Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 00:14, 15 November 2007 (UTC)
[edit]Proteins without matches (5)
[edit]Proteins with a High Potential Match (13)
[edit]Redirected Proteins (7)
[edit]Manual Inspection (Page not found) (18)
[edit]
Protein Status Grid - Date: 00:14, 15 November 2007 (UTC)
[edit]Vebose Log - Date: 00:14, 15 November 2007 (UTC)
[edit]- INFO: Beginning work on ACTN1... {November 14, 2007 3:48:22 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:48:54 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_ACTN1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1sjj.
| PDB = {{PDB2|1sjj}}, {{PDB2|2eyi}}, {{PDB2|2eyn}}
| Name = Actinin, alpha 1
| HGNCid = 163
| Symbol = ACTN1
| AltSymbols =; FLJ40884
| OMIM = 102575
| ECnumber =
| Homologene = 55553
| MGIid = 2137706
| GeneAtlas_image1 = PBB_GE_ACTN1_208636_at_tn.png
| GeneAtlas_image2 = PBB_GE_ACTN1_208637_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_ACTN1_211160_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0017166 |text = vinculin binding}} {{GNF_GO|id=GO:0051015 |text = actin filament binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005925 |text = focal adhesion}} {{GNF_GO|id=GO:0030018 |text = Z disc}} {{GNF_GO|id=GO:0031143 |text = pseudopodium}}
| Process = {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0048041 |text = focal adhesion formation}} {{GNF_GO|id=GO:0051017 |text = actin filament bundle formation}} {{GNF_GO|id=GO:0051271 |text = negative regulation of cell motility}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 87
| Hs_Ensembl = ENSG00000072110
| Hs_RefseqProtein = NP_001093
| Hs_RefseqmRNA = NM_001102
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 68410793
| Hs_GenLoc_end = 68515747
| Hs_Uniprot = P12814
| Mm_EntrezGene = 109711
| Mm_Ensembl = ENSMUSG00000015143
| Mm_RefseqmRNA = NM_134156
| Mm_RefseqProtein = NP_598917
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 81086385
| Mm_GenLoc_end = 81179156
| Mm_Uniprot = A1BN54
}}
}}
'''Actinin, alpha 1''', also known as '''ACTN1''', 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 = Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments. This gene encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene.<ref>{{cite web | title = Entrez Gene: ACTN1 actinin, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=87| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Snásel J, Pichová I |title=The cleavage of host cell proteins by HIV-1 protease. |journal=Folia Biol. (Praha) |volume=42 |issue= 5 |pages= 227-30 |year= 1997 |pmid= 8997639 |doi= }}
*{{cite journal | author=Menko S, Philp N, Veneziale B, Walker J |title=Integrins and development: how might these receptors regulate differentiation of the lens. |journal=Ann. N. Y. Acad. Sci. |volume=842 |issue= |pages= 36-41 |year= 1998 |pmid= 9599291 |doi= }}
*{{cite journal | author=Yürüker B, Niggli V |title=Alpha-actinin and vinculin in human neutrophils: reorganization during adhesion and relation to the actin network. |journal=J. Cell. Sci. |volume=101 ( Pt 2) |issue= |pages= 403-14 |year= 1992 |pmid= 1629252 |doi= }}
*{{cite journal | author=Tokuue Y, Goto S, Imamura M, ''et al.'' |title=Transfection of chicken skeletal muscle alpha-actinin cDNA into nonmuscle and myogenic cells: dimerization is not essential for alpha-actinin to bind to microfilaments. |journal=Exp. Cell Res. |volume=197 |issue= 2 |pages= 158-67 |year= 1992 |pmid= 1720388 |doi= }}
*{{cite journal | author=Shoeman RL, Kesselmier C, Mothes E, ''et al.'' |title=Non-viral cellular substrates for human immunodeficiency virus type 1 protease. |journal=FEBS Lett. |volume=278 |issue= 2 |pages= 199-203 |year= 1991 |pmid= 1991513 |doi= }}
*{{cite journal | author=Nishiyama M, Ozturk M, Frohlich M, ''et al.'' |title=Expression of human alpha-actinin in human hepatocellular carcinoma. |journal=Cancer Res. |volume=50 |issue= 19 |pages= 6291-4 |year= 1990 |pmid= 2169343 |doi= }}
*{{cite journal | author=Youssoufian H, McAfee M, Kwiatkowski DJ |title=Cloning and chromosomal localization of the human cytoskeletal alpha-actinin gene reveals linkage to the beta-spectrin gene. |journal=Am. J. Hum. Genet. |volume=47 |issue= 1 |pages= 62-71 |year= 1990 |pmid= 2349951 |doi= }}
*{{cite journal | author=Millake DB, Blanchard AD, Patel B, Critchley DR |title=The cDNA sequence of a human placental alpha-actinin. |journal=Nucleic Acids Res. |volume=17 |issue= 16 |pages= 6725 |year= 1989 |pmid= 2780298 |doi= }}
*{{cite journal | author=Dubernard V, Faucher D, Launay JM, Legrand C |title=Identification of the cytoskeletal protein alpha-actinin as a platelet thrombospondin-binding protein. |journal=FEBS Lett. |volume=364 |issue= 2 |pages= 109-14 |year= 1995 |pmid= 7750553 |doi= }}
*{{cite journal | author=Knudsen KA, Soler AP, Johnson KR, Wheelock MJ |title=Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin. |journal=J. Cell Biol. |volume=130 |issue= 1 |pages= 67-77 |year= 1995 |pmid= 7790378 |doi= }}
*{{cite journal | author=Glück U, Ben-Ze'ev A |title=Modulation of alpha-actinin levels affects cell motility and confers tumorigenicity on 3T3 cells. |journal=J. Cell. Sci. |volume=107 ( Pt 7) |issue= |pages= 1773-82 |year= 1995 |pmid= 7983147 |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=Egerton M, Moritz RL, Druker B, ''et al.'' |title=Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes. |journal=Biochem. Biophys. Res. Commun. |volume=224 |issue= 3 |pages= 666-74 |year= 1996 |pmid= 8713105 |doi= 10.1006/bbrc.1996.1082 }}
*{{cite journal | author=Mukai H, Toshimori M, Shibata H, ''et al.'' |title=Interaction of PKN with alpha-actinin. |journal=J. Biol. Chem. |volume=272 |issue= 8 |pages= 4740-6 |year= 1997 |pmid= 9030526 |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=Hazan RB, Norton L |title=The epidermal growth factor receptor modulates the interaction of E-cadherin with the actin cytoskeleton. |journal=J. Biol. Chem. |volume=273 |issue= 15 |pages= 9078-84 |year= 1998 |pmid= 9535896 |doi= }}
*{{cite journal | author=Bunn RC, Jensen MA, Reed BC |title=Protein interactions with the glucose transporter binding protein GLUT1CBP that provide a link between GLUT1 and the cytoskeleton. |journal=Mol. Biol. Cell |volume=10 |issue= 4 |pages= 819-32 |year= 1999 |pmid= 10198040 |doi= }}
*{{cite journal | author=Reinhard M, Zumbrunn J, Jaquemar D, ''et al.'' |title=An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment. |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 13410-8 |year= 1999 |pmid= 10224105 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ADAM17... {November 14, 2007 4:03:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:04:41 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_ADAM17_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bkc.
| PDB = {{PDB2|1bkc}}, {{PDB2|1zxc}}, {{PDB2|2a8h}}, {{PDB2|2ddf}}, {{PDB2|2fv5}}, {{PDB2|2fv9}}, {{PDB2|2i47}}
| Name = ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme)
| HGNCid = 195
| Symbol = ADAM17
| AltSymbols =; CD156b; MGC71942; TACE; cSVP
| OMIM = 603639
| ECnumber =
| Homologene = 2395
| MGIid = 1096335
| GeneAtlas_image1 = PBB_GE_ADAM17_205746_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ADAM17_205745_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_ADAM17_213532_at_tn.png
| Function = {{GNF_GO|id=GO:0004222 |text = metalloendopeptidase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007219 |text = Notch signaling pathway}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6868
| Hs_Ensembl = ENSG00000151694
| Hs_RefseqProtein = NP_003174
| Hs_RefseqmRNA = NM_003183
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 9546066
| Hs_GenLoc_end = 9613368
| Hs_Uniprot = P78536
| Mm_EntrezGene = 11491
| Mm_Ensembl = ENSMUSG00000052593
| Mm_RefseqmRNA = NM_009615
| Mm_RefseqProtein = NP_033745
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 21569999
| Mm_GenLoc_end = 21620083
| Mm_Uniprot = Q3UEC0
}}
}}
'''ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme)''', also known as '''ADAM17''', 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 ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biologic processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. The protein encoded by this gene functions as a tumor necrosis factor-alpha converting enzyme; binds mitotic arrest deficient 2 protein; and also plays a prominent role in the activation of the Notch signaling pathway.<ref>{{cite web | title = Entrez Gene: ADAM17 ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6868| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Black RA |title=Tumor necrosis factor-alpha converting enzyme. |journal=Int. J. Biochem. Cell Biol. |volume=34 |issue= 1 |pages= 1-5 |year= 2002 |pmid= 11733179 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Black RA, Rauch CT, Kozlosky CJ, ''et al.'' |title=A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. |journal=Nature |volume=385 |issue= 6618 |pages= 729-33 |year= 1997 |pmid= 9034190 |doi= 10.1038/385729a0 }}
*{{cite journal | author=Moss ML, Jin SL, Milla ME, ''et al.'' |title=Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. |journal=Nature |volume=385 |issue= 6618 |pages= 733-6 |year= 1997 |pmid= 9034191 |doi= 10.1038/385733a0 }}
*{{cite journal | author=Maskos K, Fernandez-Catalan C, Huber R, ''et al.'' |title=Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 7 |pages= 3408-12 |year= 1998 |pmid= 9520379 |doi= }}
*{{cite journal | author=Patel IR, Attur MG, Patel RN, ''et al.'' |title=TNF-alpha convertase enzyme from human arthritis-affected cartilage: isolation of cDNA by differential display, expression of the active enzyme, and regulation of TNF-alpha. |journal=J. Immunol. |volume=160 |issue= 9 |pages= 4570-9 |year= 1998 |pmid= 9574564 |doi= }}
*{{cite journal | author=Schroeter EH, Kisslinger JA, Kopan R |title=Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. |journal=Nature |volume=393 |issue= 6683 |pages= 382-6 |year= 1998 |pmid= 9620803 |doi= 10.1038/30756 }}
*{{cite journal | author=Hirohata S, Seldin MF, Apte SS |title=Chromosomal assignment of two ADAM genes, TACE (ADAM17) and MLTNB (ADAM19), to human chromosomes 2 and 5, respectively, and of Mltnb to mouse chromosome 11. |journal=Genomics |volume=54 |issue= 1 |pages= 178-9 |year= 1999 |pmid= 9806848 |doi= 10.1006/geno.1998.5544 }}
*{{cite journal | author=Lum L, Wong BR, Josien R, ''et al.'' |title=Evidence for a role of a tumor necrosis factor-alpha (TNF-alpha)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival. |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 13613-8 |year= 1999 |pmid= 10224132 |doi= }}
*{{cite journal | author=Cerretti DP, Poindexter K, Castner BJ, ''et al.'' |title=Characterization of the cDNA and gene for mouse tumour necrosis factor alpha converting enzyme (TACE/ADAM17) and its location to mouse chromosome 12 and human chromosome 2p25. |journal=Cytokine |volume=11 |issue= 8 |pages= 541-51 |year= 1999 |pmid= 10433800 |doi= 10.1006/cyto.1998.0466 }}
*{{cite journal | author=Nelson KK, Schlöndorff J, Blobel CP |title=Evidence for an interaction of the metalloprotease-disintegrin tumour necrosis factor alpha convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease-disintegrin MDC9 with a novel MAD2-related protein, MAD2beta. |journal=Biochem. J. |volume=343 Pt 3 |issue= |pages= 673-80 |year= 2000 |pmid= 10527948 |doi= }}
*{{cite journal | author=Kärkkäinen I, Rybnikova E, Pelto-Huikko M, Huovila AP |title=Metalloprotease-disintegrin (ADAM) genes are widely and differentially expressed in the adult CNS. |journal=Mol. Cell. Neurosci. |volume=15 |issue= 6 |pages= 547-60 |year= 2000 |pmid= 10860581 |doi= 10.1006/mcne.2000.0848 }}
*{{cite journal | author=Brou C, Logeat F, Gupta N, ''et al.'' |title=A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. |journal=Mol. Cell |volume=5 |issue= 2 |pages= 207-16 |year= 2000 |pmid= 10882063 |doi= }}
*{{cite journal | author=Lee MH, Verma V, Maskos K, ''et al.'' |title=Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-alpha-converting enzyme. |journal=Biochem. J. |volume=364 |issue= Pt 1 |pages= 227-34 |year= 2002 |pmid= 11988096 |doi= }}
*{{cite journal | author=Lee MH, Verma V, Maskos K, ''et al.'' |title=The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3. |journal=FEBS Lett. |volume=520 |issue= 1-3 |pages= 102-6 |year= 2002 |pmid= 12044879 |doi= }}
*{{cite journal | author=Díaz-Rodríguez E, Montero JC, Esparís-Ogando A, ''et al.'' |title=Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding. |journal=Mol. Biol. Cell |volume=13 |issue= 6 |pages= 2031-44 |year= 2002 |pmid= 12058067 |doi= 10.1091/mbc.01-11-0561 }}
*{{cite journal | author=Mohan MJ, Seaton T, Mitchell J, ''et al.'' |title=The tumor necrosis factor-alpha converting enzyme (TACE): a unique metalloproteinase with highly defined substrate selectivity. |journal=Biochemistry |volume=41 |issue= 30 |pages= 9462-9 |year= 2002 |pmid= 12135369 |doi= }}
*{{cite journal | author=Gómez-Gaviro MV, González-Alvaro I, Domínguez-Jiménez C, ''et al.'' |title=Structure-function relationship and role of tumor necrosis factor-alpha-converting enzyme in the down-regulation of L-selectin by non-steroidal anti-inflammatory drugs. |journal=J. Biol. Chem. |volume=277 |issue= 41 |pages= 38212-21 |year= 2002 |pmid= 12147693 |doi= 10.1074/jbc.M205142200 }}
*{{cite journal | author=Zheng Y, Schlondorff J, Blobel CP |title=Evidence for regulation of the tumor necrosis factor alpha-convertase (TACE) by protein-tyrosine phosphatase PTPH1. |journal=J. Biol. Chem. |volume=277 |issue= 45 |pages= 42463-70 |year= 2003 |pmid= 12207026 |doi= 10.1074/jbc.M207459200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ADORA2A... {November 14, 2007 3:48:54 PM PST}
- SEARCH REDIRECT: Control Box Found: ADORA2A {November 14, 2007 3:49:36 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 3:49:38 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 3:49:38 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 3:49:38 PM PST}
- UPDATED: Updated protein page: ADORA2A {November 14, 2007 3:49:45 PM PST}
- INFO: Beginning work on APOC3... {November 14, 2007 3:49:45 PM PST}
- SEARCH REDIRECT: Control Box Found: APOC3 {November 14, 2007 3:50:14 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 3:50:16 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 3:50:16 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 3:50:16 PM PST}
- UPDATED: Updated protein page: APOC3 {November 14, 2007 3:50:23 PM PST}
- INFO: Beginning work on ARSA... {November 14, 2007 3:50:23 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:50:50 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_ARSA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1auk.
| PDB = {{PDB2|1auk}}, {{PDB2|1e1z}}, {{PDB2|1e2s}}, {{PDB2|1e33}}, {{PDB2|1e3c}}, {{PDB2|1n2k}}, {{PDB2|1n2l}}
| Name = Arylsulfatase A
| HGNCid = 713
| Symbol = ARSA
| AltSymbols =; MLD
| OMIM = 607574
| ECnumber =
| Homologene = 20138
| MGIid = 88077
| GeneAtlas_image1 = PBB_GE_ARSA_204443_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0004065 |text = arylsulfatase activity}} {{GNF_GO|id=GO:0004098 |text = cerebroside-sulfatase activity}} {{GNF_GO|id=GO:0008484 |text = sulfuric ester hydrolase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0000299 |text = integral to membrane of membrane fraction}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0007339 |text = binding of sperm to zona pellucida}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 410
| Hs_Ensembl = ENSG00000100299
| Hs_RefseqProtein = NP_000478
| Hs_RefseqmRNA = NM_000487
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 49410316
| Hs_GenLoc_end = 49413442
| Hs_Uniprot = P15289
| Mm_EntrezGene = 11883
| Mm_Ensembl = ENSMUSG00000022620
| Mm_RefseqmRNA = NM_009713
| Mm_RefseqProtein = NP_033843
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 89300257
| Mm_GenLoc_end = 89305192
| Mm_Uniprot = Q9DC66
}}
}}
'''Arylsulfatase A''', also known as '''ARSA''', 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 hydrolyzes cerebroside sulfate to cerebroside and sulfate. Defects in this gene lead to metachromatic leucodystrophy (MLD), a progressive demyelination disease which results in a variety of neurological symptoms and ultimately death. Multiple alternatively spliced transcript variants, one of which encodes a distinct protein, have been described for this gene.<ref>{{cite web | title = Entrez Gene: ARSA arylsulfatase A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=410| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Narahara K, Takahashi Y, Murakami M, ''et al.'' |title=Terminal 22q deletion associated with a partial deficiency of arylsulphatase A. |journal=J. Med. Genet. |volume=29 |issue= 6 |pages= 432-3 |year= 1992 |pmid= 1352356 |doi= }}
*{{cite journal | author=Gieselmann V, Zlotogora J, Harris A, ''et al.'' |title=Molecular genetics of metachromatic leukodystrophy. |journal=Hum. Mutat. |volume=4 |issue= 4 |pages= 233-42 |year= 1995 |pmid= 7866401 |doi= 10.1002/humu.1380040402 }}
*{{cite journal | author=DeLuca C, Brown JA, Shows TB |title=Lysosomal arylsulfatase deficiencies in humans: chromosome assignments for arylsulfatase A and B. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=76 |issue= 4 |pages= 1957-61 |year= 1979 |pmid= 36611 |doi= }}
*{{cite journal | author=Fujii T, Kobayashi T, Honke K, ''et al.'' |title=Proteolytic processing of human lysosomal arylsulfatase A. |journal=Biochim. Biophys. Acta |volume=1122 |issue= 1 |pages= 93-8 |year= 1992 |pmid= 1352993 |doi= }}
*{{cite journal | author=Kappler J, von Figura K, Gieselmann V |title=Late-onset metachromatic leukodystrophy: molecular pathology in two siblings. |journal=Ann. Neurol. |volume=31 |issue= 3 |pages= 256-61 |year= 1992 |pmid= 1353340 |doi= 10.1002/ana.410310305 }}
*{{cite journal | author=Li ZG, Waye JS, Chang PL |title=Diagnosis of arylsulfatase A deficiency. |journal=Am. J. Med. Genet. |volume=43 |issue= 6 |pages= 976-82 |year= 1992 |pmid= 1357970 |doi= 10.1002/ajmg.1320430614 }}
*{{cite journal | author=Polten A, Fluharty AL, Fluharty CB, ''et al.'' |title=Molecular basis of different forms of metachromatic leukodystrophy. |journal=N. Engl. J. Med. |volume=324 |issue= 1 |pages= 18-22 |year= 1991 |pmid= 1670590 |doi= }}
*{{cite journal | author=Kondo R, Wakamatsu N, Yoshino H, ''et al.'' |title=Identification of a mutation in the arylsulfatase A gene of a patient with adult-type metachromatic leukodystrophy. |journal=Am. J. Hum. Genet. |volume=48 |issue= 5 |pages= 971-8 |year= 1991 |pmid= 1673291 |doi= }}
*{{cite journal | author=Nelson PV, Carey WF, Morris CP |title=Population frequency of the arylsulphatase A pseudo-deficiency allele. |journal=Hum. Genet. |volume=87 |issue= 1 |pages= 87-8 |year= 1991 |pmid= 1674719 |doi= }}
*{{cite journal | author=Bohne W, von Figura K, Gieselmann V |title=An 11-bp deletion in the arylsulfatase A gene of a patient with late infantile metachromatic leukodystrophy. |journal=Hum. Genet. |volume=87 |issue= 2 |pages= 155-8 |year= 1991 |pmid= 1676699 |doi= }}
*{{cite journal | author=Gieselmann V, Fluharty AL, Tønnesen T, Von Figura K |title=Mutations in the arylsulfatase A pseudodeficiency allele causing metachromatic leukodystrophy. |journal=Am. J. Hum. Genet. |volume=49 |issue= 2 |pages= 407-13 |year= 1991 |pmid= 1678251 |doi= }}
*{{cite journal | author=Fluharty AL, Fluharty CB, Bohne W, ''et al.'' |title=Two new arylsulfatase A (ARSA) mutations in a juvenile metachromatic leukodystrophy (MLD) patient. |journal=Am. J. Hum. Genet. |volume=49 |issue= 6 |pages= 1340-50 |year= 1992 |pmid= 1684088 |doi= }}
*{{cite journal | author=Kreysing J, von Figura K, Gieselmann V |title=Structure of the arylsulfatase A gene. |journal=Eur. J. Biochem. |volume=191 |issue= 3 |pages= 627-31 |year= 1990 |pmid= 1975241 |doi= }}
*{{cite journal | author=Stein C, Gieselmann V, Kreysing J, ''et al.'' |title=Cloning and expression of human arylsulfatase A. |journal=J. Biol. Chem. |volume=264 |issue= 2 |pages= 1252-9 |year= 1989 |pmid= 2562955 |doi= }}
*{{cite journal | author=Gieselmann V, Polten A, Kreysing J, von Figura K |title=Arylsulfatase A pseudodeficiency: loss of a polyadenylylation signal and N-glycosylation site. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 23 |pages= 9436-40 |year= 1990 |pmid= 2574462 |doi= }}
*{{cite journal | author=Geurts van Kessel AH, Westerveld A, de Groot PG, ''et al.'' |title=Regional localization of the genes coding for human ACO2, ARSA, and NAGA on chromosome 22. |journal=Cytogenet. Cell Genet. |volume=28 |issue= 3 |pages= 169-72 |year= 1981 |pmid= 7192199 |doi= }}
*{{cite journal | author=Barth ML, Fensom A, Harris A |title=Identification of seven novel mutations associated with metachromatic leukodystrophy. |journal=Hum. Mutat. |volume=6 |issue= 2 |pages= 170-6 |year= 1995 |pmid= 7581401 |doi= 10.1002/humu.1380060210 }}
*{{cite journal | author=Schmidt B, Selmer T, Ingendoh A, von Figura K |title=A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. |journal=Cell |volume=82 |issue= 2 |pages= 271-8 |year= 1995 |pmid= 7628016 |doi= }}
*{{cite journal | author=Barth ML, Ward C, Harris A, ''et al.'' |title=Frequency of arylsulphatase A pseudodeficiency associated mutations in a healthy population. |journal=J. Med. Genet. |volume=31 |issue= 9 |pages= 667-71 |year= 1995 |pmid= 7815433 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AVPR2... {November 14, 2007 3:50:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:51:32 PM PST}
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Arginine vasopressin receptor 2 (nephrogenic diabetes insipidus)
| HGNCid = 897
| Symbol = AVPR2
| AltSymbols =; ADHR; DI1; DIR; DIR3; MGC126533; MGC138386; NDI; V2R
| OMIM = 300538
| ECnumber =
| Homologene = 20064
| MGIid = 88123
| GeneAtlas_image1 = PBB_GE_AVPR2_208111_at_tn.png
| GeneAtlas_image2 = PBB_GE_AVPR2_208108_s_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005000 |text = vasopressin receptor activity}}
| Component = {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007188 |text = G-protein signaling, coupled to cAMP nucleotide second messenger}} {{GNF_GO|id=GO:0007190 |text = adenylate cyclase activation}} {{GNF_GO|id=GO:0007588 |text = excretion}} {{GNF_GO|id=GO:0007599 |text = hemostasis}} {{GNF_GO|id=GO:0008150 |text = biological_process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 554
| Hs_Ensembl = ENSG00000126895
| Hs_RefseqProtein = NP_000045
| Hs_RefseqmRNA = NM_000054
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 152823383
| Hs_GenLoc_end = 152825834
| Hs_Uniprot = P30518
| Mm_EntrezGene = 12000
| Mm_Ensembl = ENSMUSG00000031390
| Mm_RefseqmRNA = NM_019404
| Mm_RefseqProtein = NP_062277
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 70126278
| Mm_GenLoc_end = 70147147
| Mm_Uniprot = Q3KNZ4
}}
}}
'''Arginine vasopressin receptor 2 (nephrogenic diabetes insipidus)''', also known as '''AVPR2''', 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 human AVPR2 locus encodes the vasopressin receptor, type 2, also known as the V2 receptor, located in cytogenetic band Xq28. The gene's three exons and two introns are contained within 2.1 kilobases. The L1CAM gene lies some 29 kb centromeric to AVPR2, and the C1 gene immediately teleomeric. Both are apparently transcribed in opposite orientation to AVPR2 (see NID g1302657). The AVPR2 protein product belongs to the seven-transmembrane-domain G protein-coupled receptor (GPCR) superfamily, and it couples to Gs thus stimulating adenylate cyclase. The subfamily that includes the V2 receptor, the V1a and V1b vasopressin receptors, the oxytocin receptor, and isotocin and mesotocin receptors in non-mammals, is well conserved, though several members signal via other G proteins. All bind similar cyclic nonapeptide hormones. The V2 receptor is expressed in the kidney tubule, predominantly in the distal convoluted tubule and collecting ducts, where its primary property is to respond to the pituitary hormone arginine vasopressin (AVP) by stimulating mechanisms that concentrate the urine and maintain water homeostasis in the organism. When the function of this gene is lost, the disease Nephrogenic Diabetes Insipidus (NDI) results. The V2 receptor is also expressed outside the kidney although its tissue localization is uncertain. When these 'extrarenal receptors' are stimulated by infusion of a V2 selective agonist (dDAVP), a variety of clotting factors are released into the bloodstream. The physiologic importance of this property is not known - its absence does not appear to be detrimental in NDI patients. AVPR2 expression has also been described in fetal lung tissue and lung cancer associated with alternative splicing.<ref>{{cite web | title = Entrez Gene: AVPR2 arginine vasopressin receptor 2 (nephrogenic diabetes insipidus)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=554| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Birnbaumer M |title=The V2 vasopressin receptor mutations and fluid homeostasis. |journal=Cardiovasc. Res. |volume=51 |issue= 3 |pages= 409-15 |year= 2001 |pmid= 11476731 |doi= }}
*{{cite journal | author=Ishikawa SE |title=[Nephrogenic diabetes insipidus associated with mutations of vasopressin V2 receptors and aquaporin-2] |journal=Nippon Rinsho |volume=60 |issue= 2 |pages= 350-5 |year= 2002 |pmid= 11857925 |doi= }}
*{{cite journal | author=Thibonnier M, Coles P, Thibonnier A, Shoham M |title=Molecular pharmacology and modeling of vasopressin receptors. |journal=Prog. Brain Res. |volume=139 |issue= |pages= 179-96 |year= 2002 |pmid= 12436935 |doi= }}
*{{cite journal | author=Bichet DG |title=Nephrogenic diabetes insipidus. |journal=Advances in chronic kidney disease |volume=13 |issue= 2 |pages= 96-104 |year= 2006 |pmid= 16580609 |doi= 10.1053/j.ackd.2006.01.006 }}
*{{cite journal | author=Robben JH, Knoers NV, Deen PM |title=Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water channel in nephrogenic diabetes insipidus. |journal=Am. J. Physiol. Renal Physiol. |volume=291 |issue= 2 |pages= F257-70 |year= 2006 |pmid= 16825342 |doi= 10.1152/ajprenal.00491.2005 }}
*{{cite journal | author=Pan Y, Metzenberg A, Das S, ''et al.'' |title=Mutations in the V2 vasopressin receptor gene are associated with X-linked nephrogenic diabetes insipidus. |journal=Nat. Genet. |volume=2 |issue= 2 |pages= 103-6 |year= 1993 |pmid= 1303257 |doi= 10.1038/ng1092-103 }}
*{{cite journal | author=van den Ouweland AM, Dreesen JC, Verdijk M, ''et al.'' |title=Mutations in the vasopressin type 2 receptor gene (AVPR2) associated with nephrogenic diabetes insipidus. |journal=Nat. Genet. |volume=2 |issue= 2 |pages= 99-102 |year= 1993 |pmid= 1303271 |doi= 10.1038/ng1092-99 }}
*{{cite journal | author=van den Ouweland AM, Knoop MT, Knoers VV, ''et al.'' |title=Colocalization of the gene for nephrogenic diabetes insipidus (DIR) and the vasopressin type 2 receptor gene (AVPR2) in the Xq28 region. |journal=Genomics |volume=13 |issue= 4 |pages= 1350-2 |year= 1992 |pmid= 1324225 |doi= }}
*{{cite journal | author=Rosenthal W, Seibold A, Antaramian A, ''et al.'' |title=Molecular identification of the gene responsible for congenital nephrogenic diabetes insipidus. |journal=Nature |volume=359 |issue= 6392 |pages= 233-5 |year= 1992 |pmid= 1356229 |doi= 10.1038/359233a0 }}
*{{cite journal | author=Seibold A, Brabet P, Rosenthal W, Birnbaumer M |title=Structure and chromosomal localization of the human antidiuretic hormone receptor gene. |journal=Am. J. Hum. Genet. |volume=51 |issue= 5 |pages= 1078-83 |year= 1992 |pmid= 1415251 |doi= }}
*{{cite journal | author=Birnbaumer M, Seibold A, Gilbert S, ''et al.'' |title=Molecular cloning of the receptor for human antidiuretic hormone. |journal=Nature |volume=357 |issue= 6376 |pages= 333-5 |year= 1992 |pmid= 1534149 |doi= 10.1038/357333a0 }}
*{{cite journal | author=Lolait SJ, O'Carroll AM, McBride OW, ''et al.'' |title=Cloning and characterization of a vasopressin V2 receptor and possible link to nephrogenic diabetes insipidus. |journal=Nature |volume=357 |issue= 6376 |pages= 336-9 |year= 1992 |pmid= 1534150 |doi= 10.1038/357336a0 }}
*{{cite journal | author=Knoers N, van der Heyden H, van Oost BA, ''et al.'' |title=Three-point linkage analysis using multiple DNA polymorphic markers in families with X-linked nephrogenic diabetes insipidus. |journal=Genomics |volume=4 |issue= 3 |pages= 434-7 |year= 1989 |pmid= 2714800 |doi= }}
*{{cite journal | author=Tsukaguchi H, Matsubara H, Taketani S, ''et al.'' |title=Binding-, intracellular transport-, and biosynthesis-defective mutants of vasopressin type 2 receptor in patients with X-linked nephrogenic diabetes insipidus. |journal=J. Clin. Invest. |volume=96 |issue= 4 |pages= 2043-50 |year= 1995 |pmid= 7560098 |doi= }}
*{{cite journal | author=Faà V, Ventruto ML, Loche S, ''et al.'' |title=Mutations in the vasopressin V2-receptor gene in three families of Italian descent with nephrogenic diabetes insipidus. |journal=Hum. Mol. Genet. |volume=3 |issue= 9 |pages= 1685-6 |year= 1995 |pmid= 7833930 |doi= }}
*{{cite journal | author=Birnbaumer M, Gilbert S, Rosenthal W |title=An extracellular congenital nephrogenic diabetes insipidus mutation of the vasopressin receptor reduces cell surface expression, affinity for ligand, and coupling to the Gs/adenylyl cyclase system. |journal=Mol. Endocrinol. |volume=8 |issue= 7 |pages= 886-94 |year= 1995 |pmid= 7984150 |doi= }}
*{{cite journal | author=Wenkert D, Merendino JJ, Shenker A, ''et al.'' |title=Novel mutations in the V2 vasopressin receptor gene of patients with X-linked nephrogenic diabetes insipidus. |journal=Hum. Mol. Genet. |volume=3 |issue= 8 |pages= 1429-30 |year= 1995 |pmid= 7987330 |doi= }}
*{{cite journal | author=Oksche A, Dickson J, Schülein R, ''et al.'' |title=Two novel mutations in the vasopressin V2 receptor gene in patients with congenital nephrogenic diabetes insipidus. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 1 |pages= 552-7 |year= 1995 |pmid= 7999078 |doi= 10.1006/bbrc.1994.2700 }}
*{{cite journal | author=Bichet DG, Birnbaumer M, Lonergan M, ''et al.'' |title=Nature and recurrence of AVPR2 mutations in X-linked nephrogenic diabetes insipidus. |journal=Am. J. Hum. Genet. |volume=55 |issue= 2 |pages= 278-86 |year= 1994 |pmid= 8037205 |doi= }}
*{{cite journal | author=Yuasa H, Ito M, Oiso Y, ''et al.'' |title=Novel mutations in the V2 vasopressin receptor gene in two pedigrees with congenital nephrogenic diabetes insipidus. |journal=J. Clin. Endocrinol. Metab. |volume=79 |issue= 2 |pages= 361-5 |year= 1994 |pmid= 8045948 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CAMP... {November 14, 2007 3:51:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:52:11 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cathelicidin antimicrobial peptide
| HGNCid = 1472
| Symbol = CAMP
| AltSymbols =; CAP18; FALL-39; FALL39; HSD26; LL37
| OMIM = 600474
| ECnumber =
| Homologene = 3206
| MGIid = 108443
| GeneAtlas_image1 = PBB_GE_CAMP_210244_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 820
| Hs_Ensembl = ENSG00000164047
| Hs_RefseqProtein = NP_004336
| Hs_RefseqmRNA = NM_004345
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 48239866
| Hs_GenLoc_end = 48241979
| Hs_Uniprot = P49913
| Mm_EntrezGene = 12796
| Mm_Ensembl = ENSMUSG00000038357
| Mm_RefseqmRNA = NM_009921
| Mm_RefseqProtein = NP_034051
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 109704793
| Mm_GenLoc_end = 109706855
| Mm_Uniprot = Q0VB78
}}
}}
'''Cathelicidin antimicrobial peptide''', also known as '''CAMP''', 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 = Cathelicidin antimicrobial protein is an antimicrobial protein found in specific granules of polymorphonuclear leukocytes (PMNs).[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: CAMP cathelicidin antimicrobial peptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=820| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lehrer RI, Ganz T |title=Cathelicidins: a family of endogenous antimicrobial peptides. |journal=Curr. Opin. Hematol. |volume=9 |issue= 1 |pages= 18-22 |year= 2002 |pmid= 11753073 |doi= }}
*{{cite journal | author=Niyonsaba F, Hirata M, Ogawa H, Nagaoka I |title=Epithelial cell-derived antibacterial peptides human beta-defensins and cathelicidin: multifunctional activities on mast cells. |journal=Current drug targets. Inflammation and allergy |volume=2 |issue= 3 |pages= 224-31 |year= 2003 |pmid= 14561157 |doi= }}
*{{cite journal | author=van Wetering S, Tjabringa GS, Hiemstra PS |title=Interactions between neutrophil-derived antimicrobial peptides and airway epithelial cells. |journal=J. Leukoc. Biol. |volume=77 |issue= 4 |pages= 444-50 |year= 2005 |pmid= 15591123 |doi= 10.1189/jlb.0604367 }}
*{{cite journal | author=Agerberth B, Gunne H, Odeberg J, ''et al.'' |title=FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 1 |pages= 195-9 |year= 1995 |pmid= 7529412 |doi= }}
*{{cite journal | author=Cowland JB, Johnsen AH, Borregaard N |title=hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil specific granules. |journal=FEBS Lett. |volume=368 |issue= 1 |pages= 173-6 |year= 1995 |pmid= 7615076 |doi= }}
*{{cite journal | author=Gudmundsson GH, Magnusson KP, Chowdhary BP, ''et al.'' |title=Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 15 |pages= 7085-9 |year= 1995 |pmid= 7624374 |doi= }}
*{{cite journal | author=Larrick JW, Hirata M, Balint RF, ''et al.'' |title=Human CAP18: a novel antimicrobial lipopolysaccharide-binding protein. |journal=Infect. Immun. |volume=63 |issue= 4 |pages= 1291-7 |year= 1995 |pmid= 7890387 |doi= }}
*{{cite journal | author=Gudmundsson GH, Agerberth B, Odeberg J, ''et al.'' |title=The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. |journal=Eur. J. Biochem. |volume=238 |issue= 2 |pages= 325-32 |year= 1996 |pmid= 8681941 |doi= }}
*{{cite journal | author=Larrick JW, Lee J, Ma S, ''et al.'' |title=Structural, functional analysis and localization of the human CAP18 gene. |journal=FEBS Lett. |volume=398 |issue= 1 |pages= 74-80 |year= 1997 |pmid= 8946956 |doi= }}
*{{cite journal | author=Frohm M, Agerberth B, Ahangari G, ''et al.'' |title=The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. |journal=J. Biol. Chem. |volume=272 |issue= 24 |pages= 15258-63 |year= 1997 |pmid= 9182550 |doi= }}
*{{cite journal | author=Bals R, Wang X, Zasloff M, Wilson JM |title=The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 16 |pages= 9541-6 |year= 1998 |pmid= 9689116 |doi= }}
*{{cite journal | author=Frohm Nilsson M, Sandstedt B, Sørensen O, ''et al.'' |title=The human cationic antimicrobial protein (hCAP18), a peptide antibiotic, is widely expressed in human squamous epithelia and colocalizes with interleukin-6. |journal=Infect. Immun. |volume=67 |issue= 5 |pages= 2561-6 |year= 1999 |pmid= 10225921 |doi= }}
*{{cite journal | author=Malm J, Sørensen O, Persson T, ''et al.'' |title=The human cationic antimicrobial protein (hCAP-18) is expressed in the epithelium of human epididymis, is present in seminal plasma at high concentrations, and is attached to spermatozoa. |journal=Infect. Immun. |volume=68 |issue= 7 |pages= 4297-302 |year= 2000 |pmid= 10858248 |doi= }}
*{{cite journal | author=De Yang , Chen Q, Schmidt AP, ''et al.'' |title=LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. |journal=J. Exp. Med. |volume=192 |issue= 7 |pages= 1069-74 |year= 2000 |pmid= 11015447 |doi= }}
*{{cite journal | author=Agerberth B, Charo J, Werr J, ''et al.'' |title=The human antimicrobial and chemotactic peptides LL-37 and alpha-defensins are expressed by specific lymphocyte and monocyte populations. |journal=Blood |volume=96 |issue= 9 |pages= 3086-93 |year= 2000 |pmid= 11049988 |doi= }}
*{{cite journal | author=Bals R, Lang C, Weiner DJ, ''et al.'' |title=Rhesus monkey (Macaca mulatta) mucosal antimicrobial peptides are close homologues of human molecules. |journal=Clin. Diagn. Lab. Immunol. |volume=8 |issue= 2 |pages= 370-5 |year= 2001 |pmid= 11238224 |doi= 10.1128/CDLI.8.2.370-375.2001 }}
*{{cite journal | author=Sørensen OE, Follin P, Johnsen AH, ''et al.'' |title=Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. |journal=Blood |volume=97 |issue= 12 |pages= 3951-9 |year= 2001 |pmid= 11389039 |doi= }}
*{{cite journal | author=Nagaoka I, Hirota S, Niyonsaba F, ''et al.'' |title=Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-alpha by blocking the binding of LPS to CD14(+) cells. |journal=J. Immunol. |volume=167 |issue= 6 |pages= 3329-38 |year= 2001 |pmid= 11544322 |doi= }}
*{{cite journal | author=Hase K, Eckmann L, Leopard JD, ''et al.'' |title=Cell differentiation is a key determinant of cathelicidin LL-37/human cationic antimicrobial protein 18 expression by human colon epithelium. |journal=Infect. Immun. |volume=70 |issue= 2 |pages= 953-63 |year= 2002 |pmid= 11796631 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD9... {November 14, 2007 3:52:11 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:52:54 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 = CD9 molecule
| HGNCid = 1709
| Symbol = CD9
| AltSymbols =; 5H9; BA2; BTCC-1; DRAP-27; GIG2; MIC3; MRP-1; P24; TSPAN29
| OMIM = 143030
| ECnumber =
| Homologene = 20420
| MGIid = 88348
| GeneAtlas_image1 = PBB_GE_CD9_201005_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:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007342 |text = fusion of sperm to egg plasma membrane}} {{GNF_GO|id=GO:0030168 |text = platelet activation}} {{GNF_GO|id=GO:0030913 |text = paranodal junction assembly}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 928
| Hs_Ensembl = ENSG00000010278
| Hs_RefseqProtein = NP_001760
| Hs_RefseqmRNA = NM_001769
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 6179134
| Hs_GenLoc_end = 6217686
| Hs_Uniprot = P21926
| Mm_EntrezGene = 12527
| Mm_Ensembl = ENSMUSG00000030342
| Mm_RefseqmRNA = NM_007657
| Mm_RefseqProtein = NP_031683
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 125425885
| Mm_GenLoc_end = 125460379
| Mm_Uniprot = P40240
}}
}}
'''CD9 molecule''', also known as '''CD9''', 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 transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is a cell surface glycoprotein that is known to complex with integrins and other transmembrane 4 superfamily proteins. It can modulate cell adhesion and migration and also trigger platelet activation and aggregation. In addition, the protein appears to promote muscle cell fusion and support myotube maintenance.<ref>{{cite web | title = Entrez Gene: CD9 CD9 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=928| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Horejsí V, Vlcek C |title=Novel structurally distinct family of leucocyte surface glycoproteins including CD9, CD37, CD53 and CD63. |journal=FEBS Lett. |volume=288 |issue= 1-2 |pages= 1-4 |year= 1991 |pmid= 1879540 |doi= }}
*{{cite journal | author=Berditchevski F |title=Complexes of tetraspanins with integrins: more than meets the eye. |journal=J. Cell. Sci. |volume=114 |issue= Pt 23 |pages= 4143-51 |year= 2002 |pmid= 11739647 |doi= }}
*{{cite journal | author=Ninomiya H, Sims PJ |title=The human complement regulatory protein CD59 binds to the alpha-chain of C8 and to the "b"domain of C9. |journal=J. Biol. Chem. |volume=267 |issue= 19 |pages= 13675-80 |year= 1992 |pmid= 1377690 |doi= }}
*{{cite journal | author=Miyake M, Koyama M, Seno M, Ikeyama S |title=Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility. |journal=J. Exp. Med. |volume=174 |issue= 6 |pages= 1347-54 |year= 1992 |pmid= 1720807 |doi= }}
*{{cite journal | author=Boucheix C, Benoit P, Frachet P, ''et al.'' |title=Molecular cloning of the CD9 antigen. A new family of cell surface proteins. |journal=J. Biol. Chem. |volume=266 |issue= 1 |pages= 117-22 |year= 1991 |pmid= 1840589 |doi= }}
*{{cite journal | author=Iwamoto R, Senoh H, Okada Y, ''et al.'' |title=An antibody that inhibits the binding of diphtheria toxin to cells revealed the association of a 27-kDa membrane protein with the diphtheria toxin receptor. |journal=J. Biol. Chem. |volume=266 |issue= 30 |pages= 20463-9 |year= 1991 |pmid= 1939101 |doi= }}
*{{cite journal | author=Benoit P, Gross MS, Frachet P, ''et al.'' |title=Assignment of the human CD9 gene to chromosome 12 (region P13) by use of human specific DNA probes. |journal=Hum. Genet. |volume=86 |issue= 3 |pages= 268-72 |year= 1991 |pmid= 1997380 |doi= }}
*{{cite journal | author=Lanza F, Wolf D, Fox CF, ''et al.'' |title=cDNA cloning and expression of platelet p24/CD9. Evidence for a new family of multiple membrane-spanning proteins. |journal=J. Biol. Chem. |volume=266 |issue= 16 |pages= 10638-45 |year= 1991 |pmid= 2037603 |doi= }}
*{{cite journal | author=Higashihara M, Takahata K, Yatomi Y, ''et al.'' |title=Purification and partial characterization of CD9 antigen of human platelets. |journal=FEBS Lett. |volume=264 |issue= 2 |pages= 270-4 |year= 1990 |pmid= 2358073 |doi= }}
*{{cite journal | author=Katz F, Povey S, Parkar M, ''et al.'' |title=Chromosome assignment of monoclonal antibody-defined determinants on human leukemic cells. |journal=Eur. J. Immunol. |volume=13 |issue= 12 |pages= 1008-13 |year= 1984 |pmid= 6198179 |doi= }}
*{{cite journal | author=Masellis-Smith A, Shaw AR |title=CD9-regulated adhesion. Anti-CD9 monoclonal antibody induce pre-B cell adhesion to bone marrow fibroblasts through de novo recognition of fibronectin. |journal=J. Immunol. |volume=152 |issue= 6 |pages= 2768-77 |year= 1994 |pmid= 7511626 |doi= }}
*{{cite journal | author=Chalupny NJ, Kanner SB, Schieven GL, ''et al.'' |title=Tyrosine phosphorylation of CD19 in pre-B and mature B cells. |journal=EMBO J. |volume=12 |issue= 7 |pages= 2691-6 |year= 1993 |pmid= 7687539 |doi= }}
*{{cite journal | author=Ikeyama S, Koyama M, Yamaoko M, ''et al.'' |title=Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1/CD9) DNA. |journal=J. Exp. Med. |volume=177 |issue= 5 |pages= 1231-7 |year= 1993 |pmid= 8478605 |doi= }}
*{{cite journal | author=Rubinstein E, Benoit P, Billard M, ''et al.'' |title=Organization of the human CD9 gene. |journal=Genomics |volume=16 |issue= 1 |pages= 132-8 |year= 1993 |pmid= 8486348 |doi= 10.1006/geno.1993.1150 }}
*{{cite journal | author=Radford KJ, Thorne RF, Hersey P |title=CD63 associates with transmembrane 4 superfamily members, CD9 and CD81, and with beta 1 integrins in human melanoma. |journal=Biochem. Biophys. Res. Commun. |volume=222 |issue= 1 |pages= 13-8 |year= 1996 |pmid= 8630057 |doi= 10.1006/bbrc.1996.0690 }}
*{{cite journal | author=Schmidt C, Künemund V, Wintergerst ES, ''et al.'' |title=CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the alpha 6/beta 1 integrin and the neural adhesion molecule L1. |journal=J. Neurosci. Res. |volume=43 |issue= 1 |pages= 12-31 |year= 1996 |pmid= 8838570 |doi= 10.1002/jnr.490430103 }}
*{{cite journal | author=Sincock PM, Mayrhofer G, Ashman LK |title=Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and alpha5beta1 integrin. |journal=J. Histochem. Cytochem. |volume=45 |issue= 4 |pages= 515-25 |year= 1997 |pmid= 9111230 |doi= }}
*{{cite journal | author=Rubinstein E, Poindessous-Jazat V, Le Naour F, ''et al.'' |title=CD9, but not other tetraspans, associates with the beta1 integrin precursor. |journal=Eur. J. Immunol. |volume=27 |issue= 8 |pages= 1919-27 |year= 1997 |pmid= 9295027 |doi= }}
*{{cite journal | author=Tachibana I, Bodorova J, Berditchevski F, ''et al.'' |title=NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins. |journal=J. Biol. Chem. |volume=272 |issue= 46 |pages= 29181-9 |year= 1997 |pmid= 9360996 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CHRNA7... {November 14, 2007 3:52:54 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:53:24 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 = Cholinergic receptor, nicotinic, alpha 7
| HGNCid = 1960
| Symbol = CHRNA7
| AltSymbols =; NACHRA7
| OMIM = 118511
| ECnumber =
| Homologene = 593
| MGIid = 99779
| Function = {{GNF_GO|id=GO:0004889 |text = nicotinic acetylcholine-activated cation-selective channel activity}} {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005230 |text = extracellular ligand-gated ion channel activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015464 |text = acetylcholine receptor activity}} {{GNF_GO|id=GO:0030594 |text = neurotransmitter receptor activity}}
| Component = {{GNF_GO|id=GO:0005892 |text = nicotinic acetylcholine-gated receptor-channel complex}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0045211 |text = postsynaptic membrane}}
| Process = {{GNF_GO|id=GO:0000187 |text = activation of MAPK activity}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1139
| Hs_Ensembl =
| Hs_RefseqProtein = XP_001127577
| Hs_RefseqmRNA = XM_001127577
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 11441
| Mm_Ensembl = ENSMUSG00000030525
| Mm_RefseqmRNA = NM_007390
| Mm_RefseqProtein = NP_031416
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 62977642
| Mm_GenLoc_end = 63091519
| Mm_Uniprot = Q53YJ9
}}
}}
'''Cholinergic receptor, nicotinic, alpha 7''', also known as '''CHRNA7''', 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 nicotinic acetylcholine receptors (nAChRs) are members of a superfamily of ligand-gated ion channels that mediate fast signal transmission at synapses. The nAChRs are thought to be hetero-pentamers composed of homologous subunits. The proposed structure for each subunit is a conserved N-terminal extracellular domain followed by three conserved transmembrane domains, a variable cytoplasmic loop, a fourth conserved transmembrane domain, and a short C-terminal extracellular region. The protein encoded by this gene forms a homo-oligomeric channel, displays marked permeability to calcium ions and is a major component of brain nicotinic receptors that are blocked by, and highly sensitive to, alpha-bungarotoxin. Once this receptor binds acetylcholine, it undergoes an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. This gene is located in a region identified as a major susceptibility locus for juvenile myoclonic epilepsy and a chromosomal location involved in the genetic transmission of schizophrenia. An evolutionarily recent partial duplication event in this region results in a hybrid containing sequence from this gene and a novel FAM7A gene.<ref>{{cite web | title = Entrez Gene: CHRNA7 cholinergic receptor, nicotinic, alpha 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1139| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Green WN, Millar NS |title=Ion-channel assembly. |journal=Trends Neurosci. |volume=18 |issue= 6 |pages= 280-7 |year= 1995 |pmid= 7571003 |doi= }}
*{{cite journal | author=Hogg RC, Raggenbass M, Bertrand D |title=Nicotinic acetylcholine receptors: from structure to brain function. |journal=Rev. Physiol. Biochem. Pharmacol. |volume=147 |issue= |pages= 1-46 |year= 2003 |pmid= 12783266 |doi= 10.1007/s10254-003-0005-1 }}
*{{cite journal | author=Gallowitsch-Puerta M, Tracey KJ |title=Immunologic role of the cholinergic anti-inflammatory pathway and the nicotinic acetylcholine alpha 7 receptor. |journal=Ann. N. Y. Acad. Sci. |volume=1062 |issue= |pages= 209-19 |year= 2006 |pmid= 16461803 |doi= 10.1196/annals.1358.024 }}
*{{cite journal | author=Peng X, Katz M, Gerzanich V, ''et al.'' |title=Human alpha 7 acetylcholine receptor: cloning of the alpha 7 subunit from the SH-SY5Y cell line and determination of pharmacological properties of native receptors and functional alpha 7 homomers expressed in Xenopus oocytes. |journal=Mol. Pharmacol. |volume=45 |issue= 3 |pages= 546-54 |year= 1994 |pmid= 8145738 |doi= }}
*{{cite journal | author=Chini B, Raimond E, Elgoyhen AB, ''et al.'' |title=Molecular cloning and chromosomal localization of the human alpha 7-nicotinic receptor subunit gene (CHRNA7). |journal=Genomics |volume=19 |issue= 2 |pages= 379-81 |year= 1994 |pmid= 8188270 |doi= 10.1006/geno.1994.1075 }}
*{{cite journal | author=Hillier LD, Lennon G, Becker M, ''et al.'' |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807-28 |year= 1997 |pmid= 8889549 |doi= }}
*{{cite journal | author=Elliott KJ, Ellis SB, Berckhan KJ, ''et al.'' |title=Comparative structure of human neuronal alpha 2-alpha 7 and beta 2-beta 4 nicotinic acetylcholine receptor subunits and functional expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and beta 4 subunits. |journal=J. Mol. Neurosci. |volume=7 |issue= 3 |pages= 217-28 |year= 1997 |pmid= 8906617 |doi= }}
*{{cite journal | author=Chavez-Noriega LE, Crona JH, Washburn MS, ''et al.'' |title=Pharmacological characterization of recombinant human neuronal nicotinic acetylcholine receptors h alpha 2 beta 2, h alpha 2 beta 4, h alpha 3 beta 2, h alpha 3 beta 4, h alpha 4 beta 2, h alpha 4 beta 4 and h alpha 7 expressed in Xenopus oocytes. |journal=J. Pharmacol. Exp. Ther. |volume=280 |issue= 1 |pages= 346-56 |year= 1997 |pmid= 8996215 |doi= }}
*{{cite journal | author=Groot Kormelink PJ, Luyten WH |title=Cloning and sequence of full-length cDNAs encoding the human neuronal nicotinic acetylcholine receptor (nAChR) subunits beta3 and beta4 and expression of seven nAChR subunits in the human neuroblastoma cell line SH-SY5Y and/or IMR-32. |journal=FEBS Lett. |volume=400 |issue= 3 |pages= 309-14 |year= 1997 |pmid= 9009220 |doi= }}
*{{cite journal | author=Navaneetham D, Penn A, Howard J, Conti-Fine BM |title=Expression of the alpha 7 subunit of the nicotinic acetylcholine receptor in normal and myasthenic human thymuses. |journal=Cell. Mol. Biol. (Noisy-le-grand) |volume=43 |issue= 3 |pages= 433-42 |year= 1997 |pmid= 9193799 |doi= }}
*{{cite journal | author=Gault J, Robinson M, Berger R, ''et al.'' |title=Genomic organization and partial duplication of the human alpha7 neuronal nicotinic acetylcholine receptor gene (CHRNA7). |journal=Genomics |volume=52 |issue= 2 |pages= 173-85 |year= 1998 |pmid= 9782083 |doi= 10.1006/geno.1998.5363 }}
*{{cite journal | author=Curtis L, Blouin JL, Radhakrishna U, ''et al.'' |title=No evidence for linkage between schizophrenia and markers at chromosome 15q13-14. |journal=Am. J. Med. Genet. |volume=88 |issue= 2 |pages= 109-12 |year= 1999 |pmid= 10206225 |doi= }}
*{{cite journal | author=Sander T, Schulz H, Vieira-Saeker AM, ''et al.'' |title=Evaluation of a putative major susceptibility locus for juvenile myoclonic epilepsy on chromosome 15q14. |journal=Am. J. Med. Genet. |volume=88 |issue= 2 |pages= 182-7 |year= 1999 |pmid= 10206240 |doi= }}
*{{cite journal | author=Sato KZ, Fujii T, Watanabe Y, ''et al.'' |title=Diversity of mRNA expression for muscarinic acetylcholine receptor subtypes and neuronal nicotinic acetylcholine receptor subunits in human mononuclear leukocytes and leukemic cell lines. |journal=Neurosci. Lett. |volume=266 |issue= 1 |pages= 17-20 |year= 1999 |pmid= 10336173 |doi= }}
*{{cite journal | author=Wang HY, Lee DH, D'Andrea MR, ''et al.'' |title=beta-Amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology. |journal=J. Biol. Chem. |volume=275 |issue= 8 |pages= 5626-32 |year= 2000 |pmid= 10681545 |doi= }}
*{{cite journal | author=Schuller HM, Jull BA, Sheppard BJ, Plummer HK |title=Interaction of tobacco-specific toxicants with the neuronal alpha(7) nicotinic acetylcholine receptor and its associated mitogenic signal transduction pathway: potential role in lung carcinogenesis and pediatric lung disorders. |journal=Eur. J. Pharmacol. |volume=393 |issue= 1-3 |pages= 265-77 |year= 2000 |pmid= 10771023 |doi= }}
*{{cite journal | author=Kihara T, Shimohama S, Sawada H, ''et al.'' |title=alpha 7 nicotinic receptor transduces signals to phosphatidylinositol 3-kinase to block A beta-amyloid-induced neurotoxicity. |journal=J. Biol. Chem. |volume=276 |issue= 17 |pages= 13541-6 |year= 2001 |pmid= 11278378 |doi= 10.1074/jbc.M008035200 }}
*{{cite journal | author=Freedman R, Leonard S, Gault JM, ''et al.'' |title=Linkage disequilibrium for schizophrenia at the chromosome 15q13-14 locus of the alpha7-nicotinic acetylcholine receptor subunit gene (CHRNA7). |journal=Am. J. Med. Genet. |volume=105 |issue= 1 |pages= 20-2 |year= 2001 |pmid= 11424985 |doi= }}
*{{cite journal | author=Engidawork E, Gulesserian T, Balic N, ''et al.'' |title=Changes in nicotinic acetylcholine receptor subunits expression in brain of patients with Down syndrome and Alzheimer's disease. |journal=J. Neural Transm. Suppl. |volume= |issue= 61 |pages= 211-22 |year= 2002 |pmid= 11771745 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CR1... {November 14, 2007 3:53:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:54:05 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_CR1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gkg.
| PDB = {{PDB2|1gkg}}, {{PDB2|1gkn}}, {{PDB2|1ppq}}
| Name = Complement component (3b/4b) receptor 1 (Knops blood group)
| HGNCid = 2334
| Symbol = CR1
| AltSymbols =; C3BR; CD35; KN
| OMIM = 120620
| ECnumber =
| Homologene = 55474
| MGIid =
| GeneAtlas_image1 = PBB_GE_CR1_206244_at_tn.png
| GeneAtlas_image2 = PBB_GE_CR1_208488_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_CR1_217552_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004877 |text = complement component C3b receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006958 |text = complement activation, classical pathway}} {{GNF_GO|id=GO:0045087 |text = innate immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1378
| Hs_Ensembl = ENSG00000203710
| Hs_RefseqProtein = XP_001126036
| Hs_RefseqmRNA = XM_001126036
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 205736125
| Hs_GenLoc_end = 205880615
| Hs_Uniprot = P17927
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Complement component (3b/4b) receptor 1 (Knops blood group)''', also known as '''CR1''', 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 a member of the receptors of complement activation (RCA) family and is located in the 'cluster RCA' region of chromosome 1. The gene encodes a monomeric single-pass type I membrane glycoprotein found on erythrocytes, leukocytes, glomerular podocytes, and splenic follicular dendritic cells. The Knops blood group system is a system of antigens located on this protein. The protein mediates cellular binding to particles and immune complexes that have activated complement. Decreases in expression of this protein and/or mutations in its gene have been associated with gallbladder carcinomas, mesangiocapillary glomerulonephritis, systemic lupus erythematosus and sarcoidosis. Mutations in this gene have also been associated with a reduction in Plasmodium falciparum rosetting, conferring protection against severe malaria. Alternate allele-specific splice variants, encoding different isoforms, have been characterized. Additional allele specific isoforms, including a secreted form, have been described but have not been fully characterized.<ref>{{cite web | title = Entrez Gene: CR1 complement component (3b/4b) receptor 1 (Knops blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1378| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ahearn JM, Fearon DT |title=Structure and function of the complement receptors, CR1 (CD35) and CR2 (CD21). |journal=Adv. Immunol. |volume=46 |issue= |pages= 183-219 |year= 1989 |pmid= 2551147 |doi= }}
*{{cite journal | author=Wong WW, Farrell SA |title=Proposed structure of the F' allotype of human CR1. Loss of a C3b binding site may be associated with altered function. |journal=J. Immunol. |volume=146 |issue= 2 |pages= 656-62 |year= 1991 |pmid= 1670949 |doi= }}
*{{cite journal | author=Tuveson DA, Ahearn JM, Matsumoto AK, Fearon DT |title=Molecular interactions of complement receptors on B lymphocytes: a CR1/CR2 complex distinct from the CR2/CD19 complex. |journal=J. Exp. Med. |volume=173 |issue= 5 |pages= 1083-9 |year= 1991 |pmid= 1708808 |doi= }}
*{{cite journal | author=Moulds JM, Nickells MW, Moulds JJ, ''et al.'' |title=The C3b/C4b receptor is recognized by the Knops, McCoy, Swain-langley, and York blood group antisera. |journal=J. Exp. Med. |volume=173 |issue= 5 |pages= 1159-63 |year= 1991 |pmid= 1708809 |doi= }}
*{{cite journal | author=Rao N, Ferguson DJ, Lee SF, Telen MJ |title=Identification of human erythrocyte blood group antigens on the C3b/C4b receptor. |journal=J. Immunol. |volume=146 |issue= 10 |pages= 3502-7 |year= 1991 |pmid= 1827486 |doi= }}
*{{cite journal | author=Hourcade D, Miesner DR, Bee C, ''et al.'' |title=Duplication and divergence of the amino-terminal coding region of the complement receptor 1 (CR1) gene. An example of concerted (horizontal) evolution within a gene. |journal=J. Biol. Chem. |volume=265 |issue= 2 |pages= 974-80 |year= 1990 |pmid= 2295627 |doi= }}
*{{cite journal | author=Reynes M, Aubert JP, Cohen JH, ''et al.'' |title=Human follicular dendritic cells express CR1, CR2, and CR3 complement receptor antigens. |journal=J. Immunol. |volume=135 |issue= 4 |pages= 2687-94 |year= 1985 |pmid= 2411809 |doi= }}
*{{cite journal | author=Hinglais N, Kazatchkine MD, Mandet C, ''et al.'' |title=Human liver Kupffer cells express CR1, CR3, and CR4 complement receptor antigens. An immunohistochemical study. |journal=Lab. Invest. |volume=61 |issue= 5 |pages= 509-14 |year= 1989 |pmid= 2478758 |doi= }}
*{{cite journal | author=Fearon DT, Klickstein LB, Wong WW, ''et al.'' |title=Immunoregulatory functions of complement: structural and functional studies of complement receptor type 1 (CR1; CD35) and type 2 (CR2; CD21). |journal=Prog. Clin. Biol. Res. |volume=297 |issue= |pages= 211-20 |year= 1989 |pmid= 2531419 |doi= }}
*{{cite journal | author=Wong WW, Cahill JM, Rosen MD, ''et al.'' |title=Structure of the human CR1 gene. Molecular basis of the structural and quantitative polymorphisms and identification of a new CR1-like allele. |journal=J. Exp. Med. |volume=169 |issue= 3 |pages= 847-63 |year= 1989 |pmid= 2564414 |doi= }}
*{{cite journal | author=Wong WW, Kennedy CA, Bonaccio ET, ''et al.'' |title=Analysis of multiple restriction fragment length polymorphisms of the gene for the human complement receptor type I. Duplication of genomic sequences occurs in association with a high molecular mass receptor allotype. |journal=J. Exp. Med. |volume=164 |issue= 5 |pages= 1531-46 |year= 1986 |pmid= 2877046 |doi= }}
*{{cite journal | author=Wong WW, Klickstein LB, Smith JA, ''et al.'' |title=Identification of a partial cDNA clone for the human receptor for complement fragments C3b/C4b. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 22 |pages= 7711-5 |year= 1985 |pmid= 2933745 |doi= }}
*{{cite journal | author=Klickstein LB, Wong WW, Smith JA, ''et al.'' |title=Human C3b/C4b receptor (CR1). Demonstration of long homologous repeating domains that are composed of the short consensus repeats characteristics of C3/C4 binding proteins. |journal=J. Exp. Med. |volume=165 |issue= 4 |pages= 1095-112 |year= 1987 |pmid= 2951479 |doi= }}
*{{cite journal | author=Moldenhauer F, David J, Fielder AH, ''et al.'' |title=Inherited deficiency of erythrocyte complement receptor type 1 does not cause susceptibility to systemic lupus erythematosus. |journal=Arthritis Rheum. |volume=30 |issue= 9 |pages= 961-6 |year= 1987 |pmid= 2959289 |doi= }}
*{{cite journal | author=Hourcade D, Miesner DR, Atkinson JP, Holers VM |title=Identification of an alternative polyadenylation site in the human C3b/C4b receptor (complement receptor type 1) transcriptional unit and prediction of a secreted form of complement receptor type 1. |journal=J. Exp. Med. |volume=168 |issue= 4 |pages= 1255-70 |year= 1988 |pmid= 2971757 |doi= }}
*{{cite journal | author=Klickstein LB, Bartow TJ, Miletic V, ''et al.'' |title=Identification of distinct C3b and C4b recognition sites in the human C3b/C4b receptor (CR1, CD35) by deletion mutagenesis. |journal=J. Exp. Med. |volume=168 |issue= 5 |pages= 1699-717 |year= 1988 |pmid= 2972794 |doi= }}
*{{cite journal | author=Hing S, Day AJ, Linton SJ, ''et al.'' |title=Assignment of complement components C4 binding protein (C4BP) and factor H (FH) to human chromosome 1q, using cDNA probes. |journal=Ann. Hum. Genet. |volume=52 |issue= Pt 2 |pages= 117-22 |year= 1989 |pmid= 2977721 |doi= }}
*{{cite journal | author=Fearon DT |title=Human complement receptors for C3b (CR1) and C3d (CR2). |journal=J. Invest. Dermatol. |volume=85 |issue= 1 Suppl |pages= 53s-57s |year= 1985 |pmid= 2989379 |doi= }}
*{{cite journal | author=Wilson JG, Murphy EE, Wong WW, ''et al.'' |title=Identification of a restriction fragment length polymorphism by a CR1 cDNA that correlates with the number of CR1 on erythrocytes. |journal=J. Exp. Med. |volume=164 |issue= 1 |pages= 50-9 |year= 1986 |pmid= 3014040 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CRKL... {November 14, 2007 3:54:05 PM PST}
- SEARCH REDIRECT: Control Box Found: CRKL {November 14, 2007 3:54:40 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 3:54:43 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 3:54:43 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 3:54:43 PM PST}
- UPDATED: Updated protein page: CRKL {November 14, 2007 3:54:50 PM PST}
- INFO: Beginning work on DLG1... {November 14, 2007 3:54:50 PM PST}
- SEARCH REDIRECT: Control Box Found: DLG1 {November 14, 2007 3:55:44 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 3:55:45 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 3:55:45 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 3:55:45 PM PST}
- UPDATED: Updated protein page: DLG1 {November 14, 2007 3:55:51 PM PST}
- INFO: Beginning work on ETV6... {November 14, 2007 3:55:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:57:18 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ETV6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ji7.
| PDB = {{PDB2|1ji7}}, {{PDB2|1lky}}, {{PDB2|2dao}}
| Name = Ets variant gene 6 (TEL oncogene)
| HGNCid = 3495
| Symbol = ETV6
| AltSymbols =; TEL; TEL/ABL
| OMIM = 600618
| ECnumber =
| Homologene = 37560
| MGIid = 109336
| GeneAtlas_image1 = PBB_GE_ETV6_205585_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2120
| Hs_Ensembl = ENSG00000139083
| Hs_RefseqProtein = NP_001978
| Hs_RefseqmRNA = NM_001987
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 11694055
| Hs_GenLoc_end = 11939588
| Hs_Uniprot = P41212
| Mm_EntrezGene = 14011
| Mm_Ensembl = ENSMUSG00000030199
| Mm_RefseqmRNA = NM_007961
| Mm_RefseqProtein = NP_031987
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 134091327
| Mm_GenLoc_end = 134235851
| Mm_Uniprot = Q3U037
}}
}}
'''Ets variant gene 6 (TEL oncogene)''', also known as '''ETV6''', 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 an ETS family transcription factor. The product of this gene contains two functional domains: a N-terminal pointed (PNT) domain that is involved in the protein-protein interactions with itself and other proteins, and a C-terminal DNA-binding domain. Gene knockout studies in mice suggest that it is required for hematopoiesis and maintenance of the developing vascular network. This gene is known to be involved in a large number of chromosomal rearrangements associated with leukemia and congenital fibrosarcoma.<ref>{{cite web | title = Entrez Gene: ETV6 ets variant gene 6 (TEL oncogene)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2120| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Keung YK, Beaty M, Steward W, ''et al.'' |title=Chronic myelocytic leukemia with eosinophilia, t(9;12)(q34;p13), and ETV6-ABL gene rearrangement: case report and review of the literature. |journal=Cancer Genet. Cytogenet. |volume=138 |issue= 2 |pages= 139-42 |year= 2003 |pmid= 12505259 |doi= }}
*{{cite journal | author=Fainstein E, Einat M, Gokkel E, ''et al.'' |title=Nucleotide sequence analysis of human abl and bcr-abl cDNAs. |journal=Oncogene |volume=4 |issue= 12 |pages= 1477-81 |year= 1990 |pmid= 2687768 |doi= }}
*{{cite journal | author=Buijs A, Sherr S, van Baal S, ''et al.'' |title=Translocation (12;22) (p13;q11) in myeloproliferative disorders results in fusion of the ETS-like TEL gene on 12p13 to the MN1 gene on 22q11. |journal=Oncogene |volume=10 |issue= 8 |pages= 1511-9 |year= 1995 |pmid= 7731705 |doi= }}
*{{cite journal | author=Golub TR, Barker GF, Bohlander SK, ''et al.'' |title=Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute lymphoblastic leukemia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 11 |pages= 4917-21 |year= 1995 |pmid= 7761424 |doi= }}
*{{cite journal | author=Romana SP, Mauchauffé M, Le Coniat M, ''et al.'' |title=The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1 gene fusion. |journal=Blood |volume=85 |issue= 12 |pages= 3662-70 |year= 1995 |pmid= 7780150 |doi= }}
*{{cite journal | author=Papadopoulos P, Ridge SA, Boucher CA, ''et al.'' |title=The novel activation of ABL by fusion to an ets-related gene, TEL. |journal=Cancer Res. |volume=55 |issue= 1 |pages= 34-8 |year= 1995 |pmid= 7805037 |doi= }}
*{{cite journal | author=Golub TR, Barker GF, Lovett M, Gilliland DG |title=Fusion of PDGF receptor beta to a novel ets-like gene, tel, in chronic myelomonocytic leukemia with t(5;12) chromosomal translocation. |journal=Cell |volume=77 |issue= 2 |pages= 307-16 |year= 1994 |pmid= 8168137 |doi= }}
*{{cite journal | author=Wlodarska I, Baens M, Peeters P, ''et al.'' |title=Biallelic alterations of both ETV6 and CDKN1B genes in a t(12;21) childhood acute lymphoblastic leukemia case. |journal=Cancer Res. |volume=56 |issue= 11 |pages= 2655-61 |year= 1996 |pmid= 8653712 |doi= }}
*{{cite journal | author=Baens M, Peeters P, Guo C, ''et al.'' |title=Genomic organization of TEL: the human ETS-variant gene 6. |journal=Genome Res. |volume=6 |issue= 5 |pages= 404-13 |year= 1996 |pmid= 8743990 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Hillier LD, Lennon G, Becker M, ''et al.'' |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807-28 |year= 1997 |pmid= 8889549 |doi= }}
*{{cite journal | author=Andreasson P, Johansson B, Arheden K, ''et al.'' |title=Deletions of CDKN1B and ETV6 in acute myeloid leukemia and myelodysplastic syndromes without cytogenetic evidence of 12p abnormalities. |journal=Genes Chromosomes Cancer |volume=19 |issue= 2 |pages= 77-83 |year= 1997 |pmid= 9171997 |doi= }}
*{{cite journal | author=Lacronique V, Boureux A, Valle VD, ''et al.'' |title=A TEL-JAK2 fusion protein with constitutive kinase activity in human leukemia. |journal=Science |volume=278 |issue= 5341 |pages= 1309-12 |year= 1997 |pmid= 9360930 |doi= }}
*{{cite journal | author=Knezevich SR, McFadden DE, Tao W, ''et al.'' |title=A novel ETV6-NTRK3 gene fusion in congenital fibrosarcoma. |journal=Nat. Genet. |volume=18 |issue= 2 |pages= 184-7 |year= 1998 |pmid= 9462753 |doi= 10.1038/ng0298-184 }}
*{{cite journal | author=Kwiatkowski BA, Bastian LS, Bauer TR, ''et al.'' |title=The ets family member Tel binds to the Fli-1 oncoprotein and inhibits its transcriptional activity. |journal=J. Biol. Chem. |volume=273 |issue= 28 |pages= 17525-30 |year= 1998 |pmid= 9651344 |doi= }}
*{{cite journal | author=Hannemann JR, McManus DM, Kabarowski JH, Wiedemann LM |title=Haemopoietic transformation by the TEL/ABL oncogene. |journal=Br. J. Haematol. |volume=102 |issue= 2 |pages= 475-85 |year= 1998 |pmid= 9695962 |doi= }}
*{{cite journal | author=Chakrabarti SR, Sood R, Ganguly S, ''et al.'' |title=Modulation of TEL transcription activity by interaction with the ubiquitin-conjugating enzyme UBC9. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 13 |pages= 7467-72 |year= 1999 |pmid= 10377438 |doi= }}
*{{cite journal | author=Cools J, Bilhou-Nabera C, Wlodarska I, ''et al.'' |title=Fusion of a novel gene, BTL, to ETV6 in acute myeloid leukemias with a t(4;12)(q11-q12;p13). |journal=Blood |volume=94 |issue= 5 |pages= 1820-4 |year= 1999 |pmid= 10477709 |doi= }}
*{{cite journal | author=Yagasaki F, Jinnai I, Yoshida S, ''et al.'' |title=Fusion of TEL/ETV6 to a novel ACS2 in myelodysplastic syndrome and acute myelogenous leukemia with t(5;12)(q31;p13). |journal=Genes Chromosomes Cancer |volume=26 |issue= 3 |pages= 192-202 |year= 2000 |pmid= 10502316 |doi= }}
*{{cite journal | author=Wai DH, Knezevich SR, Lucas T, ''et al.'' |title=The ETV6-NTRK3 gene fusion encodes a chimeric protein tyrosine kinase that transforms NIH3T3 cells. |journal=Oncogene |volume=19 |issue= 7 |pages= 906-15 |year= 2000 |pmid= 10702799 |doi= 10.1038/sj.onc.1203396 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GRIN2A... {November 14, 2007 3:57:18 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:57:49 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
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GRIN2A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2a5s.
| PDB = {{PDB2|2a5s}}, {{PDB2|2a5t}}
| Name = Glutamate receptor, ionotropic, N-methyl D-aspartate 2A
| HGNCid = 4585
| Symbol = GRIN2A
| AltSymbols =; NMDAR2A; NR2A
| OMIM = 138253
| ECnumber =
| Homologene = 645
| MGIid = 95820
| GeneAtlas_image1 = PBB_GE_GRIN2A_206534_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:0004970 |text = ionotropic glutamate receptor activity}} {{GNF_GO|id=GO:0004972 |text = N-methyl-D-aspartate selective glutamate receptor activity}} {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005234 |text = extracellular-glutamate-gated ion channel activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0042734 |text = presynaptic membrane}} {{GNF_GO|id=GO:0045202 |text = synapse}} {{GNF_GO|id=GO:0045211 |text = postsynaptic membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0007215 |text = glutamate signaling pathway}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007611 |text = learning and/or memory}} {{GNF_GO|id=GO:0048167 |text = regulation of synaptic plasticity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2903
| Hs_Ensembl = ENSG00000183454
| Hs_RefseqProtein = NP_000824
| Hs_RefseqmRNA = NM_000833
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 9764507
| Hs_GenLoc_end = 10181769
| Hs_Uniprot = Q12879
| Mm_EntrezGene = 14811
| Mm_Ensembl = ENSMUSG00000059003
| Mm_RefseqmRNA = XM_988553
| Mm_RefseqProtein = XP_993647
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 9491382
| Mm_GenLoc_end = 9906111
| Mm_Uniprot = P35436
}}
}}
'''Glutamate receptor, ionotropic, N-methyl D-aspartate 2A''', also known as '''GRIN2A''', 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 = N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate receptors. NMDA channel has been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of the key receptor subunit NMDAR1 (GRIN1) and 1 or more of the 4 NMDAR2 subunits: NMDAR2A (GRIN2A), NMDAR2B (GRIN2B), NMDAR2C (GRIN2C), and NMDAR2D (GRIN2D).<ref>{{cite web | title = Entrez Gene: GRIN2A glutamate receptor, ionotropic, N-methyl D-aspartate 2A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2903| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schröder HC, Perovic S, Kavsan V, ''et al.'' |title=Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death. |journal=Neurotoxicology |volume=19 |issue= 4-5 |pages= 683-8 |year= 1998 |pmid= 9745929 |doi= }}
*{{cite journal | author=King JE, Eugenin EA, Buckner CM, Berman JW |title=HIV tat and neurotoxicity. |journal=Microbes Infect. |volume=8 |issue= 5 |pages= 1347-57 |year= 2006 |pmid= 16697675 |doi= 10.1016/j.micinf.2005.11.014 }}
*{{cite journal | author=Monyer H, Sprengel R, Schoepfer R, ''et al.'' |title=Heteromeric NMDA receptors: molecular and functional distinction of subtypes. |journal=Science |volume=256 |issue= 5060 |pages= 1217-21 |year= 1992 |pmid= 1350383 |doi= }}
*{{cite journal | author=Kornau HC, Schenker LT, Kennedy MB, Seeburg PH |title=Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. |journal=Science |volume=269 |issue= 5231 |pages= 1737-40 |year= 1995 |pmid= 7569905 |doi= }}
*{{cite journal | author=Magnuson DS, Knudsen BE, Geiger JD, ''et al.'' |title=Human immunodeficiency virus type 1 tat activates non-N-methyl-D-aspartate excitatory amino acid receptors and causes neurotoxicity. |journal=Ann. Neurol. |volume=37 |issue= 3 |pages= 373-80 |year= 1995 |pmid= 7695237 |doi= 10.1002/ana.410370314 }}
*{{cite journal | author=Sakimura K, Kutsuwada T, Ito I, ''et al.'' |title=Reduced hippocampal LTP and spatial learning in mice lacking NMDA receptor epsilon 1 subunit. |journal=Nature |volume=373 |issue= 6510 |pages= 151-5 |year= 1995 |pmid= 7816096 |doi= 10.1038/373151a0 }}
*{{cite journal | author=Foldes RL, Adams SL, Fantaske RP, Kamboj RK |title=Human N-methyl-D-aspartate receptor modulatory subunit hNR2A: cloning and sequencing of the cDNA and primary structure of the protein. |journal=Biochim. Biophys. Acta |volume=1223 |issue= 1 |pages= 155-9 |year= 1994 |pmid= 8061049 |doi= }}
*{{cite journal | author=Sheng M, Cummings J, Roldan LA, ''et al.'' |title=Changing subunit composition of heteromeric NMDA receptors during development of rat cortex. |journal=Nature |volume=368 |issue= 6467 |pages= 144-7 |year= 1994 |pmid= 8139656 |doi= 10.1038/368144a0 }}
*{{cite journal | author=Roche KW, Raymond LA, Blackstone C, Huganir RL |title=Transmembrane topology of the glutamate receptor subunit GluR6. |journal=J. Biol. Chem. |volume=269 |issue= 16 |pages= 11679-82 |year= 1994 |pmid= 8163463 |doi= }}
*{{cite journal | author=Takano H, Onodera O, Tanaka H, ''et al.'' |title=Chromosomal localization of the epsilon 1, epsilon 3 and zeta 1 subunit genes of the human NMDA receptor channel. |journal=Biochem. Biophys. Res. Commun. |volume=197 |issue= 2 |pages= 922-6 |year= 1994 |pmid= 8267632 |doi= }}
*{{cite journal | author=Lannuzel A, Lledo PM, Lamghitnia HO, ''et al.'' |title=HIV-1 envelope proteins gp120 and gp160 potentiate NMDA-induced [Ca2+]i increase, alter [Ca2+]i homeostasis and induce neurotoxicity in human embryonic neurons. |journal=Eur. J. Neurosci. |volume=7 |issue= 11 |pages= 2285-93 |year= 1996 |pmid= 8563977 |doi= }}
*{{cite journal | author=Corasaniti MT, Melino G, Navarra M, ''et al.'' |title=Death of cultured human neuroblastoma cells induced by HIV-1 gp120 is prevented by NMDA receptor antagonists and inhibitors of nitric oxide and cyclooxygenase. |journal=Neurodegeneration : a journal for neurodegenerative disorders, neuroprotection, and neuroregeneration |volume=4 |issue= 3 |pages= 315-21 |year= 1996 |pmid= 8581564 |doi= }}
*{{cite journal | author=Niethammer M, Kim E, Sheng M |title=Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases. |journal=J. Neurosci. |volume=16 |issue= 7 |pages= 2157-63 |year= 1996 |pmid= 8601796 |doi= }}
*{{cite journal | author=Pittaluga A, Pattarini R, Severi P, Raiteri M |title=Human brain N-methyl-D-aspartate receptors regulating noradrenaline release are positively modulated by HIV-1 coat protein gp120. |journal=AIDS |volume=10 |issue= 5 |pages= 463-8 |year= 1996 |pmid= 8724036 |doi= }}
*{{cite journal | author=Hess SD, Daggett LP, Crona J, ''et al.'' |title=Cloning and functional characterization of human heteromeric N-methyl-D-aspartate receptors. |journal=J. Pharmacol. Exp. Ther. |volume=278 |issue= 2 |pages= 808-16 |year= 1996 |pmid= 8768735 |doi= }}
*{{cite journal | author=Wu P, Price P, Du B, ''et al.'' |title=Direct cytotoxicity of HIV-1 envelope protein gp120 on human NT neurons. |journal=Neuroreport |volume=7 |issue= 5 |pages= 1045-9 |year= 1996 |pmid= 8804048 |doi= }}
*{{cite journal | author=Bennett BA, Rusyniak DE, Hollingsworth CK |title=HIV-1 gp120-induced neurotoxicity to midbrain dopamine cultures. |journal=Brain Res. |volume=705 |issue= 1-2 |pages= 168-76 |year= 1996 |pmid= 8821747 |doi= }}
*{{cite journal | author=Toggas SM, Masliah E, Mucke L |title=Prevention of HIV-1 gp120-induced neuronal damage in the central nervous system of transgenic mice by the NMDA receptor antagonist memantine. |journal=Brain Res. |volume=706 |issue= 2 |pages= 303-7 |year= 1996 |pmid= 8822372 |doi= }}
*{{cite journal | author=Dreyer EB, Lipton SA |title=The coat protein gp120 of HIV-1 inhibits astrocyte uptake of excitatory amino acids via macrophage arachidonic acid. |journal=Eur. J. Neurosci. |volume=7 |issue= 12 |pages= 2502-7 |year= 1996 |pmid= 8845955 |doi= }}
*{{cite journal | author=Raber J, Toggas SM, Lee S, ''et al.'' |title=Central nervous system expression of HIV-1 Gp120 activates the hypothalamic-pituitary-adrenal axis: evidence for involvement of NMDA receptors and nitric oxide synthase. |journal=Virology |volume=226 |issue= 2 |pages= 362-73 |year= 1997 |pmid= 8955056 |doi= 10.1006/viro.1996.0664 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL5... {November 14, 2007 3:57:49 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:58:20 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_IL5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hul.
| PDB = {{PDB2|1hul}}
| Name = Interleukin 5 (colony-stimulating factor, eosinophil)
| HGNCid = 6016
| Symbol = IL5
| AltSymbols =; EDF; IL-5; TRF
| OMIM = 147850
| ECnumber =
| Homologene = 679
| MGIid = 96557
| GeneAtlas_image1 = PBB_GE_IL5_207952_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005137 |text = interleukin-5 receptor binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0050731 |text = positive regulation of peptidyl-tyrosine phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3567
| Hs_Ensembl = ENSG00000113525
| Hs_RefseqProtein = NP_000870
| Hs_RefseqmRNA = NM_000879
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 131905035
| Hs_GenLoc_end = 131907113
| Hs_Uniprot = P05113
| Mm_EntrezGene = 16191
| Mm_Ensembl = ENSMUSG00000036117
| Mm_RefseqmRNA = NM_010558
| Mm_RefseqProtein = NP_034688
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 53564217
| Mm_GenLoc_end = 53568526
| Mm_Uniprot = Q05A89
}}
}}
'''Interleukin 5 (colony-stimulating factor, eosinophil)''', also known as '''IL5''', 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 cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. This cytokine is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of this cytokine is reported to be related to asthma or hypereosinophilic syndromes. The receptor of this cytokine is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. This cytokine, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.<ref>{{cite web | title = Entrez Gene: IL5 interleukin 5 (colony-stimulating factor, eosinophil)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3567| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Broide DH, Hoffman H, Sriramarao P |title=Genes that regulate eosinophilic inflammation. |journal=Am. J. Hum. Genet. |volume=65 |issue= 2 |pages= 302-7 |year= 1999 |pmid= 10417272 |doi= }}
*{{cite journal | author=Martinez-Moczygemba M, Huston DP |title=Biology of common beta receptor-signaling cytokines: IL-3, IL-5, and GM-CSF. |journal=J. Allergy Clin. Immunol. |volume=112 |issue= 4 |pages= 653-65; quiz 666 |year= 2003 |pmid= 14564341 |doi= 10.1016/S0091 }}
*{{cite journal | author=Tavernier J, Tuypens T, Plaetinck G, ''et al.'' |title=Molecular basis of the membrane-anchored and two soluble isoforms of the human interleukin 5 receptor alpha subunit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 15 |pages= 7041-5 |year= 1992 |pmid= 1495999 |doi= }}
*{{cite journal | author=Lopez AF, Eglinton JM, Lyons AB, ''et al.'' |title=Human interleukin-3 inhibits the binding of granulocyte-macrophage colony-stimulating factor and interleukin-5 to basophils and strongly enhances their functional activity. |journal=J. Cell. Physiol. |volume=145 |issue= 1 |pages= 69-77 |year= 1990 |pmid= 1698795 |doi= 10.1002/jcp.1041450111 }}
*{{cite journal | author=Murata Y, Takaki S, Migita M, ''et al.'' |title=Molecular cloning and expression of the human interleukin 5 receptor. |journal=J. Exp. Med. |volume=175 |issue= 2 |pages= 341-51 |year= 1992 |pmid= 1732409 |doi= }}
*{{cite journal | author=Tavernier J, Devos R, Cornelis S, ''et al.'' |title=A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CSF. |journal=Cell |volume=66 |issue= 6 |pages= 1175-84 |year= 1991 |pmid= 1833065 |doi= }}
*{{cite journal | author=Proudfoot AE, Davies JG, Turcatti G, Wingfield PT |title=Human interleukin-5 expressed in Escherichia coli: assignment of the disulfide bridges of the purified unglycosylated protein. |journal=FEBS Lett. |volume=283 |issue= 1 |pages= 61-4 |year= 1991 |pmid= 2037074 |doi= }}
*{{cite journal | author=Minamitake Y, Kodama S, Katayama T, ''et al.'' |title=Structure of recombinant human interleukin 5 produced by Chinese hamster ovary cells. |journal=J. Biochem. |volume=107 |issue= 2 |pages= 292-7 |year= 1990 |pmid= 2361960 |doi= }}
*{{cite journal | author=Takahashi M, Yoshida MC, Satoh H, ''et al.'' |title=Chromosomal mapping of the mouse IL-4 and human IL-5 genes. |journal=Genomics |volume=4 |issue= 1 |pages= 47-52 |year= 1989 |pmid= 2563351 |doi= }}
*{{cite journal | author=Yokota T, Coffman RL, Hagiwara H, ''et al.'' |title=Isolation and characterization of lymphokine cDNA clones encoding mouse and human IgA-enhancing factor and eosinophil colony-stimulating factor activities: relationship to interleukin 5. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 21 |pages= 7388-92 |year= 1987 |pmid= 2823259 |doi= }}
*{{cite journal | author=Tanabe T, Konishi M, Mizuta T, ''et al.'' |title=Molecular cloning and structure of the human interleukin-5 gene. |journal=J. Biol. Chem. |volume=262 |issue= 34 |pages= 16580-4 |year= 1988 |pmid= 2824500 |doi= }}
*{{cite journal | author=Azuma C, Tanabe T, Konishi M, ''et al.'' |title=Cloning of cDNA for human T-cell replacing factor (interleukin-5) and comparison with the murine homologue. |journal=Nucleic Acids Res. |volume=14 |issue= 22 |pages= 9149-58 |year= 1987 |pmid= 3024129 |doi= }}
*{{cite journal | author=Campbell HD, Tucker WQ, Hort Y, ''et al.'' |title=Molecular cloning, nucleotide sequence, and expression of the gene encoding human eosinophil differentiation factor (interleukin 5). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 19 |pages= 6629-33 |year= 1987 |pmid= 3498940 |doi= }}
*{{cite journal | author=Dickason RR, Huston MM, Huston DP |title=Enhanced detection of human IL-5 in biological fluids utilizing murine monoclonal antibodies which delineate distinct neutralizing epitopes. |journal=Cytokine |volume=6 |issue= 6 |pages= 647-56 |year= 1995 |pmid= 7534492 |doi= }}
*{{cite journal | author=Johanson K, Appelbaum E, Doyle M, ''et al.'' |title=Binding interactions of human interleukin 5 with its receptor alpha subunit. Large scale production, structural, and functional studies of Drosophila-expressed recombinant proteins. |journal=J. Biol. Chem. |volume=270 |issue= 16 |pages= 9459-71 |year= 1995 |pmid= 7721873 |doi= }}
*{{cite journal | author=Schandené L, Ferster A, Mascart-Lemone F, ''et al.'' |title=T helper type 2-like cells and therapeutic effects of interferon-gamma in combined immunodeficiency with hypereosinophilia (Omenn's syndrome). |journal=Eur. J. Immunol. |volume=23 |issue= 1 |pages= 56-60 |year= 1993 |pmid= 8419187 |doi= }}
*{{cite journal | author=Willman CL, Sever CE, Pallavicini MG, ''et al.'' |title=Deletion of IRF-1, mapping to chromosome 5q31.1, in human leukemia and preleukemic myelodysplasia. |journal=Science |volume=259 |issue= 5097 |pages= 968-71 |year= 1993 |pmid= 8438156 |doi= }}
*{{cite journal | author=Milburn MV, Hassell AM, Lambert MH, ''et al.'' |title=A novel dimer configuration revealed by the crystal structure at 2.4 A resolution of human interleukin-5. |journal=Nature |volume=363 |issue= 6425 |pages= 172-6 |year= 1993 |pmid= 8483502 |doi= 10.1038/363172a0 }}
*{{cite journal | author=Kishimoto S, Shimadzu W, Izumi T, ''et al.'' |title=Regulation by IL-5 of expression of functional platelet-activating factor receptors on human eosinophils. |journal=J. Immunol. |volume=157 |issue= 9 |pages= 4126-32 |year= 1996 |pmid= 8892648 |doi= }}
*{{cite journal | author=Jans DA, Briggs LJ, Gustin SE, ''et al.'' |title=A functional bipartite nuclear localisation signal in the cytokine interleukin-5. |journal=FEBS Lett. |volume=406 |issue= 3 |pages= 315-20 |year= 1997 |pmid= 9136909 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL8RA... {November 14, 2007 3:58:20 PM PST}
- SEARCH REDIRECT: Control Box Found: IL8RA {November 14, 2007 3:59:07 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 3:59:09 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 3:59:09 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 3:59:09 PM PST}
- UPDATED: Updated protein page: IL8RA {November 14, 2007 3:59:16 PM PST}
- INFO: Beginning work on INHA... {November 14, 2007 3:59:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:59:44 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Inhibin, alpha
| HGNCid = 6065
| Symbol = INHA
| AltSymbols =;
| OMIM = 147380
| ECnumber =
| Homologene = 1652
| MGIid = 96569
| GeneAtlas_image1 = PBB_GE_INHA_210141_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0017106 |text = activin inhibitor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0043512 |text = inhibin A complex}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0001541 |text = ovarian follicle development}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0009605 |text = response to external stimulus}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030218 |text = erythrocyte differentiation}} {{GNF_GO|id=GO:0042127 |text = regulation of cell proliferation}} {{GNF_GO|id=GO:0042326 |text = negative regulation of phosphorylation}} {{GNF_GO|id=GO:0042541 |text = hemoglobin biosynthetic process}} {{GNF_GO|id=GO:0045077 |text = negative regulation of interferon-gamma biosynthetic process}} {{GNF_GO|id=GO:0045578 |text = negative regulation of B cell differentiation}} {{GNF_GO|id=GO:0045650 |text = negative regulation of macrophage differentiation}} {{GNF_GO|id=GO:0046881 |text = positive regulation of follicle-stimulating hormone secretion}} {{GNF_GO|id=GO:0046882 |text = negative regulation of follicle-stimulating hormone secretion}} {{GNF_GO|id=GO:0051726 |text = regulation of cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3623
| Hs_Ensembl = ENSG00000123999
| Hs_RefseqProtein = NP_002182
| Hs_RefseqmRNA = NM_002191
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 220145161
| Hs_GenLoc_end = 220148679
| Hs_Uniprot = P05111
| Mm_EntrezGene = 16322
| Mm_Ensembl = ENSMUSG00000032968
| Mm_RefseqmRNA = NM_010564
| Mm_RefseqProtein = NP_034694
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 75390225
| Mm_GenLoc_end = 75393502
| Mm_Uniprot = Q6GTG7
}}
}}
'''Inhibin, alpha''', also known as '''INHA''', 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 inhibin alpha subunit joins either the beta A or beta B subunit to form a pituitary FSH secretion inhibitor. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumour-suppressor activity. In addition, serum levels of inhibin have been shown to reflect the size of granulosa-cell tumors and can therefore be used as a marker for primary as well as recurrent disease. However, in prostate cancer, expression of the inhibin alpha-subunit gene was suppressed and was not detectable in poorly differentiated tumor cells. Furthermore, because expression in gonadal and various extragonadal tissues may vary severalfold in a tissue-specific fashion, it is proposed that inhibin may be both a growth/differentiation factor and a hormone.<ref>{{cite web | title = Entrez Gene: INHA inhibin, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3623| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mellor SL, Richards MG, Pedersen JS, ''et al.'' |title=Loss of the expression and localization of inhibin alpha-subunit in high grade prostate cancer. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 3 |pages= 969-75 |year= 1998 |pmid= 9506758 |doi= }}
*{{cite journal | author=Munz B, Hübner G, Tretter Y, ''et al.'' |title=A novel role of activin in inflammation and repair. |journal=J. Endocrinol. |volume=161 |issue= 2 |pages= 187-93 |year= 1999 |pmid= 10320815 |doi= }}
*{{cite journal | author=Welt C, Sidis Y, Keutmann H, Schneyer A |title=Activins, inhibins, and follistatins: from endocrinology to signaling. A paradigm for the new millennium. |journal=Exp. Biol. Med. (Maywood) |volume=227 |issue= 9 |pages= 724-52 |year= 2002 |pmid= 12324653 |doi= }}
*{{cite journal | author=Shav-Tal Y, Zipori D |title=The role of activin a in regulation of hemopoiesis. |journal=Stem Cells |volume=20 |issue= 6 |pages= 493-500 |year= 2003 |pmid= 12456957 |doi= }}
*{{cite journal | author=Shao L, Frigon NL, Young AL, ''et al.'' |title=Effect of activin A on globin gene expression in purified human erythroid progenitors. |journal=Blood |volume=79 |issue= 3 |pages= 773-81 |year= 1992 |pmid= 1310063 |doi= }}
*{{cite journal | author=Vannelli GB, Barni T, Forti G, ''et al.'' |title=Immunolocalization of inhibin alpha-subunit in the human testis. A light- and electron-microscopy study. |journal=Cell Tissue Res. |volume=269 |issue= 2 |pages= 221-7 |year= 1992 |pmid= 1423490 |doi= }}
*{{cite journal | author=Matzuk MM, Finegold MJ, Su JG, ''et al.'' |title=Alpha-inhibin is a tumour-suppressor gene with gonadal specificity in mice. |journal=Nature |volume=360 |issue= 6402 |pages= 313-9 |year= 1992 |pmid= 1448148 |doi= 10.1038/360313a0 }}
*{{cite journal | author=Shimonaka M, Inouye S, Shimasaki S, Ling N |title=Follistatin binds to both activin and inhibin through the common subunit. |journal=Endocrinology |volume=128 |issue= 6 |pages= 3313-5 |year= 1991 |pmid= 2036994 |doi= }}
*{{cite journal | author=Mason AJ, Berkemeier LM, Schmelzer CH, Schwall RH |title=Activin B: precursor sequences, genomic structure and in vitro activities. |journal=Mol. Endocrinol. |volume=3 |issue= 9 |pages= 1352-8 |year= 1990 |pmid= 2575216 |doi= }}
*{{cite journal | author=Barton DE, Yang-Feng TL, Mason AJ, ''et al.'' |title=Mapping of genes for inhibin subunits alpha, beta A, and beta B on human and mouse chromosomes and studies of jsd mice. |journal=Genomics |volume=5 |issue= 1 |pages= 91-9 |year= 1989 |pmid= 2767687 |doi= }}
*{{cite journal | author=Lappöhn RE, Burger HG, Bouma J, ''et al.'' |title=Inhibin as a marker for granulosa-cell tumors. |journal=N. Engl. J. Med. |volume=321 |issue= 12 |pages= 790-3 |year= 1989 |pmid= 2770810 |doi= }}
*{{cite journal | author=Mayo KE, Cerelli GM, Spiess J, ''et al.'' |title=Inhibin A-subunit cDNAs from porcine ovary and human placenta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 16 |pages= 5849-53 |year= 1986 |pmid= 3016724 |doi= }}
*{{cite journal | author=Ramasharma K, Li CH |title=Characteristics of binding of human seminal alpha-inhibin-92 to human pituitary membranes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 11 |pages= 3595-8 |year= 1987 |pmid= 3035540 |doi= }}
*{{cite journal | author=Murata M, Eto Y, Shibai H, ''et al.'' |title=Erythroid differentiation factor is encoded by the same mRNA as that of the inhibin beta A chain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 8 |pages= 2434-8 |year= 1988 |pmid= 3267209 |doi= }}
*{{cite journal | author=Burger HG, Igarashi M |title=Inhibin: definition and nomenclature, including related substances. |journal=Endocrinology |volume=122 |issue= 4 |pages= 1701-2 |year= 1988 |pmid= 3345731 |doi= }}
*{{cite journal | author=Mason AJ, Niall HD, Seeburg PH |title=Structure of two human ovarian inhibins. |journal=Biochem. Biophys. Res. Commun. |volume=135 |issue= 3 |pages= 957-64 |year= 1986 |pmid= 3754442 |doi= }}
*{{cite journal | author=Stewart AG, Milborrow HM, Ring JM, ''et al.'' |title=Human inhibin genes. Genomic characterisation and sequencing. |journal=FEBS Lett. |volume=206 |issue= 2 |pages= 329-34 |year= 1986 |pmid= 3758355 |doi= }}
*{{cite journal | author=Xu J, McKeehan K, Matsuzaki K, McKeehan WL |title=Inhibin antagonizes inhibition of liver cell growth by activin by a dominant-negative mechanism. |journal=J. Biol. Chem. |volume=270 |issue= 11 |pages= 6308-13 |year= 1995 |pmid= 7890768 |doi= }}
*{{cite journal | author=Nishihara T, Okahashi N, Ueda N |title=Activin A induces apoptotic cell death. |journal=Biochem. Biophys. Res. Commun. |volume=197 |issue= 2 |pages= 985-91 |year= 1994 |pmid= 8267637 |doi= 10.1006/bbrc.1993.2576 }}
*{{cite journal | author=Mason AJ, Farnworth PG, Sullivan J |title=Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. |journal=Mol. Endocrinol. |volume=10 |issue= 9 |pages= 1055-65 |year= 1997 |pmid= 8885240 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KRT5... {November 14, 2007 3:59:44 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:00:26 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 = Keratin 5 (epidermolysis bullosa simplex, Dowling-Meara/Kobner/Weber-Cockayne types)
| HGNCid = 6442
| Symbol = KRT5
| AltSymbols =; CK5; DDD; EBS2; K5; KRT5A
| OMIM = 148040
| ECnumber =
| Homologene = 55461
| MGIid = 96702
| GeneAtlas_image1 = PBB_GE_KRT5_201820_at_tn.png
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005882 |text = intermediate filament}}
| Process = {{GNF_GO|id=GO:0008544 |text = epidermis development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3852
| Hs_Ensembl = ENSG00000186081
| Hs_RefseqProtein = NP_000415
| Hs_RefseqmRNA = NM_000424
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 51194628
| Hs_GenLoc_end = 51200347
| Hs_Uniprot = P13647
| Mm_EntrezGene = 110308
| Mm_Ensembl = ENSMUSG00000061527
| Mm_RefseqmRNA = NM_027011
| Mm_RefseqProtein = NP_081287
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 101535104
| Mm_GenLoc_end = 101540925
| Mm_Uniprot = Q32P04
}}
}}
'''Keratin 5 (epidermolysis bullosa simplex, Dowling-Meara/Kobner/Weber-Cockayne types)''', also known as '''KRT5''', 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 keratin gene family. The type II cytokeratins consist of basic or neutral proteins which are arranged in pairs of heterotypic keratin chains coexpressed during differentiation of simple and stratified epithelial tissues. This type II cytokeratin is specifically expressed in the basal layer of the epidermis with family member KRT14. Mutations in these genes have been associated with a complex of diseases termed epidermolysis bullosa simplex. The type II cytokeratins are clustered in a region of chromosome 12q12-q13.<ref>{{cite web | title = Entrez Gene: KRT5 keratin 5 (epidermolysis bullosa simplex, Dowling-Meara/Kobner/Weber-Cockayne types)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3852| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schuilenga-Hut PH, Vlies P, Jonkman MF, ''et al.'' |title=Mutation analysis of the entire keratin 5 and 14 genes in patients with epidermolysis bullosa simplex and identification of novel mutations. |journal=Hum. Mutat. |volume=21 |issue= 4 |pages= 447 |year= 2003 |pmid= 12655565 |doi= 10.1002/humu.9124 }}
*{{cite journal | author=Seibert JA, Boone JM |title=X-ray imaging physics for nuclear medicine technologists. Part 2: X-ray interactions and image formation. |journal=Journal of nuclear medicine technology |volume=33 |issue= 1 |pages= 3-18 |year= 2005 |pmid= 15731015 |doi= }}
*{{cite journal | author=Ohtsuki M, Tomic-Canic M, Freedberg IM, Blumenberg M |title=Regulation of epidermal keratin expression by retinoic acid and thyroid hormone. |journal=J. Dermatol. |volume=19 |issue= 11 |pages= 774-80 |year= 1993 |pmid= 1284070 |doi= }}
*{{cite journal | author=Lane EB, Rugg EL, Navsaria H, ''et al.'' |title=A mutation in the conserved helix termination peptide of keratin 5 in hereditary skin blistering. |journal=Nature |volume=356 |issue= 6366 |pages= 244-6 |year= 1992 |pmid= 1372711 |doi= 10.1038/356244a0 }}
*{{cite journal | author=Tavakkol A, Griffiths CE, Keane KM, ''et al.'' |title=Cellular localization of mRNA for cellular retinoic acid-binding protein II and nuclear retinoic acid receptor-gamma 1 in retinoic acid-treated human skin. |journal=J. Invest. Dermatol. |volume=99 |issue= 2 |pages= 146-50 |year= 1992 |pmid= 1378478 |doi= }}
*{{cite journal | author=Rosenberg M, Fuchs E, Le Beau MM, ''et al.'' |title=Three epidermal and one simple epithelial type II keratin genes map to human chromosome 12. |journal=Cytogenet. Cell Genet. |volume=57 |issue= 1 |pages= 33-8 |year= 1991 |pmid= 1713141 |doi= }}
*{{cite journal | author=Ryynänen M, Knowlton RG, Uitto J |title=Mapping of epidermolysis bullosa simplex mutation to chromosome 12. |journal=Am. J. Hum. Genet. |volume=49 |issue= 5 |pages= 978-84 |year= 1991 |pmid= 1718160 |doi= }}
*{{cite journal | author=Bonifas JM, Rothman AL, Epstein EH |title=Epidermolysis bullosa simplex: evidence in two families for keratin gene abnormalities. |journal=Science |volume=254 |issue= 5035 |pages= 1202-5 |year= 1991 |pmid= 1720261 |doi= }}
*{{cite journal | author=Lersch R, Fuchs E |title=Sequence and expression of a type II keratin, K5, in human epidermal cells. |journal=Mol. Cell. Biol. |volume=8 |issue= 1 |pages= 486-93 |year= 1988 |pmid= 2447486 |doi= }}
*{{cite journal | author=Galup C, Darmon MY |title=Isolation and characterization of a cDNA clone coding for human epidermal keratin K5. Sequence of the carboxyterminal half of this keratin. |journal=J. Invest. Dermatol. |volume=91 |issue= 1 |pages= 39-42 |year= 1988 |pmid= 2455002 |doi= }}
*{{cite journal | author=Eckert RL, Rorke EA |title=The sequence of the human epidermal 58-kD (#5) type II keratin reveals an absence of 5' upstream sequence conservation between coexpressed epidermal keratins. |journal=DNA |volume=7 |issue= 5 |pages= 337-45 |year= 1988 |pmid= 2456903 |doi= }}
*{{cite journal | author=Lersch R, Stellmach V, Stocks C, ''et al.'' |title=Isolation, sequence, and expression of a human keratin K5 gene: transcriptional regulation of keratins and insights into pairwise control. |journal=Mol. Cell. Biol. |volume=9 |issue= 9 |pages= 3685-97 |year= 1989 |pmid= 2476664 |doi= }}
*{{cite journal | author=Rugg EL, Morley SM, Smith FJ, ''et al.'' |title=Missing links: Weber-Cockayne keratin mutations implicate the L12 linker domain in effective cytoskeleton function. |journal=Nat. Genet. |volume=5 |issue= 3 |pages= 294-300 |year= 1994 |pmid= 7506097 |doi= 10.1038/ng1193-294 }}
*{{cite journal | author=Chan YM, Yu QC, LeBlanc-Straceski J, ''et al.'' |title=Mutations in the non-helical linker segment L1-2 of keratin 5 in patients with Weber-Cockayne epidermolysis bullosa simplex. |journal=J. Cell. Sci. |volume=107 ( Pt 4) |issue= |pages= 765-74 |year= 1994 |pmid= 7520042 |doi= }}
*{{cite journal | author=Kouklis PD, Hutton E, Fuchs E |title=Making a connection: direct binding between keratin intermediate filaments and desmosomal proteins. |journal=J. Cell Biol. |volume=127 |issue= 4 |pages= 1049-60 |year= 1994 |pmid= 7525601 |doi= }}
*{{cite journal | author=Stephens K, Zlotogorski A, Smith L, ''et al.'' |title=Epidermolysis bullosa simplex: a keratin 5 mutation is a fully dominant allele in epidermal cytoskeleton function. |journal=Am. J. Hum. Genet. |volume=56 |issue= 3 |pages= 577-85 |year= 1995 |pmid= 7534039 |doi= }}
*{{cite journal | author=Ehrlich P, Sybert VP, Spencer A, Stephens K |title=A common keratin 5 gene mutation in epidermolysis bullosa simplex--Weber-Cockayne. |journal=J. Invest. Dermatol. |volume=104 |issue= 5 |pages= 877-9 |year= 1995 |pmid= 7537780 |doi= }}
*{{cite journal | author=Wanner R, Förster HH, Tilmans I, Mischke D |title=Allelic variations of human keratins K4 and K5 provide polymorphic markers within the type II keratin gene cluster on chromosome 12. |journal=J. Invest. Dermatol. |volume=100 |issue= 6 |pages= 735-41 |year= 1993 |pmid= 7684424 |doi= }}
*{{cite journal | author=Dong W, Ryynänen M, Uitto J |title=Identification of a leucine-to-proline mutation in the keratin 5 gene in a family with the generalized Köbner type of epidermolysis bullosa simplex. |journal=Hum. Mutat. |volume=2 |issue= 2 |pages= 94-102 |year= 1993 |pmid= 7686424 |doi= 10.1002/humu.1380020206 }}
*{{cite journal | author=Chan YM, Yu QC, Fine JD, Fuchs E |title=The genetic basis of Weber-Cockayne epidermolysis bullosa simplex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 15 |pages= 7414-8 |year= 1993 |pmid= 7688477 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NCOR2... {November 14, 2007 4:06:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:07:55 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_NCOR2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xc5.
| PDB = {{PDB2|1xc5}}
| Name = Nuclear receptor co-repressor 2
| HGNCid = 7673
| Symbol = NCOR2
| AltSymbols =; CTG26; TNRC14; TRAC1; SMRT; SMRTE; SMRTE-tau; TRAC-1
| OMIM = 600848
| ECnumber =
| Homologene = 31370
| MGIid = 1337080
| GeneAtlas_image1 = PBB_GE_NCOR2_207760_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NCOR2_208888_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_NCOR2_208889_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005112 |text = Notch binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0016604 |text = nuclear body}}
| Process = {{GNF_GO|id=GO:0045892 |text = negative regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9612
| Hs_Ensembl = ENSG00000196498
| Hs_RefseqProtein = NP_001070729
| Hs_RefseqmRNA = NM_001077261
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 123374915
| Hs_GenLoc_end = 123545750
| Hs_Uniprot = Q9Y618
| Mm_EntrezGene = 20602
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_011424
| Mm_RefseqProtein = NP_035554
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Nuclear receptor co-repressor 2''', also known as '''NCOR2''', 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=Hörlein AJ, Näär AM, Heinzel T, ''et al.'' |title=Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. |journal=Nature |volume=377 |issue= 6548 |pages= 397-404 |year= 1995 |pmid= 7566114 |doi= 10.1038/377397a0 }}
*{{cite journal | author=Chen JD, Evans RM |title=A transcriptional co-repressor that interacts with nuclear hormone receptors. |journal=Nature |volume=377 |issue= 6548 |pages= 454-7 |year= 1995 |pmid= 7566127 |doi= 10.1038/377454a0 }}
*{{cite journal | author=Sande S, Privalsky ML |title=Identification of TRACs (T3 receptor-associating cofactors), a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors. |journal=Mol. Endocrinol. |volume=10 |issue= 7 |pages= 813-25 |year= 1997 |pmid= 8813722 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Margolis RL, Abraham MR, Gatchell SB, ''et al.'' |title=cDNAs with long CAG trinucleotide repeats from human brain. |journal=Hum. Genet. |volume=100 |issue= 1 |pages= 114-22 |year= 1997 |pmid= 9225980 |doi= }}
*{{cite journal | author=Hong SH, David G, Wong CW, ''et al.'' |title=SMRT corepressor interacts with PLZF and with the PML-retinoic acid receptor alpha (RARalpha) and PLZF-RARalpha oncoproteins associated with acute promyelocytic leukemia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 17 |pages= 9028-33 |year= 1997 |pmid= 9256429 |doi= }}
*{{cite journal | author=Chen H, Lin RJ, Schiltz RL, ''et al.'' |title=Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. |journal=Cell |volume=90 |issue= 3 |pages= 569-80 |year= 1997 |pmid= 9267036 |doi= }}
*{{cite journal | author=Lin RJ, Nagy L, Inoue S, ''et al.'' |title=Role of the histone deacetylase complex in acute promyelocytic leukaemia. |journal=Nature |volume=391 |issue= 6669 |pages= 811-4 |year= 1998 |pmid= 9486654 |doi= 10.1038/35895 }}
*{{cite journal | author=Laherty CD, Billin AN, Lavinsky RM, ''et al.'' |title=SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors. |journal=Mol. Cell |volume=2 |issue= 1 |pages= 33-42 |year= 1998 |pmid= 9702189 |doi= }}
*{{cite journal | author=Liu Y, Takeshita A, Misiti S, ''et al.'' |title=Lack of coactivator interaction can be a mechanism for dominant negative activity by mutant thyroid hormone receptors. |journal=Endocrinology |volume=139 |issue= 10 |pages= 4197-204 |year= 1998 |pmid= 9751500 |doi= }}
*{{cite journal | author=Wong CW, Privalsky ML |title=Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6. |journal=J. Biol. Chem. |volume=273 |issue= 42 |pages= 27695-702 |year= 1998 |pmid= 9765306 |doi= }}
*{{cite journal | author=Ordentlich P, Downes M, Xie W, ''et al.'' |title=Unique forms of human and mouse nuclear receptor corepressor SMRT. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 6 |pages= 2639-44 |year= 1999 |pmid= 10077563 |doi= }}
*{{cite journal | author=Park EJ, Schroen DJ, Yang M, ''et al.'' |title=SMRTe, a silencing mediator for retinoid and thyroid hormone receptors-extended isoform that is more related to the nuclear receptor corepressor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 7 |pages= 3519-24 |year= 1999 |pmid= 10097068 |doi= }}
*{{cite journal | author=Nguyen TA, Hoivik D, Lee JE, Safe S |title=Interactions of nuclear receptor coactivator/corepressor proteins with the aryl hydrocarbon receptor complex. |journal=Arch. Biochem. Biophys. |volume=367 |issue= 2 |pages= 250-7 |year= 1999 |pmid= 10395741 |doi= 10.1006/abbi.1999.1282 }}
*{{cite journal | author=Bailey P, Downes M, Lau P, ''et al.'' |title=The nuclear receptor corepressor N-CoR regulates differentiation: N-CoR directly interacts with MyoD. |journal=Mol. Endocrinol. |volume=13 |issue= 7 |pages= 1155-68 |year= 1999 |pmid= 10406466 |doi= }}
*{{cite journal | author=Kao HY, Downes M, Ordentlich P, Evans RM |title=Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. |journal=Genes Dev. |volume=14 |issue= 1 |pages= 55-66 |year= 2000 |pmid= 10640276 |doi= }}
*{{cite journal | author=Zhou S, Fujimuro M, Hsieh JJ, ''et al.'' |title=SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function. |journal=Mol. Cell. Biol. |volume=20 |issue= 7 |pages= 2400-10 |year= 2000 |pmid= 10713164 |doi= }}
*{{cite journal | author=Lee SK, Kim JH, Lee YC, ''et al.'' |title=Silencing mediator of retinoic acid and thyroid hormone receptors, as a novel transcriptional corepressor molecule of activating protein-1, nuclear factor-kappaB, and serum response factor. |journal=J. Biol. Chem. |volume=275 |issue= 17 |pages= 12470-4 |year= 2000 |pmid= 10777532 |doi= }}
*{{cite journal | author=Guenther MG, Lane WS, Fischle W, ''et al.'' |title=A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness. |journal=Genes Dev. |volume=14 |issue= 9 |pages= 1048-57 |year= 2000 |pmid= 10809664 |doi= }}
*{{cite journal | author=Grozinger CM, Schreiber SL |title=Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 14 |pages= 7835-40 |year= 2000 |pmid= 10869435 |doi= 10.1073/pnas.140199597 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on OTC... {November 14, 2007 4:00:26 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:01:34 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_OTC_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1c9y.
| PDB = {{PDB2|1c9y}}, {{PDB2|1ep9}}, {{PDB2|1fb5}}, {{PDB2|1fvo}}, {{PDB2|1oth}}
| Name = Ornithine carbamoyltransferase
| HGNCid = 8512
| Symbol = OTC
| AltSymbols =; OCTD; MGC129967; MGC129968; MGC138856
| OMIM = 300461
| ECnumber =
| Homologene = 446
| MGIid = 97448
| GeneAtlas_image1 = PBB_GE_OTC_207200_at_tn.png
| Function = {{GNF_GO|id=GO:0004585 |text = ornithine carbamoyltransferase activity}} {{GNF_GO|id=GO:0016597 |text = amino acid binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0005759 |text = mitochondrial matrix}} {{GNF_GO|id=GO:0009348 |text = ornithine carbamoyltransferase complex}}
| Process = {{GNF_GO|id=GO:0000050 |text = urea cycle}} {{GNF_GO|id=GO:0006526 |text = arginine biosynthetic process}} {{GNF_GO|id=GO:0008652 |text = amino acid biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5009
| Hs_Ensembl = ENSG00000036473
| Hs_RefseqProtein = NP_000522
| Hs_RefseqmRNA = NM_000531
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 38096302
| Hs_GenLoc_end = 38165553
| Hs_Uniprot = P00480
| Mm_EntrezGene = 18416
| Mm_Ensembl = ENSMUSG00000031173
| Mm_RefseqmRNA = NM_008769
| Mm_RefseqProtein = NP_032795
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 9409318
| Mm_GenLoc_end = 9477983
| Mm_Uniprot = Q543H3
}}
}}
'''Ornithine carbamoyltransferase''', also known as '''OTC''', 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 nuclear gene encodes a mitochondrial matrix enzyme. Missense, nonsense, and frameshift mutations in this enzyme lead to ornithine transcarbamylase deficiency, which causes hyperammonemia. Since the gene for this enzyme maps close to that for Duchenne muscular dystrophy, it may play a role in that disease also.<ref>{{cite web | title = Entrez Gene: OTC ornithine carbamoyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5009| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tuchman M, Plante RJ |title=Mutations and polymorphisms in the human ornithine transcarbamylase gene: mutation update addendum. |journal=Hum. Mutat. |volume=5 |issue= 4 |pages= 293-5 |year= 1995 |pmid= 7627182 |doi= 10.1002/humu.1380050404 }}
*{{cite journal | author=Tuchman M |title=Mutations and polymorphisms in the human ornithine transcarbamylase gene. |journal=Hum. Mutat. |volume=2 |issue= 3 |pages= 174-8 |year= 1993 |pmid= 8364586 |doi= 10.1002/humu.1380020304 }}
*{{cite journal | author=Matsuda I, Tanase S |title=The ornithine transcarbamylase (OTC) gene: mutations in 50 Japanese families with OTC deficiency. |journal=Am. J. Med. Genet. |volume=71 |issue= 4 |pages= 378-83 |year= 1997 |pmid= 9286441 |doi= }}
*{{cite journal | author=Wakabayashi Y |title=Tissue-selective expression of enzymes of arginine synthesis. |journal=Current opinion in clinical nutrition and metabolic care |volume=1 |issue= 4 |pages= 335-9 |year= 1999 |pmid= 10565370 |doi= }}
*{{cite journal | author=Tuchman M, Jaleel N, Morizono H, ''et al.'' |title=Mutations and polymorphisms in the human ornithine transcarbamylase gene. |journal=Hum. Mutat. |volume=19 |issue= 2 |pages= 93-107 |year= 2002 |pmid= 11793468 |doi= 10.1002/humu.10035 }}
*{{cite journal | author=Feldmann D, Rozet JM, Pelet A, ''et al.'' |title=Site specific screening for point mutations in ornithine transcarbamylase deficiency. |journal=J. Med. Genet. |volume=29 |issue= 7 |pages= 471-5 |year= 1992 |pmid= 1353535 |doi= }}
*{{cite journal | author=Tuchman M, Holzknecht RA, Gueron AB, ''et al.'' |title=Six new mutations in the ornithine transcarbamylase gene detected by single-strand conformational polymorphism. |journal=Pediatr. Res. |volume=32 |issue= 5 |pages= 600-4 |year= 1993 |pmid= 1480464 |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=Suess PJ, Tsai MY, Holzknecht RA, ''et al.'' |title=Screening for gene deletions and known mutations in 13 patients with ornithine transcarbamylase deficiency. |journal=Biochem. Med. Metab. Biol. |volume=47 |issue= 3 |pages= 250-9 |year= 1992 |pmid= 1627356 |doi= }}
*{{cite journal | author=Grompe M, Caskey CT, Fenwick RG |title=Improved molecular diagnostics for ornithine transcarbamylase deficiency. |journal=Am. J. Hum. Genet. |volume=48 |issue= 2 |pages= 212-22 |year= 1991 |pmid= 1671317 |doi= }}
*{{cite journal | author=Hentzen D, Pelet A, Feldman D, ''et al.'' |title=Fatal hyperammonemia resulting from a C-to-T mutation at a MspI site of the ornithine transcarbamylase gene. |journal=Hum. Genet. |volume=88 |issue= 2 |pages= 153-6 |year= 1992 |pmid= 1721894 |doi= }}
*{{cite journal | author=Strautnieks S, Rutland P, Malcolm S |title=Arginine 109 to glutamine mutation in a girl with ornithine carbamoyl transferase deficiency. |journal=J. Med. Genet. |volume=28 |issue= 12 |pages= 871-4 |year= 1992 |pmid= 1757964 |doi= }}
*{{cite journal | author=Carstens RP, Fenton WA, Rosenberg LR |title=Identification of RNA splicing errors resulting in human ornithine transcarbamylase deficiency. |journal=Am. J. Hum. Genet. |volume=48 |issue= 6 |pages= 1105-14 |year= 1991 |pmid= 2035531 |doi= }}
*{{cite journal | author=Hata A, Matsuura T, Setoyama C, ''et al.'' |title=A novel missense mutation in exon 8 of the ornithine transcarbamylase gene in two unrelated male patients with mild ornithine transcarbamylase deficiency. |journal=Hum. Genet. |volume=87 |issue= 1 |pages= 28-32 |year= 1991 |pmid= 2037279 |doi= }}
*{{cite journal | author=Legius E, Baten E, Stul M, ''et al.'' |title=Sporadic late onset ornithine transcarbamylase deficiency in a boy with somatic mosaicism for an intragenic deletion. |journal=Clin. Genet. |volume=38 |issue= 2 |pages= 155-9 |year= 1990 |pmid= 2208768 |doi= }}
*{{cite journal | author=Finkelstein JE, Francomano CA, Brusilow SW, Traystman MD |title=Use of denaturing gradient gel electrophoresis for detection of mutation and prospective diagnosis in late onset ornithine transcarbamylase deficiency. |journal=Genomics |volume=7 |issue= 2 |pages= 167-72 |year= 1990 |pmid= 2347583 |doi= }}
*{{cite journal | author=Grompe M, Muzny DM, Caskey CT |title=Scanning detection of mutations in human ornithine transcarbamoylase by chemical mismatch cleavage. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 15 |pages= 5888-92 |year= 1989 |pmid= 2474822 |doi= }}
*{{cite journal | author=Lee JT, Nussbaum RL |title=An arginine to glutamine mutation in residue 109 of human ornithine transcarbamylase completely abolishes enzymatic activity in Cos1 cells. |journal=J. Clin. Invest. |volume=84 |issue= 6 |pages= 1762-6 |year= 1990 |pmid= 2556444 |doi= }}
*{{cite journal | author=Chu TW, Eftime R, Sztul E, Strauss AW |title=Synthetic transit peptides inhibit import and processing of mitochondrial precursor proteins. |journal=J. Biol. Chem. |volume=264 |issue= 16 |pages= 9552-8 |year= 1989 |pmid= 2722850 |doi= }}
*{{cite journal | author=Hata A, Setoyama C, Shimada K, ''et al.'' |title=Ornithine transcarbamylase deficiency resulting from a C-to-T substitution in exon 5 of the ornithine transcarbamylase gene. |journal=Am. J. Hum. Genet. |volume=45 |issue= 1 |pages= 123-7 |year= 1989 |pmid= 2741942 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on POU2F1... {November 14, 2007 4:01:34 PM PST}
- SEARCH REDIRECT: Control Box Found: POU2F1 {November 14, 2007 4:02:46 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 4:02:47 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 4:02:47 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 4:02:47 PM PST}
- UPDATED: Updated protein page: POU2F1 {November 14, 2007 4:02:55 PM PST}
- INFO: Beginning work on PRKAR2A... {November 14, 2007 4:02:55 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:03:33 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 = PBB_Protein_PRKAR2A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1l6e.
| PDB = {{PDB2|1l6e}}, {{PDB2|1r2a}}, {{PDB2|2drn}}, {{PDB2|2h9r}}, {{PDB2|2hwn}}, {{PDB2|2izx}}, {{PDB2|2izy}}
| Name = Protein kinase, cAMP-dependent, regulatory, type II, alpha
| HGNCid = 9391
| Symbol = PRKAR2A
| AltSymbols =; MGC3606; PKR2; PRKAR2
| OMIM = 176910
| ECnumber =
| Homologene = 3064
| MGIid = 108025
| GeneAtlas_image1 = PBB_GE_PRKAR2A_204842_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_PRKAR2A_204843_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PRKAR2A_213052_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008603 |text = cAMP-dependent protein kinase regulator activity}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0030552 |text = cAMP binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005952 |text = cAMP-dependent protein kinase complex}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5576
| Hs_Ensembl = ENSG00000114302
| Hs_RefseqProtein = NP_004148
| Hs_RefseqmRNA = NM_004157
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 48762099
| Hs_GenLoc_end = 48860274
| Hs_Uniprot = P13861
| Mm_EntrezGene = 19087
| Mm_Ensembl = ENSMUSG00000032601
| Mm_RefseqmRNA = NM_008924
| Mm_RefseqProtein = NP_032950
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 108549547
| Mm_GenLoc_end = 108606747
| Mm_Uniprot = Q8K1M3
}}
}}
'''Protein kinase, cAMP-dependent, regulatory, type II, alpha''', also known as '''PRKAR2A''', 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 = cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase (AMPK), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of AMPK is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of AMPK have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. It may interact with various A-kinase anchoring proteins and determine the subcellular localization of AMPK. This subunit has been shown to regulate protein transport from endosomes to the Golgi apparatus and further to the endoplasmic reticulum (ER).<ref>{{cite web | title = Entrez Gene: PRKAR2A protein kinase, cAMP-dependent, regulatory, type II, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5576| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Cho-Chung YS, Nesterova MV |title=Tumor reversion: protein kinase A isozyme switching. |journal=Ann. N. Y. Acad. Sci. |volume=1058 |issue= |pages= 76-86 |year= 2006 |pmid= 16394127 |doi= 10.1196/annals.1359.014 }}
*{{cite journal | author=Harrich D, McMillan N, Munoz L, ''et al.'' |title=Will diverse Tat interactions lead to novel antiretroviral drug targets? |journal=Current drug targets |volume=7 |issue= 12 |pages= 1595-606 |year= 2007 |pmid= 17168834 |doi= }}
*{{cite journal | author=Skålhegg BS, Landmark B, Foss KB, ''et al.'' |title=Identification, purification, and characterization of subunits of cAMP-dependent protein kinase in human testis. Reverse mobilities of human RII alpha and RII beta on sodium dodecyl sulfate-polyacrylamide gel electrophoresis compared with rat and bovine RIIs. |journal=J. Biol. Chem. |volume=267 |issue= 8 |pages= 5374-9 |year= 1992 |pmid= 1544918 |doi= }}
*{{cite journal | author=Carr DW, Hausken ZE, Fraser ID, ''et al.'' |title=Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain. |journal=J. Biol. Chem. |volume=267 |issue= 19 |pages= 13376-82 |year= 1992 |pmid= 1618839 |doi= }}
*{{cite journal | author=Hofmann B, Nishanian P, Baldwin RL, ''et al.'' |title=HIV inhibits the early steps of lymphocyte activation, including initiation of inositol phospholipid metabolism. |journal=J. Immunol. |volume=145 |issue= 11 |pages= 3699-705 |year= 1991 |pmid= 1978848 |doi= }}
*{{cite journal | author=Scott JD, Stofko RE, McDonald JR, ''et al.'' |title=Type II regulatory subunit dimerization determines the subcellular localization of the cAMP-dependent protein kinase. |journal=J. Biol. Chem. |volume=265 |issue= 35 |pages= 21561-6 |year= 1991 |pmid= 2147685 |doi= }}
*{{cite journal | author=Oyen O, Myklebust F, Scott JD, ''et al.'' |title=Human testis cDNA for the regulatory subunit RII alpha of cAMP-dependent protein kinase encodes an alternate amino-terminal region. |journal=FEBS Lett. |volume=246 |issue= 1-2 |pages= 57-64 |year= 1989 |pmid= 2540040 |doi= }}
*{{cite journal | author=Obar RA, Dingus J, Bayley H, Vallee RB |title=The RII subunit of cAMP-dependent protein kinase binds to a common amino-terminal domain in microtubule-associated proteins 2A, 2B, and 2C. |journal=Neuron |volume=3 |issue= 5 |pages= 639-45 |year= 1990 |pmid= 2561973 |doi= }}
*{{cite journal | author=Rubino HM, Dammerman M, Shafit-Zagardo B, Erlichman J |title=Localization and characterization of the binding site for the regulatory subunit of type II cAMP-dependent protein kinase on MAP2. |journal=Neuron |volume=3 |issue= 5 |pages= 631-8 |year= 1990 |pmid= 2701845 |doi= }}
*{{cite journal | author=Hemmings BA, Aitken A, Cohen P, ''et al.'' |title=Phosphorylation of the type-II regulatory subunit of cyclic-AMP-dependent protein kinase by glycogen synthase kinase 3 and glycogen synthase kinase 5. |journal=Eur. J. Biochem. |volume=127 |issue= 3 |pages= 473-81 |year= 1983 |pmid= 6293815 |doi= }}
*{{cite journal | author=Hofmann B, Nishanian P, Nguyen T, ''et al.'' |title=Human immunodeficiency virus proteins induce the inhibitory cAMP/protein kinase A pathway in normal lymphocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 14 |pages= 6676-80 |year= 1993 |pmid= 7688126 |doi= }}
*{{cite journal | author=Pariset C, Weinman S |title=Differential localization of two isoforms of the regulatory subunit RII alpha of cAMP-dependent protein kinase in human sperm: biochemical and cytochemical study. |journal=Mol. Reprod. Dev. |volume=39 |issue= 4 |pages= 415-22 |year= 1995 |pmid= 7893490 |doi= 10.1002/mrd.1080390410 }}
*{{cite journal | author=Cheley S, Panchal RG, Carr DW, ''et al.'' |title=Type II regulatory subunits of cAMP-dependent protein kinase and their binding proteins in the nervous system of Aplysia californica. |journal=J. Biol. Chem. |volume=269 |issue= 4 |pages= 2911-20 |year= 1994 |pmid= 7905481 |doi= }}
*{{cite journal | author=Hausken ZE, Coghlan VM, Hastings CA, ''et al.'' |title=Type II regulatory subunit (RII) of the cAMP-dependent protein kinase interaction with A-kinase anchor proteins requires isoleucines 3 and 5. |journal=J. Biol. Chem. |volume=269 |issue= 39 |pages= 24245-51 |year= 1994 |pmid= 7929081 |doi= }}
*{{cite journal | author=Hofmann B, Nishanian P, Fan J, ''et al.'' |title=HIV Gag p17 protein impairs proliferation of normal lymphocytes in vitro. |journal=AIDS |volume=8 |issue= 7 |pages= 1016-7 |year= 1994 |pmid= 7946090 |doi= }}
*{{cite journal | author=Beebe SJ, Salomonsky P, Holroyd C, Becker D |title=Differential expression of cyclic AMP-dependent protein kinase isozymes in normal human melanocytes and malignant melanomas. |journal=Cell Growth Differ. |volume=4 |issue= 12 |pages= 1005-12 |year= 1994 |pmid= 8117614 |doi= }}
*{{cite journal | author=Coghlan VM, Langeberg LK, Fernandez A, ''et al.'' |title=Cloning and characterization of AKAP 95, a nuclear protein that associates with the regulatory subunit of type II cAMP-dependent protein kinase. |journal=J. Biol. Chem. |volume=269 |issue= 10 |pages= 7658-65 |year= 1994 |pmid= 8125992 |doi= }}
*{{cite journal | author=Lester LB, Coghlan VM, Nauert B, Scott JD |title=Cloning and characterization of a novel A-kinase anchoring protein. AKAP 220, association with testicular peroxisomes. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9460-5 |year= 1996 |pmid= 8621616 |doi= }}
*{{cite journal | author=Foss KB, Solberg R, Simard J, ''et al.'' |title=Molecular cloning, upstream sequence and promoter studies of the human gene for the regulatory subunit RII alpha of cAMP-dependent protein kinase. |journal=Biochim. Biophys. Acta |volume=1350 |issue= 1 |pages= 98-108 |year= 1997 |pmid= 9003463 |doi= }}
*{{cite journal | author=Dransfield DT, Bradford AJ, Smith J, ''et al.'' |title=Ezrin is a cyclic AMP-dependent protein kinase anchoring protein. |journal=EMBO J. |volume=16 |issue= 1 |pages= 35-43 |year= 1997 |pmid= 9009265 |doi= 10.1093/emboj/16.1.35 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTH... {November 14, 2007 4:03:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:03:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PTH_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bwx.
| PDB = {{PDB2|1bwx}}, {{PDB2|1et1}}, {{PDB2|1fvy}}, {{PDB2|1hph}}, {{PDB2|1hpy}}, {{PDB2|1zwa}}, {{PDB2|1zwb}}, {{PDB2|1zwc}}, {{PDB2|1zwd}}, {{PDB2|1zwe}}, {{PDB2|1zwf}}, {{PDB2|1zwg}}
| Name = Parathyroid hormone
| HGNCid = 9606
| Symbol = PTH
| AltSymbols =;
| OMIM = 168450
| ECnumber =
| Homologene = 266
| MGIid = 97799
| GeneAtlas_image1 = PBB_GE_PTH_206977_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007595 |text = lactation}} {{GNF_GO|id=GO:0008628 |text = induction of apoptosis by hormones}} {{GNF_GO|id=GO:0045453 |text = bone resorption}} {{GNF_GO|id=GO:0046058 |text = cAMP metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5741
| Hs_Ensembl = ENSG00000152266
| Hs_RefseqProtein = NP_000306
| Hs_RefseqmRNA = NM_000315
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 13470178
| Hs_GenLoc_end = 13474143
| Hs_Uniprot = P01270
| Mm_EntrezGene = 19226
| Mm_Ensembl = ENSMUSG00000059077
| Mm_RefseqmRNA = NM_020623
| Mm_RefseqProtein = NP_065648
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 113176759
| Mm_GenLoc_end = 113179753
| Mm_Uniprot =
}}
}}
'''Parathyroid hormone''', also known as '''PTH''', 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 hormone secreted by parathyroid cells. This hormone elevates blood Ca2+ level by dissolving the salts in bone and preventing their renal excretion. Defects in this gene are a cause of familial isolated hypoparathyroidism (FIH).<ref>{{cite web | title = Entrez Gene: PTH parathyroid hormone| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5741| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Drüeke TB, Massy ZA |title=Advanced oxidation protein products, parathyroid hormone and vascular calcification in uremia. |journal=Blood Purif. |volume=20 |issue= 5 |pages= 494-7 |year= 2003 |pmid= 12207101 |doi= }}
*{{cite journal | author=Parfitt AM |title=Parathyroid hormone and periosteal bone expansion. |journal=J. Bone Miner. Res. |volume=17 |issue= 10 |pages= 1741-3 |year= 2003 |pmid= 12369776 |doi= }}
*{{cite journal | author=Martin TJ |title=Does bone resorption inhibition affect the anabolic response to parathyroid hormone? |journal=Trends Endocrinol. Metab. |volume=15 |issue= 2 |pages= 49-50 |year= 2004 |pmid= 15080150 |doi= }}
*{{cite journal | author=Keutmann HT, Sauer MM, Hendy GN, ''et al.'' |title=Complete amino acid sequence of human parathyroid hormone. |journal=Biochemistry |volume=17 |issue= 26 |pages= 5723-9 |year= 1979 |pmid= 728431 |doi= }}
*{{cite journal | author=Keutmann HT, Niall HD, O'Riordan JL, Potts JT |title=A reinvestigation of the amino-terminal sequence of human parathyroid hormone. |journal=Biochemistry |volume=14 |issue= 9 |pages= 1842-7 |year= 1975 |pmid= 1125201 |doi= }}
*{{cite journal | author=Parkinson DB, Thakker RV |title=A donor splice site mutation in the parathyroid hormone gene is associated with autosomal recessive hypoparathyroidism. |journal=Nat. Genet. |volume=1 |issue= 2 |pages= 149-52 |year= 1993 |pmid= 1302009 |doi= 10.1038/ng0592-149 }}
*{{cite journal | author=Handt O, Reis A, Schmidtke J |title=Ectopic transcription of the parathyroid hormone gene in lymphocytes, lymphoblastoid cells and tumour tissue. |journal=J. Endocrinol. |volume=135 |issue= 2 |pages= 249-56 |year= 1993 |pmid= 1474331 |doi= }}
*{{cite journal | author=Tonoki H, Narahara K, Matsumoto T, Niikawa N |title=Regional mapping of the parathyroid hormone gene (PTH) by cytogenetic and molecular studies. |journal=Cytogenet. Cell Genet. |volume=56 |issue= 2 |pages= 103-4 |year= 1991 |pmid= 1672845 |doi= }}
*{{cite journal | author=Klaus W, Dieckmann T, Wray V, ''et al.'' |title=Investigation of the solution structure of the human parathyroid hormone fragment (1-34) by 1H NMR spectroscopy, distance geometry, and molecular dynamics calculations. |journal=Biochemistry |volume=30 |issue= 28 |pages= 6936-42 |year= 1991 |pmid= 2069952 |doi= }}
*{{cite journal | author=Arnold A, Horst SA, Gardella TJ, ''et al.'' |title=Mutation of the signal peptide-encoding region of the preproparathyroid hormone gene in familial isolated hypoparathyroidism. |journal=J. Clin. Invest. |volume=86 |issue= 4 |pages= 1084-7 |year= 1990 |pmid= 2212001 |doi= }}
*{{cite journal | author=Nussbaum SR, Gaz RD, Arnold A |title=Hypercalcemia and ectopic secretion of parathyroid hormone by an ovarian carcinoma with rearrangement of the gene for parathyroid hormone. |journal=N. Engl. J. Med. |volume=323 |issue= 19 |pages= 1324-8 |year= 1990 |pmid= 2215618 |doi= }}
*{{cite journal | author=Ahn TG, Antonarakis SE, Kronenberg HM, ''et al.'' |title=Familial isolated hypoparathyroidism: a molecular genetic analysis of 8 families with 23 affected persons. |journal=Medicine (Baltimore) |volume=65 |issue= 2 |pages= 73-81 |year= 1986 |pmid= 3005800 |doi= }}
*{{cite journal | author=Tregear GW, van Rietschoten J, Greene E, ''et al.'' |title=Solid-phase synthesis of the biologically active N-terminal 1 - 34 peptide of human parathyroid hormone. |journal=Hoppe-Seyler's Z. Physiol. Chem. |volume=355 |issue= 4 |pages= 415-21 |year= 1975 |pmid= 4474131 |doi= }}
*{{cite journal | author=Niall HD, Sauer RT, Jacobs JW, ''et al.'' |title=The amino-acid sequence of the amino-terminal 37 residues of human parathyroid hormone. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=71 |issue= 2 |pages= 384-8 |year= 1974 |pmid= 4521809 |doi= }}
*{{cite journal | author=Andreatta RH, Hartmann A, Jöhl A, ''et al.'' |title=[Synthesis of sequence 1-34 of human parathyroid hormone] |journal=Helv. Chim. Acta |volume=56 |issue= 1 |pages= 470-3 |year= 1973 |pmid= 4721748 |doi= 10.1002/hlca.19730560139 }}
*{{cite journal | author=Jacobs JW, Kemper B, Niall HD, ''et al.'' |title=Structural analysis of human proparathyroid hormone by a new microsequencing approach. |journal=Nature |volume=249 |issue= 453 |pages= 155-7 |year= 1974 |pmid= 4833516 |doi= }}
*{{cite journal | author=Vasicek TJ, McDevitt BE, Freeman MW, ''et al.'' |title=Nucleotide sequence of the human parathyroid hormone gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 8 |pages= 2127-31 |year= 1983 |pmid= 6220408 |doi= }}
*{{cite journal | author=Mayer H, Breyel E, Bostock C, Schmidtke J |title=Assignment of the human parathyroid hormone gene to chromosome 11. |journal=Hum. Genet. |volume=64 |issue= 3 |pages= 283-5 |year= 1983 |pmid= 6885073 |doi= }}
*{{cite journal | author=Hendy GN, Kronenberg HM, Potts JT, Rich A |title=Nucleotide sequence of cloned cDNAs encoding human preproparathyroid hormone. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=78 |issue= 12 |pages= 7365-9 |year= 1982 |pmid= 6950381 |doi= }}
*{{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= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on THRA... {November 14, 2007 4:04:41 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 4:05:27 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 = PBB_Protein_THRA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nav.
| PDB = {{PDB2|1nav}}, {{PDB2|2h77}}, {{PDB2|2h79}}
| Name = Thyroid hormone receptor, alpha (erythroblastic leukemia viral (v-erb-a) oncogene homolog, avian)
| HGNCid = 11796
| Symbol = THRA
| AltSymbols =; AR7; EAR7; ERB-T-1; ERBA; ERBA1; MGC000261; MGC43240; NR1A1; THRA1; THRA2; c-ERBA-1
| OMIM = 190120
| ECnumber =
| Homologene = 37747
| MGIid = 98742
| GeneAtlas_image1 = PBB_GE_THRA_35846_at_tn.png
| GeneAtlas_image2 = PBB_GE_THRA_204100_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0004887 |text = thyroid hormone receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001502 |text = cartilage condensation}} {{GNF_GO|id=GO:0001503 |text = ossification}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0008016 |text = regulation of heart contraction}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7067
| Hs_Ensembl = ENSG00000126351
| Hs_RefseqProtein = NP_003241
| Hs_RefseqmRNA = NM_003250
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 35472686
| Hs_GenLoc_end = 35503644
| Hs_Uniprot = P10827
| Mm_EntrezGene = 21833
| Mm_Ensembl = ENSMUSG00000058756
| Mm_RefseqmRNA = XM_994382
| Mm_RefseqProtein = XP_999476
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 98557963
| Mm_GenLoc_end = 98585094
| Mm_Uniprot = Q80Y90
}}
}}
'''Thyroid hormone receptor, alpha (erythroblastic leukemia viral (v-erb-a) oncogene homolog, avian)''', also known as '''THRA''', 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 nuclear hormone receptor for triiodothyronine. It is one of the several receptors for thyroid hormone, and has been shown to mediate the biological activities of thyroid hormone. Knockout studies in mice suggest that the different receptors, while having certain extent of redundancy, may mediate different functions of thyroid hormone. Alternatively spliced transcript variants encoding distinct isoforms have been reported.<ref>{{cite web | title = Entrez Gene: THRA thyroid hormone receptor, alpha (erythroblastic leukemia viral (v-erb-a) oncogene homolog, avian)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7067| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Forrest D, Reh TA, Rüsch A |title=Neurodevelopmental control by thyroid hormone receptors. |journal=Curr. Opin. Neurobiol. |volume=12 |issue= 1 |pages= 49-56 |year= 2002 |pmid= 11861164 |doi= }}
*{{cite journal | author=Sakurai A, Bell GI, DeGroot LJ |title=Dinucleotide repeat polymorphism in the human thyroid hormone receptor alpha gene (THRA1) on chromosome 17. |journal=Hum. Mol. Genet. |volume=1 |issue= 7 |pages= 553 |year= 1993 |pmid= 1307263 |doi= }}
*{{cite journal | author=Berrodin TJ, Marks MS, Ozato K, ''et al.'' |title=Heterodimerization among thyroid hormone receptor, retinoic acid receptor, retinoid X receptor, chicken ovalbumin upstream promoter transcription factor, and an endogenous liver protein. |journal=Mol. Endocrinol. |volume=6 |issue= 9 |pages= 1468-78 |year= 1992 |pmid= 1331778 |doi= }}
*{{cite journal | author=Schmidt ED, Schmidt ED, van der Gaag R, ''et al.'' |title=Distribution of the nuclear thyroid-hormone receptor in extraocular and skeletal muscles. |journal=J. Endocrinol. |volume=133 |issue= 1 |pages= 67-74 |year= 1992 |pmid= 1517709 |doi= }}
*{{cite journal | author=Yen PM, Sunday ME, Darling DS, Chin WW |title=Isoform-specific thyroid hormone receptor antibodies detect multiple thyroid hormone receptors in rat and human pituitaries. |journal=Endocrinology |volume=130 |issue= 3 |pages= 1539-46 |year= 1992 |pmid= 1537303 |doi= }}
*{{cite journal | author=Laudet V, Begue A, Henry-Duthoit C, ''et al.'' |title=Genomic organization of the human thyroid hormone receptor alpha (c-erbA-1) gene. |journal=Nucleic Acids Res. |volume=19 |issue= 5 |pages= 1105-12 |year= 1991 |pmid= 1850510 |doi= }}
*{{cite journal | author=Nakai A, Sakurai A, Bell GI, DeGroot LJ |title=Characterization of a third human thyroid hormone receptor coexpressed with other thyroid hormone receptors in several tissues. |journal=Mol. Endocrinol. |volume=2 |issue= 11 |pages= 1087-92 |year= 1989 |pmid= 2464749 |doi= }}
*{{cite journal | author=Miyajima N, Horiuchi R, Shibuya Y, ''et al.'' |title=Two erbA homologs encoding proteins with different T3 binding capacities are transcribed from opposite DNA strands of the same genetic locus. |journal=Cell |volume=57 |issue= 1 |pages= 31-9 |year= 1989 |pmid= 2539258 |doi= }}
*{{cite journal | author=Sakurai A, Nakai A, DeGroot LJ |title=Expression of three forms of thyroid hormone receptor in human tissues. |journal=Mol. Endocrinol. |volume=3 |issue= 2 |pages= 392-9 |year= 1989 |pmid= 2710139 |doi= }}
*{{cite journal | author=Sap J, Muñoz A, Damm K, ''et al.'' |title=The c-erb-A protein is a high-affinity receptor for thyroid hormone. |journal=Nature |volume=324 |issue= 6098 |pages= 635-40 |year= 1987 |pmid= 2879242 |doi= 10.1038/324635a0 }}
*{{cite journal | author=Nakai A, Seino S, Sakurai A, ''et al.'' |title=Characterization of a thyroid hormone receptor expressed in human kidney and other tissues. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 8 |pages= 2781-5 |year= 1988 |pmid= 3357890 |doi= }}
*{{cite journal | author=Mitelman F, Manolov G, Manolova Y, ''et al.'' |title=High resolution chromosome analysis of constitutional and acquired t(15;17) maps c-erbA to subband 17q11.2. |journal=Cancer Genet. Cytogenet. |volume=22 |issue= 2 |pages= 95-8 |year= 1986 |pmid= 3458521 |doi= }}
*{{cite journal | author=Benbrook D, Pfahl M |title=A novel thyroid hormone receptor encoded by a cDNA clone from a human testis library. |journal=Science |volume=238 |issue= 4828 |pages= 788-91 |year= 1987 |pmid= 3672126 |doi= }}
*{{cite journal | author=Pfahl M, Benbrook D |title=Nucleotide sequence of cDNA encoding a novel human thyroid hormone receptor. |journal=Nucleic Acids Res. |volume=15 |issue= 22 |pages= 9613 |year= 1988 |pmid= 3684612 |doi= }}
*{{cite journal | author=Spurr NK, Solomon E, Jansson M, ''et al.'' |title=Chromosomal localisation of the human homologues to the oncogenes erbA and B. |journal=EMBO J. |volume=3 |issue= 1 |pages= 159-63 |year= 1984 |pmid= 6323162 |doi= }}
*{{cite journal | author=Dayton AI, Selden JR, Laws G, ''et al.'' |title=A human c-erbA oncogene homologue is closely proximal to the chromosome 17 breakpoint in acute promyelocytic leukemia. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 14 |pages= 4495-9 |year= 1984 |pmid= 6589608 |doi= }}
*{{cite journal | author=Chen JD, Evans RM |title=A transcriptional co-repressor that interacts with nuclear hormone receptors. |journal=Nature |volume=377 |issue= 6548 |pages= 454-7 |year= 1995 |pmid= 7566127 |doi= 10.1038/377454a0 }}
*{{cite journal | author=Desai-Yajnik V, Hadzic E, Modlinger P, ''et al.'' |title=Interactions of thyroid hormone receptor with the human immunodeficiency virus type 1 (HIV-1) long terminal repeat and the HIV-1 Tat transactivator. |journal=J. Virol. |volume=69 |issue= 8 |pages= 5103-12 |year= 1995 |pmid= 7609079 |doi= }}
*{{cite journal | author=Lee JW, Choi HS, Gyuris J, ''et al.'' |title=Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. |journal=Mol. Endocrinol. |volume=9 |issue= 2 |pages= 243-54 |year= 1995 |pmid= 7776974 |doi= }}
*{{cite journal | author=Desai-Yajnik V, Samuels HH |title=Regulation of the human immunodeficiency virus type 1 long terminal repeat: interactions of thyroid hormone receptor with retinoid-X receptor, nuclear factor kappa B, Sp1, and Tat. |journal=Trans. Assoc. Am. Physicians |volume=106 |issue= |pages= 13-32 |year= 1994 |pmid= 8036737 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TJP1... {November 14, 2007 4:05:27 PM PST}
- SEARCH REDIRECT: Control Box Found: TJP1 {November 14, 2007 4:06:37 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 4:06:38 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 4:06:38 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 4:06:38 PM PST}
- UPDATED: Updated protein page: TJP1 {November 14, 2007 4:06:45 PM PST}
end log.
