Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 03:27, 13 November 2007 (UTC)
[edit]Proteins without matches (11)
[edit]Proteins with a High Potential Match (9)
[edit]Redirected Proteins (5)
[edit]Manual Inspection (Page not found) (20)
[edit]Updated with Warning (1)
[edit]
Protein Status Grid - Date: 03:27, 13 November 2007 (UTC)
[edit]Vebose Log - Date: 03:27, 13 November 2007 (UTC)
[edit]- INFO: Beginning work on ANGPT2... {November 12, 2007 6:58:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:00:49 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_ANGPT2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1z3s.
| PDB = {{PDB2|1z3s}}, {{PDB2|1z3u}}, {{PDB2|2gy7}}
| Name = Angiopoietin 2
| HGNCid = 485
| Symbol = ANGPT2
| AltSymbols =; AGPT2; ANG2
| OMIM = 601922
| ECnumber =
| Homologene = 22401
| MGIid = 1202890
| GeneAtlas_image1 = PBB_GE_ANGPT2_211148_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ANGPT2_205572_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0016525 |text = negative regulation of angiogenesis}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 285
| Hs_Ensembl = ENSG00000091879
| Hs_RefseqProtein = NP_001138
| Hs_RefseqmRNA = NM_001147
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 6344580
| Hs_GenLoc_end = 6408338
| Hs_Uniprot = O15123
| Mm_EntrezGene = 11601
| Mm_Ensembl = ENSMUSG00000031465
| Mm_RefseqmRNA = NM_007426
| Mm_RefseqProtein = NP_031452
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 18691314
| Mm_GenLoc_end = 18741528
| Mm_Uniprot = O35608
}}
}}
'''Angiopoietin 2''', also known as '''ANGPT2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Naturally occurring antagonist for both ANGPT1 and TIE2; expressed only at the sites of vascular remodeling; similar to angiopoietin-1<ref>{{cite web | title = Entrez Gene: ANGPT2 angiopoietin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=285| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{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=Maisonpierre PC, Suri C, Jones PF, ''et al.'' |title=Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis. |journal=Science |volume=277 |issue= 5322 |pages= 55-60 |year= 1997 |pmid= 9204896 |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=Cheung AH, Stewart RJ, Marsden PA |title=Endothelial Tie2/Tek ligands angiopoietin-1 (ANGPT1) and angiopoietin-2 (ANGPT2): regional localization of the human genes to 8q22.3-q23 and 8p23. |journal=Genomics |volume=48 |issue= 3 |pages= 389-91 |year= 1998 |pmid= 9545648 |doi= 10.1006/geno.1997.5207 }}
*{{cite journal | author=Sato A, Iwama A, Takakura N, ''et al.'' |title=Characterization of TEK receptor tyrosine kinase and its ligands, Angiopoietins, in human hematopoietic progenitor cells. |journal=Int. Immunol. |volume=10 |issue= 8 |pages= 1217-27 |year= 1998 |pmid= 9723709 |doi= }}
*{{cite journal | author=Tanaka S, Mori M, Sakamoto Y, ''et al.'' |title=Biologic significance of angiopoietin-2 expression in human hepatocellular carcinoma. |journal=J. Clin. Invest. |volume=103 |issue= 3 |pages= 341-5 |year= 1999 |pmid= 9927494 |doi= }}
*{{cite journal | author=Valenzuela DM, Griffiths JA, Rojas J, ''et al.'' |title=Angiopoietins 3 and 4: diverging gene counterparts in mice and humans. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 5 |pages= 1904-9 |year= 1999 |pmid= 10051567 |doi= }}
*{{cite journal | author=Grosios K, Leek JP, Markham AF, ''et al.'' |title=Assignment of ANGPT4, ANGPT1, and ANGPT2 encoding angiopoietins 4, 1 and 2 to human chromosome bands 20p13, 8q22.3-->q23 and 8p23.1, respectively, by in situ hybridization and radiation hybrid mapping. |journal=Cytogenet. Cell Genet. |volume=84 |issue= 1-2 |pages= 118-20 |year= 1999 |pmid= 10343124 |doi= }}
*{{cite journal | author=Procopio WN, Pelavin PI, Lee WM, Yeilding NM |title=Angiopoietin-1 and -2 coiled coil domains mediate distinct homo-oligomerization patterns, but fibrinogen-like domains mediate ligand activity. |journal=J. Biol. Chem. |volume=274 |issue= 42 |pages= 30196-201 |year= 1999 |pmid= 10514510 |doi= }}
*{{cite journal | author=Kim I, Kim JH, Ryu YS, ''et al.'' |title=Characterization and expression of a novel alternatively spliced human angiopoietin-2. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18550-6 |year= 2000 |pmid= 10766762 |doi= 10.1074/jbc.M910084199 }}
*{{cite journal | author=Mezquita J, Mezquita P, Montserrat P, ''et al.'' |title=Genomic structure and alternative splicing of chicken angiopoietin-2. |journal=Biochem. Biophys. Res. Commun. |volume=275 |issue= 2 |pages= 643-51 |year= 2000 |pmid= 10964717 |doi= 10.1006/bbrc.2000.3345 }}
*{{cite journal | author=Xu Y, Yu Q |title=Angiopoietin-1, unlike angiopoietin-2, is incorporated into the extracellular matrix via its linker peptide region. |journal=J. Biol. Chem. |volume=276 |issue= 37 |pages= 34990-8 |year= 2001 |pmid= 11447223 |doi= 10.1074/jbc.M103661200 }}
*{{cite journal | author=Acker T, Beck H, Plate KH |title=Cell type specific expression of vascular endothelial growth factor and angiopoietin-1 and -2 suggests an important role of astrocytes in cerebellar vascularization. |journal=Mech. Dev. |volume=108 |issue= 1-2 |pages= 45-57 |year= 2002 |pmid= 11578860 |doi= }}
*{{cite journal | author=Ward EG, Grosios K, Markham AF, Jones PF |title=Genomic structures of the human angiopoietins show polymorphism in angiopoietin-2. |journal=Cytogenet. Cell Genet. |volume=94 |issue= 3-4 |pages= 147-54 |year= 2002 |pmid= 11856872 |doi= }}
*{{cite journal | author=Huang YQ, Li JJ, Hu L, ''et al.'' |title=Thrombin induces increased expression and secretion of angiopoietin-2 from human umbilical vein endothelial cells. |journal=Blood |volume=99 |issue= 5 |pages= 1646-50 |year= 2002 |pmid= 11861279 |doi= }}
*{{cite journal | author=Hata K, Udagawa J, Fujiwaki R, ''et al.'' |title=Expression of angiopoietin-1, angiopoietin-2, and Tie2 genes in normal ovary with corpus luteum and in ovarian cancer. |journal=Oncology |volume=62 |issue= 4 |pages= 340-8 |year= 2002 |pmid= 12138242 |doi= }}
*{{cite journal | author=Lin S, Shyu KG, Lee CC, ''et al.'' |title=Hyperbaric oxygen selectively induces angiopoietin-2 in human umbilical vein endothelial cells. |journal=Biochem. Biophys. Res. Commun. |volume=296 |issue= 3 |pages= 710-5 |year= 2002 |pmid= 12176040 |doi= }}
*{{cite journal | author=Geva E, Ginzinger DG, Zaloudek CJ, ''et al.'' |title=Human placental vascular development: vasculogenic and angiogenic (branching and nonbranching) transformation is regulated by vascular endothelial growth factor-A, angiopoietin-1, and angiopoietin-2. |journal=J. Clin. Endocrinol. Metab. |volume=87 |issue= 9 |pages= 4213-24 |year= 2002 |pmid= 12213874 |doi= }}
*{{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 }}
*{{cite journal | author=Paradis V, Bièche I, Dargère D, ''et al.'' |title=A quantitative gene expression study suggests a role for angiopoietins in focal nodular hyperplasia. |journal=Gastroenterology |volume=124 |issue= 3 |pages= 651-9 |year= 2003 |pmid= 12612904 |doi= 10.1053/gast.2003.50104 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on APOH... {November 12, 2007 7:00:49 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:01:21 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 = PBB_Protein_APOH_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c1z.
| PDB = {{PDB2|1c1z}}, {{PDB2|1g4f}}, {{PDB2|1g4g}}, {{PDB2|1qub}}
| Name = Apolipoprotein H (beta-2-glycoprotein I)
| HGNCid = 616
| Symbol = APOH
| AltSymbols =; B2G1; BG
| OMIM = 138700
| ECnumber =
| Homologene = 26
| MGIid = 88058
| GeneAtlas_image1 = PBB_GE_APOH_205216_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005319 |text = lipid transporter activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006952 |text = defense response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 350
| Hs_Ensembl = ENSG00000091583
| Hs_RefseqProtein = NP_000033
| Hs_RefseqmRNA = NM_000042
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 61638577
| Hs_GenLoc_end = 61655974
| Hs_Uniprot = P02749
| Mm_EntrezGene = 11818
| Mm_Ensembl = ENSMUSG00000000049
| Mm_RefseqmRNA = NM_013475
| Mm_RefseqProtein = NP_038503
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 108211381
| Mm_GenLoc_end = 108230485
| Mm_Uniprot = Q6LAL7
}}
}}
'''Apolipoprotein H (beta-2-glycoprotein I)''', also known as '''APOH''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Apolipoprotein H has been implicated in a variety of physiologic pathways including lipoprotein metabolism, coagulation, and the production of antiphospholipid autoantibodies. APOH may be a required cofactor for anionic phospholipid binding by the antiphospholipid autoantibodies found in sera of many patients with lupus and primary antiphospholipid syndrome, but it does not seem to be required for the reactivity of antiphospholipid autoantibodies associated with infections.<ref>{{cite web | title = Entrez Gene: APOH apolipoprotein H (beta-2-glycoprotein I)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=350| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Miyakis S, Giannakopoulos B, Krilis SA |title=Beta 2 glycoprotein I--function in health and disease. |journal=Thromb. Res. |volume=114 |issue= 5-6 |pages= 335-46 |year= 2005 |pmid= 15507263 |doi= 10.1016/j.thromres.2004.07.017 }}
*{{cite journal | author=Kuwana M |title=Beta2-glycoprotein I: antiphospholipid syndrome and T-cell reactivity. |journal=Thromb. Res. |volume=114 |issue= 5-6 |pages= 347-55 |year= 2005 |pmid= 15507264 |doi= 10.1016/j.thromres.2004.06.029 }}
*{{cite journal | author=Day JR, O'Hara PJ, Grant FJ, ''et al.'' |title=Molecular cloning and sequence analysis of the cDNA encoding human apolipoprotein H (beta 2-glycoprotein I). |journal=Int. J. Clin. Lab. Res. |volume=21 |issue= 3 |pages= 256-63 |year= 1992 |pmid= 1339416 |doi= }}
*{{cite journal | author=Steinkasserer A, Barlow PN, Willis AC, ''et al.'' |title=Activity, disulphide mapping and structural modelling of the fifth domain of human beta 2-glycoprotein I. |journal=FEBS Lett. |volume=313 |issue= 2 |pages= 193-7 |year= 1992 |pmid= 1426288 |doi= }}
*{{cite journal | author=Steinkasserer A, Cockburn DJ, Black DM, ''et al.'' |title=Assignment of apolipoprotein H (APOH: beta-2-glycoprotein I) to human chromosome 17q23----qter; determination of the major expression site. |journal=Cytogenet. Cell Genet. |volume=60 |issue= 1 |pages= 31-3 |year= 1992 |pmid= 1582254 |doi= }}
*{{cite journal | author=Matsuura E, Igarashi Y, Fujimoto M, ''et al.'' |title=Heterogeneity of anticardiolipin antibodies defined by the anticardiolipin cofactor. |journal=J. Immunol. |volume=148 |issue= 12 |pages= 3885-91 |year= 1992 |pmid= 1602135 |doi= }}
*{{cite journal | author=Steinkasserer A, Estaller C, Weiss EH, ''et al.'' |title=Complete nucleotide and deduced amino acid sequence of human beta 2-glycoprotein I. |journal=Biochem. J. |volume=277 ( Pt 2) |issue= |pages= 387-91 |year= 1991 |pmid= 1650181 |doi= }}
*{{cite journal | author=Kristensen T, Schousboe I, Boel E, ''et al.'' |title=Molecular cloning and mammalian expression of human beta 2-glycoprotein I cDNA. |journal=FEBS Lett. |volume=289 |issue= 2 |pages= 183-6 |year= 1991 |pmid= 1655523 |doi= }}
*{{cite journal | author=Mehdi H, Nunn M, Steel DM, ''et al.'' |title=Nucleotide sequence and expression of the human gene encoding apolipoprotein H (beta 2-glycoprotein I). |journal=Gene |volume=108 |issue= 2 |pages= 293-8 |year= 1992 |pmid= 1748314 |doi= }}
*{{cite journal | author=Matsuura E, Igarashi M, Igarashi Y, ''et al.'' |title=Molecular definition of human beta 2-glycoprotein I (beta 2-GPI) by cDNA cloning and inter-species differences of beta 2-GPI in alternation of anticardiolipin binding. |journal=Int. Immunol. |volume=3 |issue= 12 |pages= 1217-21 |year= 1992 |pmid= 1777418 |doi= }}
*{{cite journal | author=McNeil HP, Simpson RJ, Chesterman CN, Krilis SA |title=Anti-phospholipid antibodies are directed against a complex antigen that includes a lipid-binding inhibitor of coagulation: beta 2-glycoprotein I (apolipoprotein H). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 11 |pages= 4120-4 |year= 1990 |pmid= 2349221 |doi= }}
*{{cite journal | author=Henry ML, Everson B, Ratnoff OD |title=Inhibition of the activation of Hageman factor (factor XII) by beta 2-glycoprotein I. |journal=J. Lab. Clin. Med. |volume=111 |issue= 5 |pages= 519-23 |year= 1988 |pmid= 3361230 |doi= }}
*{{cite journal | author=Lee NS, Brewer HB, Osborne JC |title=beta 2-Glycoprotein I. Molecular properties of an unusual apolipoprotein, apolipoprotein H. |journal=J. Biol. Chem. |volume=258 |issue= 8 |pages= 4765-70 |year= 1983 |pmid= 6403535 |doi= }}
*{{cite journal | author=Lozier J, Takahashi N, Putnam FW |title=Complete amino acid sequence of human plasma beta 2-glycoprotein I. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 12 |pages= 3640-4 |year= 1984 |pmid= 6587378 |doi= }}
*{{cite journal | author=Steinkasserer A, Dörner C, Würzner R, Sim RB |title=Human beta 2-glycoprotein I: molecular analysis of DNA and amino acid polymorphism. |journal=Hum. Genet. |volume=91 |issue= 4 |pages= 401-2 |year= 1993 |pmid= 8099061 |doi= }}
*{{cite journal | author=Mehdi H, Kaplan MJ, Anlar FY, ''et al.'' |title=Hepatitis B virus surface antigen binds to apolipoprotein H. |journal=J. Virol. |volume=68 |issue= 4 |pages= 2415-24 |year= 1994 |pmid= 8139027 |doi= }}
*{{cite journal | author=Hunt JE, Simpson RJ, Krilis SA |title=Identification of a region of beta 2-glycoprotein I critical for lipid binding and anti-cardiolipin antibody cofactor activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 6 |pages= 2141-5 |year= 1993 |pmid= 8460120 |doi= }}
*{{cite journal | author=Stefas E, Rucheton M, Graafland H, ''et al.'' |title=Human plasmatic apolipoprotein H binds human immunodeficiency virus type 1 and type 2 proteins. |journal=AIDS Res. Hum. Retroviruses |volume=13 |issue= 1 |pages= 97-104 |year= 1997 |pmid= 8989432 |doi= }}
*{{cite journal | author=Sanghera DK, Wagenknecht DR, McIntyre JA, Kamboh MI |title=Identification of structural mutations in the fifth domain of apolipoprotein H (beta 2-glycoprotein I) which affect phospholipid binding. |journal=Hum. Mol. Genet. |volume=6 |issue= 2 |pages= 311-6 |year= 1997 |pmid= 9063752 |doi= }}
*{{cite journal | author=Gambino R, Ruiu G, Pagano G, Cassader M |title=Qualitative analysis of the carbohydrate composition of apolipoprotein H. |journal=J. Protein Chem. |volume=16 |issue= 3 |pages= 205-12 |year= 1997 |pmid= 9155091 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BAD... {November 12, 2007 7:01:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:02:03 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 = BCL2-antagonist of cell death
| HGNCid = 936
| Symbol = BAD
| AltSymbols =; BBC2; BCL2L8
| OMIM = 603167
| ECnumber =
| Homologene = 3189
| MGIid = 1096330
| GeneAtlas_image1 = PBB_GE_BAD_1861_at_tn.png
| GeneAtlas_image2 = PBB_GE_BAD_209364_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005741 |text = mitochondrial outer membrane}}
| Process = {{GNF_GO|id=GO:0006007 |text = glucose catabolic process}} {{GNF_GO|id=GO:0008624 |text = induction of apoptosis by extracellular signals}} {{GNF_GO|id=GO:0008632 |text = apoptotic program}} {{GNF_GO|id=GO:0042593 |text = glucose homeostasis}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0045579 |text = positive regulation of B cell differentiation}} {{GNF_GO|id=GO:0045582 |text = positive regulation of T cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 572
| Hs_Ensembl = ENSG00000002330
| Hs_RefseqProtein = NP_004313
| Hs_RefseqmRNA = NM_004322
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 63793878
| Hs_GenLoc_end = 63808740
| Hs_Uniprot = Q92934
| Mm_EntrezGene = 12015
| Mm_Ensembl = ENSMUSG00000024959
| Mm_RefseqmRNA = NM_007522
| Mm_RefseqProtein = NP_031548
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 7008905
| Mm_GenLoc_end = 7018937
| Mm_Uniprot = Q3TFU7
}}
}}
'''BCL2-antagonist of cell death''', also known as '''BAD''', is a human [[gene]].
<!-- 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 BCL-2 family. BCL-2 family members are known to be regulators of programmed cell death. This protein positively regulates cell apoptosis by forming heterodimers with BCL-xL and BCL-2, and reversing their death repressor activity. Proapoptotic activity of this protein is regulated through its phosphorylation. Protein kinases AKT and MAP kinase, as well as protein phosphatase calcineurin were found to be involved in the regulation of this protein. Alternative splicing of this gene results in two transcript variants which encode the same isoform.<ref>{{cite web | title = Entrez Gene: BAD BCL2-antagonist of cell death| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=572| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tolstrup M, Ostergaard L, Laursen AL, ''et al.'' |title=HIV/SIV escape from immune surveillance: focus on Nef. |journal=Curr. HIV Res. |volume=2 |issue= 2 |pages= 141-51 |year= 2004 |pmid= 15078178 |doi= }}
*{{cite journal | author=Jiang P, Du W, Wu M |title=p53 and Bad: remote strangers become close friends. |journal=Cell Res. |volume=17 |issue= 4 |pages= 283-5 |year= 2007 |pmid= 17404594 |doi= 10.1038/cr.2007.19 }}
*{{cite journal | author=Yang E, Zha J, Jockel J, ''et al.'' |title=Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. |journal=Cell |volume=80 |issue= 2 |pages= 285-91 |year= 1995 |pmid= 7834748 |doi= }}
*{{cite journal | author=Zha J, Harada H, Yang E, ''et al.'' |title=Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L) |journal=Cell |volume=87 |issue= 4 |pages= 619-28 |year= 1997 |pmid= 8929531 |doi= }}
*{{cite journal | author=Wang HG, Rapp UR, Reed JC |title=Bcl-2 targets the protein kinase Raf-1 to mitochondria. |journal=Cell |volume=87 |issue= 4 |pages= 629-38 |year= 1997 |pmid= 8929532 |doi= }}
*{{cite journal | author=Inohara N, Ding L, Chen S, Núñez G |title=harakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins Bcl-2 and Bcl-X(L). |journal=EMBO J. |volume=16 |issue= 7 |pages= 1686-94 |year= 1997 |pmid= 9130713 |doi= 10.1093/emboj/16.7.1686 }}
*{{cite journal | author=Zha J, Harada H, Osipov K, ''et al.'' |title=BH3 domain of BAD is required for heterodimerization with BCL-XL and pro-apoptotic activity. |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24101-4 |year= 1997 |pmid= 9305851 |doi= }}
*{{cite journal | author=Hsu SY, Kaipia A, Zhu L, Hsueh AJ |title=Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11. |journal=Mol. Endocrinol. |volume=11 |issue= 12 |pages= 1858-67 |year= 1997 |pmid= 9369453 |doi= }}
*{{cite journal | author=del Peso L, González-García M, Page C, ''et al.'' |title=Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. |journal=Science |volume=278 |issue= 5338 |pages= 687-9 |year= 1997 |pmid= 9381178 |doi= }}
*{{cite journal | author=Ottilie S, Diaz JL, Horne W, ''et al.'' |title=Dimerization properties of human BAD. Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteins. |journal=J. Biol. Chem. |volume=272 |issue= 49 |pages= 30866-72 |year= 1998 |pmid= 9388232 |doi= }}
*{{cite journal | author=Huang DC, Adams JM, Cory S |title=The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4. |journal=EMBO J. |volume=17 |issue= 4 |pages= 1029-39 |year= 1998 |pmid= 9463381 |doi= 10.1093/emboj/17.4.1029 }}
*{{cite journal | author=Blume-Jensen P, Janknecht R, Hunter T |title=The kit receptor promotes cell survival via activation of PI 3-kinase and subsequent Akt-mediated phosphorylation of Bad on Ser136. |journal=Curr. Biol. |volume=8 |issue= 13 |pages= 779-82 |year= 1998 |pmid= 9651683 |doi= }}
*{{cite journal | author=Strobel T, Tai YT, Korsmeyer S, Cannistra SA |title=BAD partly reverses paclitaxel resistance in human ovarian cancer cells. |journal=Oncogene |volume=17 |issue= 19 |pages= 2419-27 |year= 1998 |pmid= 9824152 |doi= 10.1038/sj.onc.1202180 }}
*{{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=Yasuda M, Han JW, Dionne CA, ''et al.'' |title=BNIP3alpha: a human homolog of mitochondrial proapoptotic protein BNIP3. |journal=Cancer Res. |volume=59 |issue= 3 |pages= 533-7 |year= 1999 |pmid= 9973195 |doi= }}
*{{cite journal | author=Wang HG, Pathan N, Ethell IM, ''et al.'' |title=Ca2+-induced apoptosis through calcineurin dephosphorylation of BAD. |journal=Science |volume=284 |issue= 5412 |pages= 339-43 |year= 1999 |pmid= 10195903 |doi= }}
*{{cite journal | author=Holmgreen SP, Huang DC, Adams JM, Cory S |title=Survival activity of Bcl-2 homologs Bcl-w and A1 only partially correlates with their ability to bind pro-apoptotic family members. |journal=Cell Death Differ. |volume=6 |issue= 6 |pages= 525-32 |year= 1999 |pmid= 10381646 |doi= 10.1038/sj.cdd.4400519 }}
*{{cite journal | author=Ostrerova N, Petrucelli L, Farrer M, ''et al.'' |title=alpha-Synuclein shares physical and functional homology with 14-3-3 proteins. |journal=J. Neurosci. |volume=19 |issue= 14 |pages= 5782-91 |year= 1999 |pmid= 10407019 |doi= }}
*{{cite journal | author=Scheid MP, Schubert KM, Duronio V |title=Regulation of bad phosphorylation and association with Bcl-x(L) by the MAPK/Erk kinase. |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 31108-13 |year= 1999 |pmid= 10521512 |doi= }}
*{{cite journal | author=Bonni A, Brunet A, West AE, ''et al.'' |title=Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms. |journal=Science |volume=286 |issue= 5443 |pages= 1358-62 |year= 1999 |pmid= 10558990 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CA2... {November 12, 2007 7:02:03 PM PST}
- SEARCH REDIRECT: Control Box Found: Carbonic anhydrase II {November 12, 2007 7:02:39 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 12, 2007 7:02:40 PM PST}
- SKIP SUMMARY: SKIPPING Summary, No Errors. {November 12, 2007 7:02:40 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 12, 2007 7:02:40 PM PST}
- UPDATED: Warning while updating page: Could not find summary box. {November 12, 2007 7:02:49 PM PST}
- UPDATED: Updated protein page (with warnings): Carbonic anhydrase II {November 12, 2007 7:02:49 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_CA2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 12ca.
| PDB = {{PDB2|12ca}}, {{PDB2|1a42}}, {{PDB2|1am6}}, {{PDB2|1avn}}, {{PDB2|1bcd}}, {{PDB2|1bic}}, {{PDB2|1bn1}}, {{PDB2|1bn3}}, {{PDB2|1bn4}}, {{PDB2|1bnm}}, {{PDB2|1bnn}}, {{PDB2|1bnq}}, {{PDB2|1bnt}}, {{PDB2|1bnu}}, {{PDB2|1bnv}}, {{PDB2|1bnw}}, {{PDB2|1bv3}}, {{PDB2|1ca2}}, {{PDB2|1ca3}}, {{PDB2|1cah}}, {{PDB2|1cai}}, {{PDB2|1caj}}, {{PDB2|1cak}}, {{PDB2|1cal}}, {{PDB2|1cam}}, {{PDB2|1can}}, {{PDB2|1cao}}, {{PDB2|1cay}}, {{PDB2|1caz}}, {{PDB2|1ccs}}, {{PDB2|1cct}}, {{PDB2|1ccu}}, {{PDB2|1cil}}, {{PDB2|1cim}}, {{PDB2|1cin}}, {{PDB2|1cnb}}, {{PDB2|1cnc}}, {{PDB2|1cng}}, {{PDB2|1cnh}}, {{PDB2|1cni}}, {{PDB2|1cnj}}, {{PDB2|1cnk}}, {{PDB2|1cnw}}, {{PDB2|1cnx}}, {{PDB2|1cny}}, {{PDB2|1cra}}, {{PDB2|1cva}}, {{PDB2|1cvb}}, {{PDB2|1cvc}}, {{PDB2|1cvd}}, {{PDB2|1cve}}, {{PDB2|1cvf}}, {{PDB2|1cvh}}, {{PDB2|1dca}}, {{PDB2|1dcb}}, {{PDB2|1eou}}, {{PDB2|1f2w}}, {{PDB2|1fql}}, {{PDB2|1fqm}}, {{PDB2|1fqn}}, {{PDB2|1fqr}}, {{PDB2|1fr4}}, {{PDB2|1fr7}}, {{PDB2|1fsn}}, {{PDB2|1fsq}}, {{PDB2|1fsr}}, {{PDB2|1g0e}}, {{PDB2|1g0f}}, {{PDB2|1g1d}}, {{PDB2|1g3z}}, {{PDB2|1g45}}, {{PDB2|1g46}}, {{PDB2|1g48}}, {{PDB2|1g4j}}, {{PDB2|1g4o}}, {{PDB2|1g52}}, {{PDB2|1g53}}, {{PDB2|1g54}}, {{PDB2|1g6v}}, {{PDB2|1h4n}}, {{PDB2|1h9n}}, {{PDB2|1h9q}}, {{PDB2|1hca}}, {{PDB2|1hea}}, {{PDB2|1heb}}, {{PDB2|1hec}}, {{PDB2|1hed}}, {{PDB2|1hva}}, {{PDB2|1i8z}}, {{PDB2|1i90}}, {{PDB2|1i91}}, {{PDB2|1i9l}}, {{PDB2|1i9m}}, {{PDB2|1i9n}}, {{PDB2|1i9o}}, {{PDB2|1i9p}}, {{PDB2|1i9q}}, {{PDB2|1if4}}, {{PDB2|1if5}}, {{PDB2|1if6}}, {{PDB2|1if7}}, {{PDB2|1if8}}, {{PDB2|1if9}}, {{PDB2|1kwq}}, {{PDB2|1kwr}}, {{PDB2|1lg5}}, {{PDB2|1lg6}}, {{PDB2|1lgd}}, {{PDB2|1lug}}, {{PDB2|1lzv}}, {{PDB2|1moo}}, {{PDB2|1mua}}, {{PDB2|1okl}}, {{PDB2|1okm}}, {{PDB2|1okn}}, {{PDB2|1oq5}}, {{PDB2|1ray}}, {{PDB2|1raz}}, {{PDB2|1rza}}, {{PDB2|1rzb}}, {{PDB2|1rzc}}, {{PDB2|1rzd}}, {{PDB2|1rze}}, {{PDB2|1t9n}}, {{PDB2|1tb0}}, {{PDB2|1tbt}}, {{PDB2|1te3}}, {{PDB2|1teq}}, {{PDB2|1teu}}, {{PDB2|1tg3}}, {{PDB2|1tg9}}, {{PDB2|1th9}}, {{PDB2|1thk}}, {{PDB2|1ttm}}, {{PDB2|1uga}}, {{PDB2|1ugb}}, {{PDB2|1ugc}}, {{PDB2|1ugd}}, {{PDB2|1uge}}, {{PDB2|1ugf}}, {{PDB2|1ugg}}, {{PDB2|1xeg}}, {{PDB2|1xev}}, {{PDB2|1xpz}}, {{PDB2|1xq0}}, {{PDB2|1yda}}, {{PDB2|1ydb}}, {{PDB2|1ydc}}, {{PDB2|1ydd}}, {{PDB2|1yo0}}, {{PDB2|1yo1}}, {{PDB2|1yo2}}, {{PDB2|1z9y}}, {{PDB2|1ze8}}, {{PDB2|1zfk}}, {{PDB2|1zfq}}, {{PDB2|1zge}}, {{PDB2|1zgf}}, {{PDB2|1zh9}}, {{PDB2|1zsa}}, {{PDB2|1zsb}}, {{PDB2|1zsc}}, {{PDB2|2abe}}, {{PDB2|2aw1}}, {{PDB2|2ax2}}, {{PDB2|2ca2}}, {{PDB2|2cba}}, {{PDB2|2cbb}}, {{PDB2|2cbc}}, {{PDB2|2cbd}}, {{PDB2|2cbe}}, {{PDB2|2eu2}}, {{PDB2|2eu3}}, {{PDB2|2ez7}}, {{PDB2|2f14}}, {{PDB2|2fmg}}, {{PDB2|2fmz}}, {{PDB2|2fnk}}, {{PDB2|2fnm}}, {{PDB2|2fnn}}, {{PDB2|2foq}}, {{PDB2|2fos}}, {{PDB2|2fou}}, {{PDB2|2fov}}, {{PDB2|2gd8}}, {{PDB2|2geh}}, {{PDB2|2h15}}, {{PDB2|2h4n}}, {{PDB2|2hd6}}, {{PDB2|2hkk}}, {{PDB2|2hl4}}, {{PDB2|2hnc}}, {{PDB2|2hoc}}, {{PDB2|2ili}}, {{PDB2|2nng}}, {{PDB2|2nno}}, {{PDB2|2nns}}, {{PDB2|2nnv}}, {{PDB2|2nwo}}, {{PDB2|2nwp}}, {{PDB2|2nwy}}, {{PDB2|2nwz}}, {{PDB2|2nxr}}, {{PDB2|2nxs}}, {{PDB2|2nxt}}, {{PDB2|2o4z}}, {{PDB2|3ca2}}, {{PDB2|4ca2}}, {{PDB2|4cac}}, {{PDB2|5ca2}}, {{PDB2|5cac}}, {{PDB2|6ca2}}, {{PDB2|7ca2}}, {{PDB2|8ca2}}, {{PDB2|9ca2}}
| Name = Carbonic anhydrase II
| HGNCid = 1373
| Symbol = CA2
| AltSymbols =; CA II; CA-II; CAII; Car2
| OMIM = 259730
| ECnumber =
| Homologene = 37256
| MGIid = 88269
| GeneAtlas_image1 = PBB_GE_CA2_209301_at_tn.png
| Function = {{GNF_GO|id=GO:0004089 |text = carbonate dehydratase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0002009 |text = morphogenesis of an epithelium}} {{GNF_GO|id=GO:0006730 |text = one-carbon compound metabolic process}} {{GNF_GO|id=GO:0015670 |text = carbon dioxide transport}} {{GNF_GO|id=GO:0046903 |text = secretion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 760
| Hs_Ensembl = ENSG00000104267
| Hs_RefseqProtein = NP_000058
| Hs_RefseqmRNA = NM_000067
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 86563433
| Hs_GenLoc_end = 86580945
| Hs_Uniprot = P00918
| Mm_EntrezGene = 12349
| Mm_Ensembl = ENSMUSG00000027562
| Mm_RefseqmRNA = NM_009801
| Mm_RefseqProtein = NP_033931
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 14863450
| Mm_GenLoc_end = 14877513
| Mm_Uniprot = Q6LDQ7
}}
}}
'''Carbonic anhydrase II''', also known as '''CA2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = CA2 is one of several (at least 7) isozymes of carbonic anhydrase. Carbonic anhydrase catalyzes reversible hydration of carbon dioxide. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis.<ref>{{cite web | title = Entrez Gene: CA2 carbonic anhydrase II| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=760| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sly WS, Hu PY |title=Human carbonic anhydrases and carbonic anhydrase deficiencies. |journal=Annu. Rev. Biochem. |volume=64 |issue= |pages= 375-401 |year= 1995 |pmid= 7574487 |doi= 10.1146/annurev.bi.64.070195.002111 }}
*{{cite journal | author=Kumpulainen T |title=Immunohistochemical localization of human carbonic anhydrase isoenzyme C. |journal=Histochemistry |volume=62 |issue= 3 |pages= 271-80 |year= 1979 |pmid= 114507 |doi= }}
*{{cite journal | author=Henderson LE, Henriksson D, Nyman PO |title=Primary structure of human carbonic anhydrase C. |journal=J. Biol. Chem. |volume=251 |issue= 18 |pages= 5457-63 |year= 1976 |pmid= 823150 |doi= }}
*{{cite journal | author=Hu PY, Roth DE, Skaggs LA, ''et al.'' |title=A splice junction mutation in intron 2 of the carbonic anhydrase II gene of osteopetrosis patients from Arabic countries. |journal=Hum. Mutat. |volume=1 |issue= 4 |pages= 288-92 |year= 1993 |pmid= 1301935 |doi= 10.1002/humu.1380010404 }}
*{{cite journal | author=Roth DE, Venta PJ, Tashian RE, Sly WS |title=Molecular basis of human carbonic anhydrase II deficiency. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 5 |pages= 1804-8 |year= 1992 |pmid= 1542674 |doi= }}
*{{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=Schwartz GJ, Brion LP, Corey HE, Dorfman HD |title=Case report 668. Carbonic anhydrase II deficiency syndrome (osteopetrosis associated with renal tubular acidosis and cerebral calcification). |journal=Skeletal Radiol. |volume=20 |issue= 6 |pages= 447-52 |year= 1991 |pmid= 1925679 |doi= }}
*{{cite journal | author=Venta PJ, Welty RJ, Johnson TM, ''et al.'' |title=Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His----Tyr): complete structure of the normal human CA II gene. |journal=Am. J. Hum. Genet. |volume=49 |issue= 5 |pages= 1082-90 |year= 1991 |pmid= 1928091 |doi= }}
*{{cite journal | author=Venta PJ, Tashian RE |title=PCR detection of the TAQ1 polymorphism at the CA2 locus. |journal=Nucleic Acids Res. |volume=18 |issue= 18 |pages= 5585 |year= 1990 |pmid= 1977133 |doi= }}
*{{cite journal | author=Sato S, Zhu XL, Sly WS |title=Carbonic anhydrase isozymes IV and II in urinary membranes from carbonic anhydrase II-deficient patients. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 16 |pages= 6073-6 |year= 1990 |pmid= 2117271 |doi= }}
*{{cite journal | author=Kaunisto K, Parkkila S, Tammela T, ''et al.'' |title=Immunohistochemical localization of carbonic anhydrase isoenzymes in the human male reproductive tract. |journal=Histochemistry |volume=94 |issue= 4 |pages= 381-6 |year= 1990 |pmid= 2121671 |doi= }}
*{{cite journal | author=Backman U, Danielsson B, Wistrand PJ |title=The excretion of carbonic anhydrase isozymes CA I and CA II in the urine of apparently healthy subjects and in patients with kidney disease. |journal=Scand. J. Clin. Lab. Invest. |volume=50 |issue= 6 |pages= 627-33 |year= 1991 |pmid= 2123360 |doi= }}
*{{cite journal | author=Forsman C, Behravan G, Osterman A, Jonsson BH |title=Production of active human carbonic anhydrase II in E. coli. |journal=Acta Chem. Scand., B, Org. Chem. Biochem. |volume=42 |issue= 5 |pages= 314-8 |year= 1989 |pmid= 2850697 |doi= }}
*{{cite journal | author=Venta PJ, Montgomery JC, Hewett-Emmett D, Tashian RE |title=Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements. |journal=Biochim. Biophys. Acta |volume=826 |issue= 4 |pages= 195-201 |year= 1986 |pmid= 3000449 |doi= }}
*{{cite journal | author=Ohlsson A, Cumming WA, Paul A, Sly WS |title=Carbonic anhydrase II deficiency syndrome: recessive osteopetrosis with renal tubular acidosis and cerebral calcification. |journal=Pediatrics |volume=77 |issue= 3 |pages= 371-81 |year= 1986 |pmid= 3081869 |doi= }}
*{{cite journal | author=Nakai H, Byers MG, Venta PJ, ''et al.'' |title=The gene for human carbonic anhydrase II (CA2) is located at chromosome 8q22. |journal=Cytogenet. Cell Genet. |volume=44 |issue= 4 |pages= 234-5 |year= 1987 |pmid= 3107918 |doi= }}
*{{cite journal | author=Montgomery JC, Venta PJ, Tashian RE, Hewett-Emmett D |title=Nucleotide sequence of human liver carbonic anhydrase II cDNA. |journal=Nucleic Acids Res. |volume=15 |issue= 11 |pages= 4687 |year= 1987 |pmid= 3108857 |doi= }}
*{{cite journal | author=Murakami H, Marelich GP, Grubb JH, ''et al.'' |title=Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II. |journal=Genomics |volume=1 |issue= 2 |pages= 159-66 |year= 1988 |pmid= 3121496 |doi= }}
*{{cite journal | author=Eriksson AE, Jones TA, Liljas A |title=Refined structure of human carbonic anhydrase II at 2.0 A resolution. |journal=Proteins |volume=4 |issue= 4 |pages= 274-82 |year= 1989 |pmid= 3151019 |doi= 10.1002/prot.340040406 }}
*{{cite journal | author=Eriksson AE, Kylsten PM, Jones TA, Liljas A |title=Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN- ion to the zinc at high pH. |journal=Proteins |volume=4 |issue= 4 |pages= 283-93 |year= 1989 |pmid= 3151020 |doi= 10.1002/prot.340040407 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CDC25C... {November 12, 2007 7:02:49 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:03:22 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 = Cell division cycle 25 homolog C (S. pombe)
| HGNCid = 1727
| Symbol = CDC25C
| AltSymbols =; CDC25
| OMIM = 157680
| ECnumber =
| Homologene = 1356
| MGIid = 88350
| GeneAtlas_image1 = PBB_GE_CDC25C_205167_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CDC25C_217010_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000079 |text = regulation of cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0000087 |text = M phase of mitotic cell cycle}} {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007088 |text = regulation of mitosis}} {{GNF_GO|id=GO:0007089 |text = traversing start control point of mitotic cell cycle}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0051301 |text = cell division}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 995
| Hs_Ensembl = ENSG00000158402
| Hs_RefseqProtein = NP_001781
| Hs_RefseqmRNA = NM_001790
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 137649168
| Hs_GenLoc_end = 137701943
| Hs_Uniprot = P30307
| Mm_EntrezGene = 12532
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_009860
| Mm_RefseqProtein = NP_033990
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Cell division cycle 25 homolog C (S. pombe)''', also known as '''CDC25C''', is a human [[gene]].
<!-- 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 highly conserved during evolution and it plays a key role in the regulation of cell division. The encoded protein is a tyrosine phosphatase and belongs to the Cdc25 phosphatase family. It directs dephosphorylation of cyclin B-bound CDC2 and triggers entry into mitosis. It is also thought to suppress p53-induced growth arrest. Multiple alternatively spliced transcript variants of this gene have been described, however, the full-length nature of many of them is not known.<ref>{{cite web | title = Entrez Gene: CDC25C cell division cycle 25 homolog C (S. pombe)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=995| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Draetta G, Eckstein J |title=Cdc25 protein phosphatases in cell proliferation. |journal=Biochim. Biophys. Acta |volume=1332 |issue= 2 |pages= M53-63 |year= 1997 |pmid= 9141461 |doi= }}
*{{cite journal | author=Nilsson I, Hoffmann I |title=Cell cycle regulation by the Cdc25 phosphatase family. |journal=Progress in cell cycle research |volume=4 |issue= |pages= 107-14 |year= 2000 |pmid= 10740819 |doi= }}
*{{cite journal | author=Amini S, Khalili K, Sawaya BE |title=Effect of HIV-1 Vpr on cell cycle regulators. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 249-60 |year= 2004 |pmid= 15142382 |doi= 10.1089/104454904773819833 }}
*{{cite journal | author=Kino T, Chrousos GP |title=Human immunodeficiency virus type-1 accessory protein Vpr: a causative agent of the AIDS-related insulin resistance/lipodystrophy syndrome? |journal=Ann. N. Y. Acad. Sci. |volume=1024 |issue= |pages= 153-67 |year= 2004 |pmid= 15265780 |doi= 10.1196/annals.1321.013 }}
*{{cite journal | author=Andersen JL, Planelles V |title=The role of Vpr in HIV-1 pathogenesis. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 43-51 |year= 2005 |pmid= 15638722 |doi= }}
*{{cite journal | author=Sartor H, Ehlert F, Grzeschik KH, ''et al.'' |title=Assignment of two human cell cycle genes, CDC25C and CCNB1, to 5q31 and 5q12, respectively. |journal=Genomics |volume=13 |issue= 3 |pages= 911-2 |year= 1992 |pmid= 1386342 |doi= }}
*{{cite journal | author=Gould KL, Moreno S, Tonks NK, Nurse P |title=Complementation of the mitotic activator, p80cdc25, by a human protein-tyrosine phosphatase. |journal=Science |volume=250 |issue= 4987 |pages= 1573-6 |year= 1991 |pmid= 1703321 |doi= }}
*{{cite journal | author=Strausfeld U, Labbé JC, Fesquet D, ''et al.'' |title=Dephosphorylation and activation of a p34cdc2/cyclin B complex in vitro by human CDC25 protein. |journal=Nature |volume=351 |issue= 6323 |pages= 242-5 |year= 1991 |pmid= 1828290 |doi= 10.1038/351242a0 }}
*{{cite journal | author=Galaktionov K, Beach D |title=Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins. |journal=Cell |volume=67 |issue= 6 |pages= 1181-94 |year= 1992 |pmid= 1836978 |doi= }}
*{{cite journal | author=Sadhu K, Reed SI, Richardson H, Russell P |title=Human homolog of fission yeast cdc25 mitotic inducer is predominantly expressed in G2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 13 |pages= 5139-43 |year= 1990 |pmid= 2195549 |doi= }}
*{{cite journal | author=Re F, Braaten D, Franke EK, Luban J |title=Human immunodeficiency virus type 1 Vpr arrests the cell cycle in G2 by inhibiting the activation of p34cdc2-cyclin B. |journal=J. Virol. |volume=69 |issue= 11 |pages= 6859-64 |year= 1995 |pmid= 7474100 |doi= }}
*{{cite journal | author=Zwicker J, Gross C, Lucibello FC, ''et al.'' |title=Cell cycle regulation of cdc25C transcription is mediated by the periodic repression of the glutamine-rich activators NF-Y and Sp1. |journal=Nucleic Acids Res. |volume=23 |issue= 19 |pages= 3822-30 |year= 1995 |pmid= 7479023 |doi= }}
*{{cite journal | author=Di Marzio P, Choe S, Ebright M, ''et al.'' |title=Mutational analysis of cell cycle arrest, nuclear localization and virion packaging of human immunodeficiency virus type 1 Vpr. |journal=J. Virol. |volume=69 |issue= 12 |pages= 7909-16 |year= 1996 |pmid= 7494303 |doi= }}
*{{cite journal | author=Strausfeld U, Fernandez A, Capony JP, ''et al.'' |title=Activation of p34cdc2 protein kinase by microinjection of human cdc25C into mammalian cells. Requirement for prior phosphorylation of cdc25C by p34cdc2 on sites phosphorylated at mitosis. |journal=J. Biol. Chem. |volume=269 |issue= 8 |pages= 5989-6000 |year= 1994 |pmid= 8119945 |doi= }}
*{{cite journal | author=Zheng XF, Ruderman JV |title=Functional analysis of the P box, a domain in cyclin B required for the activation of Cdc25. |journal=Cell |volume=75 |issue= 1 |pages= 155-64 |year= 1993 |pmid= 8402895 |doi= }}
*{{cite journal | author=Taviaux SA, Demaille JG |title=Localization of human cell cycle regulatory genes CDC25C to 5q31 and WEE1 to 11p15.3-11p15.1 by fluorescence in situ hybridization. |journal=Genomics |volume=15 |issue= 1 |pages= 194-6 |year= 1993 |pmid= 8432534 |doi= 10.1006/geno.1993.1032 }}
*{{cite journal | author=Honda R, Ohba Y, Nagata A, ''et al.'' |title=Dephosphorylation of human p34cdc2 kinase on both Thr-14 and Tyr-15 by human cdc25B phosphatase. |journal=FEBS Lett. |volume=318 |issue= 3 |pages= 331-4 |year= 1993 |pmid= 8440392 |doi= }}
*{{cite journal | author=Booher RN, Holman PS, Fattaey A |title=Human Myt1 is a cell cycle-regulated kinase that inhibits Cdc2 but not Cdk2 activity. |journal=J. Biol. Chem. |volume=272 |issue= 35 |pages= 22300-6 |year= 1997 |pmid= 9268380 |doi= }}
*{{cite journal | author=Sanchez Y, Wong C, Thoma RS, ''et al.'' |title=Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25. |journal=Science |volume=277 |issue= 5331 |pages= 1497-501 |year= 1997 |pmid= 9278511 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ERBB3... {November 12, 2007 7:03:22 PM PST}
- SEARCH REDIRECT: Control Box Found: ERBB3 {November 12, 2007 7:04:55 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 12, 2007 7:04:57 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 12, 2007 7:04:57 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 12, 2007 7:04:57 PM PST}
- UPDATED: Updated protein page: ERBB3 {November 12, 2007 7:05:04 PM PST}
- INFO: Beginning work on FURIN... {November 12, 2007 7:12:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:13:28 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_FURIN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1p8j.
| PDB = {{PDB2|1p8j}}
| Name = Furin (paired basic amino acid cleaving enzyme)
| HGNCid = 8568
| Symbol = FURIN
| AltSymbols =; FUR; PACE; PCSK3; SPC1
| OMIM = 136950
| ECnumber =
| Homologene = 1930
| MGIid = 97513
| GeneAtlas_image1 = PBB_GE_FURIN_201945_at_tn.png
| Function = {{GNF_GO|id=GO:0004276 |text = furin activity}} {{GNF_GO|id=GO:0004289 |text = subtilase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030140 |text = trans-Golgi network transport vesicle}}
| Process = {{GNF_GO|id=GO:0006465 |text = signal peptide processing}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5045
| Hs_Ensembl = ENSG00000140564
| Hs_RefseqProtein = NP_002560
| Hs_RefseqmRNA = NM_002569
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 15
| Hs_GenLoc_start = 89212889
| Hs_GenLoc_end = 89227691
| Hs_Uniprot = P09958
| Mm_EntrezGene = 18550
| Mm_Ensembl = ENSMUSG00000030530
| Mm_RefseqmRNA = XM_980423
| Mm_RefseqProtein = XP_985517
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 80262709
| Mm_GenLoc_end = 80276275
| Mm_Uniprot = Q6GTN6
}}
}}
'''Furin (paired basic amino acid cleaving enzyme)''', also known as '''FURIN''', is a human [[gene]].
<!-- 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 belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein is a calcium-dependent serine endoprotease that can efficiently cleave precursor proteins at their paired basic amino acid processing sites. Some of its substrates are: proparathyroid hormone, transforming growth factor beta 1 precursor, proalbumin, pro-beta-secretase, membrane type-1 matrix metalloproteinase, beta subunit of pro-nerve growth factor and von Willebrand factor. It is also thought to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 and gp140. This gene is thought to play a role in tumor progression. The use of alternate polyadenylation sites has been found for this gene.<ref>{{cite web | title = Entrez Gene: FURIN furin (paired basic amino acid cleaving enzyme)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5045| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nakayama K |title=Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. |journal=Biochem. J. |volume=327 ( Pt 3) |issue= |pages= 625-35 |year= 1998 |pmid= 9599222 |doi= }}
*{{cite journal | author=Bassi DE, Mahloogi H, Klein-Szanto AJ |title=The proprotein convertases furin and PACE4 play a significant role in tumor progression. |journal=Mol. Carcinog. |volume=28 |issue= 2 |pages= 63-9 |year= 2000 |pmid= 10900462 |doi= }}
*{{cite journal | author=Hallenberger S, Bosch V, Angliker H, ''et al.'' |title=Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. |journal=Nature |volume=360 |issue= 6402 |pages= 358-61 |year= 1992 |pmid= 1360148 |doi= 10.1038/360358a0 }}
*{{cite journal | author=Rehemtulla A, Kaufman RJ |title=Preferred sequence requirements for cleavage of pro-von Willebrand factor by propeptide-processing enzymes. |journal=Blood |volume=79 |issue= 9 |pages= 2349-55 |year= 1992 |pmid= 1571548 |doi= }}
*{{cite journal | author=Leduc R, Molloy SS, Thorne BA, Thomas G |title=Activation of human furin precursor processing endoprotease occurs by an intramolecular autoproteolytic cleavage. |journal=J. Biol. Chem. |volume=267 |issue= 20 |pages= 14304-8 |year= 1992 |pmid= 1629222 |doi= }}
*{{cite journal | author=Barr PJ, Mason OB, Landsberg KE, ''et al.'' |title=cDNA and gene structure for a human subtilisin-like protease with cleavage specificity for paired basic amino acid residues. |journal=DNA Cell Biol. |volume=10 |issue= 5 |pages= 319-28 |year= 1991 |pmid= 1713771 |doi= }}
*{{cite journal | author=Kiefer MC, Tucker JE, Joh R, ''et al.'' |title=Identification of a second human subtilisin-like protease gene in the fes/fps region of chromosome 15. |journal=DNA Cell Biol. |volume=10 |issue= 10 |pages= 757-69 |year= 1992 |pmid= 1741956 |doi= }}
*{{cite journal | author=Herz J, Kowal RC, Goldstein JL, Brown MS |title=Proteolytic processing of the 600 kd low density lipoprotein receptor-related protein (LRP) occurs in a trans-Golgi compartment. |journal=EMBO J. |volume=9 |issue= 6 |pages= 1769-76 |year= 1990 |pmid= 2112085 |doi= }}
*{{cite journal | author=Wise RJ, Barr PJ, Wong PA, ''et al.'' |title=Expression of a human proprotein processing enzyme: correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 23 |pages= 9378-82 |year= 1991 |pmid= 2251280 |doi= }}
*{{cite journal | author=van den Ouweland AM, van Duijnhoven HL, Keizer GD, ''et al.'' |title=Structural homology between the human fur gene product and the subtilisin-like protease encoded by yeast KEX2. |journal=Nucleic Acids Res. |volume=18 |issue= 3 |pages= 664 |year= 1990 |pmid= 2408021 |doi= }}
*{{cite journal | author=Van den Ouweland AM, Van Groningen JJ, Roebroek AJ, ''et al.'' |title=Nucleotide sequence analysis of the human fur gene. |journal=Nucleic Acids Res. |volume=17 |issue= 17 |pages= 7101-2 |year= 1989 |pmid= 2674906 |doi= }}
*{{cite journal | author=Roebroek AJ, Schalken JA, Leunissen JA, ''et al.'' |title=Evolutionary conserved close linkage of the c-fes/fps proto-oncogene and genetic sequences encoding a receptor-like protein. |journal=EMBO J. |volume=5 |issue= 9 |pages= 2197-202 |year= 1986 |pmid= 3023061 |doi= }}
*{{cite journal | author=Molloy SS, Thomas L, VanSlyke JK, ''et al.'' |title=Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface. |journal=EMBO J. |volume=13 |issue= 1 |pages= 18-33 |year= 1994 |pmid= 7508380 |doi= }}
*{{cite journal | author=Brakch N, Dettin M, Scarinci C, ''et al.'' |title=Structural investigation and kinetic characterization of potential cleavage sites of HIV GP160 by human furin and PC1. |journal=Biochem. Biophys. Res. Commun. |volume=213 |issue= 1 |pages= 356-61 |year= 1995 |pmid= 7639757 |doi= }}
*{{cite journal | author=Takahashi S, Kasai K, Hatsuzawa K, ''et al.'' |title=A mutation of furin causes the lack of precursor-processing activity in human colon carcinoma LoVo cells. |journal=Biochem. Biophys. Res. Commun. |volume=195 |issue= 2 |pages= 1019-26 |year= 1993 |pmid= 7690548 |doi= 10.1006/bbrc.1993.2146 }}
*{{cite journal | author=Hendy GN, Bennett HP, Gibbs BF, ''et al.'' |title=Proparathyroid hormone is preferentially cleaved to parathyroid hormone by the prohormone convertase furin. A mass spectrometric study. |journal=J. Biol. Chem. |volume=270 |issue= 16 |pages= 9517-25 |year= 1995 |pmid= 7721880 |doi= }}
*{{cite journal | author=Dubois CM, Laprise MH, Blanchette F, ''et al.'' |title=Processing of transforming growth factor beta 1 precursor by human furin convertase. |journal=J. Biol. Chem. |volume=270 |issue= 18 |pages= 10618-24 |year= 1995 |pmid= 7737999 |doi= }}
*{{cite journal | author=Gu M, Rappaport J, Leppla SH |title=Furin is important but not essential for the proteolytic maturation of gp160 of HIV-1. |journal=FEBS Lett. |volume=365 |issue= 1 |pages= 95-7 |year= 1995 |pmid= 7774724 |doi= }}
*{{cite journal | author=Schäfer W, Stroh A, Berghöfer S, ''et al.'' |title=Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin. |journal=EMBO J. |volume=14 |issue= 11 |pages= 2424-35 |year= 1995 |pmid= 7781597 |doi= }}
*{{cite journal | author=Mbikay M, Seidah NG, Chrétien M, Simpson EM |title=Chromosomal assignment of the genes for proprotein convertases PC4, PC5, and PACE 4 in mouse and human. |journal=Genomics |volume=26 |issue= 1 |pages= 123-9 |year= 1995 |pmid= 7782070 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GNB2L1... {November 12, 2007 7:19:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:20:19 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 = Guanine nucleotide binding protein (G protein), beta polypeptide 2-like 1
| HGNCid = 4399
| Symbol = GNB2L1
| AltSymbols =; Gnb2-rs1; H12.3; HLC-7; PIG21; RACK1
| OMIM = 176981
| ECnumber =
| Homologene = 4446
| MGIid = 101849
| Function = {{GNF_GO|id=GO:0005080 |text = protein kinase C binding}} {{GNF_GO|id=GO:0005102 |text = receptor binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0043025 |text = cell soma}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007205 |text = protein kinase C activation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10399
| Hs_Ensembl =
| Hs_RefseqProtein = NP_006089
| Hs_RefseqmRNA = NM_006098
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 14694
| Mm_Ensembl = ENSMUSG00000020372
| Mm_RefseqmRNA = NM_008143
| Mm_RefseqProtein = NP_032169
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 48643783
| Mm_GenLoc_end = 48649857
| Mm_Uniprot = Q3THP0
}}
}}
'''Guanine nucleotide binding protein (G protein), beta polypeptide 2-like 1''', also known as '''GNB2L1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Liu YV, Semenza GL |title=RACK1 vs. HSP90: competition for HIF-1 alpha degradation vs. stabilization. |journal=Cell Cycle |volume=6 |issue= 6 |pages= 656-9 |year= 2007 |pmid= 17361105 |doi= }}
*{{cite journal | author=Mochly-Rosen D, Miller KG, Scheller RH, ''et al.'' |title=p65 fragments, homologous to the C2 region of protein kinase C, bind to the intracellular receptors for protein kinase C. |journal=Biochemistry |volume=31 |issue= 35 |pages= 8120-4 |year= 1992 |pmid= 1326322 |doi= }}
*{{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=Guillemot F, Billault A, Auffray C |title=Physical linkage of a guanine nucleotide-binding protein-related gene to the chicken major histocompatibility complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 12 |pages= 4594-8 |year= 1989 |pmid= 2499885 |doi= }}
*{{cite journal | author=Pumiglia KM, LeVine H, Haske T, ''et al.'' |title=A direct interaction between G-protein beta gamma subunits and the Raf-1 protein kinase. |journal=J. Biol. Chem. |volume=270 |issue= 24 |pages= 14251-4 |year= 1995 |pmid= 7782277 |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=Disatnik MH, Hernandez-Sotomayor SM, Jones G, ''et al.'' |title=Phospholipase C-gamma 1 binding to intracellular receptors for activated protein kinase C. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 2 |pages= 559-63 |year= 1994 |pmid= 8290562 |doi= }}
*{{cite journal | author=Ron D, Chen CH, Caldwell J, ''et al.'' |title=Cloning of an intracellular receptor for protein kinase C: a homolog of the beta subunit of G proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 3 |pages= 839-43 |year= 1994 |pmid= 8302854 |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=Liliental J, Chang DD |title=Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit. |journal=J. Biol. Chem. |volume=273 |issue= 4 |pages= 2379-83 |year= 1998 |pmid= 9442085 |doi= }}
*{{cite journal | author=Chang BY, Conroy KB, Machleder EM, Cartwright CA |title=RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells. |journal=Mol. Cell. Biol. |volume=18 |issue= 6 |pages= 3245-56 |year= 1998 |pmid= 9584165 |doi= }}
*{{cite journal | author=Rietzler M, Bittner M, Kolanus W, ''et al.'' |title=The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins. |journal=J. Biol. Chem. |volume=273 |issue= 42 |pages= 27459-66 |year= 1998 |pmid= 9765275 |doi= }}
*{{cite journal | author=Shimohama S, Kamiya S, Taniguchi T, Kimura J |title=Intracellular receptors for activated C-kinase in the postmortem human brain: no alteration in Alzheimer disease. |journal=Alzheimer disease and associated disorders |volume=12 |issue= 4 |pages= 384-6 |year= 1999 |pmid= 9876970 |doi= }}
*{{cite journal | author=Yarwood SJ, Steele MR, Scotland G, ''et al.'' |title=The RACK1 signaling scaffold protein selectively interacts with the cAMP-specific phosphodiesterase PDE4D5 isoform. |journal=J. Biol. Chem. |volume=274 |issue= 21 |pages= 14909-17 |year= 1999 |pmid= 10329691 |doi= }}
*{{cite journal | author=Ron D, Jiang Z, Yao L, ''et al.'' |title=Coordinated movement of RACK1 with activated betaIIPKC. |journal=J. Biol. Chem. |volume=274 |issue= 38 |pages= 27039-46 |year= 1999 |pmid= 10480917 |doi= }}
*{{cite journal | author=Geijsen N, Spaargaren M, Raaijmakers JA, ''et al.'' |title=Association of RACK1 and PKCbeta with the common beta-chain of the IL-5/IL-3/GM-CSF receptor. |journal=Oncogene |volume=18 |issue= 36 |pages= 5126-30 |year= 1999 |pmid= 10490850 |doi= 10.1038/sj.onc.1202896 }}
*{{cite journal | author=Smith PR, de Jesus O, Turner D, ''et al.'' |title=Structure and coding content of CST (BART) family RNAs of Epstein-Barr virus. |journal=J. Virol. |volume=74 |issue= 7 |pages= 3082-92 |year= 2000 |pmid= 10708423 |doi= }}
*{{cite journal | author=Ellis JH, Ashman C, Burden MN, ''et al.'' |title=GRID: a novel Grb-2-related adapter protein that interacts with the activated T cell costimulatory receptor CD28. |journal=J. Immunol. |volume=164 |issue= 11 |pages= 5805-14 |year= 2000 |pmid= 10820259 |doi= }}
*{{cite journal | author=Croze E, Usacheva A, Asarnow D, ''et al.'' |title=Receptor for activated C-kinase (RACK-1), a WD motif-containing protein, specifically associates with the human type I IFN receptor. |journal=J. Immunol. |volume=165 |issue= 9 |pages= 5127-32 |year= 2000 |pmid= 11046044 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HLA-DQA1... {November 12, 2007 7:05:04 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:06:17 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_HLA-DQA1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jk8.
| PDB = {{PDB2|1jk8}}, {{PDB2|1s9v}}, {{PDB2|1uvq}}
| Name = Major histocompatibility complex, class II, DQ alpha 1
| HGNCid = 4942
| Symbol = HLA-DQA1
| AltSymbols =; GSE; CD; CELIAC1; DQ-A1; FLJ27088; FLJ27328; HLA DQA1; HLA-DQA
| OMIM = 146880
| ECnumber =
| Homologene = 7750
| MGIid = 95895
| GeneAtlas_image1 = PBB_GE_HLA-DQA1_212671_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_HLA-DQA1_213831_at_tn.png
| GeneAtlas_image3 = PBB_GE_HLA-DQA1_203290_at_tn.png
| 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}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3117
| Hs_Ensembl = ENSG00000196735
| Hs_RefseqProtein = XP_001134217
| Hs_RefseqmRNA = XM_001134217
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 32713112
| Hs_GenLoc_end = 32719345
| Hs_Uniprot = P01907
| Mm_EntrezGene = 14960
| Mm_Ensembl = ENSMUSG00000036594
| Mm_RefseqmRNA = NM_010378
| Mm_RefseqProtein = NP_034508
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 33891095
| Mm_GenLoc_end = 33896139
| Mm_Uniprot = Q3TB90
}}
}}
'''Major histocompatibility complex, class II, DQ alpha 1''', also known as '''HLA-DQA1''', is a human [[gene]].
<!-- 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-DQA1 belongs to the HLA class II alpha chain paralogues. The class II molecule is a heterodimer consisting of an alpha (DQA) and a beta chain (DQB), 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 alpha chain is approximately 33-35 kDa. It is encoded by 5 exons; exon 1 encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, and exon 4 encodes the transmembrane domain and the cytoplasmic tail. Within the DQ molecule both the alpha chain and the beta chain contain the polymorphisms specifying the peptide binding specificities, resulting in up to four different molecules. Typing for these polymorphisms is routinely done for bone marrow transplantation.<ref>{{cite web | title = Entrez Gene: HLA-DQA1 major histocompatibility complex, class II, DQ alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3117| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schmidt H, Williamson D, Ashley-Koch A |title=HLA-DR15 haplotype and multiple sclerosis: a HuGE review. |journal=Am. J. Epidemiol. |volume=165 |issue= 10 |pages= 1097-109 |year= 2007 |pmid= 17329717 |doi= 10.1093/aje/kwk118 }}
*{{cite journal | author=Marsh SG, Bodmer JG |title=HLA class II nucleotide sequences, 1992. |journal=Tissue Antigens |volume=40 |issue= 5 |pages= 229-43 |year= 1993 |pmid= 1362295 |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=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=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=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=Todd JA, Fukui Y, Kitagawa T, Sasazuki T |title=The A3 allele of the HLA-DQA1 locus is associated with susceptibility to type 1 diabetes in Japanese. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 3 |pages= 1094-8 |year= 1990 |pmid= 2300572 |doi= }}
*{{cite journal | author=Kao HT, Gregersen PK, Tang JC, ''et al.'' |title=Molecular analysis of the HLA class II genes in two DRw6-related haplotypes, DRw13 DQw1 and DRw14 DQw3. |journal=J. Immunol. |volume=142 |issue= 5 |pages= 1743-7 |year= 1989 |pmid= 2493052 |doi= }}
*{{cite journal | author=Gyllensten UB, Erlich HA |title=Ancient roots for polymorphism at the HLA-DQ alpha locus in primates. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 24 |pages= 9986-90 |year= 1990 |pmid= 2513578 |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=Jonsson AK, Andersson L, Rask L |title=Complete sequences of DQA1 and DQB1 cDNA clones corresponding to the DQw4 specificity. |journal=Immunogenetics |volume=30 |issue= 3 |pages= 232-4 |year= 1989 |pmid= 2777341 |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=Turco E, Care A, Compagnone-Post P, ''et al.'' |title=Allelic forms of the alpha- and beta-chain genes encoding DQw1-positive heterodimers. |journal=Immunogenetics |volume=26 |issue= 4-5 |pages= 282-90 |year= 1987 |pmid= 2888727 |doi= }}
*{{cite journal | author=Hurley CK, Gregersen P, Steiner N, ''et al.'' |title=Polymorphism of the HLA-D region in American blacks. A DR3 haplotype generated by recombination. |journal=J. Immunol. |volume=140 |issue= 3 |pages= 885-92 |year= 1988 |pmid= 2892884 |doi= }}
*{{cite journal | author=Jonsson AK, Hyldig-Nielsen JJ, Servenius B, ''et al.'' |title=Class II genes of the human major histocompatibility complex. Comparisons of the DQ and DX alpha and beta genes. |journal=J. Biol. Chem. |volume=262 |issue= 18 |pages= 8767-77 |year= 1987 |pmid= 3036828 |doi= }}
*{{cite journal | author=Liu CP, Bach FH, Wu SK |title=Molecular studies of a rare DR2/LD-5a/DQw3 HLA class II haplotype. Multiple genetic mechanisms in the generation of polymorphic HLA class II genes. |journal=J. Immunol. |volume=140 |issue= 10 |pages= 3631-9 |year= 1988 |pmid= 3129499 |doi= }}
*{{cite journal | author=Lock CB, So AK, Welsh KI, ''et al.'' |title=MHC class II sequences of an HLA-DR2 narcoleptic. |journal=Immunogenetics |volume=27 |issue= 6 |pages= 449-55 |year= 1988 |pmid= 3259543 |doi= }}
*{{cite journal | author=Horn GT, Bugawan TL, Long CM, ''et al.'' |title=Sequence analysis of HLA class II genes from insulin-dependent diabetic individuals. |journal=Hum. Immunol. |volume=21 |issue= 4 |pages= 249-63 |year= 1988 |pmid= 3372263 |doi= }}
*{{cite journal | author=Andrieu JM, Even P, Venet A |title=AIDS and related syndromes as a viral-induced autoimmune disease of the immune system: an anti-MHC II disorder. Therapeutic implications. |journal=AIDS research |volume=2 |issue= 3 |pages= 163-74 |year= 1986 |pmid= 3489470 |doi= }}
*{{cite journal | author=Schiffenbauer J, Didier DK, Klearman M, ''et al.'' |title=Complete sequence of the HLA DQ alpha and DQ beta cDNA from a DR5/DQw3 cell line. |journal=J. Immunol. |volume=139 |issue= 1 |pages= 228-33 |year= 1987 |pmid= 3584986 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IKBKG... {November 12, 2007 7:17:42 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:18:33 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
}}
<!-- 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 = Inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma
| HGNCid = 5961
| Symbol = IKBKG
| AltSymbols =; IP; FIP-3; FIP3; Fip3p; IKK-gamma; IP1; IP2; NEMO
| OMIM = 300248
| ECnumber =
| Homologene = 2698
| MGIid = 1338074
| GeneAtlas_image1 = PBB_GE_IKBKG_36004_at_tn.png
| GeneAtlas_image2 = PBB_GE_IKBKG_209929_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0008385 |text = IkappaB kinase complex}} {{GNF_GO|id=GO:0044444 |text = cytoplasmic part}}
| Process = {{GNF_GO|id=GO:0001782 |text = B cell homeostasis}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007250 |text = activation of NF-kappaB-inducing kinase}} {{GNF_GO|id=GO:0050852 |text = T cell receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8517
| Hs_Ensembl = ENSG00000073009
| Hs_RefseqProtein = NP_003630
| Hs_RefseqmRNA = NM_003639
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 153423653
| Hs_GenLoc_end = 153446455
| Hs_Uniprot = Q9Y6K9
| Mm_EntrezGene = 16151
| Mm_Ensembl = ENSMUSG00000004221
| Mm_RefseqmRNA = NM_010547
| Mm_RefseqProtein = NP_034677
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 70677332
| Mm_GenLoc_end = 70704240
| Mm_Uniprot = Q3UG24
}}
}}
'''Inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma''', also known as '''IKBKG''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Familial incontinentia pigmenti (IP) is a genodermatosis that segregates as an X-linked dominant disorder and is usually lethal prenatally in males (The International Incontinentia Pigmenti Consortium, 2000 [PubMed 10839543]). In affected females it causes highly variable abnormalities of the skin, hair, nails, teeth, eyes, and central nervous system. The prominent skin signs occur in 4 classic cutaneous stages: perinatal inflammatory vesicles, verrucous patches, a distinctive pattern of hyperpigmentation, and dermal scarring. Cells expressing the mutated X chromosome are eliminated selectively around the time of birth, so females with IP exhibit extremely skewed X-inactivation. Familial incontinentia pigmenti is caused by mutations in the NEMO gene and is here referred to as IP2, or 'classical' incontinentia pigmenti. Sporadic incontinentia pigmenti, the so-called IP1, which maps to Xp11, is categorized as hypomelanosis of Ito (MIM 300337).[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: IKBKG inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8517| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rothwarf DM, Zandi E, Natoli G, Karin M |title=IKK-gamma is an essential regulatory subunit of the IkappaB kinase complex. |journal=Nature |volume=395 |issue= 6699 |pages= 297-300 |year= 1998 |pmid= 9751060 |doi= 10.1038/26261 }}
*{{cite journal | author=Mercurio F, Murray BW, Shevchenko A, ''et al.'' |title=IkappaB kinase (IKK)-associated protein 1, a common component of the heterogeneous IKK complex. |journal=Mol. Cell. Biol. |volume=19 |issue= 2 |pages= 1526-38 |year= 1999 |pmid= 9891086 |doi= }}
*{{cite journal | author=Li Y, Kang J, Friedman J, ''et al.'' |title=Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 3 |pages= 1042-7 |year= 1999 |pmid= 9927690 |doi= }}
*{{cite journal | author=Jin DY, Jeang KT |title=Isolation of full-length cDNA and chromosomal localization of human NF-kappaB modulator NEMO to Xq28. |journal=J. Biomed. Sci. |volume=6 |issue= 2 |pages= 115-20 |year= 1999 |pmid= 10087442 |doi= }}
*{{cite journal | author=Jin DY, Giordano V, Kibler KV, ''et al.'' |title=Role of adapter function in oncoprotein-mediated activation of NF-kappaB. Human T-cell leukemia virus type I Tax interacts directly with IkappaB kinase gamma. |journal=J. Biol. Chem. |volume=274 |issue= 25 |pages= 17402-5 |year= 1999 |pmid= 10364167 |doi= }}
*{{cite journal | author=Zhang SQ, Kovalenko A, Cantarella G, Wallach D |title=Recruitment of the IKK signalosome to the p55 TNF receptor: RIP and A20 bind to NEMO (IKKgamma) upon receptor stimulation. |journal=Immunity |volume=12 |issue= 3 |pages= 301-11 |year= 2000 |pmid= 10755617 |doi= }}
*{{cite journal | author=Smahi A, Courtois G, Vabres P, ''et al.'' |title=Genomic rearrangement in NEMO impairs NF-kappaB activation and is a cause of incontinentia pigmenti. The International Incontinentia Pigmenti (IP) Consortium. |journal=Nature |volume=405 |issue= 6785 |pages= 466-72 |year= 2000 |pmid= 10839543 |doi= 10.1038/35013114 }}
*{{cite journal | author=Inohara N, Koseki T, Lin J, ''et al.'' |title=An induced proximity model for NF-kappa B activation in the Nod1/RICK and RIP signaling pathways. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 27823-31 |year= 2000 |pmid= 10880512 |doi= 10.1074/jbc.M003415200 }}
*{{cite journal | author=Ye Z, Connor JR |title=cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs. |journal=Biochem. Biophys. Res. Commun. |volume=275 |issue= 1 |pages= 223-7 |year= 2000 |pmid= 10944468 |doi= 10.1006/bbrc.2000.3282 }}
*{{cite journal | author=Li X, Commane M, Nie H, ''et al.'' |title=Act1, an NF-kappa B-activating protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 19 |pages= 10489-93 |year= 2000 |pmid= 10962024 |doi= 10.1073/pnas.160265197 }}
*{{cite journal | author=Leonardi A, Chariot A, Claudio E, ''et al.'' |title=CIKS, a connection to Ikappa B kinase and stress-activated protein kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 19 |pages= 10494-9 |year= 2000 |pmid= 10962033 |doi= 10.1073/pnas.190245697 }}
*{{cite journal | author=May MJ, D'Acquisto F, Madge LA, ''et al.'' |title=Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex. |journal=Science |volume=289 |issue= 5484 |pages= 1550-4 |year= 2000 |pmid= 10968790 |doi= }}
*{{cite journal | author=Zonana J, Elder ME, Schneider LC, ''et al.'' |title=A novel X-linked disorder of immune deficiency and hypohidrotic ectodermal dysplasia is allelic to incontinentia pigmenti and due to mutations in IKK-gamma (NEMO). |journal=Am. J. Hum. Genet. |volume=67 |issue= 6 |pages= 1555-62 |year= 2001 |pmid= 11047757 |doi= }}
*{{cite journal | author=Xiao G, Sun SC |title=Activation of IKKalpha and IKKbeta through their fusion with HTLV-I tax protein. |journal=Oncogene |volume=19 |issue= 45 |pages= 5198-203 |year= 2000 |pmid= 11064457 |doi= 10.1038/sj.onc.1203894 }}
*{{cite journal | author=Li XH, Fang X, Gaynor RB |title=Role of IKKgamma/nemo in assembly of the Ikappa B kinase complex. |journal=J. Biol. Chem. |volume=276 |issue= 6 |pages= 4494-500 |year= 2001 |pmid= 11080499 |doi= 10.1074/jbc.M008353200 }}
*{{cite journal | author=Poyet JL, Srinivasula SM, Alnemri ES |title=vCLAP, a caspase-recruitment domain-containing protein of equine Herpesvirus-2, persistently activates the Ikappa B kinases through oligomerization of IKKgamma. |journal=J. Biol. Chem. |volume=276 |issue= 5 |pages= 3183-7 |year= 2001 |pmid= 11113112 |doi= 10.1074/jbc.C000792200 }}
*{{cite journal | author=Jain A, Ma CA, Liu S, ''et al.'' |title=Specific missense mutations in NEMO result in hyper-IgM syndrome with hypohydrotic ectodermal dysplasia. |journal=Nat. Immunol. |volume=2 |issue= 3 |pages= 223-8 |year= 2001 |pmid= 11224521 |doi= 10.1038/85277 }}
*{{cite journal | author=Döffinger R, Smahi A, Bessia C, ''et al.'' |title=X-linked anhidrotic ectodermal dysplasia with immunodeficiency is caused by impaired NF-kappaB signaling. |journal=Nat. Genet. |volume=27 |issue= 3 |pages= 277-85 |year= 2001 |pmid= 11242109 |doi= 10.1038/85837 }}
*{{cite journal | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal | author=Galgóczy P, Rosenthal A, Platzer M |title=Human-mouse comparative sequence analysis of the NEMO gene reveals an alternative promoter within the neighboring G6PD gene. |journal=Gene |volume=271 |issue= 1 |pages= 93-8 |year= 2001 |pmid= 11410370 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL12B... {November 12, 2007 7:07:05 PM PST}
- SEARCH REDIRECT: Control Box Found: Interleukin-12 subunit beta {November 12, 2007 7:07:45 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 12, 2007 7:07:46 PM PST}
- SKIP SUMMARY: SKIPPING Summary, No Errors. {November 12, 2007 7:07:46 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 12, 2007 7:07:46 PM PST}
- UPDATED: Updated protein page: Interleukin-12 subunit beta {November 12, 2007 7:07:54 PM PST}
- INFO: Beginning work on IL6ST... {November 12, 2007 7:06:17 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:07:05 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
| 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_IL6ST_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bj8.
| PDB = {{PDB2|1bj8}}, {{PDB2|1bqu}}, {{PDB2|1i1r}}, {{PDB2|1p9m}}, {{PDB2|1pvh}}
| Name = Interleukin 6 signal transducer (gp130, oncostatin M receptor)
| HGNCid = 6021
| Symbol = IL6ST
| AltSymbols =; CD130; CDw130; GP130; GP130-RAPS; IL6R-beta
| OMIM = 600694
| ECnumber =
| Homologene = 1645
| MGIid = 96560
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004915 |text = interleukin-6 receptor activity}} {{GNF_GO|id=GO:0004924 |text = oncostatin-M receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0008593 |text = regulation of Notch signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3572
| Hs_Ensembl =
| Hs_RefseqProtein = NP_002175
| Hs_RefseqmRNA = NM_002184
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 16195
| Mm_Ensembl = ENSMUSG00000021756
| Mm_RefseqmRNA = NM_010560
| Mm_RefseqProtein = NP_034690
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 113584987
| Mm_GenLoc_end = 113627719
| Mm_Uniprot = Q3TDT5
}}
}}
'''Interleukin 6 signal transducer (gp130, oncostatin M receptor)''', also known as '''IL6ST''', is a human [[gene]].
<!-- 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 signal transducer shared by many cytokines, including interleukin 6 (IL6), ciliary neurotrophic factor (CNTF), leukemia inhibitory factor (LIF), and oncostatin M (OSM). This protein functions as a part of the cytokine receptor complex. The activation of this protein is dependent upon the binding of cytokines to their receptors. vIL6, a protein related to IL6 and encoded by the Kaposi sarcoma-associated herpesvirus, can bypass the interleukin 6 receptor (IL6R) and directly activate this protein. Knockout studies in mice suggested a critical role of the gene encoding this protein in regulating myocyte apoptosis. Alternatively spliced transcript variants encoding distinct isoforms have been described.<ref>{{cite web | title = Entrez Gene: IL6ST interleukin 6 signal transducer (gp130, oncostatin M receptor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3572| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ip NY, Nye SH, Boulton TG, ''et al.'' |title=CNTF and LIF act on neuronal cells via shared signaling pathways that involve the IL-6 signal transducing receptor component gp130. |journal=Cell |volume=69 |issue= 7 |pages= 1121-32 |year= 1992 |pmid= 1617725 |doi= }}
*{{cite journal | author=Hibi M, Murakami M, Saito M, ''et al.'' |title=Molecular cloning and expression of an IL-6 signal transducer, gp130. |journal=Cell |volume=63 |issue= 6 |pages= 1149-57 |year= 1991 |pmid= 2261637 |doi= }}
*{{cite journal | author=Taga T, Hibi M, Hirata Y, ''et al.'' |title=Interleukin-6 triggers the association of its receptor with a possible signal transducer, gp130. |journal=Cell |volume=58 |issue= 3 |pages= 573-81 |year= 1989 |pmid= 2788034 |doi= }}
*{{cite journal | author=Rodriguez C, Grosgeorge J, Nguyen VC, ''et al.'' |title=Human gp130 transducer chain gene (IL6ST) is localized to chromosome band 5q11 and possesses a pseudogene on chromosome band 17p11. |journal=Cytogenet. Cell Genet. |volume=70 |issue= 1-2 |pages= 64-7 |year= 1995 |pmid= 7736792 |doi= }}
*{{cite journal | author=Narazaki M, Yasukawa K, Saito T, ''et al.'' |title=Soluble forms of the interleukin-6 signal-transducing receptor component gp130 in human serum possessing a potential to inhibit signals through membrane-anchored gp130. |journal=Blood |volume=82 |issue= 4 |pages= 1120-6 |year= 1993 |pmid= 8353278 |doi= }}
*{{cite journal | author=Davis S, Aldrich TH, Stahl N, ''et al.'' |title=LIFR beta and gp130 as heterodimerizing signal transducers of the tripartite CNTF receptor. |journal=Science |volume=260 |issue= 5115 |pages= 1805-8 |year= 1993 |pmid= 8390097 |doi= }}
*{{cite journal | author=Murakami M, Hibi M, Nakagawa N, ''et al.'' |title=IL-6-induced homodimerization of gp130 and associated activation of a tyrosine kinase. |journal=Science |volume=260 |issue= 5115 |pages= 1808-10 |year= 1993 |pmid= 8511589 |doi= }}
*{{cite journal | author=Sharkey AM, Dellow K, Blayney M, ''et al.'' |title=Stage-specific expression of cytokine and receptor messenger ribonucleic acids in human preimplantation embryos. |journal=Biol. Reprod. |volume=53 |issue= 4 |pages= 974-81 |year= 1996 |pmid= 8547494 |doi= }}
*{{cite journal | author=Mosley B, De Imus C, Friend D, ''et al.'' |title=Dual oncostatin M (OSM) receptors. Cloning and characterization of an alternative signaling subunit conferring OSM-specific receptor activation. |journal=J. Biol. Chem. |volume=271 |issue= 51 |pages= 32635-43 |year= 1997 |pmid= 8999038 |doi= }}
*{{cite journal | author=Lee IS, Liu Y, Narazaki M, ''et al.'' |title=Vav is associated with signal transducing molecules gp130, Grb2 and Erk2, and is tyrosine phosphorylated in response to interleukin-6. |journal=FEBS Lett. |volume=401 |issue= 2-3 |pages= 133-7 |year= 1997 |pmid= 9013873 |doi= }}
*{{cite journal | author=Auguste P, Guillet C, Fourcin M, ''et al.'' |title=Signaling of type II oncostatin M receptor. |journal=J. Biol. Chem. |volume=272 |issue= 25 |pages= 15760-4 |year= 1997 |pmid= 9188471 |doi= }}
*{{cite journal | author=Schiemann WP, Bartoe JL, Nathanson NM |title=Box 3-independent signaling mechanisms are involved in leukemia inhibitory factor receptor alpha- and gp130-mediated stimulation of mitogen-activated protein kinase. Evidence for participation of multiple signaling pathways which converge at Ras. |journal=J. Biol. Chem. |volume=272 |issue= 26 |pages= 16631-6 |year= 1997 |pmid= 9195977 |doi= }}
*{{cite journal | author=Diamant M, Rieneck K, Mechti N, ''et al.'' |title=Cloning and expression of an alternatively spliced mRNA encoding a soluble form of the human interleukin-6 signal transducer gp130. |journal=FEBS Lett. |volume=412 |issue= 2 |pages= 379-84 |year= 1997 |pmid= 9256256 |doi= }}
*{{cite journal | author=Koshelnick Y, Ehart M, Hufnagl P, ''et al.'' |title=Urokinase receptor is associated with the components of the JAK1/STAT1 signaling pathway and leads to activation of this pathway upon receptor clustering in the human kidney epithelial tumor cell line TCL-598. |journal=J. Biol. Chem. |volume=272 |issue= 45 |pages= 28563-7 |year= 1997 |pmid= 9353320 |doi= }}
*{{cite journal | author=Kim H, Baumann H |title=Transmembrane domain of gp130 contributes to intracellular signal transduction in hepatic cells. |journal=J. Biol. Chem. |volume=272 |issue= 49 |pages= 30741-7 |year= 1998 |pmid= 9388212 |doi= }}
*{{cite journal | author=Bravo J, Staunton D, Heath JK, Jones EY |title=Crystal structure of a cytokine-binding region of gp130. |journal=EMBO J. |volume=17 |issue= 6 |pages= 1665-74 |year= 1998 |pmid= 9501088 |doi= 10.1093/emboj/17.6.1665 }}
*{{cite journal | author=Barton VA, Hudson KR, Heath JK |title=Identification of three distinct receptor binding sites of murine interleukin-11. |journal=J. Biol. Chem. |volume=274 |issue= 9 |pages= 5755-61 |year= 1999 |pmid= 10026196 |doi= }}
*{{cite journal | author=Hirota H, Chen J, Betz UA, ''et al.'' |title=Loss of a gp130 cardiac muscle cell survival pathway is a critical event in the onset of heart failure during biomechanical stress. |journal=Cell |volume=97 |issue= 2 |pages= 189-98 |year= 1999 |pmid= 10219240 |doi= }}
*{{cite journal | author=Tacken I, Dahmen H, Boisteau O, ''et al.'' |title=Definition of receptor binding sites on human interleukin-11 by molecular modeling-guided mutagenesis. |journal=Eur. J. Biochem. |volume=265 |issue= 2 |pages= 645-55 |year= 1999 |pmid= 10504396 |doi= }}
*{{cite journal | author=Chung TD, Yu JJ, Kong TA, ''et al.'' |title=Interleukin-6 activates phosphatidylinositol-3 kinase, which inhibits apoptosis in human prostate cancer cell lines. |journal=Prostate |volume=42 |issue= 1 |pages= 1-7 |year= 2000 |pmid= 10579793 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ITGA4... {November 12, 2007 7:07:54 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:08:50 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 = Integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor)
| HGNCid = 6140
| Symbol = ITGA4
| AltSymbols =; CD49D; IA4; MGC90518
| OMIM = 192975
| ECnumber =
| Homologene = 37364
| MGIid = 96603
| GeneAtlas_image1 = PBB_GE_ITGA4_213416_at_tn.png
| GeneAtlas_image2 = PBB_GE_ITGA4_205884_at_tn.png
| GeneAtlas_image3 = PBB_GE_ITGA4_205885_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0042802 |text = identical 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:0001974 |text = blood vessel remodeling}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0016477 |text = cell migration}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3676
| Hs_Ensembl = ENSG00000115232
| Hs_RefseqProtein = NP_000876
| Hs_RefseqmRNA = NM_000885
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 182029864
| Hs_GenLoc_end = 182110711
| Hs_Uniprot = P13612
| Mm_EntrezGene = 16401
| Mm_Ensembl = ENSMUSG00000027009
| Mm_RefseqmRNA = NM_010576
| Mm_RefseqProtein = NP_034706
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 79056339
| Mm_GenLoc_end = 79133962
| Mm_Uniprot = Q78E20
}}
}}
'''Integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor)''', also known as '''ITGA4''', is a human [[gene]].
<!-- 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 product of this gene belongs to the integrin alpha chain family of proteins. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This gene encodes an alpha 4 chain. Unlike other integrin alpha chains, alpha 4 neither contains an I-domain, nor undergoes disulfide-linked cleavage. Alpha 4 chain associates with either beta 1 chain or beta 7 chain.<ref>{{cite web | title = Entrez Gene: ITGA4 integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3676| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Humphries MJ, Sheridan J, Mould AP, Newham P |title=Mechanisms of VCAM-1 and fibronectin binding to integrin alpha 4 beta 1: implications for integrin function and rational drug design. |journal=Ciba Found. Symp. |volume=189 |issue= |pages= 177-91; discussion 191-9 |year= 1995 |pmid= 7587632 |doi= }}
*{{cite journal | author=Oostendorp RA, Dörmer P |title=VLA-4-mediated interactions between normal human hematopoietic progenitors and stromal cells. |journal=Leuk. Lymphoma |volume=24 |issue= 5-6 |pages= 423-35 |year= 1997 |pmid= 9086434 |doi= }}
*{{cite journal | author=Porter JC, Hogg N |title=Integrins take partners: cross-talk between integrins and other membrane receptors. |journal=Trends Cell Biol. |volume=8 |issue= 10 |pages= 390-6 |year= 1999 |pmid= 9789327 |doi= }}
*{{cite journal | author=Rose DM, Han J, Ginsberg MH |title=Alpha4 integrins and the immune response. |journal=Immunol. Rev. |volume=186 |issue= |pages= 118-24 |year= 2003 |pmid= 12234367 |doi= }}
*{{cite journal | author=O'Connor P |title=Natalizumab and the role of alpha 4-integrin antagonism in the treatment of multiple sclerosis. |journal=Expert opinion on biological therapy |volume=7 |issue= 1 |pages= 123-36 |year= 2007 |pmid= 17150024 |doi= 10.1517/14712598.7.1.123 }}
*{{cite journal | author=Chan BM, Elices MJ, Murphy E, Hemler ME |title=Adhesion to vascular cell adhesion molecule 1 and fibronectin. Comparison of alpha 4 beta 1 (VLA-4) and alpha 4 beta 7 on the human B cell line JY. |journal=J. Biol. Chem. |volume=267 |issue= 12 |pages= 8366-70 |year= 1992 |pmid= 1373725 |doi= }}
*{{cite journal | author=Fernández-Ruiz E, Pardo-Manuel de Villena F, Rubio MA, ''et al.'' |title=Mapping of the human VLA-alpha 4 gene to chromosome 2q31-q32. |journal=Eur. J. Immunol. |volume=22 |issue= 2 |pages= 587-90 |year= 1992 |pmid= 1537388 |doi= }}
*{{cite journal | author=Rubio M, Nueda A, Vara A, Corbí Lopez AL |title=A single mRNA encodes the alpha 150 and alpha 80/70 forms of the alpha subunit of VLA4. |journal=Eur. J. Immunol. |volume=22 |issue= 4 |pages= 1099-102 |year= 1992 |pmid= 1551405 |doi= }}
*{{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=Teixidó J, Parker CM, Kassner PD, Hemler ME |title=Functional and structural analysis of VLA-4 integrin alpha 4 subunit cleavage. |journal=J. Biol. Chem. |volume=267 |issue= 3 |pages= 1786-91 |year= 1992 |pmid= 1730718 |doi= }}
*{{cite journal | author=Rosemblatt M, Vuillet-Gaugler MH, Leroy C, Coulombel L |title=Coexpression of two fibronectin receptors, VLA-4 and VLA-5, by immature human erythroblastic precursor cells. |journal=J. Clin. Invest. |volume=87 |issue= 1 |pages= 6-11 |year= 1991 |pmid= 1824634 |doi= }}
*{{cite journal | author=Rosen GD, Birkenmeier TM, Dean DC |title=Characterization of the alpha 4 integrin gene promoter. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 10 |pages= 4094-8 |year= 1991 |pmid= 2034655 |doi= }}
*{{cite journal | author=Takada Y, Elices MJ, Crouse C, Hemler ME |title=The primary structure of the alpha 4 subunit of VLA-4: homology to other integrins and a possible cell-cell adhesion function. |journal=EMBO J. |volume=8 |issue= 5 |pages= 1361-8 |year= 1989 |pmid= 2788572 |doi= }}
*{{cite journal | author=Takada Y, Strominger JL, Hemler ME |title=The very late antigen family of heterodimers is part of a superfamily of molecules involved in adhesion and embryogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 10 |pages= 3239-43 |year= 1987 |pmid= 3033641 |doi= }}
*{{cite journal | author=Hemler ME, Huang C, Schwarz L |title=The VLA protein family. Characterization of five distinct cell surface heterodimers each with a common 130,000 molecular weight beta subunit. |journal=J. Biol. Chem. |volume=262 |issue= 7 |pages= 3300-9 |year= 1987 |pmid= 3546305 |doi= }}
*{{cite journal | author=Gailit J, Pierschbacher M, Clark RA |title=Expression of functional alpha 4 beta 1 integrin by human dermal fibroblasts. |journal=J. Invest. Dermatol. |volume=100 |issue= 3 |pages= 323-8 |year= 1993 |pmid= 8440915 |doi= }}
*{{cite journal | author=Pujades C, Teixidó J, Bazzoni G, Hemler ME |title=Integrin alpha 4 cysteines 278 and 717 modulate VLA-4 ligand binding and also contribute to alpha 4/180 formation. |journal=Biochem. J. |volume=313 ( Pt 3) |issue= |pages= 899-908 |year= 1996 |pmid= 8611173 |doi= }}
*{{cite journal | author=Szabo M, McIntyre BW |title=Identification of two variants of the human integrin alpha 4 subunit. |journal=Mol. Immunol. |volume=32 |issue= 17-18 |pages= 1453-4 |year= 1996 |pmid= 8643114 |doi= }}
*{{cite journal | author=Mannion BA, Berditchevski F, Kraeft SK, ''et al.'' |title=Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associated with integrin alpha 4 beta 1 (CD49d/CD29). |journal=J. Immunol. |volume=157 |issue= 5 |pages= 2039-47 |year= 1996 |pmid= 8757325 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ITGAL... {November 12, 2007 7:08:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:09:30 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_ITGAL_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1cqp.
| PDB = {{PDB2|1cqp}}, {{PDB2|1dgq}}, {{PDB2|1lfa}}, {{PDB2|1mjn}}, {{PDB2|1mq8}}, {{PDB2|1mq9}}, {{PDB2|1mqa}}, {{PDB2|1rd4}}, {{PDB2|1t0p}}, {{PDB2|1xdd}}, {{PDB2|1xdg}}, {{PDB2|1xuo}}, {{PDB2|1zon}}, {{PDB2|1zoo}}, {{PDB2|1zop}}, {{PDB2|2ica}}, {{PDB2|2o7n}}
| Name = Integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)
| HGNCid = 6148
| Symbol = ITGAL
| AltSymbols =; CD11A; LFA-1; LFA1A
| OMIM = 153370
| ECnumber =
| Homologene = 1666
| MGIid = 96606
| GeneAtlas_image1 = PBB_GE_ITGAL_213475_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{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:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0050798 |text = activated T cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3683
| Hs_Ensembl = ENSG00000005844
| Hs_RefseqProtein = NP_002200
| Hs_RefseqmRNA = NM_002209
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 30391551
| Hs_GenLoc_end = 30441772
| Hs_Uniprot = P20701
| Mm_EntrezGene = 16408
| Mm_Ensembl = ENSMUSG00000030830
| Mm_RefseqmRNA = NM_008400
| Mm_RefseqProtein = NP_032426
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 127087558
| Mm_GenLoc_end = 127124876
| Mm_Uniprot = Q3T9N8
}}
}}
'''Integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)''', also known as '''ITGAL''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = ITGAL encodes the integrin alpha L chain. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. This I-domain containing alpha integrin combines with the beta 2 chain (ITGB2) to form the integrin lymphocyte function-associated antigen-1 (LFA-1), which is expressed on all leukocytes. LFA-1 plays a central role in leukocyte intercellular adhesion through interactions with its ligands, ICAMs 1-3 (intercellular adhesion molecules 1 through 3), and also functions in lymphocyte costimulatory signaling.<ref>{{cite web | title = Entrez Gene: ITGAL integrin, alpha L (antigen CD11A (p180), lymphocyte function-associated antigen 1; alpha polypeptide)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3683| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lub M, van Kooyk Y, Figdor CG |title=Ins and outs of LFA-1. |journal=Immunol. Today |volume=16 |issue= 10 |pages= 479-83 |year= 1995 |pmid= 7576051 |doi= }}
*{{cite journal | author=Dickeson SK, Santoro SA |title=Ligand recognition by the I domain-containing integrins. |journal=Cell. Mol. Life Sci. |volume=54 |issue= 6 |pages= 556-66 |year= 1998 |pmid= 9676575 |doi= }}
*{{cite journal | author=Porter JC, Hogg N |title=Integrins take partners: cross-talk between integrins and other membrane receptors. |journal=Trends Cell Biol. |volume=8 |issue= 10 |pages= 390-6 |year= 1999 |pmid= 9789327 |doi= }}
*{{cite journal | author=Giblin PA, Lemieux RM |title=LFA-1 as a key regulator of immune function: approaches toward the development of LFA-1-based therapeutics. |journal=Curr. Pharm. Des. |volume=12 |issue= 22 |pages= 2771-95 |year= 2006 |pmid= 16918410 |doi= }}
*{{cite journal | author=Maurer D, Holter W, Majdic O, ''et al.'' |title=CD27 expression by a distinct subpopulation of human B lymphocytes. |journal=Eur. J. Immunol. |volume=20 |issue= 12 |pages= 2679-84 |year= 1991 |pmid= 1702722 |doi= }}
*{{cite journal | author=Kalter DC, Gendelman HE, Meltzer MS |title=Inhibition of human immunodeficiency virus infection in monocytes by monoclonal antibodies against leukocyte adhesion molecules. |journal=Immunol. Lett. |volume=30 |issue= 2 |pages= 219-27 |year= 1992 |pmid= 1757107 |doi= }}
*{{cite journal | author=Alvarez V, Pulido R, Campanero MR, ''et al.'' |title=Differentially regulated cell surface expression of leukocyte adhesion receptors on neutrophils. |journal=Kidney Int. |volume=40 |issue= 5 |pages= 899-905 |year= 1992 |pmid= 1762294 |doi= }}
*{{cite journal | author=Valentin A, Lundin K, Patarroyo M, Asjö B |title=The leukocyte adhesion glycoprotein CD18 participates in HIV-1-induced syncytia formation in monocytoid and T cells. |journal=J. Immunol. |volume=144 |issue= 3 |pages= 934-7 |year= 1990 |pmid= 1967280 |doi= }}
*{{cite journal | author=Larson RS, Corbi AL, Berman L, Springer T |title=Primary structure of the leukocyte function-associated molecule-1 alpha subunit: an integrin with an embedded domain defining a protein superfamily. |journal=J. Cell Biol. |volume=108 |issue= 2 |pages= 703-12 |year= 1989 |pmid= 2537322 |doi= }}
*{{cite journal | author=Hildreth JE, Orentas RJ |title=Involvement of a leukocyte adhesion receptor (LFA-1) in HIV-induced syncytium formation. |journal=Science |volume=244 |issue= 4908 |pages= 1075-8 |year= 1989 |pmid= 2543075 |doi= }}
*{{cite journal | author=Sanders ME, Makgoba MW, Sharrow SO, ''et al.'' |title=Human memory T lymphocytes express increased levels of three cell adhesion molecules (LFA-3, CD2, and LFA-1) and three other molecules (UCHL1, CDw29, and Pgp-1) and have enhanced IFN-gamma production. |journal=J. Immunol. |volume=140 |issue= 5 |pages= 1401-7 |year= 1988 |pmid= 2894392 |doi= }}
*{{cite journal | author=Corbi AL, Larson RS, Kishimoto TK, ''et al.'' |title=Chromosomal location of the genes encoding the leukocyte adhesion receptors LFA-1, Mac-1 and p150,95. Identification of a gene cluster involved in cell adhesion. |journal=J. Exp. Med. |volume=167 |issue= 5 |pages= 1597-607 |year= 1988 |pmid= 3284962 |doi= }}
*{{cite journal | author=te Velde AA, Keizer GD, Figdor CG |title=Differential function of LFA-1 family molecules (CD11 and CD18) in adhesion of human monocytes to melanoma and endothelial cells. |journal=Immunology |volume=61 |issue= 3 |pages= 261-7 |year= 1987 |pmid= 3301632 |doi= }}
*{{cite journal | author=Qu A, Leahy DJ |title=Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 22 |pages= 10277-81 |year= 1995 |pmid= 7479767 |doi= }}
*{{cite journal | author=Turner ML, McIlwaine K, Anthony RS, Parker AC |title=Differential expression of cell adhesion molecules by human hematopoietic progenitor cells from bone marrow and mobilized adult peripheral blood. |journal=Stem Cells |volume=13 |issue= 3 |pages= 311-6 |year= 1995 |pmid= 7542116 |doi= }}
*{{cite journal | author=Marzusch K, Ruck P, Geiselhart A, ''et al.'' |title=Distribution of cell adhesion molecules on CD56++, CD3-, CD16- large granular lymphocytes and endothelial cells in first-trimester human decidua. |journal=Hum. Reprod. |volume=8 |issue= 8 |pages= 1203-8 |year= 1993 |pmid= 7691868 |doi= }}
*{{cite journal | author=Capobianchi MR, Ameglio F, Cordiali Fei P, ''et al.'' |title=Coordinate induction of interferon alpha and gamma by recombinant HIV-1 glycoprotein 120. |journal=AIDS Res. Hum. Retroviruses |volume=9 |issue= 10 |pages= 957-62 |year= 1994 |pmid= 7904170 |doi= }}
*{{cite journal | author=Berman PW, Nakamura GR |title=Adhesion mediated by intercellular adhesion molecule 1 attenuates the potency of antibodies that block HIV-1 gp160-dependent syncytium formation. |journal=AIDS Res. Hum. Retroviruses |volume=10 |issue= 5 |pages= 585-93 |year= 1994 |pmid= 7917519 |doi= }}
*{{cite journal | author=Chirmule N, Oyaizu N, Saxinger C, Pahwa S |title=Nef protein of HIV-1 has B-cell stimulatory activity. |journal=AIDS |volume=8 |issue= 6 |pages= 733-4 |year= 1994 |pmid= 8086129 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KCNJ11... {November 12, 2007 7:09:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:10:28 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 =
| image_source =
| PDB =
| Name = Potassium inwardly-rectifying channel, subfamily J, member 11
| HGNCid = 6257
| Symbol = KCNJ11
| AltSymbols =; BIR; HHF2; IKATP; KIR6.2; MGC133230; PHHI; TNDM3
| OMIM = 600937
| ECnumber =
| Homologene = 441
| MGIid = 107501
| Function = {{GNF_GO|id=GO:0005244 |text = voltage-gated ion channel activity}} {{GNF_GO|id=GO:0015272 |text = ATP-activated inward rectifier potassium channel activity}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3767
| Hs_Ensembl = ENSG00000187486
| Hs_RefseqProtein = NP_000516
| Hs_RefseqmRNA = NM_000525
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 17365042
| Hs_GenLoc_end = 17366214
| Hs_Uniprot = Q14654
| Mm_EntrezGene = 16514
| Mm_Ensembl = ENSMUSG00000070561
| Mm_RefseqmRNA = NM_010602
| Mm_RefseqProtein = NP_034732
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 45966767
| Mm_GenLoc_end = 45967939
| Mm_Uniprot = Q8CCI6
}}
}}
'''Potassium inwardly-rectifying channel, subfamily J, member 11''', also known as '''KCNJ11''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, is controlled by G-proteins and is found associated with the sulfonylurea receptor SUR. Mutations in this gene are a cause of familial persistent hyperinsulinemic hypoglycemia of infancy (PHHI), an autosomal recessive disorder characterized by unregulated insulin secretion. Defects in this gene may also contribute to autosomal dominant non-insulin-dependent diabetes mellitus type II (NIDDM).<ref>{{cite web | title = Entrez Gene: KCNJ11 potassium inwardly-rectifying channel, subfamily J, member 11| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3767| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Aguilar-Bryan L, Bryan J |title=Molecular biology of adenosine triphosphate-sensitive potassium channels. |journal=Endocr. Rev. |volume=20 |issue= 2 |pages= 101-35 |year= 1999 |pmid= 10204114 |doi= }}
*{{cite journal | author=Meissner T, Beinbrech B, Mayatepek E |title=Congenital hyperinsulinism: molecular basis of a heterogeneous disease. |journal=Hum. Mutat. |volume=13 |issue= 5 |pages= 351-61 |year= 1999 |pmid= 10338089 |doi= 10.1002/(SICI)1098-1004(1999)13:5<351::AID-HUMU3>3.0.CO;2-R }}
*{{cite journal | author=Kubo Y, Adelman JP, Clapham DE, ''et al.'' |title=International Union of Pharmacology. LIV. Nomenclature and molecular relationships of inwardly rectifying potassium channels. |journal=Pharmacol. Rev. |volume=57 |issue= 4 |pages= 509-26 |year= 2006 |pmid= 16382105 |doi= 10.1124/pr.57.4.11 }}
*{{cite journal | author=Gloyn AL, Siddiqui J, Ellard S |title=Mutations in the genes encoding the pancreatic beta-cell KATP channel subunits Kir6.2 (KCNJ11) and SUR1 (ABCC8) in diabetes mellitus and hyperinsulinism. |journal=Hum. Mutat. |volume=27 |issue= 3 |pages= 220-31 |year= 2006 |pmid= 16416420 |doi= 10.1002/humu.20292 }}
*{{cite journal | author=Flechtner I, de Lonlay P, Polak M |title=Diabetes and hypoglycaemia in young children and mutations in the Kir6.2 subunit of the potassium channel: therapeutic consequences. |journal=Diabetes Metab. |volume=32 |issue= 6 |pages= 569-80 |year= 2007 |pmid= 17296510 |doi= 10.1016/S1262-3636(07)70311-7 }}
*{{cite journal | author=Inagaki N, Gonoi T, Clement JP, ''et al.'' |title=Reconstitution of IKATP: an inward rectifier subunit plus the sulfonylurea receptor. |journal=Science |volume=270 |issue= 5239 |pages= 1166-70 |year= 1996 |pmid= 7502040 |doi= }}
*{{cite journal | author=Thomas PM, Cote GJ, Hallman DM, Mathew PM |title=Homozygosity mapping, to chromosome 11p, of the gene for familial persistent hyperinsulinemic hypoglycemia of infancy. |journal=Am. J. Hum. Genet. |volume=56 |issue= 2 |pages= 416-21 |year= 1995 |pmid= 7847376 |doi= }}
*{{cite journal | author=Iwasaki N, Kawamura M, Yamagata K, ''et al.'' |title=Identification of microsatellite markers near the human genes encoding the beta-cell ATP-sensitive K+ channel and linkage studies with NIDDM in Japanese. |journal=Diabetes |volume=45 |issue= 2 |pages= 267-9 |year= 1996 |pmid= 8549873 |doi= }}
*{{cite journal | author=Sakura H, Wat N, Horton V, ''et al.'' |title=Sequence variations in the human Kir6.2 gene, a subunit of the beta-cell ATP-sensitive K-channel: no association with NIDDM in while Caucasian subjects or evidence of abnormal function when expressed in vitro. |journal=Diabetologia |volume=39 |issue= 10 |pages= 1233-6 |year= 1997 |pmid= 8897013 |doi= }}
*{{cite journal | author=Thomas P, Ye Y, Lightner E |title=Mutation of the pancreatic islet inward rectifier Kir6.2 also leads to familial persistent hyperinsulinemic hypoglycemia of infancy. |journal=Hum. Mol. Genet. |volume=5 |issue= 11 |pages= 1809-12 |year= 1997 |pmid= 8923010 |doi= }}
*{{cite journal | author=Inoue H, Ferrer J, Warren-Perry M, ''et al.'' |title=Sequence variants in the pancreatic islet beta-cell inwardly rectifying K+ channel Kir6.2 (Bir) gene: identification and lack of role in Caucasian patients with NIDDM. |journal=Diabetes |volume=46 |issue= 3 |pages= 502-7 |year= 1997 |pmid= 9032109 |doi= }}
*{{cite journal | author=Tucker SJ, Gribble FM, Zhao C, ''et al.'' |title=Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor. |journal=Nature |volume=387 |issue= 6629 |pages= 179-83 |year= 1997 |pmid= 9144288 |doi= 10.1038/387179a0 }}
*{{cite journal | author=Halushka MK, Fan JB, Bentley K, ''et al.'' |title=Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 239-47 |year= 1999 |pmid= 10391210 |doi= 10.1038/10297 }}
*{{cite journal | author=Tucker SJ, Ashcroft FM |title=Mapping of the physical interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2. |journal=J. Biol. Chem. |volume=274 |issue= 47 |pages= 33393-7 |year= 1999 |pmid= 10559219 |doi= }}
*{{cite journal | author=Cui Y, Giblin JP, Clapp LH, Tinker A |title=A mechanism for ATP-sensitive potassium channel diversity: Functional coassembly of two pore-forming subunits. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 2 |pages= 729-34 |year= 2001 |pmid= 11136227 |doi= 10.1073/pnas.011370498 }}
*{{cite journal | author=Giblin JP, Cui Y, Clapp LH, Tinker A |title=Assembly limits the pharmacological complexity of ATP-sensitive potassium channels. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 13717-23 |year= 2002 |pmid= 11825905 |doi= 10.1074/jbc.M112209200 }}
*{{cite journal | author=Crawford RM, Budas GR, Jovanović S, ''et al.'' |title=M-LDH serves as a sarcolemmal K(ATP) channel subunit essential for cell protection against ischemia. |journal=EMBO J. |volume=21 |issue= 15 |pages= 3936-48 |year= 2002 |pmid= 12145195 |doi= 10.1093/emboj/cdf388 }}
*{{cite journal | author=Tschritter O, Stumvoll M, Machicao F, ''et al.'' |title=The prevalent Glu23Lys polymorphism in the potassium inward rectifier 6.2 (KIR6.2) gene is associated with impaired glucagon suppression in response to hyperglycemia. |journal=Diabetes |volume=51 |issue= 9 |pages= 2854-60 |year= 2002 |pmid= 12196481 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KNG1... {November 12, 2007 7:10:28 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:11:27 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 = Kininogen 1
| HGNCid = 6383
| Symbol = KNG1
| AltSymbols =; BDK; KNG
| OMIM = 228960
| ECnumber =
| Homologene = 88343
| MGIid = 3027157
| GeneAtlas_image1 = PBB_GE_KNG1_206054_at_tn.png
| GeneAtlas_image2 = PBB_GE_KNG1_217512_at_tn.png
| Function = {{GNF_GO|id=GO:0004869 |text = cysteine protease inhibitor activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0006939 |text = smooth muscle contraction}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007162 |text = negative regulation of cell adhesion}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0030146 |text = diuresis}} {{GNF_GO|id=GO:0030147 |text = natriuresis}} {{GNF_GO|id=GO:0030195 |text = negative regulation of blood coagulation}} {{GNF_GO|id=GO:0042311 |text = vasodilation}} {{GNF_GO|id=GO:0043065 |text = positive regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3827
| Hs_Ensembl = ENSG00000113889
| Hs_RefseqProtein = NP_000884
| Hs_RefseqmRNA = NM_000893
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 187917814
| Hs_GenLoc_end = 187944435
| Hs_Uniprot = P01042
| Mm_EntrezGene = 385643
| Mm_Ensembl = ENSMUSG00000060459
| Mm_RefseqmRNA = XM_989028
| Mm_RefseqProtein = XP_994122
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 22902680
| Mm_GenLoc_end = 22944351
| Mm_Uniprot =
}}
}}
'''Kininogen 1''', also known as '''KNG1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Iarovaia GA |title=[Kallikrein-kinin system: novel facts and concepts (literature review)] |journal=Vopr. Med. Khim. |volume=47 |issue= 1 |pages= 20-42 |year= 2001 |pmid= 11385996 |doi= }}
*{{cite journal | author=Matthews KW, Mueller-Ortiz SL, Wetsel RA |title=Carboxypeptidase N: a pleiotropic regulator of inflammation. |journal=Mol. Immunol. |volume=40 |issue= 11 |pages= 785-93 |year= 2004 |pmid= 14687935 |doi= }}
*{{cite journal | author=Scharfstein J, Schmitz V, Svensjö E, ''et al.'' |title=Kininogens coordinate adaptive immunity through the proteolytic release of bradykinin, an endogenous danger signal driving dendritic cell maturation. |journal=Scand. J. Immunol. |volume=66 |issue= 2-3 |pages= 128-36 |year= 2007 |pmid= 17635790 |doi= 10.1111/j.1365-3083.2007.01983.x }}
*{{cite journal | author=Thompson RE, Mandle R, Kaplan AP |title=Studies of binding of prekallikrein and Factor XI to high molecular weight kininogen and its light chain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=76 |issue= 10 |pages= 4862-6 |year= 1980 |pmid= 291905 |doi= }}
*{{cite journal | author=Kerbiriou DM, Griffin JH |title=Human high molecular weight kininogen. Studies of structure-function relationships and of proteolysis of the molecule occurring during contact activation of plasma. |journal=J. Biol. Chem. |volume=254 |issue= 23 |pages= 12020-7 |year= 1980 |pmid= 500690 |doi= }}
*{{cite journal | author=Colman RW, Bagdasarian A, Talamo RC, ''et al.'' |title=Williams trait. Human kininogen deficiency with diminished levels of plasminogen proactivator and prekallikrein associated with abnormalities of the Hageman factor-dependent pathways. |journal=J. Clin. Invest. |volume=56 |issue= 6 |pages= 1650-62 |year= 1976 |pmid= 1202089 |doi= }}
*{{cite journal | author=Gailani D, Broze GJ |title=Factor XI activation in a revised model of blood coagulation. |journal=Science |volume=253 |issue= 5022 |pages= 909-12 |year= 1991 |pmid= 1652157 |doi= }}
*{{cite journal | author=Cheung PP, Cannizzaro LA, Colman RW |title=Chromosomal mapping of human kininogen gene (KNG) to 3q26----qter. |journal=Cytogenet. Cell Genet. |volume=59 |issue= 1 |pages= 24-6 |year= 1992 |pmid= 1733668 |doi= }}
*{{cite journal | author=Fong D, Smith DI, Hsieh WT |title=The human kininogen gene (KNG) mapped to chromosome 3q26-qter by analysis of somatic cell hybrids using the polymerase chain reaction. |journal=Hum. Genet. |volume=87 |issue= 2 |pages= 189-92 |year= 1991 |pmid= 2066106 |doi= }}
*{{cite journal | author=Schmaier AH, Kuo A, Lundberg D, ''et al.'' |title=The expression of high molecular weight kininogen on human umbilical vein endothelial cells. |journal=J. Biol. Chem. |volume=263 |issue= 31 |pages= 16327-33 |year= 1988 |pmid= 2460446 |doi= }}
*{{cite journal | author=Takagaki Y, Kitamura N, Nakanishi S |title=Cloning and sequence analysis of cDNAs for human high molecular weight and low molecular weight prekininogens. Primary structures of two human prekininogens. |journal=J. Biol. Chem. |volume=260 |issue= 14 |pages= 8601-9 |year= 1985 |pmid= 2989293 |doi= }}
*{{cite journal | author=Kitamura N, Kitagawa H, Fukushima D, ''et al.'' |title=Structural organization of the human kininogen gene and a model for its evolution. |journal=J. Biol. Chem. |volume=260 |issue= 14 |pages= 8610-7 |year= 1985 |pmid= 2989294 |doi= }}
*{{cite journal | author=Ishiguro H, Higashiyama S, Namikawa C, ''et al.'' |title=Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: mechanism of interaction and the role of divalent cations. |journal=Biochemistry |volume=26 |issue= 10 |pages= 2863-70 |year= 1987 |pmid= 3038169 |doi= }}
*{{cite journal | author=Vogel R, Assfalg-Machleidt I, Esterl A, ''et al.'' |title=Proteinase-sensitive regions in the heavy chain of low molecular weight kininogen map to the inter-domain junctions. |journal=J. Biol. Chem. |volume=263 |issue= 25 |pages= 12661-8 |year= 1988 |pmid= 3045123 |doi= }}
*{{cite journal | author=Maeda H, Matsumura Y, Kato H |title=Purification and identification of [hydroxyprolyl3]bradykinin in ascitic fluid from a patient with gastric cancer. |journal=J. Biol. Chem. |volume=263 |issue= 31 |pages= 16051-4 |year= 1988 |pmid= 3182782 |doi= }}
*{{cite journal | author=Kato H, Matsumura Y, Maeda H |title=Isolation and identification of hydroxyproline analogues of bradykinin in human urine. |journal=FEBS Lett. |volume=232 |issue= 1 |pages= 252-4 |year= 1988 |pmid= 3366244 |doi= }}
*{{cite journal | author=Kellermann J, Lottspeich F, Henschen A, Müller-Esterl W |title=Completion of the primary structure of human high-molecular-mass kininogen. The amino acid sequence of the entire heavy chain and evidence for its evolution by gene triplication. |journal=Eur. J. Biochem. |volume=154 |issue= 2 |pages= 471-8 |year= 1986 |pmid= 3484703 |doi= }}
*{{cite journal | author=Kellermann J, Thelen C, Lottspeich F, ''et al.'' |title=Arrangement of the disulphide bridges in human low-Mr kininogen. |journal=Biochem. J. |volume=247 |issue= 1 |pages= 15-21 |year= 1988 |pmid= 3689342 |doi= }}
*{{cite journal | author=Warn-Cramer BJ, Bajaj SP |title=Stoichiometry of binding of high molecular weight kininogen to factor XI/XIa. |journal=Biochem. Biophys. Res. Commun. |volume=133 |issue= 2 |pages= 417-22 |year= 1986 |pmid= 3936495 |doi= }}
*{{cite journal | author=Lottspeich F, Kellermann J, Henschen A, ''et al.'' |title=The amino acid sequence of the light chain of human high-molecular-mass kininogen. |journal=Eur. J. Biochem. |volume=152 |issue= 2 |pages= 307-14 |year= 1985 |pmid= 4054110 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MC1R... {November 12, 2007 7:11:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:12:03 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 = Melanocortin 1 receptor (alpha melanocyte stimulating hormone receptor)
| HGNCid = 6929
| Symbol = MC1R
| AltSymbols =; MGC14337; MSH-R
| OMIM = 155555
| ECnumber =
| Homologene = 1789
| MGIid = 99456
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004980 |text = melanocyte stimulating hormone receptor activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0015630 |text = microtubule cytoskeleton}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007187 |text = G-protein signaling, coupled to cyclic nucleotide second messenger}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0009650 |text = UV protection}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4157
| Hs_Ensembl =
| Hs_RefseqProtein = NP_002377
| Hs_RefseqmRNA = NM_002386
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 17199
| Mm_Ensembl = ENSMUSG00000074037
| Mm_RefseqmRNA = NM_008559
| Mm_RefseqProtein = NP_032585
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 126293586
| Mm_GenLoc_end = 126294846
| Mm_Uniprot = Q75NA2
}}
}}
'''Melanocortin 1 receptor (alpha melanocyte stimulating hormone receptor)''', also known as '''MC1R''', is a human [[gene]].
<!-- 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 intronless gene encodes the receptor protein for melanocyte-stimulating hormone (MSH). The encoded protein, a seven pass transmembrane G protein coupled receptor, controls melanogenesis. Two types of melanin exist: red pheomelanin and black eumelanin. Gene mutations that lead to a loss in function are associated with increased pheomelanin production, which leads to lighter skin and hair color. Eumelanin is photoprotective but pheomelanin may contribute to UV-induced skin damage by generating free radicals upon UV radiation. Binding of MSH to its receptor activates the receptor and stimulates eumelanin synthesis. This receptor is a major determining factor in sun sensitivity and is a genetic risk factor for melanoma and non-melanoma skin cancer. Over 30 variant alleles have been identified which correlate with skin and hair color, providing evidence that this gene is an important component in determining normal human pigment variation.<ref>{{cite web | title = Entrez Gene: MC1R melanocortin 1 receptor (alpha melanocyte stimulating hormone receptor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4157| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Venter JC |title=Identification of new human receptor and transporter genes by high throughput cDNA (EST) sequencing. |journal=J. Pharm. Pharmacol. |volume=45 Suppl 1 |issue= |pages= 355-60 |year= 1993 |pmid= 8098743 |doi= }}
*{{cite journal | author=Abdel-Malek Z, Suzuki I, Tada A, ''et al.'' |title=The melanocortin-1 receptor and human pigmentation. |journal=Ann. N. Y. Acad. Sci. |volume=885 |issue= |pages= 117-33 |year= 2000 |pmid= 10816645 |doi= }}
*{{cite journal | author=Rees JL |title=The melanocortin 1 receptor (MC1R): more than just red hair. |journal=Pigment Cell Res. |volume=13 |issue= 3 |pages= 135-40 |year= 2000 |pmid= 10885670 |doi= }}
*{{cite journal | author=Sturm RA, Duffy DL, Box NF, ''et al.'' |title=The role of melanocortin-1 receptor polymorphism in skin cancer risk phenotypes. |journal=Pigment Cell Res. |volume=16 |issue= 3 |pages= 266-72 |year= 2004 |pmid= 12753400 |doi= }}
*{{cite journal | author=Mountjoy KG, Robbins LS, Mortrud MT, Cone RD |title=The cloning of a family of genes that encode the melanocortin receptors. |journal=Science |volume=257 |issue= 5074 |pages= 1248-51 |year= 1992 |pmid= 1325670 |doi= }}
*{{cite journal | author=Chhajlani V, Wikberg JE |title=Molecular cloning and expression of the human melanocyte stimulating hormone receptor cDNA. |journal=FEBS Lett. |volume=309 |issue= 3 |pages= 417-20 |year= 1992 |pmid= 1516719 |doi= }}
*{{cite journal | author=Valverde P, Healy E, Jackson I, ''et al.'' |title=Variants of the melanocyte-stimulating hormone receptor gene are associated with red hair and fair skin in humans. |journal=Nat. Genet. |volume=11 |issue= 3 |pages= 328-30 |year= 1995 |pmid= 7581459 |doi= 10.1038/ng1195-328 }}
*{{cite journal | author=Magenis RE, Smith L, Nadeau JH, ''et al.'' |title=Mapping of the ACTH, MSH, and neural (MC3 and MC4) melanocortin receptors in the mouse and human. |journal=Mamm. Genome |volume=5 |issue= 8 |pages= 503-8 |year= 1994 |pmid= 7949735 |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=Gantz I, Yamada T, Tashiro T, ''et al.'' |title=Mapping of the gene encoding the melanocortin-1 (alpha-melanocyte stimulating hormone) receptor (MC1R) to human chromosome 16q24.3 by Fluorescence in situ hybridization. |journal=Genomics |volume=19 |issue= 2 |pages= 394-5 |year= 1994 |pmid= 8188275 |doi= 10.1006/geno.1994.1080 }}
*{{cite journal | author=Robbins LS, Nadeau JH, Johnson KR, ''et al.'' |title=Pigmentation phenotypes of variant extension locus alleles result from point mutations that alter MSH receptor function. |journal=Cell |volume=72 |issue= 6 |pages= 827-34 |year= 1993 |pmid= 8458079 |doi= }}
*{{cite journal | author=Gantz I, Konda Y, Tashiro T, ''et al.'' |title=Molecular cloning of a novel melanocortin receptor. |journal=J. Biol. Chem. |volume=268 |issue= 11 |pages= 8246-50 |year= 1993 |pmid= 8463333 |doi= }}
*{{cite journal | author=Chhajlani V, Xu X, Blauw J, Sudarshi S |title=Identification of ligand binding residues in extracellular loops of the melanocortin 1 receptor. |journal=Biochem. Biophys. Res. Commun. |volume=219 |issue= 2 |pages= 521-5 |year= 1996 |pmid= 8605020 |doi= 10.1006/bbrc.1996.0266 }}
*{{cite journal | author=Chhajlani V, Wikberg JE |title=Molecular cloning and expression of the human melanocyte stimulating hormone receptor cDNA (FEBS 11553). |journal=FEBS Lett. |volume=390 |issue= 2 |pages= 238 |year= 1996 |pmid= 8706868 |doi= }}
*{{cite journal | author=Valverde P, Healy E, Sikkink S, ''et al.'' |title=The Asp84Glu variant of the melanocortin 1 receptor (MC1R) is associated with melanoma. |journal=Hum. Mol. Genet. |volume=5 |issue= 10 |pages= 1663-6 |year= 1997 |pmid= 8894704 |doi= }}
*{{cite journal | author=Koppula SV, Robbins LS, Lu D, ''et al.'' |title=Identification of common polymorphisms in the coding sequence of the human MSH receptor (MCIR) with possible biological effects. |journal=Hum. Mutat. |volume=9 |issue= 1 |pages= 30-6 |year= 1997 |pmid= 8990005 |doi= 10.1002/(SICI)1098-1004(1997)9:1<30::AID-HUMU5>3.0.CO;2-T }}
*{{cite journal | author=Haskell-Luevano C, Sawyer TK, Trumpp-Kallmeyer S, ''et al.'' |title=Three-dimensional molecular models of the hMC1R melanocortin receptor: complexes with melanotropin peptide agonists. |journal=Drug design and discovery |volume=14 |issue= 3 |pages= 197-211 |year= 1997 |pmid= 9017363 |doi= }}
*{{cite journal | author=Yang YK, Ollmann MM, Wilson BD, ''et al.'' |title=Effects of recombinant agouti-signaling protein on melanocortin action. |journal=Mol. Endocrinol. |volume=11 |issue= 3 |pages= 274-80 |year= 1997 |pmid= 9058374 |doi= }}
*{{cite journal | author=Box NF, Wyeth JR, O'Gorman LE, ''et al.'' |title=Characterization of melanocyte stimulating hormone receptor variant alleles in twins with red hair. |journal=Hum. Mol. Genet. |volume=6 |issue= 11 |pages= 1891-7 |year= 1998 |pmid= 9302268 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NCK1... {November 12, 2007 7:12:03 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:12:50 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_NCK1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2ci8.
| PDB = {{PDB2|2ci8}}, {{PDB2|2ci9}}, {{PDB2|2cub}}
| Name = NCK adaptor protein 1
| HGNCid = 7664
| Symbol = NCK1
| AltSymbols =; MGC12668; NCK; NCKalpha
| OMIM = 600508
| ECnumber =
| Homologene = 38148
| MGIid = 109601
| GeneAtlas_image1 = PBB_GE_NCK1_204725_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NCK1_211063_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0008093 |text = cytoskeletal adaptor activity}} {{GNF_GO|id=GO:0030159 |text = receptor signaling complex scaffold activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0012506 |text = vesicle membrane}}
| Process = {{GNF_GO|id=GO:0007015 |text = actin filament organization}} {{GNF_GO|id=GO:0007172 |text = signal complex assembly}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0016477 |text = cell migration}} {{GNF_GO|id=GO:0030032 |text = lamellipodium biogenesis}} {{GNF_GO|id=GO:0030838 |text = positive regulation of actin filament polymerization}} {{GNF_GO|id=GO:0042102 |text = positive regulation of T cell proliferation}} {{GNF_GO|id=GO:0042110 |text = T cell activation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4690
| Hs_Ensembl = ENSG00000158092
| Hs_RefseqProtein = NP_006144
| Hs_RefseqmRNA = NM_006153
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 138063763
| Hs_GenLoc_end = 138150657
| Hs_Uniprot = P16333
| Mm_EntrezGene = 17973
| Mm_Ensembl = ENSMUSG00000032475
| Mm_RefseqmRNA = NM_010878
| Mm_RefseqProtein = NP_035008
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 100304355
| Mm_GenLoc_end = 100355405
| Mm_Uniprot =
}}
}}
'''NCK adaptor protein 1''', also known as '''NCK1''', is a human [[gene]].
<!-- 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 one of the signaling and transforming proteins containing Src homology 2 and 3 (SH2 and SH3) domains. It is located in the cytoplasm and is an adaptor protein involved in transducing signals from receptor tyrosine kinases to downstream signal recipients such as RAS.<ref>{{cite web | title = Entrez Gene: NCK1 NCK adaptor protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4690| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Iwata S, Ohashi Y, Kamiguchi K, Morimoto C |title=Beta 1-integrin-mediated cell signaling in T lymphocytes. |journal=J. Dermatol. Sci. |volume=23 |issue= 2 |pages= 75-86 |year= 2000 |pmid= 10808124 |doi= }}
*{{cite journal | author=Park D, Rhee SG |title=Phosphorylation of Nck in response to a variety of receptors, phorbol myristate acetate, and cyclic AMP. |journal=Mol. Cell. Biol. |volume=12 |issue= 12 |pages= 5816-23 |year= 1992 |pmid= 1333046 |doi= }}
*{{cite journal | author=Meisenhelder J, Hunter T |title=The SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatment. |journal=Mol. Cell. Biol. |volume=12 |issue= 12 |pages= 5843-56 |year= 1992 |pmid= 1448108 |doi= }}
*{{cite journal | author=Lehmann JM, Riethmüller G, Johnson JP |title=Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the src homology units SH2 and SH3. |journal=Nucleic Acids Res. |volume=18 |issue= 4 |pages= 1048 |year= 1990 |pmid= 2107526 |doi= }}
*{{cite journal | author=Rivero-Lezcano OM, Sameshima JH, Marcilla A, Robbins KC |title=Physical association between Src homology 3 elements and the protein product of the c-cbl proto-oncogene. |journal=J. Biol. Chem. |volume=269 |issue= 26 |pages= 17363-6 |year= 1994 |pmid= 7517397 |doi= }}
*{{cite journal | author=Rivero-Lezcano OM, Marcilla A, Sameshima JH, Robbins KC |title=Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains. |journal=Mol. Cell. Biol. |volume=15 |issue= 10 |pages= 5725-31 |year= 1995 |pmid= 7565724 |doi= }}
*{{cite journal | author=Chou MM, Hanafusa H |title=A novel ligand for SH3 domains. The Nck adaptor protein binds to a serine/threonine kinase via an SH3 domain. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7359-64 |year= 1995 |pmid= 7706279 |doi= }}
*{{cite journal | author=Huebner K, Kastury K, Druck T, ''et al.'' |title=Chromosome locations of genes encoding human signal transduction adapter proteins, Nck (NCK), Shc (SHC1), and Grb2 (GRB2). |journal=Genomics |volume=22 |issue= 2 |pages= 281-7 |year= 1995 |pmid= 7806213 |doi= }}
*{{cite journal | author=Hu Q, Milfay D, Williams LT |title=Binding of NCK to SOS and activation of ras-dependent gene expression. |journal=Mol. Cell. Biol. |volume=15 |issue= 3 |pages= 1169-74 |year= 1995 |pmid= 7862111 |doi= }}
*{{cite journal | author=Vorobieva N, Protopopov A, Protopopova M, ''et al.'' |title=Localization of human ARF2 and NCK genes and 13 other NotI-linking clones to chromosome 3 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=68 |issue= 1-2 |pages= 91-4 |year= 1994 |pmid= 7956370 |doi= }}
*{{cite journal | author=Kitamura T, Kitamura Y, Yonezawa K, ''et al.'' |title=Molecular cloning of p125Nap1, a protein that associates with an SH3 domain of Nck. |journal=Biochem. Biophys. Res. Commun. |volume=219 |issue= 2 |pages= 509-14 |year= 1996 |pmid= 8605018 |doi= }}
*{{cite journal | author=Okada S, Pessin JE |title=Interactions between Src homology (SH) 2/SH3 adapter proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor. |journal=J. Biol. Chem. |volume=271 |issue= 41 |pages= 25533-8 |year= 1996 |pmid= 8810325 |doi= }}
*{{cite journal | author=Bokoch GM, Wang Y, Bohl BP, ''et al.'' |title=Interaction of the Nck adapter protein with p21-activated kinase (PAK1). |journal=J. Biol. Chem. |volume=271 |issue= 42 |pages= 25746-9 |year= 1996 |pmid= 8824201 |doi= }}
*{{cite journal | author=Minegishi M, Tachibana K, Sato T, ''et al.'' |title=Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes. |journal=J. Exp. Med. |volume=184 |issue= 4 |pages= 1365-75 |year= 1996 |pmid= 8879209 |doi= }}
*{{cite journal | author=Roche S, McGlade J, Jones M, ''et al.'' |title=Requirement of phospholipase C gamma, the tyrosine phosphatase Syp and the adaptor proteins Shc and Nck for PDGF-induced DNA synthesis: evidence for the existence of Ras-dependent and Ras-independent pathways. |journal=EMBO J. |volume=15 |issue= 18 |pages= 4940-8 |year= 1996 |pmid= 8890167 |doi= }}
*{{cite journal | author=Quilliam LA, Lambert QT, Mickelson-Young LA, ''et al.'' |title=Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling. |journal=J. Biol. Chem. |volume=271 |issue= 46 |pages= 28772-6 |year= 1997 |pmid= 8910519 |doi= }}
*{{cite journal | author=Lussier G, Larose L |title=A casein kinase I activity is constitutively associated with Nck. |journal=J. Biol. Chem. |volume=272 |issue= 5 |pages= 2688-94 |year= 1997 |pmid= 9006905 |doi= }}
*{{cite journal | author=Lawe DC, Hahn C, Wong AJ |title=The Nck SH2/SH3 adaptor protein is present in the nucleus and associates with the nuclear protein SAM68. |journal=Oncogene |volume=14 |issue= 2 |pages= 223-31 |year= 1997 |pmid= 9010224 |doi= 10.1038/sj.onc.1200821 }}
*{{cite journal | author=Lu W, Katz S, Gupta R, Mayer BJ |title=Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck. |journal=Curr. Biol. |volume=7 |issue= 2 |pages= 85-94 |year= 1997 |pmid= 9024622 |doi= }}
*{{cite journal | author=Su YC, Han J, Xu S, ''et al.'' |title=NIK is a new Ste20-related kinase that binds NCK and MEKK1 and activates the SAPK/JNK cascade via a conserved regulatory domain. |journal=EMBO J. |volume=16 |issue= 6 |pages= 1279-90 |year= 1997 |pmid= 9135144 |doi= 10.1093/emboj/16.6.1279 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PECAM1... {November 12, 2007 7:13:28 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:14:07 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 = Platelet/endothelial cell adhesion molecule (CD31 antigen)
| HGNCid = 8823
| Symbol = PECAM1
| AltSymbols =; CD31; PECAM-1
| OMIM = 173445
| ECnumber =
| Homologene = 47925
| MGIid = 97537
| GeneAtlas_image1 = PBB_GE_PECAM1_208982_at_tn.png
| GeneAtlas_image2 = PBB_GE_PECAM1_208981_at_tn.png
| GeneAtlas_image3 = PBB_GE_PECAM1_208983_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005911 |text = intercellular junction}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0045121 |text = lipid raft}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007266 |text = Rho protein signal transduction}} {{GNF_GO|id=GO:0008037 |text = cell recognition}} {{GNF_GO|id=GO:0030334 |text = regulation of cell migration}} {{GNF_GO|id=GO:0042060 |text = wound healing}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5175
| Hs_Ensembl = ENSG00000198802
| Hs_RefseqProtein = NP_000433
| Hs_RefseqmRNA = NM_000442
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 59754404
| Hs_GenLoc_end = 59794504
| Hs_Uniprot = P16284
| Mm_EntrezGene = 18613
| Mm_Ensembl = ENSMUSG00000020717
| Mm_RefseqmRNA = NM_001032378
| Mm_RefseqProtein = NP_001027550
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 106470307
| Mm_GenLoc_end = 106566718
| Mm_Uniprot = Q8CAW4
}}
}}
'''Platelet/endothelial cell adhesion molecule (CD31 antigen)''', also known as '''PECAM1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Jackson DE |title=The unfolding tale of PECAM-1. |journal=FEBS Lett. |volume=540 |issue= 1-3 |pages= 7-14 |year= 2003 |pmid= 12681475 |doi= }}
*{{cite journal | author=Newman PJ, Newman DK |title=Signal transduction pathways mediated by PECAM-1: new roles for an old molecule in platelet and vascular cell biology. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=23 |issue= 6 |pages= 953-64 |year= 2004 |pmid= 12689916 |doi= 10.1161/01.ATV.0000071347.69358.D9 }}
*{{cite journal | author=Ilan N, Madri JA |title=PECAM-1: old friend, new partners. |journal=Curr. Opin. Cell Biol. |volume=15 |issue= 5 |pages= 515-24 |year= 2004 |pmid= 14519385 |doi= }}
*{{cite journal | author=Wong MX, Jackson DE |title=Regulation of B cell activation by PECAM-1: implications for the development of autoimmune disorders. |journal=Curr. Pharm. Des. |volume=10 |issue= 2 |pages= 155-61 |year= 2004 |pmid= 14754395 |doi= }}
*{{cite journal | author=Kalinowska A, Losy J |title=PECAM-1, a key player in neuroinflammation. |journal=Eur. J. Neurol. |volume=13 |issue= 12 |pages= 1284-90 |year= 2007 |pmid= 17116209 |doi= 10.1111/j.1468-1331.2006.01640.x }}
*{{cite journal | author=Newman PJ, Berndt MC, Gorski J, ''et al.'' |title=PECAM-1 (CD31) cloning and relation to adhesion molecules of the immunoglobulin gene superfamily. |journal=Science |volume=247 |issue= 4947 |pages= 1219-22 |year= 1990 |pmid= 1690453 |doi= }}
*{{cite journal | author=Stockinger H, Gadd SJ, Eher R, ''et al.'' |title=Molecular characterization and functional analysis of the leukocyte surface protein CD31. |journal=J. Immunol. |volume=145 |issue= 11 |pages= 3889-97 |year= 1991 |pmid= 1700999 |doi= }}
*{{cite journal | author=Albelda SM, Muller WA, Buck CA, Newman PJ |title=Molecular and cellular properties of PECAM-1 (endoCAM/CD31): a novel vascular cell-cell adhesion molecule. |journal=J. Cell Biol. |volume=114 |issue= 5 |pages= 1059-68 |year= 1991 |pmid= 1874786 |doi= }}
*{{cite journal | author=Simmons DL, Walker C, Power C, Pigott R |title=Molecular cloning of CD31, a putative intercellular adhesion molecule closely related to carcinoembryonic antigen. |journal=J. Exp. Med. |volume=171 |issue= 6 |pages= 2147-52 |year= 1990 |pmid= 2351935 |doi= }}
*{{cite journal | author=Kirschbaum NE, Gumina RJ, Newman PJ |title=Organization of the gene for human platelet/endothelial cell adhesion molecule-1 shows alternatively spliced isoforms and a functionally complex cytoplasmic domain. |journal=Blood |volume=84 |issue= 12 |pages= 4028-37 |year= 1995 |pmid= 7994021 |doi= }}
*{{cite journal | author=Tang DG, Chen YQ, Newman PJ, ''et al.'' |title=Identification of PECAM-1 in solid tumor cells and its potential involvement in tumor cell adhesion to endothelium. |journal=J. Biol. Chem. |volume=268 |issue= 30 |pages= 22883-94 |year= 1993 |pmid= 8226797 |doi= }}
*{{cite journal | author=Behar E, Chao NJ, Hiraki DD, ''et al.'' |title=Polymorphism of adhesion molecule CD31 and its role in acute graft-versus-host disease. |journal=N. Engl. J. Med. |volume=334 |issue= 5 |pages= 286-91 |year= 1996 |pmid= 8532023 |doi= }}
*{{cite journal | author=Gumina RJ, Kirschbaum NE, Rao PN, ''et al.'' |title=The human PECAM1 gene maps to 17q23. |journal=Genomics |volume=34 |issue= 2 |pages= 229-32 |year= 1997 |pmid= 8661055 |doi= 10.1006/geno.1996.0272 }}
*{{cite journal | author=Lu TT, Yan LG, Madri JA |title=Integrin engagement mediates tyrosine dephosphorylation on platelet-endothelial cell adhesion molecule 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 21 |pages= 11808-13 |year= 1996 |pmid= 8876219 |doi= }}
*{{cite journal | author=Almendro N, Bellón T, Rius C, ''et al.'' |title=Cloning of the human platelet endothelial cell adhesion molecule-1 promoter and its tissue-specific expression. Structural and functional characterization. |journal=J. Immunol. |volume=157 |issue= 12 |pages= 5411-21 |year= 1997 |pmid= 8955189 |doi= }}
*{{cite journal | author=Jackson DE, Ward CM, Wang R, Newman PJ |title=The protein-tyrosine phosphatase SHP-2 binds platelet/endothelial cell adhesion molecule-1 (PECAM-1) and forms a distinct signaling complex during platelet aggregation. Evidence for a mechanistic link between PECAM-1- and integrin-mediated cellular signaling. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6986-93 |year= 1997 |pmid= 9054388 |doi= }}
*{{cite journal | author=Famiglietti J, Sun J, DeLisser HM, Albelda SM |title=Tyrosine residue in exon 14 of the cytoplasmic domain of platelet endothelial cell adhesion molecule-1 (PECAM-1/CD31) regulates ligand binding specificity. |journal=J. Cell Biol. |volume=138 |issue= 6 |pages= 1425-35 |year= 1997 |pmid= 9298995 |doi= }}
*{{cite journal | author=Deaglio S, Morra M, Mallone R, ''et al.'' |title=Human CD38 (ADP-ribosyl cyclase) is a counter-receptor of CD31, an Ig superfamily member. |journal=J. Immunol. |volume=160 |issue= 1 |pages= 395-402 |year= 1998 |pmid= 9551996 |doi= }}
*{{cite journal | author=Coukos G, Makrigiannakis A, Amin K, ''et al.'' |title=Platelet-endothelial cell adhesion molecule-1 is expressed by a subpopulation of human trophoblasts: a possible mechanism for trophoblast-endothelial interaction during haemochorial placentation. |journal=Mol. Hum. Reprod. |volume=4 |issue= 4 |pages= 357-67 |year= 1999 |pmid= 9620836 |doi= }}
*{{cite journal | author=Cao MY, Huber M, Beauchemin N, ''et al.'' |title=Regulation of mouse PECAM-1 tyrosine phosphorylation by the Src and Csk families of protein-tyrosine kinases. |journal=J. Biol. Chem. |volume=273 |issue= 25 |pages= 15765-72 |year= 1998 |pmid= 9624175 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RPS6KA1... {November 12, 2007 7:14:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:14:58 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 =
| image_source =
| PDB =
| Name = Ribosomal protein S6 kinase, 90kDa, polypeptide 1
| HGNCid = 10430
| Symbol = RPS6KA1
| AltSymbols =; HU-1; MAPKAPK1A; RSK; RSK1; S6K-alpha 1
| OMIM = 601684
| ECnumber =
| Homologene = 55703
| MGIid = 104558
| GeneAtlas_image1 = PBB_GE_RPS6KA1_203379_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:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{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}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6195
| Hs_Ensembl = ENSG00000117676
| Hs_RefseqProtein = NP_001006666
| Hs_RefseqmRNA = NM_001006665
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 26728836
| Hs_GenLoc_end = 26774108
| Hs_Uniprot = Q15418
| Mm_EntrezGene = 20111
| Mm_Ensembl = ENSMUSG00000003644
| Mm_RefseqmRNA = NM_009097
| Mm_RefseqProtein = NP_033123
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 133119370
| Mm_GenLoc_end = 133159860
| Mm_Uniprot = Q3TIM6
}}
}}
'''Ribosomal protein S6 kinase, 90kDa, polypeptide 1''', also known as '''RPS6KA1''', is a human [[gene]].
<!-- 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 nonidentical 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. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref>{{cite web | title = Entrez Gene: RPS6KA1 ribosomal protein S6 kinase, 90kDa, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6195| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Chen RH, Sarnecki C, Blenis J |title=Nuclear localization and regulation of erk- and rsk-encoded protein kinases. |journal=Mol. Cell. Biol. |volume=12 |issue= 3 |pages= 915-27 |year= 1992 |pmid= 1545823 |doi= }}
*{{cite journal | author=Tratner I, Ofir R, Verma IM |title=Alteration of a cyclic AMP-dependent protein kinase phosphorylation site in the c-Fos protein augments its transforming potential. |journal=Mol. Cell. Biol. |volume=12 |issue= 3 |pages= 998-1006 |year= 1992 |pmid= 1545828 |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=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=Chen RH, Abate C, Blenis J |title=Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 23 |pages= 10952-6 |year= 1994 |pmid= 8248197 |doi= }}
*{{cite journal | author=Rivera VM, Miranti CK, Misra RP, ''et al.'' |title=A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity. |journal=Mol. Cell. Biol. |volume=13 |issue= 10 |pages= 6260-73 |year= 1993 |pmid= 8413226 |doi= }}
*{{cite journal | author=Chen ZJ, Parent L, Maniatis T |title=Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity. |journal=Cell |volume=84 |issue= 6 |pages= 853-62 |year= 1996 |pmid= 8601309 |doi= }}
*{{cite journal | author=Barge RM, de Koning JP, Pouwels K, ''et al.'' |title=Tryptophan 650 of human granulocyte colony-stimulating factor (G-CSF) receptor, implicated in the activation of JAK2, is also required for G-CSF-mediated activation of signaling complexes of the p21ras route. |journal=Blood |volume=87 |issue= 6 |pages= 2148-53 |year= 1996 |pmid= 8630373 |doi= }}
*{{cite journal | author=Wong EV, Schaefer AW, Landreth G, Lemmon V |title=Involvement of p90rsk in neurite outgrowth mediated by the cell adhesion molecule L1. |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 18217-23 |year= 1996 |pmid= 8663493 |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=Nakajima T, Fukamizu A, Takahashi J, ''et al.'' |title=The signal-dependent coactivator CBP is a nuclear target for pp90RSK. |journal=Cell |volume=86 |issue= 3 |pages= 465-74 |year= 1996 |pmid= 8756728 |doi= }}
*{{cite journal | author=Zhao Y, Bjorbaek C, Moller DE |title=Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases. |journal=J. Biol. Chem. |volume=271 |issue= 47 |pages= 29773-9 |year= 1997 |pmid= 8939914 |doi= }}
*{{cite journal | author=Zaheer A, Lim R |title=Protein kinase A (PKA)- and protein kinase C-phosphorylated glia maturation factor promotes the catalytic activity of PKA. |journal=J. Biol. Chem. |volume=272 |issue= 8 |pages= 5183-6 |year= 1997 |pmid= 9030586 |doi= }}
*{{cite journal | author=Schouten GJ, Vertegaal AC, Whiteside ST, ''et al.'' |title=IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase. |journal=EMBO J. |volume=16 |issue= 11 |pages= 3133-44 |year= 1997 |pmid= 9214631 |doi= 10.1093/emboj/16.11.3133 }}
*{{cite journal | author=Li HL, Forman MS, Kurosaki T, Puré E |title=Syk is required for BCR-mediated activation of p90Rsk, but not p70S6k, via a mitogen-activated protein kinase-independent pathway in B cells. |journal=J. Biol. Chem. |volume=272 |issue= 29 |pages= 18200-8 |year= 1997 |pmid= 9218456 |doi= }}
*{{cite journal | author=Chang YW, Traugh JA |title=Phosphorylation of elongation factor 1 and ribosomal protein S6 by multipotential S6 kinase and insulin stimulation of translational elongation. |journal=J. Biol. Chem. |volume=272 |issue= 45 |pages= 28252-7 |year= 1997 |pmid= 9353277 |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=del Peso L, González-García M, Page C, ''et al.'' |title=Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt. |journal=Science |volume=278 |issue= 5338 |pages= 687-9 |year= 1997 |pmid= 9381178 |doi= }}
*{{cite journal | author=Dalby KN, Morrice N, Caudwell FB, ''et al.'' |title=Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK. |journal=J. Biol. Chem. |volume=273 |issue= 3 |pages= 1496-505 |year= 1998 |pmid= 9430688 |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= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SOCS3... {November 12, 2007 7:18:33 PM PST}
- SEARCH REDIRECT: Control Box Found: SOCS3 {November 12, 2007 7:19:37 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 12, 2007 7:19:39 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 12, 2007 7:19:39 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 12, 2007 7:19:39 PM PST}
- UPDATED: Updated protein page: SOCS3 {November 12, 2007 7:19:45 PM PST}
- INFO: Beginning work on SPARC... {November 12, 2007 7:14:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:15:32 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_SPARC_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bmo.
| PDB = {{PDB2|1bmo}}, {{PDB2|1nub}}, {{PDB2|1sra}}
| Name = Secreted protein, acidic, cysteine-rich (osteonectin)
| HGNCid = 11219
| Symbol = SPARC
| AltSymbols =; ON
| OMIM = 182120
| ECnumber =
| Homologene = 31132
| MGIid = 98373
| GeneAtlas_image1 = PBB_GE_SPARC_200665_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SPARC_212667_at_tn.png
| Function = {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005518 |text = collagen binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005604 |text = basement membrane}}
| Process = {{GNF_GO|id=GO:0001503 |text = ossification}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6678
| Hs_Ensembl = ENSG00000113140
| Hs_RefseqProtein = NP_003109
| Hs_RefseqmRNA = NM_003118
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 151021212
| Hs_GenLoc_end = 151046710
| Hs_Uniprot = P09486
| Mm_EntrezGene = 20692
| Mm_Ensembl = ENSMUSG00000018593
| Mm_RefseqmRNA = XM_990025
| Mm_RefseqProtein = XP_995119
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 55237924
| Mm_GenLoc_end = 55263289
| Mm_Uniprot = Q3TXI6
}}
}}
'''Secreted protein, acidic, cysteine-rich (osteonectin)''', also known as '''SPARC''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Secreted protein acidic and rich in cysteine/osteonectin/BM40, or SPARC, is a matrix-associated protein that elicits changes in cell shape, inhibits cell-cycle progression, and influences the synthesis of extracellular matrix (ECM) (Bradshaw et al., 2003).[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: SPARC secreted protein, acidic, cysteine-rich (osteonectin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6678| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Yan Q, Sage EH |title=SPARC, a matricellular glycoprotein with important biological functions. |journal=J. Histochem. Cytochem. |volume=47 |issue= 12 |pages= 1495-506 |year= 1999 |pmid= 10567433 |doi= }}
*{{cite journal | author=Altura BM |title=Pharmacological effects of alpha-methyldopa, alpha-methylnorepinephrine, and octopamine on rat arteriolar, arterial, and terminal vascular smooth. |journal=Circ. Res. |volume=36 |issue= 6 Suppl 1 |pages= 233-40 |year= 1975 |pmid= 1093755 |doi= }}
*{{cite journal | author=Raines EW, Lane TF, Iruela-Arispe ML, ''et al.'' |title=The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and -BB and inhibits the binding of PDGF to its receptors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 4 |pages= 1281-5 |year= 1992 |pmid= 1311092 |doi= }}
*{{cite journal | author=Mundlos S, Schwahn B, Reichert T, Zabel B |title=Distribution of osteonectin mRNA and protein during human embryonic and fetal development. |journal=J. Histochem. Cytochem. |volume=40 |issue= 2 |pages= 283-91 |year= 1992 |pmid= 1552170 |doi= }}
*{{cite journal | author=Kelm RJ, Mann KG |title=Human platelet osteonectin: release, surface expression, and partial characterization. |journal=Blood |volume=75 |issue= 5 |pages= 1105-13 |year= 1990 |pmid= 2306517 |doi= }}
*{{cite journal | author=Young MF, Day AA, Dominquez P, ''et al.'' |title=Structure and expression of osteonectin mRNA in human tissue. |journal=Connect. Tissue Res. |volume=24 |issue= 1 |pages= 17-28 |year= 1990 |pmid= 2338025 |doi= }}
*{{cite journal | author=Metsäranta M, Young MF, Sandberg M, ''et al.'' |title=Localization of osteonectin expression in human fetal skeletal tissues by in situ hybridization. |journal=Calcif. Tissue Int. |volume=45 |issue= 3 |pages= 146-52 |year= 1989 |pmid= 2505905 |doi= }}
*{{cite journal | author=Sage H, Vernon RB, Funk SE, ''et al.'' |title=SPARC, a secreted protein associated with cellular proliferation, inhibits cell spreading in vitro and exhibits Ca+2-dependent binding to the extracellular matrix. |journal=J. Cell Biol. |volume=109 |issue= 1 |pages= 341-56 |year= 1989 |pmid= 2745554 |doi= }}
*{{cite journal | author=Villarreal XC, Mann KG, Long GL |title=Structure of human osteonectin based upon analysis of cDNA and genomic sequences. |journal=Biochemistry |volume=28 |issue= 15 |pages= 6483-91 |year= 1989 |pmid= 2790009 |doi= }}
*{{cite journal | author=Swaroop A, Hogan BL, Francke U |title=Molecular analysis of the cDNA for human SPARC/osteonectin/BM-40: sequence, expression, and localization of the gene to chromosome 5q31-q33. |journal=Genomics |volume=2 |issue= 1 |pages= 37-47 |year= 1988 |pmid= 2838412 |doi= }}
*{{cite journal | author=Wewer UM, Albrechtsen R, Fisher LW, ''et al.'' |title=Osteonectin/SPARC/BM-40 in human decidua and carcinoma, tissues characterized by de novo formation of basement membrane. |journal=Am. J. Pathol. |volume=132 |issue= 2 |pages= 345-55 |year= 1988 |pmid= 3400777 |doi= }}
*{{cite journal | author=Clezardin P, Malaval L, Ehrensperger AS, ''et al.'' |title=Complex formation of human thrombospondin with osteonectin. |journal=Eur. J. Biochem. |volume=175 |issue= 2 |pages= 275-84 |year= 1988 |pmid= 3402455 |doi= }}
*{{cite journal | author=Lankat-Buttgereit B, Mann K, Deutzmann R, ''et al.'' |title=Cloning and complete amino acid sequences of human and murine basement membrane protein BM-40 (SPARC, osteonectin). |journal=FEBS Lett. |volume=236 |issue= 2 |pages= 352-6 |year= 1988 |pmid= 3410046 |doi= }}
*{{cite journal | author=Stenner DD, Tracy RP, Riggs BL, Mann KG |title=Human platelets contain and secrete osteonectin, a major protein of mineralized bone. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 18 |pages= 6892-6 |year= 1986 |pmid= 3489235 |doi= }}
*{{cite journal | author=Jundt G, Berghäuser KH, Termine JD, Schulz A |title=Osteonectin--a differentiation marker of bone cells. |journal=Cell Tissue Res. |volume=248 |issue= 2 |pages= 409-15 |year= 1987 |pmid= 3581152 |doi= }}
*{{cite journal | author=Fisher LW, Hawkins GR, Tuross N, Termine JD |title=Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone. |journal=J. Biol. Chem. |volume=262 |issue= 20 |pages= 9702-8 |year= 1987 |pmid= 3597437 |doi= }}
*{{cite journal | author=Sage H, Johnson C, Bornstein P |title=Characterization of a novel serum albumin-binding glycoprotein secreted by endothelial cells in culture. |journal=J. Biol. Chem. |volume=259 |issue= 6 |pages= 3993-4007 |year= 1984 |pmid= 6368555 |doi= }}
*{{cite journal | author=Termine JD, Kleinman HK, Whitson SW, ''et al.'' |title=Osteonectin, a bone-specific protein linking mineral to collagen. |journal=Cell |volume=26 |issue= 1 Pt 1 |pages= 99-105 |year= 1982 |pmid= 7034958 |doi= }}
*{{cite journal | author=Xie RL, Long GL |title=Role of N-linked glycosylation in human osteonectin. Effect of carbohydrate removal by N-glycanase and site-directed mutagenesis on structure and binding of type V collagen. |journal=J. Biol. Chem. |volume=270 |issue= 39 |pages= 23212-7 |year= 1995 |pmid= 7559469 |doi= }}
*{{cite journal | author=Maurer P, Hohenadl C, Hohenester E, ''et al.'' |title=The C-terminal portion of BM-40 (SPARC/osteonectin) is an autonomously folding and crystallisable domain that binds calcium and collagen IV. |journal=J. Mol. Biol. |volume=253 |issue= 2 |pages= 347-57 |year= 1995 |pmid= 7563094 |doi= 10.1006/jmbi.1995.0557 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SRF... {November 12, 2007 7:15:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:16:08 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_SRF_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hbx.
| PDB = {{PDB2|1hbx}}, {{PDB2|1k6o}}, {{PDB2|1srs}}
| Name = Serum response factor (c-fos serum response element-binding transcription factor)
| HGNCid = 11291
| Symbol = SRF
| AltSymbols =; MCM1
| OMIM = 600589
| ECnumber =
| Homologene = 31135
| MGIid = 106658
| GeneAtlas_image1 = PBB_GE_SRF_202401_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SRF_202400_s_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:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001947 |text = heart looping}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0046716 |text = muscle maintenance}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6722
| Hs_Ensembl = ENSG00000112658
| Hs_RefseqProtein = NP_003122
| Hs_RefseqmRNA = NM_003131
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 43246898
| Hs_GenLoc_end = 43257219
| Hs_Uniprot = P11831
| Mm_EntrezGene = 20807
| Mm_Ensembl = ENSMUSG00000015605
| Mm_RefseqmRNA = NM_020493
| Mm_RefseqProtein = NP_065239
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 46010028
| Mm_GenLoc_end = 46019351
| Mm_Uniprot = Q9JM73
}}
}}
'''Serum response factor (c-fos serum response element-binding transcription factor)''', also known as '''SRF''', is a human [[gene]].
<!-- 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 ubiquitous nuclear protein that stimulates both cell proliferation and differentiation. It is a member of the MADS (MCM1, Agamous, Deficiens, and SRF) box superfamily of transcription factors. This protein binds to the serum response element (SRE) in the promoter region of target genes. This protein regulates the activity of many immediate-early genes, for example c-fos, and thereby participates in cell cycle regulation, apoptosis, cell growth, and cell differentiation. This gene is the downstream target of many pathways; for example, the mitogen-activated protein kinase pathway (MAPK) that acts through the ternary complex factors (TCFs).<ref>{{cite web | title = Entrez Gene: SRF serum response factor (c-fos serum response element-binding transcription factor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6722| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Miano JM |title=Serum response factor: toggling between disparate programs of gene expression. |journal=J. Mol. Cell. Cardiol. |volume=35 |issue= 6 |pages= 577-93 |year= 2004 |pmid= 12788374 |doi= }}
*{{cite journal | author=Reason AJ, Morris HR, Panico M, ''et al.'' |title=Localization of O-GlcNAc modification on the serum response transcription factor. |journal=J. Biol. Chem. |volume=267 |issue= 24 |pages= 16911-21 |year= 1992 |pmid= 1512232 |doi= }}
*{{cite journal | author=Janknecht R, Hipskind RA, Houthaeve T, ''et al.'' |title=Identification of multiple SRF N-terminal phosphorylation sites affecting DNA binding properties. |journal=EMBO J. |volume=11 |issue= 3 |pages= 1045-54 |year= 1992 |pmid= 1547771 |doi= }}
*{{cite journal | author=Marais RM, Hsuan JJ, McGuigan C, ''et al.'' |title=Casein kinase II phosphorylation increases the rate of serum response factor-binding site exchange. |journal=EMBO J. |volume=11 |issue= 1 |pages= 97-105 |year= 1992 |pmid= 1740119 |doi= }}
*{{cite journal | author=Manak JR, Prywes R |title=Mutation of serum response factor phosphorylation sites and the mechanism by which its DNA-binding activity is increased by casein kinase II. |journal=Mol. Cell. Biol. |volume=11 |issue= 7 |pages= 3652-9 |year= 1991 |pmid= 2046671 |doi= }}
*{{cite journal | author=Norman C, Runswick M, Pollock R, Treisman R |title=Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element. |journal=Cell |volume=55 |issue= 6 |pages= 989-1003 |year= 1989 |pmid= 3203386 |doi= }}
*{{cite journal | author=Price MA, Rogers AE, Treisman R |title=Comparative analysis of the ternary complex factors Elk-1, SAP-1a and SAP-2 (ERP/NET). |journal=EMBO J. |volume=14 |issue= 11 |pages= 2589-601 |year= 1995 |pmid= 7540136 |doi= }}
*{{cite journal | author=Bonni A, Ginty DD, Dudek H, Greenberg ME |title=Serine 133-phosphorylated CREB induces transcription via a cooperative mechanism that may confer specificity to neurotrophin signals. |journal=Mol. Cell. Neurosci. |volume=6 |issue= 2 |pages= 168-83 |year= 1995 |pmid= 7551568 |doi= 10.1006/mcne.1995.1015 }}
*{{cite journal | author=Fujii M, Chuhjo T, Minamino T, ''et al.'' |title=Identification of the Tax interaction region of serum response factor that mediates the aberrant induction of immediate early genes through CArG boxes by HTLV-I Tax. |journal=Oncogene |volume=11 |issue= 1 |pages= 7-14 |year= 1995 |pmid= 7624133 |doi= }}
*{{cite journal | author=Pellegrini L, Tan S, Richmond TJ |title=Structure of serum response factor core bound to DNA. |journal=Nature |volume=376 |issue= 6540 |pages= 490-8 |year= 1995 |pmid= 7637780 |doi= 10.1038/376490a0 }}
*{{cite journal | author=Liu SH, Peng BH, Ma JT, ''et al.'' |title=Serum response element associated transcription factors in mouse embryos: serum response factor, YY1, and PEA3 factor. |journal=Dev. Genet. |volume=16 |issue= 3 |pages= 229-40 |year= 1995 |pmid= 7796532 |doi= 10.1002/dvg.1020160303 }}
*{{cite journal | author=Joliot V, Demma M, Prywes R |title=Interaction with RAP74 subunit of TFIIF is required for transcriptional activation by serum response factor. |journal=Nature |volume=373 |issue= 6515 |pages= 632-5 |year= 1995 |pmid= 7854423 |doi= 10.1038/373632a0 }}
*{{cite journal | author=Liu SH, Ng SY |title=Serum response factor associated ETS proteins: ternary complex factors and PEA3-binding factor. |journal=Biochem. Biophys. Res. Commun. |volume=201 |issue= 3 |pages= 1406-13 |year= 1994 |pmid= 8024585 |doi= 10.1006/bbrc.1994.1860 }}
*{{cite journal | author=Zhu H, Joliot V, Prywes R |title=Role of transcription factor TFIIF in serum response factor-activated transcription. |journal=J. Biol. Chem. |volume=269 |issue= 5 |pages= 3489-97 |year= 1994 |pmid= 8106390 |doi= }}
*{{cite journal | author=Janknecht R, Ernst WH, Houthaeve T, Nordheim A |title=C-terminal phosphorylation of the serum-response factor. |journal=Eur. J. Biochem. |volume=216 |issue= 2 |pages= 469-75 |year= 1993 |pmid= 8375385 |doi= }}
*{{cite journal | author=Liu SH, Ma JT, Yueh AY, ''et al.'' |title=The carboxyl-terminal transactivation domain of human serum response factor contains DNA-activated protein kinase phosphorylation sites. |journal=J. Biol. Chem. |volume=268 |issue= 28 |pages= 21147-54 |year= 1993 |pmid= 8407951 |doi= }}
*{{cite journal | author=Rivera VM, Miranti CK, Misra RP, ''et al.'' |title=A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity. |journal=Mol. Cell. Biol. |volume=13 |issue= 10 |pages= 6260-73 |year= 1993 |pmid= 8413226 |doi= }}
*{{cite journal | author=Magnaghi-Jaulin L, Masutani H, Robin P, ''et al.'' |title=SRE elements are binding sites for the fusion protein EWS-FLI-1. |journal=Nucleic Acids Res. |volume=24 |issue= 6 |pages= 1052-8 |year= 1996 |pmid= 8604338 |doi= }}
*{{cite journal | author=Groisman R, Masutani H, Leibovitch MP, ''et al.'' |title=Physical interaction between the mitogen-responsive serum response factor and myogenic basic-helix-loop-helix proteins. |journal=J. Biol. Chem. |volume=271 |issue= 9 |pages= 5258-64 |year= 1996 |pmid= 8617811 |doi= }}
*{{cite journal | author=Franzoso G, Carlson L, Brown K, ''et al.'' |title=Activation of the serum response factor by p65/NF-kappaB. |journal=EMBO J. |volume=15 |issue= 13 |pages= 3403-12 |year= 1996 |pmid= 8670842 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on STX1A... {November 12, 2007 7:16:08 PM PST}
- SEARCH REDIRECT: Control Box Found: STX1A {November 12, 2007 7:16:50 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 12, 2007 7:16:51 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 12, 2007 7:16:51 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 12, 2007 7:16:51 PM PST}
- UPDATED: Updated protein page: STX1A {November 12, 2007 7:16:58 PM PST}
- INFO: Beginning work on UBB... {November 12, 2007 7:16:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 12, 2007 7:17:42 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_UBB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aar.
| PDB = {{PDB2|1aar}}, {{PDB2|1cmx}}, {{PDB2|1d3z}}, {{PDB2|1f9j}}, {{PDB2|1fxt}}, {{PDB2|1g6j}}, {{PDB2|1gjz}}, {{PDB2|1nbf}}, {{PDB2|1ogw}}, {{PDB2|1otr}}, {{PDB2|1p3q}}, {{PDB2|1q0w}}, {{PDB2|1q5w}}, {{PDB2|1s1q}}, {{PDB2|1sif}}, {{PDB2|1tbe}}, {{PDB2|1ubi}}, {{PDB2|1ubq}}, {{PDB2|1ud7}}, {{PDB2|1uzx}}, {{PDB2|1v80}}, {{PDB2|1v81}}, {{PDB2|1wr1}}, {{PDB2|1wr6}}, {{PDB2|1wrd}}, {{PDB2|1xd3}}, {{PDB2|1xqq}}, {{PDB2|1yd8}}, {{PDB2|1yiw}}, {{PDB2|1yj1}}, {{PDB2|1yx5}}, {{PDB2|1yx6}}, {{PDB2|1zgu}}, {{PDB2|2ayo}}, {{PDB2|2bgf}}, {{PDB2|2c7m}}, {{PDB2|2c7n}}, {{PDB2|2d3g}}, {{PDB2|2den}}, {{PDB2|2dx5}}, {{PDB2|2fcm}}, {{PDB2|2fcn}}, {{PDB2|2fcq}}, {{PDB2|2fcs}}, {{PDB2|2fid}}, {{PDB2|2fif}}, {{PDB2|2fuh}}, {{PDB2|2g3q}}, {{PDB2|2g45}}, {{PDB2|2gbj}}, {{PDB2|2gbk}}, {{PDB2|2gbm}}, {{PDB2|2gbn}}, {{PDB2|2gbr}}, {{PDB2|2gmi}}, {{PDB2|2hd5}}, {{PDB2|2hth}}, {{PDB2|2ibi}}, {{PDB2|2j7q}}, {{PDB2|2nr2}}, {{PDB2|2o6v}}, {{PDB2|2oob}}
| Name = Ubiquitin B
| HGNCid = 12463
| Symbol = UBB
| AltSymbols =; FLJ25987; MGC8385
| OMIM = 191339
| ECnumber =
| Homologene = 75104
| MGIid =
| GeneAtlas_image1 = PBB_GE_UBB_200633_at_tn.png
| Function =
| Component =
| Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7314
| Hs_Ensembl = ENSG00000170315
| Hs_RefseqProtein = NP_061828
| Hs_RefseqmRNA = NM_018955
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 16225092
| Hs_GenLoc_end = 16226779
| Hs_Uniprot = P62988
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Ubiquitin B''', also known as '''UBB''', is a human [[gene]].
<!-- 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 ubiquitin, one of the most conserved proteins known. Ubiquitin is required for ATP-dependent, nonlysosomal intracellular protein degradation of abnormal proteins and normal proteins with a rapid turnover. Ubiquitin is covalently bound to proteins to be degraded, and presumably labels these proteins for degradation. Ubiquitin also binds to histone H2A in actively transcribed regions but does not cause histone H2A degradation, suggesting that ubiquitin is also involved in regulation of gene expression. This gene consists of three direct repeats of the ubiquitin coding sequence with no spacer sequence. Consequently, the protein is expressed as a polyubiquitin precursor with a final amino acid after the last repeat. Aberrant form of this protein has been noticed in patients with Alzheimer's and Down syndrome.<ref>{{cite web | title = Entrez Gene: UBB ubiquitin B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7314| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Conaway RC, Brower CS, Conaway JW |title=Emerging roles of ubiquitin in transcription regulation. |journal=Science |volume=296 |issue= 5571 |pages= 1254-8 |year= 2002 |pmid= 12016299 |doi= 10.1126/science.1067466 }}
*{{cite journal | author=Murphey RK, Godenschwege TA |title=New roles for ubiquitin in the assembly and function of neuronal circuits. |journal=Neuron |volume=36 |issue= 1 |pages= 5-8 |year= 2002 |pmid= 12367500 |doi= }}
*{{cite journal | author=Mazzé FM, Degrève L |title=The role of viral and cellular proteins in the budding of human immunodeficiency virus. |journal=Acta Virol. |volume=50 |issue= 2 |pages= 75-85 |year= 2006 |pmid= 16808324 |doi= }}
*{{cite journal | author=Schlesinger DH, Goldstein G |title=Hybrid troponin reconstituted from vertebrate and arthropod subunits. |journal=Nature |volume=255 |issue= 5507 |pages= 423-4 |year= 1975 |pmid= 124018 |doi= }}
*{{cite journal | author=Adams SM, Sharp MG, Walker RA, ''et al.'' |title=Differential expression of translation-associated genes in benign and malignant human breast tumours. |journal=Br. J. Cancer |volume=65 |issue= 1 |pages= 65-71 |year= 1992 |pmid= 1370760 |doi= }}
*{{cite journal | author=Pancré V, Pierce RJ, Fournier F, ''et al.'' |title=Effect of ubiquitin on platelet functions: possible identity with platelet activity suppressive lymphokine (PASL). |journal=Eur. J. Immunol. |volume=21 |issue= 11 |pages= 2735-41 |year= 1991 |pmid= 1657614 |doi= }}
*{{cite journal | author=Baker RT, Board PG |title=The human ubiquitin-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes. |journal=Nucleic Acids Res. |volume=19 |issue= 5 |pages= 1035-40 |year= 1991 |pmid= 1850507 |doi= }}
*{{cite journal | author=Webb GC, Baker RT, Fagan K, Board PG |title=Localization of the human UbB polyubiquitin gene to chromosome band 17p11.1-17p12. |journal=Am. J. Hum. Genet. |volume=46 |issue= 2 |pages= 308-15 |year= 1990 |pmid= 2154095 |doi= }}
*{{cite journal | author=Fornace AJ, Alamo I, Hollander MC, Lamoreaux E |title=Ubiquitin mRNA is a major stress-induced transcript in mammalian cells. |journal=Nucleic Acids Res. |volume=17 |issue= 3 |pages= 1215-30 |year= 1989 |pmid= 2537950 |doi= }}
*{{cite journal | author=Lund PK, Moats-Staats BM, Simmons JG, ''et al.'' |title=Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor. |journal=J. Biol. Chem. |volume=260 |issue= 12 |pages= 7609-13 |year= 1985 |pmid= 2581967 |doi= }}
*{{cite journal | author=Einspanier R, Sharma HS, Scheit KH |title=Cloning and sequence analysis of a cDNA encoding poly-ubiquitin in human ovarian granulosa cells. |journal=Biochem. Biophys. Res. Commun. |volume=147 |issue= 2 |pages= 581-7 |year= 1987 |pmid= 2820408 |doi= }}
*{{cite journal | author=Wiborg O, Pedersen MS, Wind A, ''et al.'' |title=The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences. |journal=EMBO J. |volume=4 |issue= 3 |pages= 755-9 |year= 1985 |pmid= 2988935 |doi= }}
*{{cite journal | author=Baker RT, Board PG |title=The human ubiquitin gene family: structure of a gene and pseudogenes from the Ub B subfamily. |journal=Nucleic Acids Res. |volume=15 |issue= 2 |pages= 443-63 |year= 1987 |pmid= 3029682 |doi= }}
*{{cite journal | author=Vijay-Kumar S, Bugg CE, Cook WJ |title=Structure of ubiquitin refined at 1.8 A resolution. |journal=J. Mol. Biol. |volume=194 |issue= 3 |pages= 531-44 |year= 1987 |pmid= 3041007 |doi= }}
*{{cite journal | author=Busch H |title=Ubiquitination of proteins. |journal=Meth. Enzymol. |volume=106 |issue= |pages= 238-62 |year= 1984 |pmid= 6092831 |doi= }}
*{{cite journal | author=Andersen MW, Ballal NR, Goldknopf IL, Busch H |title=Protein A24 lyase activity in nucleoli of thioacetamide-treated rat liver releases histone 2A and ubiquitin from conjugated protein A24. |journal=Biochemistry |volume=20 |issue= 5 |pages= 1100-4 |year= 1981 |pmid= 6261785 |doi= }}
*{{cite journal | author=Busch H, Goldknopf IL |title=Ubiquitin - protein conjugates. |journal=Mol. Cell. Biochem. |volume=40 |issue= 3 |pages= 173-87 |year= 1982 |pmid= 6275256 |doi= }}
*{{cite journal | author=Treier M, Staszewski LM, Bohmann D |title=Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. |journal=Cell |volume=78 |issue= 5 |pages= 787-98 |year= 1994 |pmid= 8087846 |doi= }}
*{{cite journal | author=Cook WJ, Jeffrey LC, Kasperek E, Pickart CM |title=Structure of tetraubiquitin shows how multiubiquitin chains can be formed. |journal=J. Mol. Biol. |volume=236 |issue= 2 |pages= 601-9 |year= 1994 |pmid= 8107144 |doi= 10.1006/jmbi.1994.1169 }}
*{{cite journal | author=Ramage R, Green J, Muir TW, ''et al.'' |title=Synthetic, structural and biological studies of the ubiquitin system: the total chemical synthesis of ubiquitin. |journal=Biochem. J. |volume=299 ( Pt 1) |issue= |pages= 151-8 |year= 1994 |pmid= 8166633 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
