacharya S, Chen JD, ''et al.'' |title=Localizing multiple X chromosome-linked retinitis pigmentosa loci using multilocus homogeneity tests. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 2 |pages= 701-4 |year= 1990 |pmid= 2300556 |doi= }}
*{{cite journal | author=McGuire RE, Sullivan LS, Blanton SH, ''et al.'' |title=X-linked dominant cone-rod degeneration: linkage mapping of a new locus for retinitis pigmentosa (RP 15) to Xp22.13-p22.11. |journal=Am. J. Hum. Genet. |volume=57 |issue= 1 |pages= 87-94 |year= 1995 |pmid= 7611300 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Meindl A, Dry K, Herrmann K, ''et al.'' |title=A gene (RPGR) with homology to the RCC1 guanine nucleotide exchange factor is mutated in X-linked retinitis pigmentosa (RP3). |journal=Nat. Genet. |volume=13 |issue= 1 |pages= 35-42 |year= 1996 |pmid= 8673101 |doi= 10.1038/ng0596-35 }}
*{{cite journal | author=Roepman R, van Duijnhoven G, Rosenberg T, ''et al.'' |title=Positional cloning of the gene for X-linked retinitis pigmentosa 3: homology with the guanine-nucleotide-exchange factor RCC1. |journal=Hum. Mol. Genet. |volume=5 |issue= 7 |pages= 1035-41 |year= 1997 |pmid= 8817343 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Fujita R, Buraczynska M, Gieser L, ''et al.'' |title=Analysis of the RPGR gene in 11 pedigrees with the retinitis pigmentosa type 3 genotype: paucity of mutations in the coding region but splice defects in two families. |journal=Am. J. Hum. Genet. |volume=61 |issue= 3 |pages= 571-80 |year= 1997 |pmid= 9326322 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Buraczynska M, Wu W, Fujita R, ''et al.'' |title=Spectrum of mutations in the RPGR gene that are identified in 20% of families with X-linked retinitis pigmentosa. |journal=Am. J. Hum. Genet. |volume=61 |issue= 6 |pages= 1287-92 |year= 1998 |pmid= 9399904 |doi= }}
*{{cite journal | author=Hardcastle AJ, David-Gray ZK, Jay M, ''et al.'' |title=Localization of CSNBX (CSNB4) between the retinitis pigmentosa loci RP2 and RP3 on proximal Xp. |journal=Invest. Ophthalmol. Vis. Sci. |volume=38 |issue= 13 |pages= 2750-5 |year= 1998 |pmid= 9418727 |doi= }}
*{{cite journal | author=Yan D, Swain PK, Breuer D, ''et al.'' |title=Biochemical characterization and subcellular localization of the mouse retinitis pigmentosa GTPase regulator (mRpgr). |journal=J. Biol. Chem. |volume=273 |issue= 31 |pages= 19656-63 |year= 1998 |pmid= 9677393 |doi= }}
*{{cite journal | author=Fishman GA, Grover S, Jacobson SG, ''et al.'' |title=X-linked retinitis pigmentosa in two families with a missense mutation in the RPGR gene and putative change of glycine to valine at codon 60. |journal=Ophthalmology |volume=105 |issue= 12 |pages= 2286-96 |year= 1998 |pmid= 9855162 |doi= 10.1016/S0161-6420(98)91231-3 }}
*{{cite journal | author=Linari M, Ueffing M, Manson F, ''et al.'' |title=The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta subunit of rod cyclic GMP phosphodiesterase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 4 |pages= 1315-20 |year= 1999 |pmid= 9990021 |doi= }}
*{{cite journal | author=Dry KL, Manson FD, Lennon A, ''et al.'' |title=Identification of a 5' splice site mutation in the RPGR gene in a family with X-linked retinitis pigmentosa (RP3). |journal=Hum. Mutat. |volume=13 |issue= 2 |pages= 141-5 |year= 1999 |pmid= 10094550 |doi= 10.1002/(SICI)1098-1004(1999)13:2<141::AID-HUMU6>3.0.CO;2-Q }}
*{{cite journal | author=Kirschner R, Rosenberg T, Schultz-Heienbrok R, ''et al.'' |title=RPGR transcription studies in mouse and human tissues reveal a retina-specific isoform that is disrupted in a patient with X-linked retinitis pigmentosa. |journal=Hum. Mol. Genet. |volume=8 |issue= 8 |pages= 1571-8 |year= 1999 |pmid= 10401007 |doi= }}
*{{cite journal | author=Zito I, Thiselton DL, Gorin MB, ''et al.'' |title=Identification of novel RPGR (retinitis pigmentosa GTPase regulator) mutations in a subset of X-linked retinitis pigmentosa families segregating with the RP3 locus. |journal=Hum. Genet. |volume=105 |issue= 1-2 |pages= 57-62 |year= 1999 |pmid= 10480356 |doi= }}
*{{cite journal | author=Miano MG, Testa F, Strazzullo M, ''et al.'' |title=Mutation analysis of the RPGR gene reveals novel mutations in south European patients with X-linked retinitis pigmentosa. |journal=Eur. J. Hum. Genet. |volume=7 |issue= 6 |pages= 687-94 |year= 1999 |pmid= 10482958 |doi= 10.1038/sj.ejhg.5200352 }}
*{{cite journal | author=Hong DH, Pawlyk BS, Shang J, ''et al.'' |title=A retinitis pigmentosa GTPase regulator (RPGR)-deficient mouse model for X-linked retinitis pigmentosa (RP3). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3649-54 |year= 2000 |pmid= 10725384 |doi= 10.1073/pnas.060037497 }}
*{{cite journal | author=Zito I, Gorin MB, Plant C, ''et al.'' |title=Novel mutations of the RPGR gene in RP3 families. |journal=Hum. Mutat. |volume=15 |issue= 4 |pages= 386 |year= 2000 |pmid= 10737996 |doi= 10.1002/(SICI)1098-1004(200004)15:4<386::AID-HUMU23>3.0.CO;2-4 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RPS6KA3... {December 15, 2007 1:01:04 PM PST}
- REDIRECT: Page directory gave bad page (RPS6KA3). Continuing with search.. Please correct entry: <6197,RPS6KA3>. {December 15, 2007 1:01:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:02:15 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Ribosomal protein S6 kinase, 90kDa, polypeptide 3
| HGNCid = 10432
| Symbol = RPS6KA3
| AltSymbols =; RSK; CLS; HU-3; ISPK-1; MAPKAPK1B; MRX19; RSK2; S6K-alpha3; p90-RSK2; pp90RSK2
| OMIM = 300075
| ECnumber =
| Homologene = 37940
| MGIid = 104557
| GeneAtlas_image1 = PBB_GE_RPS6KA3_203843_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007417 |text = central nervous system development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6197
| Hs_Ensembl = ENSG00000177189
| Hs_RefseqProtein = NP_004577
| Hs_RefseqmRNA = NM_004586
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 20077950
| Hs_GenLoc_end = 20194671
| Hs_Uniprot = P51812
| Mm_EntrezGene = 110651
| Mm_Ensembl = ENSMUSG00000031309
| Mm_RefseqmRNA = NM_148945
| Mm_RefseqProtein = NP_683747
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 154600225
| Mm_GenLoc_end = 154707590
| Mm_Uniprot = P18654
}}
}}
'''Ribosomal protein S6 kinase, 90kDa, polypeptide 3''', also known as '''RPS6KA3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RPS6KA3 ribosomal protein S6 kinase, 90kDa, polypeptide 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6197| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 non-identical kinase catalytic domains and phosphorylates various substrates, including members of the mitogen-activated kinase (MAPK) signalling pathway. The activity of this protein has been implicated in controlling cell growth and differentiation. Mutations in this gene have been associated with Coffin-Lowry syndrome (CLS).<ref name="entrez">{{cite web | title = Entrez Gene: RPS6KA3 ribosomal protein S6 kinase, 90kDa, polypeptide 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6197| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Omary MB, Baxter GT, Chou CF, ''et al.'' |title=PKC epsilon-related kinase associates with and phosphorylates cytokeratin 8 and 18. |journal=J. Cell Biol. |volume=117 |issue= 3 |pages= 583-93 |year= 1992 |pmid= 1374067 |doi= }}
*{{cite journal | author=Ku NO, Omary MB |title=Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization. |journal=J. Cell Biol. |volume=127 |issue= 1 |pages= 161-71 |year= 1994 |pmid= 7523419 |doi= }}
*{{cite journal | author=Adams MD, Kerlavage AR, Fleischmann RD, ''et al.'' |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3-174 |year= 1995 |pmid= 7566098 |doi= }}
*{{cite journal | author=Zhao Y, Bjørbaek C, Weremowicz S, ''et al.'' |title=RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation. |journal=Mol. Cell. Biol. |volume=15 |issue= 8 |pages= 4353-63 |year= 1995 |pmid= 7623830 |doi= }}
*{{cite journal | author=Bjørbaek C, Vik TA, Echwald SM, ''et al.'' |title=Cloning of a human insulin-stimulated protein kinase (ISPK-1) gene and analysis of coding regions and mRNA levels of the ISPK-1 and the protein phosphatase-1 genes in muscle from NIDDM patients. |journal=Diabetes |volume=44 |issue= 1 |pages= 90-7 |year= 1995 |pmid= 7813820 |doi= }}
*{{cite journal | author=Donnelly AJ, Choo KH, Kozman HM, ''et al.'' |title=Regional localisation of a non-specific X-linked mental retardation gene (MRX19) to Xp22. |journal=Am. J. Med. Genet. |volume=51 |issue= 4 |pages= 581-5 |year= 1994 |pmid= 7943043 |doi= 10.1002/ajmg.1320510457 }}
*{{cite journal | author=Moller DE, Xia CH, Tang W, ''et al.'' |title=Human rsk isoforms: cloning and characterization of tissue-specific expression. |journal=Am. J. Physiol. |volume=266 |issue= 2 Pt 1 |pages= C351-9 |year= 1994 |pmid= 8141249 |doi= }}
*{{cite journal | author=Xing J, Ginty DD, Greenberg ME |title=Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. |journal=Science |volume=273 |issue= 5277 |pages= 959-63 |year= 1996 |pmid= 8688081 |doi= }}
*{{cite journal | author=Trivier E, De Cesare D, Jacquot S, ''et al.'' |title=Mutations in the kinase Rsk-2 associated with Coffin-Lowry syndrome. |journal=Nature |volume=384 |issue= 6609 |pages= 567-70 |year= 1997 |pmid= 8955270 |doi= 10.1038/384567a0 }}
*{{cite journal | author=Paudel HK |title=Phosphorylation by neuronal cdc2-like protein kinase promotes dimerization of Tau protein in vitro. |journal=J. Biol. Chem. |volume=272 |issue= 45 |pages= 28328-34 |year= 1997 |pmid= 9353289 |doi= }}
*{{cite journal | author=Joel PB, Smith J, Sturgill TW, ''et al.'' |title=pp90rsk1 regulates estrogen receptor-mediated transcription through phosphorylation of Ser-167. |journal=Mol. Cell. Biol. |volume=18 |issue= 4 |pages= 1978-84 |year= 1998 |pmid= 9528769 |doi= }}
*{{cite journal | author=Zheng-Fischhöfer Q, Biernat J, Mandelkow EM, ''et al.'' |title=Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation. |journal=Eur. J. Biochem. |volume=252 |issue= 3 |pages= 542-52 |year= 1998 |pmid= 9546672 |doi= }}
*{{cite journal | author=Deak M, Clifton AD, Lucocq LM, Alessi DR |title=Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. |journal=EMBO J. |volume=17 |issue= 15 |pages= 4426-41 |year= 1998 |pmid= 9687510 |doi= 10.1093/emboj/17.15.4426 }}
*{{cite journal | author=Du K, Montminy M |title=CREB is a regulatory target for the protein kinase Akt/PKB. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32377-9 |year= 1999 |pmid= 9829964 |doi= }}
*{{cite journal | author=Hanger DP, Betts JC, Loviny TL, ''et al.'' |title=New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. |journal=J. Neurochem. |volume=71 |issue= 6 |pages= 2465-76 |year= 1998 |pmid= 9832145 |doi= }}
*{{cite journal | author=Jacquot S, Merienne K, De Cesare D, ''et al.'' |title=Mutation analysis of the RSK2 gene in Coffin-Lowry patients: extensive allelic heterogeneity and a high rate of de novo mutations. |journal=Am. J. Hum. Genet. |volume=63 |issue= 6 |pages= 1631-40 |year= 1999 |pmid= 9837815 |doi= }}
*{{cite journal | author=Jacquot S, Merienne K, Pannetier S, ''et al.'' |title=Germline mosaicism in Coffin-Lowry syndrome. |journal=Eur. J. Hum. Genet. |volume=6 |issue= 6 |pages= 578-82 |year= 1999 |pmid= 9887375 |doi= 10.1038/sj.ejhg.5200230 }}
*{{cite journal | author=Smith JA, Poteet-Smith CE, Malarkey K, Sturgill TW |title=Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo. |journal=J. Biol. Chem. |volume=274 |issue= 5 |pages= 2893-8 |year= 1999 |pmid= 9915826 |doi= }}
*{{cite journal | author=Abidi F, Jacquot S, Lassiter C, ''et al.'' |title=Novel mutations in Rsk-2, the gene for Coffin-Lowry syndrome (CLS). |journal=Eur. J. Hum. Genet. |volume=7 |issue= 1 |pages= 20-6 |year= 1999 |pmid= 10094187 |doi= 10.1038/sj.ejhg.5200231 }}
*{{cite journal | author=Merienne K, Jacquot S, Pannetier S, ''et al.'' |title=A missense mutation in RPS6KA3 (RSK2) responsible for non-specific mental retardation. |journal=Nat. Genet. |volume=22 |issue= 1 |pages= 13-4 |year= 1999 |pmid= 10319851 |doi= 10.1038/8719 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RPS6KB1... {December 15, 2007 1:02:15 PM PST}
- REDIRECT: Page directory gave bad page (RPS6KB1). Continuing with search.. Please correct entry: <6198,RPS6KB1>. {December 15, 2007 1:02:53 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:03:21 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Ribosomal protein S6 kinase, 70kDa, polypeptide 1
| HGNCid = 10436
| Symbol = RPS6KB1
| AltSymbols =; PS6K; S6K; S6K1; STK14A; p70(S6K)-alpha; p70-S6K; p70-alpha
| OMIM = 608938
| ECnumber =
| Homologene = 81703
| MGIid =
| GeneAtlas_image1 = PBB_GE_RPS6KB1_204171_at_tn.png
| GeneAtlas_image2 = PBB_GE_RPS6KB1_211578_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007281 |text = germ cell development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6198
| Hs_Ensembl = ENSG00000108443
| Hs_RefseqProtein = NP_003152
| Hs_RefseqmRNA = NM_003161
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 55325225
| Hs_GenLoc_end = 55382564
| Hs_Uniprot = P23443
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Ribosomal protein S6 kinase, 70kDa, polypeptide 1''', also known as '''RPS6KB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RPS6KB1 ribosomal protein S6 kinase, 70kDa, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6198| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the RSK (ribosomal S6 kinase) family of serine/threonine kinases. This kinase contains 2 non-identical kinase catalytic domains and phosphorylates several residues of the S6 ribosomal protein. The kinase activity of this protein leads to an increase in protein synthesis and cell proliferation. Amplification of the region of DNA encoding this gene and overexpression of this kinase are seen in some breast cancer cell lines. Alternate translational start sites have been described and alternate transcriptional splice variants have been observed but have not been thoroughly characterized.<ref name="entrez">{{cite web | title = Entrez Gene: RPS6KB1 ribosomal protein S6 kinase, 70kDa, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6198| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Proud CG |title=p70 S6 kinase: an enigma with variations. |journal=Trends Biochem. Sci. |volume=21 |issue= 5 |pages= 181-5 |year= 1997 |pmid= 8871403 |doi= }}
*{{cite journal | author=Manning BD |title=Balancing Akt with S6K: implications for both metabolic diseases and tumorigenesis. |journal=J. Cell Biol. |volume=167 |issue= 3 |pages= 399-403 |year= 2004 |pmid= 15533996 |doi= 10.1083/jcb.200408161 }}
*{{cite journal | author=Grove JR, Banerjee P, Balasubramanyam A, ''et al.'' |title=Cloning and expression of two human p70 S6 kinase polypeptides differing only at their amino termini. |journal=Mol. Cell. Biol. |volume=11 |issue= 11 |pages= 5541-50 |year= 1991 |pmid= 1922062 |doi= }}
*{{cite journal | author=Moser BA, Dennis PB, Pullen N, ''et al.'' |title=Dual requirement for a newly identified phosphorylation site in p70s6k. |journal=Mol. Cell. Biol. |volume=17 |issue= 9 |pages= 5648-55 |year= 1997 |pmid= 9271440 |doi= }}
*{{cite journal | author=Alessi DR, Kozlowski MT, Weng QP, ''et al.'' |title=3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro. |journal=Curr. Biol. |volume=8 |issue= 2 |pages= 69-81 |year= 1998 |pmid= 9427642 |doi= }}
*{{cite journal | author=Pullen N, Dennis PB, Andjelkovic M, ''et al.'' |title=Phosphorylation and activation of p70s6k by PDK1. |journal=Science |volume=279 |issue= 5351 |pages= 707-10 |year= 1998 |pmid= 9445476 |doi= }}
*{{cite journal | author=Burnett PE, Blackshaw S, Lai MM, ''et al.'' |title=Neurabin is a synaptic protein linking p70 S6 kinase and the neuronal cytoskeleton. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 14 |pages= 8351-6 |year= 1998 |pmid= 9653190 |doi= }}
*{{cite journal | author=Gout I, Minami T, Hara K, ''et al.'' |title=Molecular cloning and characterization of a novel p70 S6 kinase, p70 S6 kinase beta containing a proline-rich region. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30061-4 |year= 1998 |pmid= 9804755 |doi= }}
*{{cite journal | author=Barcova M, Speth C, Kacani L, ''et al.'' |title=Involvement of adenylate cyclase and p70(S6)-kinase activation in IL-10 up-regulation in human monocytes by gp41 envelope protein of human immunodeficiency virus type 1. |journal=Pflugers Arch. |volume=437 |issue= 4 |pages= 538-46 |year= 1999 |pmid= 10089566 |doi= }}
*{{cite journal | author=Couch FJ, Wang XY, Wu GJ, ''et al.'' |title=Localization of PS6K to chromosomal region 17q23 and determination of its amplification in breast cancer. |journal=Cancer Res. |volume=59 |issue= 7 |pages= 1408-11 |year= 1999 |pmid= 10197603 |doi= }}
*{{cite journal | author=Balendran A, Currie R, Armstrong CG, ''et al.'' |title=Evidence that 3-phosphoinositide-dependent protein kinase-1 mediates phosphorylation of p70 S6 kinase in vivo at Thr-412 as well as Thr-252. |journal=J. Biol. Chem. |volume=274 |issue= 52 |pages= 37400-6 |year= 2000 |pmid= 10601311 |doi= }}
*{{cite journal | author=Speth C, Joebstl B, Barcova M, Dierich MP |title=HIV-1 envelope protein gp41 modulates expression of interleukin-10 and chemokine receptors on monocytes, astrocytes and neurones. |journal=AIDS |volume=14 |issue= 6 |pages= 629-36 |year= 2000 |pmid= 10807185 |doi= }}
*{{cite journal | author=Wilson KF, Wu WJ, Cerione RA |title=Cdc42 stimulates RNA splicing via the S6 kinase and a novel S6 kinase target, the nuclear cap-binding complex. |journal=J. Biol. Chem. |volume=275 |issue= 48 |pages= 37307-10 |year= 2001 |pmid= 10973943 |doi= 10.1074/jbc.C000482200 }}
*{{cite journal | author=Armstrong JL, Bonavaud SM, Toole BJ, Yeaman SJ |title=Regulation of glycogen synthesis by amino acids in cultured human muscle cells. |journal=J. Biol. Chem. |volume=276 |issue= 2 |pages= 952-6 |year= 2001 |pmid= 11013237 |doi= 10.1074/jbc.M004812200 }}
*{{cite journal | author=Diggle TA, Subkhankulova T, Lilley KS, ''et al.'' |title=Phosphorylation of elongation factor-2 kinase on serine 499 by cAMP-dependent protein kinase induces Ca2+/calmodulin-independent activity. |journal=Biochem. J. |volume=353 |issue= Pt 3 |pages= 621-6 |year= 2001 |pmid= 11171059 |doi= }}
*{{cite journal | author=Sapkota GP, Kieloch A, Lizcano JM, ''et al.'' |title=Phosphorylation of the protein kinase mutated in Peutz-Jeghers cancer syndrome, LKB1/STK11, at Ser431 by p90(RSK) and cAMP-dependent protein kinase, but not its farnesylation at Cys(433), is essential for LKB1 to suppress cell vrowth. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19469-82 |year= 2001 |pmid= 11297520 |doi= 10.1074/jbc.M009953200 }}
*{{cite journal | author=Remy I, Michnick SW |title=Visualization of biochemical networks in living cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 14 |pages= 7678-83 |year= 2001 |pmid= 11438723 |doi= 10.1073/pnas.131216098 }}
*{{cite journal | author=Wang X, Li W, Williams M, ''et al.'' |title=Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase. |journal=EMBO J. |volume=20 |issue= 16 |pages= 4370-9 |year= 2001 |pmid= 11500364 |doi= 10.1093/emboj/20.16.4370 }}
*{{cite journal | author=Belham C, Comb MJ, Avruch J |title=Identification of the NIMA family kinases NEK6/7 as regulators of the p70 ribosomal S6 kinase. |journal=Curr. Biol. |volume=11 |issue= 15 |pages= 1155-67 |year= 2001 |pmid= 11516946 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on S100A8... {December 15, 2007 1:03:21 PM PST}
- REDIRECT: Page directory gave bad page (S100A8). Continuing with search.. Please correct entry: <6279,S100A8>. {December 15, 2007 1:03:42 PM PST}
- SEARCH REDIRECT: Control Box Found: S100 calcium binding protein A8 {December 15, 2007 1:04:30 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {December 15, 2007 1:04:31 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {December 15, 2007 1:04:31 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {December 15, 2007 1:04:31 PM PST}
- UPDATED: Updated protein page: S100 calcium binding protein A8 {December 15, 2007 1:04:38 PM PST}
- INFO: Beginning work on S100A9... {December 15, 2007 1:04:38 PM PST}
- REDIRECT: Page directory gave bad page (S100A9). Continuing with search.. Please correct entry: <6280,S100A9>. {December 15, 2007 1:05:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:05:51 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_S100A9_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1irj.
| PDB = {{PDB2|1irj}}, {{PDB2|1xk4}}
| Name = S100 calcium binding protein A9
| HGNCid = 10499
| Symbol = S100A9
| AltSymbols =; MIF; 60B8AG; CFAG; NIF; CAGB; CGLB; L1AG; LIAG; MAC387; MRP14; P14
| OMIM = 123886
| ECnumber =
| Homologene = 2227
| MGIid = 1338947
| GeneAtlas_image1 = PBB_GE_S100A9_203535_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6280
| Hs_Ensembl = ENSG00000163220
| Hs_RefseqProtein = NP_002956
| Hs_RefseqmRNA = NM_002965
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 151596954
| Hs_GenLoc_end = 151600127
| Hs_Uniprot = P06702
| Mm_EntrezGene = 20202
| Mm_Ensembl = ENSMUSG00000056071
| Mm_RefseqmRNA = NM_009114
| Mm_RefseqProtein = NP_033140
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 90778560
| Mm_GenLoc_end = 90781618
| Mm_Uniprot = Q3UP42
}}
}}
'''S100 calcium binding protein A9''', also known as '''S100A9''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: S100A9 S100 calcium binding protein A9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6280| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in the inhibition of casein kinase and altered expression of this protein is associated with the disease cystic fibrosis.<ref name="entrez">{{cite web | title = Entrez Gene: S100A9 S100 calcium binding protein A9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6280| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schäfer BW, Heizmann CW |title=The S100 family of EF-hand calcium-binding proteins: functions and pathology. |journal=Trends Biochem. Sci. |volume=21 |issue= 4 |pages= 134-40 |year= 1996 |pmid= 8701470 |doi= }}
*{{cite journal | author=Kerkhoff C, Klempt M, Sorg C |title=Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9). |journal=Biochim. Biophys. Acta |volume=1448 |issue= 2 |pages= 200-11 |year= 1999 |pmid= 9920411 |doi= }}
*{{cite journal | author=Nacken W, Roth J, Sorg C, Kerkhoff C |title=S100A9/S100A8: Myeloid representatives of the S100 protein family as prominent players in innate immunity. |journal=Microsc. Res. Tech. |volume=60 |issue= 6 |pages= 569-80 |year= 2003 |pmid= 12645005 |doi= 10.1002/jemt.10299 }}
*{{cite journal | author=Rasmussen HH, van Damme J, Puype M, ''et al.'' |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960-9 |year= 1993 |pmid= 1286667 |doi= }}
*{{cite journal | author=Longbottom D, Sallenave JM, van Heyningen V |title=Subunit structure of calgranulins A and B obtained from sputum, plasma, granulocytes and cultured epithelial cells. |journal=Biochim. Biophys. Acta |volume=1120 |issue= 2 |pages= 215-22 |year= 1992 |pmid= 1562590 |doi= }}
*{{cite journal | author=Dorin JR, Emslie E, van Heyningen V |title=Related calcium-binding proteins map to the same subregion of chromosome 1q and to an extended region of synteny on mouse chromosome 3. |journal=Genomics |volume=8 |issue= 3 |pages= 420-6 |year= 1991 |pmid= 2149559 |doi= }}
*{{cite journal | author=Edgeworth J, Freemont P, Hogg N |title=Ionomycin-regulated phosphorylation of the myeloid calcium-binding protein p14. |journal=Nature |volume=342 |issue= 6246 |pages= 189-92 |year= 1989 |pmid= 2478889 |doi= 10.1038/342189a0 }}
*{{cite journal | author=Murao S, Collart FR, Huberman E |title=A protein containing the cystic fibrosis antigen is an inhibitor of protein kinases. |journal=J. Biol. Chem. |volume=264 |issue= 14 |pages= 8356-60 |year= 1989 |pmid= 2656677 |doi= }}
*{{cite journal | author=Odink K, Cerletti N, Brüggen J, ''et al.'' |title=Two calcium-binding proteins in infiltrate macrophages of rheumatoid arthritis. |journal=Nature |volume=330 |issue= 6143 |pages= 80-2 |year= 1987 |pmid= 3313057 |doi= 10.1038/330080a0 }}
*{{cite journal | author=Lagasse E, Clerc RG |title=Cloning and expression of two human genes encoding calcium-binding proteins that are regulated during myeloid differentiation. |journal=Mol. Cell. Biol. |volume=8 |issue= 6 |pages= 2402-10 |year= 1988 |pmid= 3405210 |doi= }}
*{{cite journal | author=Schäfer BW, Wicki R, Engelkamp D, ''et al.'' |title=Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family. |journal=Genomics |volume=25 |issue= 3 |pages= 638-43 |year= 1995 |pmid= 7759097 |doi= }}
*{{cite journal | author=Engelkamp D, Schäfer BW, Mattei MG, ''et al.'' |title=Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 14 |pages= 6547-51 |year= 1993 |pmid= 8341667 |doi= }}
*{{cite journal | author=Roth J, Burwinkel F, van den Bos C, ''et al.'' |title=MRP8 and MRP14, S-100-like proteins associated with myeloid differentiation, are translocated to plasma membrane and intermediate filaments in a calcium-dependent manner. |journal=Blood |volume=82 |issue= 6 |pages= 1875-83 |year= 1993 |pmid= 8400238 |doi= }}
*{{cite journal | author=Miyasaki KT, Bodeau AL, Murthy AR, Lehrer RI |title=In vitro antimicrobial activity of the human neutrophil cytosolic S-100 protein complex, calprotectin, against Capnocytophaga sputigena. |journal=J. Dent. Res. |volume=72 |issue= 2 |pages= 517-23 |year= 1993 |pmid= 8423249 |doi= }}
*{{cite journal | author=Newton RA, Hogg N |title=The human S100 protein MRP-14 is a novel activator of the beta 2 integrin Mac-1 on neutrophils. |journal=J. Immunol. |volume=160 |issue= 3 |pages= 1427-35 |year= 1998 |pmid= 9570563 |doi= }}
*{{cite journal | author=Vogl T, Pröpper C, Hartmann M, ''et al.'' |title=S100A12 is expressed exclusively by granulocytes and acts independently from MRP8 and MRP14. |journal=J. Biol. Chem. |volume=274 |issue= 36 |pages= 25291-6 |year= 1999 |pmid= 10464253 |doi= }}
*{{cite journal | author=Kerkhoff C, Klempt M, Kaever V, Sorg C |title=The two calcium-binding proteins, S100A8 and S100A9, are involved in the metabolism of arachidonic acid in human neutrophils. |journal=J. Biol. Chem. |volume=274 |issue= 46 |pages= 32672-9 |year= 2000 |pmid= 10551823 |doi= }}
*{{cite journal | author=Stulík J, Koupilova K, Osterreicher J, ''et al.'' |title=Protein abundance alterations in matched sets of macroscopically normal colon mucosa and colorectal carcinoma. |journal=Electrophoresis |volume=20 |issue= 18 |pages= 3638-46 |year= 2000 |pmid= 10612291 |doi= 10.1002/(SICI)1522-2683(19991201)20:18<3638::AID-ELPS3638>3.0.CO;2-W }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SPTA1... {December 15, 2007 1:05:51 PM PST}
- REDIRECT: Page directory gave bad page (SPTA1). Continuing with search.. Please correct entry: <6708,SPTA1>. {December 15, 2007 1:06:15 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:06:28 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SPTA1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1owa.
| PDB = {{PDB2|1owa}}
| Name = Spectrin, alpha, erythrocytic 1 (elliptocytosis 2)
| HGNCid = 11272
| Symbol = SPTA1
| AltSymbols =; EL2; SPTA
| OMIM = 182860
| ECnumber =
| Homologene = 74460
| MGIid = 98385
| GeneAtlas_image1 = PBB_GE_SPTA1_206937_at_tn.png
| Function = {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0051015 |text = actin filament binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0008091 |text = spectrin}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007015 |text = actin filament organization}} {{GNF_GO|id=GO:0008360 |text = regulation of cell shape}} {{GNF_GO|id=GO:0051016 |text = barbed-end actin filament capping}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6708
| Hs_Ensembl = ENSG00000163554
| Hs_RefseqProtein = NP_003117
| Hs_RefseqmRNA = NM_003126
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 156846902
| Hs_GenLoc_end = 156923112
| Hs_Uniprot = P02549
| Mm_EntrezGene = 20739
| Mm_Ensembl = ENSMUSG00000026532
| Mm_RefseqmRNA = NM_011465
| Mm_RefseqProtein = NP_035595
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 176011002
| Mm_GenLoc_end = 176084132
| Mm_Uniprot = Q3UQ30
}}
}}
'''Spectrin, alpha, erythrocytic 1 (elliptocytosis 2)''', also known as '''SPTA1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SPTA1 spectrin, alpha, erythrocytic 1 (elliptocytosis 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6708| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is a tetramer made up of alpha-beta dimers linked in a head-to-head arrangement. This gene is one member of a family of alpha-spectrin genes. The encoded protein is primarily composed of 22 spectrin repeats which are involved in dimer formation. It forms weaker tetramer interactions than non-erythrocytic alpha spectrin, which may increase the plasma membrane elasticity and deformability of red blood cells. Mutations in this gene result in a variety of hereditary red blood cell disorders, including elliptocytosis type 2, pyropoikilocytosis, and spherocytic hemolytic anemia.<ref name="entrez">{{cite web | title = Entrez Gene: SPTA1 spectrin, alpha, erythrocytic 1 (elliptocytosis 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6708| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gallagher PG, Forget BG |title=Spectrin genes in health and disease. |journal=Semin. Hematol. |volume=30 |issue= 1 |pages= 4-20 |year= 1993 |pmid= 8094577 |doi= }}
*{{cite journal | author=Delaunay J, Dhermy D |title=Mutations involving the spectrin heterodimer contact site: clinical expression and alterations in specific function. |journal=Semin. Hematol. |volume=30 |issue= 1 |pages= 21-33 |year= 1993 |pmid= 8434258 |doi= }}
*{{cite journal | author=Snásel J, Pichová I |title=The cleavage of host cell proteins by HIV-1 protease. |journal=Folia Biol. (Praha) |volume=42 |issue= 5 |pages= 227-30 |year= 1997 |pmid= 8997639 |doi= }}
*{{cite journal | author=Iolascon A, Miraglia del Giudice E, Perrotta S, ''et al.'' |title=Hereditary spherocytosis: from clinical to molecular defects. |journal=Haematologica |volume=83 |issue= 3 |pages= 240-57 |year= 1998 |pmid= 9573679 |doi= }}
*{{cite journal | author=De Matteis MA, Morrow JS |title=Spectrin tethers and mesh in the biosynthetic pathway. |journal=J. Cell. Sci. |volume=113 ( Pt 13) |issue= |pages= 2331-43 |year= 2000 |pmid= 10852813 |doi= }}
*{{cite journal | author=Delaunay J |title=Molecular basis of red cell membrane disorders. |journal=Acta Haematol. |volume=108 |issue= 4 |pages= 210-8 |year= 2003 |pmid= 12432217 |doi= }}
*{{cite journal | author=Dhermy D, Schrével J, Lecomte MC |title=Spectrin-based skeleton in red blood cells and malaria. |journal=Curr. Opin. Hematol. |volume=14 |issue= 3 |pages= 198-202 |year= 2007 |pmid= 17414207 |doi= 10.1097/MOH.0b013e3280d21afd }}
*{{cite journal | author=Hentati A, Hu P, Asgharzadeh S, Siddique T |title=Dinucleotide repeat polymorphism at the human erythroid alpha spectrin (SPTA1) locus. |journal=Hum. Mol. Genet. |volume=1 |issue= 3 |pages= 218 |year= 1993 |pmid= 1339473 |doi= }}
*{{cite journal | author=Kanzaki A, Rabodonirina M, Yawata Y, ''et al.'' |title=A deletional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin Tokyo (beta 220/216). |journal=Blood |volume=80 |issue= 8 |pages= 2115-21 |year= 1992 |pmid= 1391962 |doi= }}
*{{cite journal | author=Gallagher PG, Tse WT, Coetzer T, ''et al.'' |title=A common type of the spectrin alpha I 46-50a-kD peptide abnormality in hereditary elliptocytosis and pyropoikilocytosis is associated with a mutation distant from the proteolytic cleavage site. Evidence for the functional importance of the triple helical model of spectrin. |journal=J. Clin. Invest. |volume=89 |issue= 3 |pages= 892-8 |year= 1992 |pmid= 1541680 |doi= }}
*{{cite journal | author=Speicher DW, Weglarz L, DeSilva TM |title=Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site. |journal=J. Biol. Chem. |volume=267 |issue= 21 |pages= 14775-82 |year= 1992 |pmid= 1634521 |doi= }}
*{{cite journal | author=Alloisio N, Wilmotte R, Morlé L, ''et al.'' |title=Spectrin Jendouba: an alpha II/31 spectrin variant that is associated with elliptocytosis and carries a mutation distant from the dimer self-association site. |journal=Blood |volume=80 |issue= 3 |pages= 809-15 |year= 1992 |pmid= 1638030 |doi= }}
*{{cite journal | author=Kotula L, Laury-Kleintop LD, Showe L, ''et al.'' |title=The exon-intron organization of the human erythrocyte alpha-spectrin gene. |journal=Genomics |volume=9 |issue= 1 |pages= 131-40 |year= 1991 |pmid= 1672285 |doi= }}
*{{cite journal | author=Coetzer TL, Sahr K, Prchal J, ''et al.'' |title=Four different mutations in codon 28 of alpha spectrin are associated with structurally and functionally abnormal spectrin alpha I/74 in hereditary elliptocytosis. |journal=J. Clin. Invest. |volume=88 |issue= 3 |pages= 743-9 |year= 1991 |pmid= 1679439 |doi= }}
*{{cite journal | author=Sahr KE, Laurila P, Kotula L, ''et al.'' |title=The complete cDNA and polypeptide sequences of human erythroid alpha-spectrin. |journal=J. Biol. Chem. |volume=265 |issue= 8 |pages= 4434-43 |year= 1990 |pmid= 1689726 |doi= }}
*{{cite journal | author=Gallagher PG, Tse WT, Marchesi SL, ''et al.'' |title=A defect in alpha-spectrin mRNA accumulation in hereditary pyropoikilocytosis. |journal=Trans. Assoc. Am. Physicians |volume=104 |issue= |pages= 32-9 |year= 1993 |pmid= 1845156 |doi= }}
*{{cite journal | author=Floyd PB, Gallagher PG, Valentino LA, ''et al.'' |title=Heterogeneity of the molecular basis of hereditary pyropoikilocytosis and hereditary elliptocytosis associated with increased levels of the spectrin alpha I/74-kilodalton tryptic peptide. |journal=Blood |volume=78 |issue= 5 |pages= 1364-72 |year= 1991 |pmid= 1878597 |doi= }}
*{{cite journal | author=Shoeman RL, Kesselmier C, Mothes E, ''et al.'' |title=Non-viral cellular substrates for human immunodeficiency virus type 1 protease. |journal=FEBS Lett. |volume=278 |issue= 2 |pages= 199-203 |year= 1991 |pmid= 1991513 |doi= }}
*{{cite journal | author=Garbarz M, Tse WT, Gallagher PG, ''et al.'' |title=Spectrin Rouen (beta 220-218), a novel shortened beta-chain variant in a kindred with hereditary elliptocytosis. Characterization of the molecular defect as exon skipping due to a splice site mutation. |journal=J. Clin. Invest. |volume=88 |issue= 1 |pages= 76-81 |year= 1991 |pmid= 2056132 |doi= }}
*{{cite journal | author=Tse WT, Gallagher PG, Pothier B, ''et al.'' |title=An insertional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin nice (beta 220/216). |journal=Blood |volume=78 |issue= 2 |pages= 517-23 |year= 1991 |pmid= 2070088 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TGFB2... {December 15, 2007 1:06:28 PM PST}
- REDIRECT: Page directory gave bad page (TGFB2). Continuing with search.. Please correct entry: <7042,TGFB2>. {December 15, 2007 1:07:05 PM PST}
- SEARCH REDIRECT: Control Box Found: TGF beta 2 {December 15, 2007 1:07:18 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {December 15, 2007 1:07:20 PM PST}
- SKIP SUMMARY: SKIPPING Summary, No Errors. {December 15, 2007 1:07:20 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {December 15, 2007 1:07:20 PM PST}
- UPDATED: Warning while updating page: Could not find summary box. {December 15, 2007 1:07:31 PM PST}
- UPDATED: Updated protein page (with warnings): TGF beta 2 {December 15, 2007 1:07:31 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TGFB2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1tfg.
| PDB = {{PDB2|1tfg}}, {{PDB2|2tgi}}
| Name = Transforming growth factor, beta 2
| HGNCid = 11768
| Symbol = TGFB2
| AltSymbols =; MGC116892; TGF-beta2
| OMIM = 190220
| ECnumber =
| Homologene = 2432
| MGIid = 98726
| GeneAtlas_image1 = PBB_GE_TGFB2_209908_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_TGFB2_209909_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_TGFB2_220407_s_at_tn.png
| Function = {{GNF_GO|id=GO:0001540 |text = beta-amyloid binding}} {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005160 |text = transforming growth factor beta receptor binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0030424 |text = axon}} {{GNF_GO|id=GO:0043025 |text = cell soma}}
| Process = {{GNF_GO|id=GO:0000902 |text = cell morphogenesis}} {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0001654 |text = eye development}} {{GNF_GO|id=GO:0001707 |text = mesoderm formation}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0008219 |text = cell death}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0009790 |text = embryonic development}} {{GNF_GO|id=GO:0010002 |text = cardioblast differentiation}} {{GNF_GO|id=GO:0016049 |text = cell growth}} {{GNF_GO|id=GO:0030097 |text = hemopoiesis}} {{GNF_GO|id=GO:0030307 |text = positive regulation of cell growth}} {{GNF_GO|id=GO:0030593 |text = neutrophil chemotaxis}} {{GNF_GO|id=GO:0031069 |text = hair follicle morphogenesis}} {{GNF_GO|id=GO:0042060 |text = wound healing}} {{GNF_GO|id=GO:0042416 |text = dopamine biosynthetic process}} {{GNF_GO|id=GO:0042637 |text = catagen}} {{GNF_GO|id=GO:0043525 |text = positive regulation of neuron apoptosis}} {{GNF_GO|id=GO:0045617 |text = negative regulation of keratinocyte differentiation}} {{GNF_GO|id=GO:0045787 |text = positive regulation of progression through cell cycle}} {{GNF_GO|id=GO:0045823 |text = positive regulation of heart contraction}} {{GNF_GO|id=GO:0048103 |text = somatic stem cell division}} {{GNF_GO|id=GO:0048666 |text = neuron development}} {{GNF_GO|id=GO:0048699 |text = generation of neurons}} {{GNF_GO|id=GO:0050777 |text = negative regulation of immune response}} {{GNF_GO|id=GO:0050778 |text = positive regulation of immune response}} {{GNF_GO|id=GO:0051795 |text = positive regulation of catagen}} {{GNF_GO|id=GO:0051891 |text = positive regulation of cardioblast differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7042
| Hs_Ensembl = ENSG00000092969
| Hs_RefseqProtein = NP_003229
| Hs_RefseqmRNA = NM_003238
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 216586200
| Hs_GenLoc_end = 216684584
| Hs_Uniprot = P61812
| Mm_EntrezGene = 21808
| Mm_Ensembl = ENSMUSG00000039239
| Mm_RefseqmRNA = NM_009367
| Mm_RefseqProtein = NP_033393
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 188324430
| Mm_GenLoc_end = 188406777
| Mm_Uniprot = Q3TWH5
}}
}}
'''Transforming growth factor, beta 2''', also known as '''TGFB2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TGFB2 transforming growth factor, beta 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7042| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Clark DA, Coker R |title=Transforming growth factor-beta (TGF-beta). |journal=Int. J. Biochem. Cell Biol. |volume=30 |issue= 3 |pages= 293-8 |year= 1998 |pmid= 9611771 |doi= }}
*{{cite journal | author=Wick W, Platten M, Weller M |title=Glioma cell invasion: regulation of metalloproteinase activity by TGF-beta. |journal=J. Neurooncol. |volume=53 |issue= 2 |pages= 177-85 |year= 2002 |pmid= 11716069 |doi= }}
*{{cite journal | author=Bissell DM |title=Chronic liver injury, TGF-beta, and cancer. |journal=Exp. Mol. Med. |volume=33 |issue= 4 |pages= 179-90 |year= 2002 |pmid= 11795478 |doi= }}
*{{cite journal | author=Kalluri R, Neilson EG |title=Epithelial-mesenchymal transition and its implications for fibrosis. |journal=J. Clin. Invest. |volume=112 |issue= 12 |pages= 1776-84 |year= 2004 |pmid= 14679171 |doi= 10.1172/JCI200320530 }}
*{{cite journal | author=Daopin S, Piez KA, Ogawa Y, Davies DR |title=Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily. |journal=Science |volume=257 |issue= 5068 |pages= 369-73 |year= 1992 |pmid= 1631557 |doi= }}
*{{cite journal | author=Schlunegger MP, Grütter MG |title=An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2. |journal=Nature |volume=358 |issue= 6385 |pages= 430-4 |year= 1992 |pmid= 1641027 |doi= 10.1038/358430a0 }}
*{{cite journal | author=Noma T, Glick AB, Geiser AG, ''et al.'' |title=Molecular cloning and structure of the human transforming growth factor-beta 2 gene promoter. |journal=Growth Factors |volume=4 |issue= 4 |pages= 247-55 |year= 1992 |pmid= 1764261 |doi= }}
*{{cite journal | author=Bodmer S, Podlisny MB, Selkoe DJ, ''et al.'' |title=Transforming growth factor-beta bound to soluble derivatives of the beta amyloid precursor protein of Alzheimer's disease. |journal=Biochem. Biophys. Res. Commun. |volume=171 |issue= 2 |pages= 890-7 |year= 1990 |pmid= 2119582 |doi= }}
*{{cite journal | author=Webb NR, Madisen L, Rose TM, Purchio AF |title=Structural and sequence analysis of TGF-beta 2 cDNA clones predicts two different precursor proteins produced by alternative mRNA splicing. |journal=DNA |volume=7 |issue= 7 |pages= 493-7 |year= 1989 |pmid= 2850146 |doi= }}
*{{cite journal | author=Madisen L, Webb NR, Rose TM, ''et al.'' |title=Transforming growth factor-beta 2: cDNA cloning and sequence analysis. |journal=DNA |volume=7 |issue= 1 |pages= 1-8 |year= 1988 |pmid= 3162414 |doi= }}
*{{cite journal | author=Barton DE, Foellmer BE, Du J, ''et al.'' |title=Chromosomal mapping of genes for transforming growth factors beta 2 and beta 3 in man and mouse: dispersion of TGF-beta gene family. |journal=Oncogene Res. |volume=3 |issue= 4 |pages= 323-31 |year= 1989 |pmid= 3226728 |doi= }}
*{{cite journal | author=de Martin R, Haendler B, Hofer-Warbinek R, ''et al.'' |title=Complementary DNA for human glioblastoma-derived T cell suppressor factor, a novel member of the transforming growth factor-beta gene family. |journal=EMBO J. |volume=6 |issue= 12 |pages= 3673-7 |year= 1988 |pmid= 3322813 |doi= }}
*{{cite journal | author=Marquardt H, Lioubin MN, Ikeda T |title=Complete amino acid sequence of human transforming growth factor type beta 2. |journal=J. Biol. Chem. |volume=262 |issue= 25 |pages= 12127-31 |year= 1987 |pmid= 3476488 |doi= }}
*{{cite journal | author=Philip A, Bostedt L, Stigbrand T, O'Connor-McCourt MD |title=Binding of transforming growth factor-beta (TGF-beta) to pregnancy zone protein (PZP). Comparison to the TGF-beta-alpha 2-macroglobulin interaction. |journal=Eur. J. Biochem. |volume=221 |issue= 2 |pages= 687-93 |year= 1994 |pmid= 7513640 |doi= }}
*{{cite journal | author=Lin HY, Moustakas A, Knaus P, ''et al.'' |title=The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands. |journal=J. Biol. Chem. |volume=270 |issue= 6 |pages= 2747-54 |year= 1995 |pmid= 7852346 |doi= }}
*{{cite journal | author=Hildebrand A, Romarís M, Rasmussen LM, ''et al.'' |title=Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta. |journal=Biochem. J. |volume=302 ( Pt 2) |issue= |pages= 527-34 |year= 1994 |pmid= 8093006 |doi= }}
*{{cite journal | author=López-Casillas F, Payne HM, Andres JL, Massagué J |title=Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites. |journal=J. Cell Biol. |volume=124 |issue= 4 |pages= 557-68 |year= 1994 |pmid= 8106553 |doi= }}
*{{cite journal | author=Fromigué O, Marie PJ, Lomri A |title=Bone morphogenetic protein-2 and transforming growth factor-beta2 interact to modulate human bone marrow stromal cell proliferation and differentiation. |journal=J. Cell. Biochem. |volume=68 |issue= 4 |pages= 411-26 |year= 1998 |pmid= 9493905 |doi= }}
*{{cite journal | author=Mori T, Kawara S, Shinozaki M, ''et al.'' |title=Role and interaction of connective tissue growth factor with transforming growth factor-beta in persistent fibrosis: A mouse fibrosis model. |journal=J. Cell. Physiol. |volume=181 |issue= 1 |pages= 153-9 |year= 1999 |pmid= 10457363 |doi= 10.1002/(SICI)1097-4652(199910)181:1<153::AID-JCP16>3.0.CO;2-K }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TGFBI... {December 15, 2007 1:07:31 PM PST}
- REDIRECT: Page directory gave bad page (TGFBI). Continuing with search.. Please correct entry: <7045,TGFBI>. {December 15, 2007 1:07:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:08:33 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TGFBI_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1x3b.
| PDB = {{PDB2|1x3b}}
| Name = Transforming growth factor, beta-induced, 68kDa
| HGNCid = 11771
| Symbol = TGFBI
| AltSymbols =; BIGH3; CDB1; CDG2; CDGG1; CSD; CSD1; CSD2; CSD3; EBMD; LCD1
| OMIM = 601692
| ECnumber =
| Homologene = 37294
| MGIid = 99959
| GeneAtlas_image1 = PBB_GE_TGFBI_201506_at_tn.png
| Function = {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007162 |text = negative regulation of cell adhesion}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7045
| Hs_Ensembl = ENSG00000120708
| Hs_RefseqProtein = NP_000349
| Hs_RefseqmRNA = NM_000358
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 135392644
| Hs_GenLoc_end = 135427253
| Hs_Uniprot = Q15582
| Mm_EntrezGene = 21810
| Mm_Ensembl = ENSMUSG00000035493
| Mm_RefseqmRNA = NM_009369
| Mm_RefseqProtein = NP_033395
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 56619208
| Mm_GenLoc_end = 56648972
| Mm_Uniprot = Q19PV3
}}
}}
'''Transforming growth factor, beta-induced, 68kDa''', also known as '''TGFBI''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TGFBI transforming growth factor, beta-induced, 68kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7045| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Fujiki K, Nakayasu K, Kanai A |title=Corneal dystrophies in Japan. |journal=J. Hum. Genet. |volume=46 |issue= 8 |pages= 431-5 |year= 2001 |pmid= 11501939 |doi= }}
*{{cite journal | author=Schmitt-Bernard CF, Pouliquen Y, Argilès A |title=[BIG-H3 protein: mutation of codon 124 and corneal amyloidosis] |journal=Journal français d'ophtalmologie |volume=27 |issue= 5 |pages= 510-22 |year= 2004 |pmid= 15179309 |doi= }}
*{{cite journal | author=Pieramici SF, Afshari NA |title=Genetics of corneal dystrophies: the evolving landscape. |journal=Current opinion in ophthalmology |volume=17 |issue= 4 |pages= 361-6 |year= 2006 |pmid= 16900028 |doi= 10.1097/01.icu.0000233955.94347.84 }}
*{{cite journal | author=Skonier J, Neubauer M, Madisen L, ''et al.'' |title=cDNA cloning and sequence analysis of beta ig-h3, a novel gene induced in a human adenocarcinoma cell line after treatment with transforming growth factor-beta. |journal=DNA Cell Biol. |volume=11 |issue= 7 |pages= 511-22 |year= 1992 |pmid= 1388724 |doi= }}
*{{cite journal | author=LeBaron RG, Bezverkov KI, Zimber MP, ''et al.'' |title=Beta IG-H3, a novel secretory protein inducible by transforming growth factor-beta, is present in normal skin and promotes the adhesion and spreading of dermal fibroblasts in vitro. |journal=J. Invest. Dermatol. |volume=104 |issue= 5 |pages= 844-9 |year= 1995 |pmid= 7738366 |doi= }}
*{{cite journal | author=Skonier J, Bennett K, Rothwell V, ''et al.'' |title=beta ig-h3: a transforming growth factor-beta-responsive gene encoding a secreted protein that inhibits cell attachment in vitro and suppresses the growth of CHO cells in nude mice. |journal=DNA Cell Biol. |volume=13 |issue= 6 |pages= 571-84 |year= 1994 |pmid= 8024701 |doi= }}
*{{cite journal | author=Escribano J, Hernando N, Ghosh S, ''et al.'' |title=cDNA from human ocular ciliary epithelium homologous to beta ig-h3 is preferentially expressed as an extracellular protein in the corneal epithelium. |journal=J. Cell. Physiol. |volume=160 |issue= 3 |pages= 511-21 |year= 1994 |pmid= 8077289 |doi= 10.1002/jcp.1041600314 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Stone EM, Mathers WD, Rosenwasser GO, ''et al.'' |title=Three autosomal dominant corneal dystrophies map to chromosome 5q. |journal=Nat. Genet. |volume=6 |issue= 1 |pages= 47-51 |year= 1994 |pmid= 8136834 |doi= 10.1038/ng0194-47 }}
*{{cite journal | author=Munier FL, Korvatska E, Djemaï A, ''et al.'' |title=Kerato-epithelin mutations in four 5q31-linked corneal dystrophies. |journal=Nat. Genet. |volume=15 |issue= 3 |pages= 247-51 |year= 1997 |pmid= 9054935 |doi= 10.1038/ng0397-247 }}
*{{cite journal | author=Hashimoto K, Noshiro M, Ohno S, ''et al.'' |title=Characterization of a cartilage-derived 66-kDa protein (RGD-CAP/beta ig-h3) that binds to collagen. |journal=Biochim. Biophys. Acta |volume=1355 |issue= 3 |pages= 303-14 |year= 1997 |pmid= 9061001 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Korvatska E, Munier FL, Djemaï A, ''et al.'' |title=Mutation hot spots in 5q31-linked corneal dystrophies. |journal=Am. J. Hum. Genet. |volume=62 |issue= 2 |pages= 320-4 |year= 1998 |pmid= 9463327 |doi= }}
*{{cite journal | author=Yamamoto S, Okada M, Tsujikawa M, ''et al.'' |title=A kerato-epithelin (betaig-h3) mutation in lattice corneal dystrophy type IIIA. |journal=Am. J. Hum. Genet. |volume=62 |issue= 3 |pages= 719-22 |year= 1998 |pmid= 9497262 |doi= }}
*{{cite journal | author=Okada M, Yamamoto S, Watanabe H, ''et al.'' |title=Granular corneal dystrophy with homozygous mutations in the kerato-epithelin gene. |journal=Am. J. Ophthalmol. |volume=126 |issue= 2 |pages= 169-76 |year= 1998 |pmid= 9727509 |doi= }}
*{{cite journal | author=Okada M, Yamamoto S, Tsujikawa M, ''et al.'' |title=Two distinct kerato-epithelin mutations in Reis-Bücklers corneal dystrophy. |journal=Am. J. Ophthalmol. |volume=126 |issue= 4 |pages= 535-42 |year= 1998 |pmid= 9780098 |doi= }}
*{{cite journal | author=Fujiki K, Hotta Y, Nakayasu K, ''et al.'' |title=A new L527R mutation of the betaIGH3 gene in patients with lattice corneal dystrophy with deep stromal opacities. |journal=Hum. Genet. |volume=103 |issue= 3 |pages= 286-9 |year= 1998 |pmid= 9799082 |doi= }}
*{{cite journal | author=Stewart H, Black GC, Donnai D, ''et al.'' |title=A mutation within exon 14 of the TGFBI (BIGH3) gene on chromosome 5q31 causes an asymmetric, late-onset form of lattice corneal dystrophy. |journal=Ophthalmology |volume=106 |issue= 5 |pages= 964-70 |year= 1999 |pmid= 10328397 |doi= 10.1016/S0161-6420(99)00539-4 }}
*{{cite journal | author=Stewart HS, Ridgway AE, Dixon MJ, ''et al.'' |title=Heterogeneity in granular corneal dystrophy: identification of three causative mutations in the TGFBI (BIGH3) gene-lessons for corneal amyloidogenesis. |journal=Hum. Mutat. |volume=14 |issue= 2 |pages= 126-32 |year= 1999 |pmid= 10425035 |doi= 10.1002/(SICI)1098-1004(1999)14:2<126::AID-HUMU4>3.0.CO;2-W }}
*{{cite journal | author=Rozzo C, Fossarello M, Galleri G, ''et al.'' |title=A common beta ig-h3 gene mutation (delta f540) in a large cohort of Sardinian Reis Bücklers corneal dystrophy patients. Mutations in brief no. 180. Online. |journal=Hum. Mutat. |volume=12 |issue= 3 |pages= 215-6 |year= 2000 |pmid= 10660331 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on VCP... {December 15, 2007 1:08:33 PM PST}
- REDIRECT: Page directory gave bad page (VCP (gene)). Continuing with search.. Please correct entry: <7415,VCP (gene)>. {December 15, 2007 1:09:04 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {December 15, 2007 1:09:23 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_VCP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e32.
| PDB = {{PDB2|1e32}}, {{PDB2|1oz4}}, {{PDB2|1r7r}}, {{PDB2|1s3s}}, {{PDB2|1ypw}}, {{PDB2|1yq0}}, {{PDB2|1yqi}}, {{PDB2|2pjh}}
| Name = Valosin-containing protein
| HGNCid = 12666
| Symbol = VCP
| AltSymbols =; p97; IBMPFD; MGC131997; MGC148092; MGC8560; TERA
| OMIM = 601023
| ECnumber =
| Homologene = 5168
| MGIid = 99919
| GeneAtlas_image1 = PBB_GE_VCP_208649_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_VCP_208648_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006302 |text = double-strand break repair}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006919 |text = caspase activation}} {{GNF_GO|id=GO:0016567 |text = protein ubiquitination}} {{GNF_GO|id=GO:0030433 |text = ER-associated protein catabolic process}} {{GNF_GO|id=GO:0030968 |text = unfolded protein response}} {{GNF_GO|id=GO:0030970 |text = retrograde protein transport, ER to cytosol}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0045184 |text = establishment of protein localization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7415
| Hs_Ensembl = ENSG00000165280
| Hs_RefseqProtein = NP_009057
| Hs_RefseqmRNA = NM_007126
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 35046061
| Hs_GenLoc_end = 35063246
| Hs_Uniprot = P55072
| Mm_EntrezGene = 269523
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_009503
| Mm_RefseqProtein = NP_033529
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Valosin-containing protein''', also known as '''VCP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: VCP valosin-containing protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7415| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Valosin-containing protein (VCP) is a member of a family that includes putative ATP-binding proteins involved in vesicle transport and fusion, 26S proteasome function, and assembly of peroxisomes. VCP, as a structural protein, is associated with clathrin, and heat-shock protein Hsc70, to form a complex. VCP has been implicated in a number of cellular events that are regulated during mitosis, including homotypic membrane fusion, spindle pole body function, and ubiquitin-dependent protein degradation.<ref name="entrez">{{cite web | title = Entrez Gene: VCP valosin-containing protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7415| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Guinto JB, Ritson GP, Taylor JP, Forman MS |title=Valosin-containing protein and the pathogenesis of frontotemporal dementia associated with inclusion body myopathy. |journal=Acta Neuropathol. |volume=114 |issue= 1 |pages= 55-61 |year= 2007 |pmid= 17457594 |doi= 10.1007/s00401-007-0224-7 }}
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Rabouille C, Levine TP, Peters JM, Warren G |title=An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments. |journal=Cell |volume=82 |issue= 6 |pages= 905-14 |year= 1995 |pmid= 7553851 |doi= }}
*{{cite journal | author=Pleasure IT, Black MM, Keen JH |title=Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein. |journal=Nature |volume=365 |issue= 6445 |pages= 459-62 |year= 1993 |pmid= 8413590 |doi= 10.1038/365459a0 }}
*{{cite journal | author=Druck T, Gu Y, Prabhala G, ''et al.'' |title=Chromosome localization of human genes for clathrin adaptor polypeptides AP2 beta and AP50 and the clathrin-binding protein, VCP. |journal=Genomics |volume=30 |issue= 1 |pages= 94-7 |year= 1996 |pmid= 8595912 |doi= 10.1006/geno.1995.0016 }}
*{{cite journal | author=Germain-Lee EL, Obie C, Valle D |title=NVL: a new member of the AAA family of ATPases localized to the nucleus. |journal=Genomics |volume=44 |issue= 1 |pages= 22-34 |year= 1997 |pmid= 9286697 |doi= 10.1006/geno.1997.4856 }}
*{{cite journal | author=Hoyle J, Tan KH, Fisher EM |title=Mapping the valosin-containing protein (VCP) gene on human chromosome 9 and mouse chromosome 4, and a likely pseudogene on the mouse X chromosome. |journal=Mamm. Genome |volume=8 |issue= 10 |pages= 778-80 |year= 1997 |pmid= 9321476 |doi= }}
*{{cite journal | author=Dai RM, Chen E, Longo DL, ''et al.'' |title=Involvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3562-73 |year= 1998 |pmid= 9452483 |doi= }}
*{{cite journal | author=Rabouille C, Kondo H, Newman R, ''et al.'' |title=Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro. |journal=Cell |volume=92 |issue= 5 |pages= 603-10 |year= 1998 |pmid= 9506515 |doi= }}
*{{cite journal | author=Zhang SH, Liu J, Kobayashi R, Tonks NK |title=Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1. |journal=J. Biol. Chem. |volume=274 |issue= 25 |pages= 17806-12 |year= 1999 |pmid= 10364224 |doi= }}
*{{cite journal | author=Zhang H, Wang Q, Kajino K, Greene MI |title=VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells. |journal=DNA Cell Biol. |volume=19 |issue= 5 |pages= 253-63 |year= 2000 |pmid= 10855792 |doi= 10.1089/10445490050021168 }}
*{{cite journal | author=Hu RM, Han ZG, Song HD, ''et al.'' |title=Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 17 |pages= 9543-8 |year= 2000 |pmid= 10931946 |doi= 10.1073/pnas.160270997 }}
*{{cite journal | author=Lavoie C, Chevet E, Roy L, ''et al.'' |title=Tyrosine phosphorylation of p97 regulates transitional endoplasmic reticulum assembly in vitro. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 25 |pages= 13637-42 |year= 2001 |pmid= 11087817 |doi= 10.1073/pnas.240278097 }}
*{{cite journal | author=Kimonis VE, Kovach MJ, Waggoner B, ''et al.'' |title=Clinical and molecular studies in a unique family with autosomal dominant limb-girdle muscular dystrophy and Paget disease of bone. |journal=Genet. Med. |volume=2 |issue= 4 |pages= 232-41 |year= 2001 |pmid= 11252708 |doi= }}
*{{cite journal | author=Seigneurin-Berny D, Verdel A, Curtet S, ''et al.'' |title=Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways. |journal=Mol. Cell. Biol. |volume=21 |issue= 23 |pages= 8035-44 |year= 2001 |pmid= 11689694 |doi= 10.1128/MCB.21.23.8035-8044.2001 }}
*{{cite journal | author=Yang CS, Weiner H |title=Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol. |journal=Arch. Biochem. Biophys. |volume=400 |issue= 1 |pages= 105-10 |year= 2002 |pmid= 11913976 |doi= 10.1006/abbi.2002.2778 }}
*{{cite journal | author=Asai T, Tomita Y, Nakatsuka S, ''et al.'' |title=VCP (p97) regulates NFkappaB signaling pathway, which is important for metastasis of osteosarcoma cell line. |journal=Jpn. J. Cancer Res. |volume=93 |issue= 3 |pages= 296-304 |year= 2002 |pmid= 11927012 |doi= }}
*{{cite journal | author=Kobayashi T, Tanaka K, Inoue K, Kakizuka A |title=Functional ATPase activity of p97/valosin-containing protein (VCP) is required for the quality control of endoplasmic reticulum in neuronally differentiated mammalian PC12 cells. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47358-65 |year= 2003 |pmid= 12351637 |doi= 10.1074/jbc.M207783200 }}
*{{cite journal | author=Uchiyama K, Jokitalo E, Kano F, ''et al.'' |title=VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo. |journal=J. Cell Biol. |volume=159 |issue= 5 |pages= 855-66 |year= 2003 |pmid= 12473691 |doi= 10.1083/jcb.200208112 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
end log.
