Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 23:52, 14 November 2007 (UTC)
[edit]Proteins without matches (9)
[edit]Proteins with a High Potential Match (9)
[edit]Redirected Proteins (7)
[edit]Manual Inspection (Page not found) (18)
[edit]
Protein Status Grid - Date: 23:52, 14 November 2007 (UTC)
[edit]Vebose Log - Date: 23:52, 14 November 2007 (UTC)
[edit]- INFO: Beginning work on ARRB2... {November 14, 2007 3:27:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:28:06 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Arrestin, beta 2
| HGNCid = 712
| Symbol = ARRB2
| AltSymbols =; ARB2; ARR2; DKFZp686L0365
| OMIM = 107941
| ECnumber =
| Homologene = 3183
| MGIid = 99474
| GeneAtlas_image1 = PBB_GE_ARRB2_203388_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007600 |text = sensory perception}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 409
| Hs_Ensembl = ENSG00000141480
| Hs_RefseqProtein = NP_004304
| Hs_RefseqmRNA = NM_004313
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 4560533
| Hs_GenLoc_end = 4571544
| Hs_Uniprot = P32121
| Mm_EntrezGene = 216869
| Mm_Ensembl = ENSMUSG00000060216
| Mm_RefseqmRNA = XM_993633
| Mm_RefseqProtein = XP_998727
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 70248840
| Mm_GenLoc_end = 70257023
| Mm_Uniprot = Q3UCU5
}}
}}
'''Arrestin, beta 2''', also known as '''ARRB2''', 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 = Members of arrestin/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of G-protein-coupled receptors and cause specific dampening of cellular responses to stimuli such as hormones, neurotransmitters, or sensory signals. Arrestin beta 2, like arrestin beta 1, was shown to inhibit beta-adrenergic receptor function in vitro. It is expressed at high levels in the central nervous system and may play a role in the regulation of synaptic receptors. Besides the brain, a cDNA for arrestin beta 2 was isolated from thyroid gland, and thus it may also be involved in hormone-specific desensitization of TSH receptors. Multiple alternatively spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been defined.<ref>{{cite web | title = Entrez Gene: ARRB2 arrestin, beta 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=409| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lefkowitz RJ |title=G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization. |journal=J. Biol. Chem. |volume=273 |issue= 30 |pages= 18677-80 |year= 1998 |pmid= 9668034 |doi= }}
*{{cite journal | author=Attramadal H, Arriza JL, Aoki C, ''et al.'' |title=Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family. |journal=J. Biol. Chem. |volume=267 |issue= 25 |pages= 17882-90 |year= 1992 |pmid= 1517224 |doi= }}
*{{cite journal | author=Rapoport B, Kaufman KD, Chazenbalk GD |title=Cloning of a member of the arrestin family from a human thyroid cDNA library. |journal=Mol. Cell. Endocrinol. |volume=84 |issue= 3 |pages= R39-43 |year= 1992 |pmid= 1587386 |doi= }}
*{{cite journal | author=Calabrese G, Sallese M, Stornaiuolo A, ''et al.'' |title=Chromosome mapping of the human arrestin (SAG), beta-arrestin 2 (ARRB2), and beta-adrenergic receptor kinase 2 (ADRBK2) genes. |journal=Genomics |volume=23 |issue= 1 |pages= 286-8 |year= 1995 |pmid= 7695743 |doi= 10.1006/geno.1994.1497 }}
*{{cite journal | author=Parruti G, Peracchia F, Sallese M, ''et al.'' |title=Molecular analysis of human beta-arrestin-1: cloning, tissue distribution, and regulation of expression. Identification of two isoforms generated by alternative splicing. |journal=J. Biol. Chem. |volume=268 |issue= 13 |pages= 9753-61 |year= 1993 |pmid= 8486659 |doi= }}
*{{cite journal | author=Le Gouill C, Parent JL, Rola-Pleszczynski M, Stanková J |title=Role of the Cys90, Cys95 and Cys173 residues in the structure and function of the human platelet-activating factor receptor. |journal=FEBS Lett. |volume=402 |issue= 2-3 |pages= 203-8 |year= 1997 |pmid= 9037196 |doi= }}
*{{cite journal | author=Barak LS, Ferguson SS, Zhang J, Caron MG |title=A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation. |journal=J. Biol. Chem. |volume=272 |issue= 44 |pages= 27497-500 |year= 1997 |pmid= 9346876 |doi= }}
*{{cite journal | author=Laporte SA, Oakley RH, Zhang J, ''et al.'' |title=The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 7 |pages= 3712-7 |year= 1999 |pmid= 10097102 |doi= }}
*{{cite journal | author=Cheng ZJ, Zhao J, Sun Y, ''et al.'' |title=beta-arrestin differentially regulates the chemokine receptor CXCR4-mediated signaling and receptor internalization, and this implicates multiple interaction sites between beta-arrestin and CXCR4. |journal=J. Biol. Chem. |volume=275 |issue= 4 |pages= 2479-85 |year= 2000 |pmid= 10644702 |doi= }}
*{{cite journal | author=Lin F, Wang H, Malbon CC |title=Gravin-mediated formation of signaling complexes in beta 2-adrenergic receptor desensitization and resensitization. |journal=J. Biol. Chem. |volume=275 |issue= 25 |pages= 19025-34 |year= 2000 |pmid= 10858453 |doi= }}
*{{cite journal | author=McDonald PH, Chow CW, Miller WE, ''et al.'' |title=Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3. |journal=Science |volume=290 |issue= 5496 |pages= 1574-7 |year= 2000 |pmid= 11090355 |doi= }}
*{{cite journal | author=Luttrell LM, Roudabush FL, Choy EW, ''et al.'' |title=Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 5 |pages= 2449-54 |year= 2001 |pmid= 11226259 |doi= 10.1073/pnas.041604898 }}
*{{cite journal | author=Cen B, Yu Q, Guo J, ''et al.'' |title=Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor. |journal=J. Neurochem. |volume=76 |issue= 6 |pages= 1887-94 |year= 2001 |pmid= 11259507 |doi= }}
*{{cite journal | author=Oakley RH, Laporte SA, Holt JA, ''et al.'' |title=Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-beta-arrestin complexes after receptor endocytosis*. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19452-60 |year= 2001 |pmid= 11279203 |doi= 10.1074/jbc.M101450200 }}
*{{cite journal | author=Miller WE, McDonald PH, Cai SF, ''et al.'' |title=Identification of a motif in the carboxyl terminus of beta -arrestin2 responsible for activation of JNK3. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 27770-7 |year= 2001 |pmid= 11356842 |doi= 10.1074/jbc.M102264200 }}
*{{cite journal | author=Claing A, Chen W, Miller WE, ''et al.'' |title=beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis. |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 42509-13 |year= 2001 |pmid= 11533043 |doi= 10.1074/jbc.M108399200 }}
*{{cite journal | author=Hilairet S, Bélanger C, Bertrand J, ''et al.'' |title=Agonist-promoted internalization of a ternary complex between calcitonin receptor-like receptor, receptor activity-modifying protein 1 (RAMP1), and beta-arrestin. |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 42182-90 |year= 2001 |pmid= 11535606 |doi= 10.1074/jbc.M107323200 }}
*{{cite journal | author=Shenoy SK, McDonald PH, Kohout TA, Lefkowitz RJ |title=Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin. |journal=Science |volume=294 |issue= 5545 |pages= 1307-13 |year= 2001 |pmid= 11588219 |doi= 10.1126/science.1063866 }}
*{{cite journal | author=Chen Z, Dupré DJ, Le Gouill C, ''et al.'' |title=Agonist-induced internalization of the platelet-activating factor receptor is dependent on arrestins but independent of G-protein activation. Role of the C terminus and the (D/N)PXXY motif. |journal=J. Biol. Chem. |volume=277 |issue= 9 |pages= 7356-62 |year= 2002 |pmid= 11729201 |doi= 10.1074/jbc.M110058200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BID... {November 14, 2007 3:28:06 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:28:53 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_BID_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2bid.
| PDB = {{PDB2|2bid}}
| Name = BH3 interacting domain death agonist
| HGNCid = 1050
| Symbol = BID
| AltSymbols =; MGC15319; MGC42355
| OMIM = 601997
| ECnumber =
| Homologene = 923
| MGIid = 108093
| GeneAtlas_image1 = PBB_GE_BID_204493_at_tn.png
| GeneAtlas_image2 = PBB_GE_BID_211725_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005123 |text = death receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0001836 |text = release of cytochrome c from mitochondria}} {{GNF_GO|id=GO:0008625 |text = induction of apoptosis via death domain receptors}} {{GNF_GO|id=GO:0043065 |text = positive regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 637
| Hs_Ensembl = ENSG00000015475
| Hs_RefseqProtein = NP_001187
| Hs_RefseqmRNA = NM_001196
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 16596908
| Hs_GenLoc_end = 16637431
| Hs_Uniprot = P55957
| Mm_EntrezGene = 12122
| Mm_Ensembl = ENSMUSG00000004446
| Mm_RefseqmRNA = NM_007544
| Mm_RefseqProtein = NP_031570
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 120858471
| Mm_GenLoc_end = 120882453
| Mm_Uniprot = P70444
}}
}}
'''BH3 interacting domain death agonist''', also known as '''BID''', 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 death agonist that heterodimerizes with either agonist BAX or antagonist BCL2. The encoded protein is a member of the BCL-2 family of cell death regulators. It is a mediator of mitochondrial damage induced by caspase-8 (CASP8); CASP8 cleaves this encoded protein, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. Multiple alternatively spliced transcript variants have been found, but the full-length nature of some variants has not been defined.<ref>{{cite web | title = Entrez Gene: BID BH3 interacting domain death agonist| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=637| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Soane L, Fiskum G |title=Inhibition of mitochondrial neural cell death pathways by protein transduction of Bcl-2 family proteins. |journal=J. Bioenerg. Biomembr. |volume=37 |issue= 3 |pages= 179-90 |year= 2006 |pmid= 16167175 |doi= 10.1007/s10863-005-6590-8 }}
*{{cite journal | author=Amagai M, Wang Y, Minoshima S, ''et al.'' |title=Assignment of the human genes for desmocollin 3 (DSC3) and desmocollin 4 (DSC4) to chromosome 18q12. |journal=Genomics |volume=25 |issue= 1 |pages= 330-2 |year= 1995 |pmid= 7774948 |doi= }}
*{{cite journal | author=Kawamura K, Watanabe K, Suzuki T, ''et al.'' |title=cDNA cloning and expression of a novel human desmocollin. |journal=J. Biol. Chem. |volume=269 |issue= 42 |pages= 26295-302 |year= 1994 |pmid= 7929347 |doi= }}
*{{cite journal | author=Wang K, Yin XM, Chao DT, ''et al.'' |title=BID: a novel BH3 domain-only death agonist. |journal=Genes Dev. |volume=10 |issue= 22 |pages= 2859-69 |year= 1996 |pmid= 8918887 |doi= }}
*{{cite journal | author=Huang DC, Adams JM, Cory S |title=The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4. |journal=EMBO J. |volume=17 |issue= 4 |pages= 1029-39 |year= 1998 |pmid= 9463381 |doi= 10.1093/emboj/17.4.1029 }}
*{{cite journal | author=Footz TK, Birren B, Minoshima S, ''et al.'' |title=The gene for death agonist BID maps to the region of human 22q11.2 duplicated in cat eye syndrome chromosomes and to mouse chromosome 6. |journal=Genomics |volume=51 |issue= 3 |pages= 472-5 |year= 1998 |pmid= 9721221 |doi= 10.1006/geno.1998.5392 }}
*{{cite journal | author=Luo X, Budihardjo I, Zou H, ''et al.'' |title=Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. |journal=Cell |volume=94 |issue= 4 |pages= 481-90 |year= 1998 |pmid= 9727491 |doi= }}
*{{cite journal | author=Li H, Zhu H, Xu CJ, Yuan J |title=Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. |journal=Cell |volume=94 |issue= 4 |pages= 491-501 |year= 1998 |pmid= 9727492 |doi= }}
*{{cite journal | author=Wang K, Yin XM, Copeland NG, ''et al.'' |title=BID, a proapoptotic BCL-2 family member, is localized to mouse chromosome 6 and human chromosome 22q11. |journal=Genomics |volume=53 |issue= 2 |pages= 235-8 |year= 1998 |pmid= 9790773 |doi= 10.1006/geno.1998.5489 }}
*{{cite journal | author=Chou JJ, Li H, Salvesen GS, ''et al.'' |title=Solution structure of BID, an intracellular amplifier of apoptotic signaling. |journal=Cell |volume=96 |issue= 5 |pages= 615-24 |year= 1999 |pmid= 10089877 |doi= }}
*{{cite journal | author=Bossy-Wetzel E, Green DR |title=Caspases induce cytochrome c release from mitochondria by activating cytosolic factors. |journal=J. Biol. Chem. |volume=274 |issue= 25 |pages= 17484-90 |year= 1999 |pmid= 10364179 |doi= }}
*{{cite journal | author=Wei MC, Lindsten T, Mootha VK, ''et al.'' |title=tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. |journal=Genes Dev. |volume=14 |issue= 16 |pages= 2060-71 |year= 2000 |pmid= 10950869 |doi= }}
*{{cite journal | author=Sutton VR, Davis JE, Cancilla M, ''et al.'' |title=Initiation of apoptosis by granzyme B requires direct cleavage of bid, but not direct granzyme B-mediated caspase activation. |journal=J. Exp. Med. |volume=192 |issue= 10 |pages= 1403-14 |year= 2000 |pmid= 11085743 |doi= }}
*{{cite journal | author=Zha J, Weiler S, Oh KJ, ''et al.'' |title=Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. |journal=Science |volume=290 |issue= 5497 |pages= 1761-5 |year= 2000 |pmid= 11099414 |doi= }}
*{{cite journal | author=Wang J, Guan E, Roderiquez G, Norcross MA |title=Synergistic induction of apoptosis in primary CD4(+) T cells by macrophage-tropic HIV-1 and TGF-beta1. |journal=J. Immunol. |volume=167 |issue= 6 |pages= 3360-6 |year= 2001 |pmid= 11544326 |doi= }}
*{{cite journal | author=Desagher S, Osen-Sand A, Montessuit S, ''et al.'' |title=Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8. |journal=Mol. Cell |volume=8 |issue= 3 |pages= 601-11 |year= 2001 |pmid= 11583622 |doi= }}
*{{cite journal | author=Cheng EH, Wei MC, Weiler S, ''et al.'' |title=BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. |journal=Mol. Cell |volume=8 |issue= 3 |pages= 705-11 |year= 2001 |pmid= 11583631 |doi= }}
*{{cite journal | author=Esposti MD, Erler JT, Hickman JA, Dive C |title=Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity. |journal=Mol. Cell. Biol. |volume=21 |issue= 21 |pages= 7268-76 |year= 2001 |pmid= 11585909 |doi= 10.1128/MCB.21.21.7268-7276.2001 }}
*{{cite journal | author=Madesh M, Antonsson B, Srinivasula SM, ''et al.'' |title=Rapid kinetics of tBid-induced cytochrome c and Smac/DIABLO release and mitochondrial depolarization. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 5651-9 |year= 2002 |pmid= 11741882 |doi= 10.1074/jbc.M108171200 }}
*{{cite journal | author=Tafani M, Karpinich NO, Hurster KA, ''et al.'' |title=Cytochrome c release upon Fas receptor activation depends on translocation of full-length bid and the induction of the mitochondrial permeability transition. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10073-82 |year= 2002 |pmid= 11790791 |doi= 10.1074/jbc.M111350200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CAT... {November 14, 2007 3:28:53 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:29:24 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
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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_CAT_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dgb.
| PDB = {{PDB2|1dgb}}, {{PDB2|1dgf}}, {{PDB2|1dgg}}, {{PDB2|1dgh}}, {{PDB2|1f4j}}, {{PDB2|1qqw}}, {{PDB2|1tgu}}, {{PDB2|1th2}}, {{PDB2|1th3}}, {{PDB2|1th4}}, {{PDB2|4blc}}, {{PDB2|7cat}}, {{PDB2|8cat}}
| Name = Catalase
| HGNCid = 1516
| Symbol = CAT
| AltSymbols =; MGC138422; MGC138424
| OMIM = 115500
| ECnumber =
| Homologene = 55514
| MGIid = 88271
| GeneAtlas_image1 = PBB_GE_CAT_201432_at_tn.png
| GeneAtlas_image2 = PBB_GE_CAT_211922_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004096 |text = catalase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005777 |text = peroxisome}} {{GNF_GO|id=GO:0005778 |text = peroxisomal membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}} {{GNF_GO|id=GO:0042744 |text = hydrogen peroxide catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 847
| Hs_Ensembl = ENSG00000121691
| Hs_RefseqProtein = NP_001743
| Hs_RefseqmRNA = NM_001752
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 34417054
| Hs_GenLoc_end = 34450176
| Hs_Uniprot = P04040
| Mm_EntrezGene = 12359
| Mm_Ensembl = ENSMUSG00000027187
| Mm_RefseqmRNA = NM_009804
| Mm_RefseqProtein = NP_033934
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 103254746
| Mm_GenLoc_end = 103285962
| Mm_Uniprot = Q3TVZ1
}}
}}
'''Catalase''', also known as '''CAT''', 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=Kishimoto Y, Murakami Y, Hayashi K, ''et al.'' |title=Detection of a common mutation of the catalase gene in Japanese acatalasemic patients. |journal=Hum. Genet. |volume=88 |issue= 5 |pages= 487-90 |year= 1992 |pmid= 1551654 |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=Shaffer JB, Preston KE |title=Molecular analysis of an acatalasemic mouse mutant. |journal=Biochem. Biophys. Res. Commun. |volume=173 |issue= 3 |pages= 1043-50 |year= 1991 |pmid= 2268310 |doi= }}
*{{cite journal | author=Wen JK, Osumi T, Hashimoto T, Ogata M |title=Molecular analysis of human acatalasemia. Identification of a splicing mutation. |journal=J. Mol. Biol. |volume=211 |issue= 2 |pages= 383-93 |year= 1990 |pmid= 2308162 |doi= }}
*{{cite journal | author=Quan F, Korneluk RG, Tropak MB, Gravel RA |title=Isolation and characterization of the human catalase gene. |journal=Nucleic Acids Res. |volume=14 |issue= 13 |pages= 5321-35 |year= 1986 |pmid= 3755525 |doi= }}
*{{cite journal | author=Bell GI, Najarian RC, Mullenbach GT, Hallewell RA |title=cDNA sequence coding for human kidney catalase. |journal=Nucleic Acids Res. |volume=14 |issue= 13 |pages= 5561-2 |year= 1986 |pmid= 3755526 |doi= }}
*{{cite journal | author=Agar NS, Sadrzadeh SM, Hallaway PE, Eaton JW |title=Erythrocyte catalase. A somatic oxidant defense? |journal=J. Clin. Invest. |volume=77 |issue= 1 |pages= 319-21 |year= 1986 |pmid= 3944256 |doi= }}
*{{cite journal | author=Junien C, Turleau C, de Grouchy J, ''et al.'' |title=Regional assignment of catalase (CAT) gene to band 11p13. Association with the aniridia-Wilms' tumor-Gonadoblastoma (WAGR) complex. |journal=Ann. Genet. |volume=23 |issue= 3 |pages= 165-8 |year= 1980 |pmid= 6252821 |doi= }}
*{{cite journal | author=Korneluk RG, Quan F, Lewis WH, ''et al.'' |title=Isolation of human fibroblast catalase cDNA clones. Sequence of clones derived from spliced and unspliced mRNA. |journal=J. Biol. Chem. |volume=259 |issue= 22 |pages= 13819-23 |year= 1984 |pmid= 6548744 |doi= }}
*{{cite journal | author=Yoo JH, Erzurum SC, Hay JG, ''et al.'' |title=Vulnerability of the human airway epithelium to hyperoxia. Constitutive expression of the catalase gene in human bronchial epithelial cells despite oxidant stress. |journal=J. Clin. Invest. |volume=93 |issue= 1 |pages= 297-302 |year= 1994 |pmid= 8282800 |doi= }}
*{{cite journal | author=Erzurum SC, Lemarchand P, Rosenfeld MA, ''et al.'' |title=Protection of human endothelial cells from oxidant injury by adenovirus-mediated transfer of the human catalase cDNA. |journal=Nucleic Acids Res. |volume=21 |issue= 7 |pages= 1607-12 |year= 1993 |pmid= 8479912 |doi= }}
*{{cite journal | author=Baumgartner MR, Verhoeven NM, Jakobs C, ''et al.'' |title=Defective peroxisome biogenesis with a neuromuscular disorder resembling Werdnig-Hoffmann disease. |journal=Neurology |volume=51 |issue= 5 |pages= 1427-32 |year= 1998 |pmid= 9818873 |doi= }}
*{{cite journal | author=Youn YK, Suh GJ, Jung SE, ''et al.'' |title=Recombinant human growth hormone decreases lung and liver tissue lipid peroxidation and increases antioxidant activity after thermal injury in rats. |journal=The Journal of burn care & rehabilitation |volume=19 |issue= 6 |pages= 542-8 |year= 1999 |pmid= 9848047 |doi= }}
*{{cite journal | author=Aksenov MY, Tucker HM, Nair P, ''et al.'' |title=The expression of key oxidative stress-handling genes in different brain regions in Alzheimer's disease. |journal=J. Mol. Neurosci. |volume=11 |issue= 2 |pages= 151-64 |year= 1999 |pmid= 10096042 |doi= }}
*{{cite journal | author=Brown MR, Miller FJ, Li WG, ''et al.'' |title=Overexpression of human catalase inhibits proliferation and promotes apoptosis in vascular smooth muscle cells. |journal=Circ. Res. |volume=85 |issue= 6 |pages= 524-33 |year= 1999 |pmid= 10488055 |doi= }}
*{{cite journal | author=Watters D, Kedar P, Spring K, ''et al.'' |title=Localization of a portion of extranuclear ATM to peroxisomes. |journal=J. Biol. Chem. |volume=274 |issue= 48 |pages= 34277-82 |year= 1999 |pmid= 10567403 |doi= }}
*{{cite journal | author=Putnam CD, Arvai AS, Bourne Y, Tainer JA |title=Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. |journal=J. Mol. Biol. |volume=296 |issue= 1 |pages= 295-309 |year= 2000 |pmid= 10656833 |doi= 10.1006/jmbi.1999.3458 }}
*{{cite journal | author=Ko TP, Safo MK, Musayev FN, ''et al.'' |title=Structure of human erythrocyte catalase. |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=56 |issue= Pt 2 |pages= 241-5 |year= 2000 |pmid= 10666617 |doi= }}
*{{cite journal | author=Fujiwara C, Imamura A, Hashiguchi N, ''et al.'' |title=Catalase-less peroxisomes. Implication in the milder forms of peroxisome biogenesis disorder. |journal=J. Biol. Chem. |volume=275 |issue= 47 |pages= 37271-7 |year= 2001 |pmid= 10960480 |doi= 10.1074/jbc.M006347200 }}
*{{cite journal | author=Jauniaux E, Watson AL, Hempstock J, ''et al.'' |title=Onset of maternal arterial blood flow and placental oxidative stress. A possible factor in human early pregnancy failure. |journal=Am. J. Pathol. |volume=157 |issue= 6 |pages= 2111-22 |year= 2001 |pmid= 11106583 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD86... {November 14, 2007 3:29:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:30:25 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_CD86_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1i85.
| PDB = {{PDB2|1i85}}, {{PDB2|1ncn}}
| Name = CD86 molecule
| HGNCid = 1705
| Symbol = CD86
| AltSymbols =; B7-2; B70; CD28LG2; LAB72; MGC34413
| OMIM = 601020
| ECnumber =
| Homologene = 10443
| MGIid = 101773
| GeneAtlas_image1 = PBB_GE_CD86_205686_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CD86_205685_at_tn.png
| GeneAtlas_image3 = PBB_GE_CD86_210895_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015026 |text = coreceptor activity}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0042110 |text = T cell activation}} {{GNF_GO|id=GO:0043017 |text = positive regulation of lymphotoxin A biosynthetic process}} {{GNF_GO|id=GO:0045086 |text = positive regulation of interleukin-2 biosynthetic process}} {{GNF_GO|id=GO:0045404 |text = positive regulation of interleukin-4 biosynthetic process}} {{GNF_GO|id=GO:0045630 |text = positive regulation of T-helper 2 cell differentiation}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 942
| Hs_Ensembl = ENSG00000114013
| Hs_RefseqProtein = NP_008820
| Hs_RefseqmRNA = NM_006889
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 123256911
| Hs_GenLoc_end = 123322672
| Hs_Uniprot = P42081
| Mm_EntrezGene = 12524
| Mm_Ensembl = ENSMUSG00000022901
| Mm_RefseqmRNA = NM_019388
| Mm_RefseqProtein = NP_062261
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 36523108
| Mm_GenLoc_end = 36585290
| Mm_Uniprot = Q3T9F8
}}
}}
'''CD86 molecule''', also known as '''CD86''', 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 type I membrane protein that is a member of the immunoglobulin superfamily. This protein is expressed by antigen-presenting cells, and it is the ligand for two proteins at the cell surface of T cells, CD28 antigen and cytotoxic T-lymphocyte-associated protein 4. Binding of this protein with CD28 antigen is a costimulatory signal for activation of the T-cell. Binding of this protein with cytotoxic T-lymphocyte-associated protein 4 negatively regulates T-cell activation and diminishes the immune response. Alternative splicing results in two transcript variants encoding different isoforms. Additional transcript variants have been described, but their full-length sequences have not been determined.<ref>{{cite web | title = Entrez Gene: CD86 CD86 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=942| accessdate = }}</ref>
}}
==References==
{{reflist}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CIITA... {November 14, 2007 3:39:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:39:54 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
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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 = Class II, major histocompatibility complex, transactivator
| HGNCid = 7067
| Symbol = CIITA
| AltSymbols =; C2TA; CIITA IV; MHC2TA; NLRA
| OMIM = 600005
| ECnumber =
| Homologene = 207
| MGIid = 108445
| GeneAtlas_image1 = PBB_GE_CIITA_211884_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CIITA_210925_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0030528 |text = transcription regulator activity}} {{GNF_GO|id=GO:0043130 |text = ubiquitin binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0045449 |text = regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4261
| Hs_Ensembl = ENSG00000179583
| Hs_RefseqProtein = NP_000237
| Hs_RefseqmRNA = NM_000246
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 10867648
| Hs_GenLoc_end = 10926340
| Hs_Uniprot = P33076
| Mm_EntrezGene = 12265
| Mm_Ensembl = ENSMUSG00000022504
| Mm_RefseqmRNA = NM_007575
| Mm_RefseqProtein = NP_031601
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 10393637
| Mm_GenLoc_end = 10441141
| Mm_Uniprot = Q3UU40
}}
}}
'''Class II, major histocompatibility complex, transactivator''', also known as '''CIITA''', 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 protein with an acidic transcriptional activation domain, 4 LRRs (leucine-rich repeats) and a GTP binding domain. The protein is located in the nucleus and acts as a positive regulator of class II major histocompatibility complex gene transcription, and is referred to as the "master control factor" for the expression of these genes. The protein also binds GTP and uses GTP binding to facilitate its own transport into the nucleus. Once in the nucleus it does not bind DNA but rather uses an intrinsic acetyltransferase (AT) activity to act in a coactivator-like fashion. Mutations in this gene have been associated with bare lymphocyte syndrome type II (also known as hereditary MHC class II deficiency or HLA class II-deficient combined immunodeficiency), increased susceptibility to rheumatoid arthritis, multiple sclerosis, and possibly myocardial infarction.<ref>{{cite web | title = Entrez Gene: CIITA class II, major histocompatibility complex, transactivator| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4261| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mach B, Steimle V, Martinez-Soria E, Reith W |title=Regulation of MHC class II genes: lessons from a disease. |journal=Annu. Rev. Immunol. |volume=14 |issue= |pages= 301-31 |year= 1996 |pmid= 8717517 |doi= 10.1146/annurev.immunol.14.1.301 }}
*{{cite journal | author=Boss JM |title=Regulation of transcription of MHC class II genes. |journal=Curr. Opin. Immunol. |volume=9 |issue= 1 |pages= 107-13 |year= 1997 |pmid= 9039770 |doi= }}
*{{cite journal | author=LeibundGut-Landmann S, Waldburger JM, Krawczyk M, ''et al.'' |title=Mini-review: Specificity and expression of CIITA, the master regulator of MHC class II genes. |journal=Eur. J. Immunol. |volume=34 |issue= 6 |pages= 1513-25 |year= 2004 |pmid= 15162420 |doi= 10.1002/eji.200424964 }}
*{{cite journal | author=Ting JP, Davis BK |title=CATERPILLER: a novel gene family important in immunity, cell death, and diseases. |journal=Annu. Rev. Immunol. |volume=23 |issue= |pages= 387-414 |year= 2005 |pmid= 15771576 |doi= 10.1146/annurev.immunol.23.021704.115616 }}
*{{cite journal | author=Pöschlová N, Masek K, Krsiak M |title=Effect of 5,6-dihydroxytryptamine on social behaviour in mice [proceedings]. |journal=Act Nerv Super (Praha) |volume=18 |issue= 3 |pages= 229-30 |year= 1977 |pmid= 1007865 |doi= }}
*{{cite journal | author=Pereira SN, Castagna RC, Gressler JF, ''et al.'' |title=[Dura-mater valve bank] |journal=Arq. Bras. Cardiol. |volume=29 |issue= 4 |pages= 277-80 |year= 1977 |pmid= 1008718 |doi= }}
*{{cite journal | author=Riley JL, Westerheide SD, Price JA, ''et al.'' |title=Activation of class II MHC genes requires both the X box region and the class II transactivator (CIITA). |journal=Immunity |volume=2 |issue= 5 |pages= 533-43 |year= 1995 |pmid= 7749984 |doi= }}
*{{cite journal | author=Steimle V, Otten LA, Zufferey M, Mach B |title=Complementation cloning of an MHC class II transactivator mutated in hereditary MHC class II deficiency (or bare lymphocyte syndrome). |journal=Cell |volume=75 |issue= 1 |pages= 135-46 |year= 1993 |pmid= 8402893 |doi= }}
*{{cite journal | author=Brown JA, He XF, Westerheide SD, Boss JM |title=Characterization of the expressed CIITA allele in the class II MHC transcriptional mutant RJ2.2.5. |journal=Immunogenetics |volume=43 |issue= 1-2 |pages= 88-91 |year= 1996 |pmid= 8537130 |doi= }}
*{{cite journal | author=Bontron S, Steimle V, Ucla C, ''et al.'' |title=Two novel mutations in the MHC class II transactivator CIITA in a second patient from MHC class II deficiency complementation group A. |journal=Hum. Genet. |volume=99 |issue= 4 |pages= 541-6 |year= 1997 |pmid= 9099848 |doi= }}
*{{cite journal | author=Mahanta SK, Scholl T, Yang FC, Strominger JL |title=Transactivation by CIITA, the type II bare lymphocyte syndrome-associated factor, requires participation of multiple regions of the TATA box binding protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 12 |pages= 6324-9 |year= 1997 |pmid= 9177216 |doi= }}
*{{cite journal | author=Scholl T, Mahanta SK, Strominger JL |title=Specific complex formation between the type II bare lymphocyte syndrome-associated transactivators CIITA and RFX5. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 12 |pages= 6330-4 |year= 1997 |pmid= 9177217 |doi= }}
*{{cite journal | author=Muhlethaler-Mottet A, Otten LA, Steimle V, Mach B |title=Expression of MHC class II molecules in different cellular and functional compartments is controlled by differential usage of multiple promoters of the transactivator CIITA. |journal=EMBO J. |volume=16 |issue= 10 |pages= 2851-60 |year= 1997 |pmid= 9184229 |doi= 10.1093/emboj/16.10.2851 }}
*{{cite journal | author=Piskurich JF, Wang Y, Linhoff MW, ''et al.'' |title=Identification of distinct regions of 5' flanking DNA that mediate constitutive, IFN-gamma, STAT1, and TGF-beta-regulated expression of the class II transactivator gene. |journal=J. Immunol. |volume=160 |issue= 1 |pages= 233-40 |year= 1998 |pmid= 9551976 |doi= }}
*{{cite journal | author=Harton JA, Cressman DE, Chin KC, ''et al.'' |title=GTP binding by class II transactivator: role in nuclear import. |journal=Science |volume=285 |issue= 5432 |pages= 1402-5 |year= 1999 |pmid= 10464099 |doi= }}
*{{cite journal | author=Quan V, Towey M, Sacks S, Kelly AP |title=Absence of MHC class II gene expression in a patient with a single amino acid substitution in the class II transactivator protein CIITA. |journal=Immunogenetics |volume=49 |issue= 11-12 |pages= 957-63 |year= 1999 |pmid= 10501838 |doi= }}
*{{cite journal | author=Abendroth A, Slobedman B, Lee E, ''et al.'' |title=Modulation of major histocompatibility class II protein expression by varicella-zoster virus. |journal=J. Virol. |volume=74 |issue= 4 |pages= 1900-7 |year= 2000 |pmid= 10644363 |doi= }}
*{{cite journal | author=Kanazawa S, Okamoto T, Peterlin BM |title=Tat competes with CIITA for the binding to P-TEFb and blocks the expression of MHC class II genes in HIV infection. |journal=Immunity |volume=12 |issue= 1 |pages= 61-70 |year= 2000 |pmid= 10661406 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYBA... {November 14, 2007 3:30:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:31:18 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cytochrome b-245, alpha polypeptide
| HGNCid = 2577
| Symbol = CYBA
| AltSymbols =;
| OMIM = 608508
| ECnumber =
| Homologene = 80
| MGIid = 1316658
| GeneAtlas_image1 = PBB_GE_CYBA_203028_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006801 |text = superoxide metabolic process}} {{GNF_GO|id=GO:0006810 |text = transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1535
| Hs_Ensembl = ENSG00000051523
| Hs_RefseqProtein = NP_000092
| Hs_RefseqmRNA = NM_000101
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 87237199
| Hs_GenLoc_end = 87244958
| Hs_Uniprot = P13498
| Mm_EntrezGene = 13057
| Mm_Ensembl = ENSMUSG00000006519
| Mm_RefseqmRNA = NM_007806
| Mm_RefseqProtein = NP_031832
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 125310866
| Mm_GenLoc_end = 125319017
| Mm_Uniprot = Q3TAM0
}}
}}
'''Cytochrome b-245, alpha polypeptide''', also known as '''CYBA''', 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 = Cytochrome b is comprised of a light chain (alpha) and a heavy chain (beta). This gene encodes the light, alpha subunit which has been proposed as a primary component of the microbicidal oxidase system of phagocytes. Mutations in this gene are associated with autosomal recessive chronic granulomatous disease (CGD), that is characterized by the failure of activated phagocytes to generate superoxide, which is important for the microbicidal activity of these cells.<ref>{{cite web | title = Entrez Gene: CYBA cytochrome b-245, alpha polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1535| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Zalba G, San José G, Moreno MU, ''et al.'' |title=NADPH oxidase-mediated oxidative stress: genetic studies of the p22(phox) gene in hypertension. |journal=Antioxid. Redox Signal. |volume=7 |issue= 9-10 |pages= 1327-36 |year= 2006 |pmid= 16115038 |doi= 10.1089/ars.2005.7.1327 }}
*{{cite journal | author=de Boer M, de Klein A, Hossle JP, ''et al.'' |title=Cytochrome b558-negative, autosomal recessive chronic granulomatous disease: two new mutations in the cytochrome b558 light chain of the NADPH oxidase (p22-phox). |journal=Am. J. Hum. Genet. |volume=51 |issue= 5 |pages= 1127-35 |year= 1992 |pmid= 1415254 |doi= }}
*{{cite journal | author=Dinauer MC, Pierce EA, Erickson RW, ''et al.'' |title=Point mutation in the cytoplasmic domain of the neutrophil p22-phox cytochrome b subunit is associated with a nonfunctional NADPH oxidase and chronic granulomatous disease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 24 |pages= 11231-5 |year= 1992 |pmid= 1763037 |doi= }}
*{{cite journal | author=Dinauer MC, Pierce EA, Bruns GA, ''et al.'' |title=Human neutrophil cytochrome b light chain (p22-phox). Gene structure, chromosomal location, and mutations in cytochrome-negative autosomal recessive chronic granulomatous disease. |journal=J. Clin. Invest. |volume=86 |issue= 5 |pages= 1729-37 |year= 1990 |pmid= 2243141 |doi= }}
*{{cite journal | author=Bu-Ghanim HN, Casimir CM, Povey S, Segal AW |title=The alpha subunit of cytochrome b-245 mapped to chromosome 16. |journal=Genomics |volume=8 |issue= 3 |pages= 568-70 |year= 1991 |pmid= 2286377 |doi= }}
*{{cite journal | author=Verhoeven AJ, Bolscher BG, Meerhof LJ, ''et al.'' |title=Characterization of two monoclonal antibodies against cytochrome b558 of human neutrophils. |journal=Blood |volume=73 |issue= 6 |pages= 1686-94 |year= 1989 |pmid= 2469497 |doi= }}
*{{cite journal | author=Parkos CA, Allen RA, Cochrane CG, Jesaitis AJ |title=Purified cytochrome b from human granulocyte plasma membrane is comprised of two polypeptides with relative molecular weights of 91,000 and 22,000. |journal=J. Clin. Invest. |volume=80 |issue= 3 |pages= 732-42 |year= 1987 |pmid= 3305576 |doi= }}
*{{cite journal | author=Parkos CA, Dinauer MC, Walker LE, ''et al.'' |title=Primary structure and unique expression of the 22-kilodalton light chain of human neutrophil cytochrome b. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 10 |pages= 3319-23 |year= 1988 |pmid= 3368442 |doi= }}
*{{cite journal | author=Leto TL, Adams AG, de Mendez I |title=Assembly of the phagocyte NADPH oxidase: binding of Src homology 3 domains to proline-rich targets. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 22 |pages= 10650-4 |year= 1994 |pmid= 7938008 |doi= }}
*{{cite journal | author=Leusen JH, Bolscher BG, Hilarius PM, ''et al.'' |title=156Pro-->Gln substitution in the light chain of cytochrome b558 of the human NADPH oxidase (p22-phox) leads to defective translocation of the cytosolic proteins p47-phox and p67-phox. |journal=J. Exp. Med. |volume=180 |issue= 6 |pages= 2329-34 |year= 1994 |pmid= 7964505 |doi= }}
*{{cite journal | author=Ushio-Fukai M, Zafari AM, Fukui T, ''et al.'' |title=p22phox is a critical component of the superoxide-generating NADH/NADPH oxidase system and regulates angiotensin II-induced hypertrophy in vascular smooth muscle cells. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 23317-21 |year= 1996 |pmid= 8798532 |doi= }}
*{{cite journal | author=Yagisawa M, Yuo A, Yonemaru M, ''et al.'' |title=Superoxide release and NADPH oxidase components in mature human phagocytes: correlation between functional capacity and amount of functional proteins. |journal=Biochem. Biophys. Res. Commun. |volume=228 |issue= 2 |pages= 510-6 |year= 1996 |pmid= 8920944 |doi= 10.1006/bbrc.1996.1691 }}
*{{cite journal | author=Sathyamoorthy M, de Mendez I, Adams AG, Leto TL |title=p40(phox) down-regulates NADPH oxidase activity through interactions with its SH3 domain. |journal=J. Biol. Chem. |volume=272 |issue= 14 |pages= 9141-6 |year= 1997 |pmid= 9083043 |doi= }}
*{{cite journal | author=Rinckel LA, Faris SL, Hitt ND, Kleinberg ME |title=Rac1 disrupts p67phox/p40phox binding: a novel role for Rac in NADPH oxidase activation. |journal=Biochem. Biophys. Res. Commun. |volume=263 |issue= 1 |pages= 118-22 |year= 1999 |pmid= 10486263 |doi= 10.1006/bbrc.1999.1334 }}
*{{cite journal | author=Yamada M, Ariga T, Kawamura N, ''et al.'' |title=Genetic studies of three Japanese patients with p22-phox-deficient chronic granulomatous disease: detection of a possible common mutant CYBA allele in Japan and a genotype-phenotype correlation in these patients. |journal=Br. J. Haematol. |volume=108 |issue= 3 |pages= 511-7 |year= 2000 |pmid= 10759707 |doi= }}
*{{cite journal | author=Grizot S, Grandvaux N, Fieschi F, ''et al.'' |title=Small angle neutron scattering and gel filtration analyses of neutrophil NADPH oxidase cytosolic factors highlight the role of the C-terminal end of p47phox in the association with p40phox. |journal=Biochemistry |volume=40 |issue= 10 |pages= 3127-33 |year= 2001 |pmid= 11258927 |doi= }}
*{{cite journal | author=Dahan I, Issaeva I, Gorzalczany Y, ''et al.'' |title=Mapping of functional domains in the p22(phox) subunit of flavocytochrome b(559) participating in the assembly of the NADPH oxidase complex by "peptide walking". |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8421-32 |year= 2002 |pmid= 11733522 |doi= 10.1074/jbc.M109778200 }}
*{{cite journal | author=Mott J, Rikihisa Y, Tsunawaki S |title=Effects of Anaplasma phagocytophila on NADPH oxidase components in human neutrophils and HL-60 cells. |journal=Infect. Immun. |volume=70 |issue= 3 |pages= 1359-66 |year= 2002 |pmid= 11854221 |doi= }}
*{{cite journal | author=Li JM, Shah AM |title=Intracellular localization and preassembly of the NADPH oxidase complex in cultured endothelial cells. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19952-60 |year= 2002 |pmid= 11893732 |doi= 10.1074/jbc.M110073200 }}
*{{cite journal | author=Pettit AI, Wong RK, Lee V, ''et al.'' |title=Increased free radical production in hypertension due to increased expression of the NADPH oxidase subunit p22(phox) in lymphoblast cell lines. |journal=J. Hypertens. |volume=20 |issue= 4 |pages= 677-83 |year= 2002 |pmid= 11910303 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DAXX... {November 14, 2007 3:31:18 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:32:08 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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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 = Death-associated protein 6
| HGNCid = 2681
| Symbol = DAXX
| AltSymbols =; BING2; DAP6; MGC126245; MGC126246
| OMIM = 603186
| ECnumber =
| Homologene = 1033
| MGIid = 1197015
| GeneAtlas_image1 = PBB_GE_DAXX_201763_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DAXX_216038_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005057 |text = receptor signaling protein activity}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}} {{GNF_GO|id=GO:0031072 |text = heat shock protein binding}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0047485 |text = protein N-terminus binding}} {{GNF_GO|id=GO:0050681 |text = androgen receptor binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016605 |text = PML body}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007257 |text = activation of JNK activity}} {{GNF_GO|id=GO:0008625 |text = induction of apoptosis via death domain receptors}} {{GNF_GO|id=GO:0030521 |text = androgen receptor signaling pathway}} {{GNF_GO|id=GO:0045892 |text = negative regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1616
| Hs_Ensembl = ENSG00000204209
| Hs_RefseqProtein = NP_001341
| Hs_RefseqmRNA = NM_001350
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 33394313
| Hs_GenLoc_end = 33398769
| Hs_Uniprot = Q9UER7
| Mm_EntrezGene = 13163
| Mm_Ensembl = ENSMUSG00000002307
| Mm_RefseqmRNA = XM_993766
| Mm_RefseqProtein = XP_998860
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 33519969
| Mm_GenLoc_end = 33526038
| Mm_Uniprot = A1A558
}}
}}
'''Death-associated protein 6''', also known as '''DAXX''', 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=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=Yang X, Khosravi-Far R, Chang HY, Baltimore D |title=Daxx, a novel Fas-binding protein that activates JNK and apoptosis. |journal=Cell |volume=89 |issue= 7 |pages= 1067-76 |year= 1997 |pmid= 9215629 |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=Kiriakidou M, Driscoll DA, Lopez-Guisa JM, Strauss JF |title=Cloning and expression of primate Daxx cDNAs and mapping of the human gene to chromosome 6p21.3 in the MHC region. |journal=DNA Cell Biol. |volume=16 |issue= 11 |pages= 1289-98 |year= 1998 |pmid= 9407001 |doi= }}
*{{cite journal | author=Herberg JA, Sgouros J, Jones T, ''et al.'' |title=Genomic analysis of the Tapasin gene, located close to the TAP loci in the MHC. |journal=Eur. J. Immunol. |volume=28 |issue= 2 |pages= 459-67 |year= 1998 |pmid= 9521053 |doi= }}
*{{cite journal | author=Herberg JA, Beck S, Trowsdale J |title=TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense cluster at the centromeric end of the MHC. |journal=J. Mol. Biol. |volume=277 |issue= 4 |pages= 839-57 |year= 1998 |pmid= 9545376 |doi= 10.1006/jmbi.1998.1637 }}
*{{cite journal | author=Pluta AF, Earnshaw WC, Goldberg IG |title=Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fas-mediated cell death. |journal=J. Cell. Sci. |volume=111 ( Pt 14) |issue= |pages= 2029-41 |year= 1998 |pmid= 9645950 |doi= }}
*{{cite journal | author=Chang HY, Nishitoh H, Yang X, ''et al.'' |title=Activation of apoptosis signal-regulating kinase 1 (ASK1) by the adapter protein Daxx. |journal=Science |volume=281 |issue= 5384 |pages= 1860-3 |year= 1998 |pmid= 9743501 |doi= }}
*{{cite journal | author=Hollenbach AD, Sublett JE, McPherson CJ, Grosveld G |title=The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx. |journal=EMBO J. |volume=18 |issue= 13 |pages= 3702-11 |year= 1999 |pmid= 10393185 |doi= 10.1093/emboj/18.13.3702 }}
*{{cite journal | author=Michaelson JS, Bader D, Kuo F, ''et al.'' |title=Loss of Daxx, a promiscuously interacting protein, results in extensive apoptosis in early mouse development. |journal=Genes Dev. |volume=13 |issue= 15 |pages= 1918-23 |year= 1999 |pmid= 10444590 |doi= }}
*{{cite journal | author=Ishov AM, Sotnikov AG, Negorev D, ''et al.'' |title=PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1. |journal=J. Cell Biol. |volume=147 |issue= 2 |pages= 221-34 |year= 1999 |pmid= 10525530 |doi= }}
*{{cite journal | author=Li H, Leo C, Zhu J, ''et al.'' |title=Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. |journal=Mol. Cell. Biol. |volume=20 |issue= 5 |pages= 1784-96 |year= 2000 |pmid= 10669754 |doi= }}
*{{cite journal | author=Zhong S, Salomoni P, Ronchetti S, ''et al.'' |title=Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis. |journal=J. Exp. Med. |volume=191 |issue= 4 |pages= 631-40 |year= 2000 |pmid= 10684855 |doi= }}
*{{cite journal | author=Li R, Pei H, Watson DK, Papas TS |title=EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes. |journal=Oncogene |volume=19 |issue= 6 |pages= 745-53 |year= 2000 |pmid= 10698492 |doi= 10.1038/sj.onc.1203385 }}
*{{cite journal | author=Charette SJ, Lavoie JN, Lambert H, Landry J |title=Inhibition of Daxx-mediated apoptosis by heat shock protein 27. |journal=Mol. Cell. Biol. |volume=20 |issue= 20 |pages= 7602-12 |year= 2000 |pmid= 11003656 |doi= }}
*{{cite journal | author=Rochat-Steiner V, Becker K, Micheau O, ''et al.'' |title=FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits fas-mediated Jun NH(2)-terminal kinase activation. |journal=J. Exp. Med. |volume=192 |issue= 8 |pages= 1165-74 |year= 2000 |pmid= 11034606 |doi= }}
*{{cite journal | author=Ryu SW, Chae SK, Kim E |title=Interaction of Daxx, a Fas binding protein, with sentrin and Ubc9. |journal=Biochem. Biophys. Res. Commun. |volume=279 |issue= 1 |pages= 6-10 |year= 2001 |pmid= 11112409 |doi= 10.1006/bbrc.2000.3882 }}
*{{cite journal | author=Charette SJ, Landry J |title=The interaction of HSP27 with Daxx identifies a potential regulatory role of HSP27 in Fas-induced apoptosis. |journal=Ann. N. Y. Acad. Sci. |volume=926 |issue= |pages= 126-31 |year= 2001 |pmid= 11193028 |doi= }}
*{{cite journal | author=Lehembre F, Müller S, Pandolfi PP, Dejean A |title=Regulation of Pax3 transcriptional activity by SUMO-1-modified PML. |journal=Oncogene |volume=20 |issue= 1 |pages= 1-9 |year= 2001 |pmid= 11244500 |doi= 10.1038/sj.onc.1204063 }}
*{{cite journal | author=Perlman R, Schiemann WP, Brooks MW, ''et al.'' |title=TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation. |journal=Nat. Cell Biol. |volume=3 |issue= 8 |pages= 708-14 |year= 2001 |pmid= 11483955 |doi= 10.1038/35087019 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EDNRB... {November 14, 2007 3:32:49 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:33:34 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
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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 = Endothelin receptor type B
| HGNCid = 3180
| Symbol = EDNRB
| AltSymbols =; ABCDS; ETB; ETRB; HSCR; HSCR2
| OMIM = 131244
| ECnumber =
| Homologene = 89
| MGIid = 102720
| GeneAtlas_image1 = PBB_GE_EDNRB_204271_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_EDNRB_204273_at_tn.png
| GeneAtlas_image3 = PBB_GE_EDNRB_206701_x_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0001600 |text = endothelin-B receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0001755 |text = neural crest cell migration}} {{GNF_GO|id=GO:0006885 |text = regulation of pH}} {{GNF_GO|id=GO:0007194 |text = negative regulation of adenylate cyclase activity}} {{GNF_GO|id=GO:0007200 |text = G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)}} {{GNF_GO|id=GO:0007422 |text = peripheral nervous system development}} {{GNF_GO|id=GO:0007497 |text = posterior midgut development}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0008217 |text = blood pressure regulation}} {{GNF_GO|id=GO:0030318 |text = melanocyte differentiation}} {{GNF_GO|id=GO:0048066 |text = pigmentation during development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1910
| Hs_Ensembl = ENSG00000136160
| Hs_RefseqProtein = NP_000106
| Hs_RefseqmRNA = NM_000115
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 77367617
| Hs_GenLoc_end = 77391904
| Hs_Uniprot = P24530
| Mm_EntrezGene = 13618
| Mm_Ensembl = ENSMUSG00000022122
| Mm_RefseqmRNA = NM_007904
| Mm_RefseqProtein = NP_031930
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 102700304
| Mm_GenLoc_end = 102729852
| Mm_Uniprot = Q8K1V9
}}
}}
'''Endothelin receptor type B''', also known as '''EDNRB''', 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 = Endothelin receptor type B is a G protein-coupled receptor which activates a phosphatidylinoitol-calcium second messenger system. Its ligand, endothelin, consists of a family of three potent vasoactive peptides: ET1, ET2, and ET3. Studies suggest that the multigenic disorder, Hirschsprung disease type 2, is due to mutation in endothelin receptor type B gene. A splice variant, named SVR, has been described; the sequence of the ETB-SVR receptor is identical to ETRB except for the intracellular C-terminal domain. While both splice variants bind ET1, they exhibit different responses upon binding which suggests that they may be functionally distinct.<ref>{{cite web | title = Entrez Gene: EDNRB endothelin receptor type B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1910| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hofstra RM, Osinga J, Buys CH |title=Mutations in Hirschsprung disease: when does a mutation contribute to the phenotype. |journal=Eur. J. Hum. Genet. |volume=5 |issue= 4 |pages= 180-5 |year= 1998 |pmid= 9359036 |doi= }}
*{{cite journal | author=Haendler B, Hechler U, Schleuning WD |title=Molecular cloning of human endothelin (ET) receptors ETA and ETB. |journal=J. Cardiovasc. Pharmacol. |volume=20 Suppl 12 |issue= |pages= S1-4 |year= 1993 |pmid= 1282938 |doi= }}
*{{cite journal | author=Arai H, Nakao K, Hosoda K, ''et al.'' |title=[Molecular cloning of human endothelin receptors and their expression in vascular endothelial cells and smooth muscle cells] |journal=Jpn. Circ. J. |volume=56 Suppl 5 |issue= |pages= 1303-7 |year= 1993 |pmid= 1291713 |doi= }}
*{{cite journal | author=Ogawa Y, Nakao K, Arai H, ''et al.'' |title=Molecular cloning of a non-isopeptide-selective human endothelin receptor. |journal=Biochem. Biophys. Res. Commun. |volume=178 |issue= 1 |pages= 248-55 |year= 1991 |pmid= 1648908 |doi= }}
*{{cite journal | author=Cyr C, Huebner K, Druck T, Kris R |title=Cloning and chromosomal localization of a human endothelin ETA receptor. |journal=Biochem. Biophys. Res. Commun. |volume=181 |issue= 1 |pages= 184-90 |year= 1992 |pmid= 1659806 |doi= }}
*{{cite journal | author=Nakamuta M, Takayanagi R, Sakai Y, ''et al.'' |title=Cloning and sequence analysis of a cDNA encoding human non-selective type of endothelin receptor. |journal=Biochem. Biophys. Res. Commun. |volume=177 |issue= 1 |pages= 34-9 |year= 1991 |pmid= 1710450 |doi= }}
*{{cite journal | author=Sakamoto A, Yanagisawa M, Sakurai T, ''et al.'' |title=Cloning and functional expression of human cDNA for the ETB endothelin receptor. |journal=Biochem. Biophys. Res. Commun. |volume=178 |issue= 2 |pages= 656-63 |year= 1991 |pmid= 1713452 |doi= }}
*{{cite journal | author=Vane J |title=Endothelins come home to roost. |journal=Nature |volume=348 |issue= 6303 |pages= 673 |year= 1991 |pmid= 2175394 |doi= 10.1038/348673a0 }}
*{{cite journal | author=Puffenberger EG, Kauffman ER, Bolk S, ''et al.'' |title=Identity-by-descent and association mapping of a recessive gene for Hirschsprung disease on human chromosome 13q22. |journal=Hum. Mol. Genet. |volume=3 |issue= 8 |pages= 1217-25 |year= 1995 |pmid= 7987295 |doi= }}
*{{cite journal | author=Puffenberger EG, Hosoda K, Washington SS, ''et al.'' |title=A missense mutation of the endothelin-B receptor gene in multigenic Hirschsprung's disease. |journal=Cell |volume=79 |issue= 7 |pages= 1257-66 |year= 1995 |pmid= 8001158 |doi= }}
*{{cite journal | author=Baynash AG, Hosoda K, Giaid A, ''et al.'' |title=Interaction of endothelin-3 with endothelin-B receptor is essential for development of epidermal melanocytes and enteric neurons. |journal=Cell |volume=79 |issue= 7 |pages= 1277-85 |year= 1995 |pmid= 8001160 |doi= }}
*{{cite journal | author=Arai H, Nakao K, Takaya K, ''et al.'' |title=The human endothelin-B receptor gene. Structural organization and chromosomal assignment. |journal=J. Biol. Chem. |volume=268 |issue= 5 |pages= 3463-70 |year= 1993 |pmid= 8429023 |doi= }}
*{{cite journal | author=Elshourbagy NA, Korman DR, Wu HL, ''et al.'' |title=Molecular characterization and regulation of the human endothelin receptors. |journal=J. Biol. Chem. |volume=268 |issue= 6 |pages= 3873-9 |year= 1993 |pmid= 8440682 |doi= }}
*{{cite journal | author=Hofstra RM, Osinga J, Tan-Sindhunata G, ''et al.'' |title=A homozygous mutation in the endothelin-3 gene associated with a combined Waardenburg type 2 and Hirschsprung phenotype (Shah-Waardenburg syndrome). |journal=Nat. Genet. |volume=12 |issue= 4 |pages= 445-7 |year= 1996 |pmid= 8630503 |doi= 10.1038/ng0496-445 }}
*{{cite journal | author=Attié T, Till M, Pelet A, ''et al.'' |title=Mutation of the endothelin-receptor B gene in Waardenburg-Hirschsprung disease. |journal=Hum. Mol. Genet. |volume=4 |issue= 12 |pages= 2407-9 |year= 1996 |pmid= 8634719 |doi= }}
*{{cite journal | author=Elshourbagy NA, Adamou JE, Gagnon AW, ''et al.'' |title=Molecular characterization of a novel human endothelin receptor splice variant. |journal=J. Biol. Chem. |volume=271 |issue= 41 |pages= 25300-7 |year= 1996 |pmid= 8810293 |doi= }}
*{{cite journal | author=Kusafuka T, Wang Y, Puri P |title=Novel mutations of the endothelin-B receptor gene in isolated patients with Hirschsprung's disease. |journal=Hum. Mol. Genet. |volume=5 |issue= 3 |pages= 347-9 |year= 1997 |pmid= 8852658 |doi= }}
*{{cite journal | author=Auricchio A, Casari G, Staiano A, Ballabio A |title=Endothelin-B receptor mutations in patients with isolated Hirschsprung disease from a non-inbred population. |journal=Hum. Mol. Genet. |volume=5 |issue= 3 |pages= 351-4 |year= 1997 |pmid= 8852659 |doi= }}
*{{cite journal | author=Amiel J, Attié T, Jan D, ''et al.'' |title=Heterozygous endothelin receptor B (EDNRB) mutations in isolated Hirschsprung disease. |journal=Hum. Mol. Genet. |volume=5 |issue= 3 |pages= 355-7 |year= 1997 |pmid= 8852660 |doi= }}
*{{cite journal | author=Freedman NJ, Ament AS, Oppermann M, ''et al.'' |title=Phosphorylation and desensitization of human endothelin A and B receptors. Evidence for G protein-coupled receptor kinase specificity. |journal=J. Biol. Chem. |volume=272 |issue= 28 |pages= 17734-43 |year= 1997 |pmid= 9211925 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EPHB2... {November 14, 2007 3:33:34 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:34:27 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_EPHB2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b4f.
| PDB = {{PDB2|1b4f}}, {{PDB2|1f0m}}, {{PDB2|1jpa}}, {{PDB2|1kgy}}, {{PDB2|1nuk}}, {{PDB2|1sgg}}, {{PDB2|1shw}}, {{PDB2|2hen}}
| Name = EPH receptor B2
| HGNCid = 3393
| Symbol = EPHB2
| AltSymbols =; CAPB; DRT; EPHT3; ERK; Hek5; MGC87492; PCBC; Tyro5
| OMIM = 600997
| ECnumber =
| Homologene = 37925
| MGIid = 99611
| GeneAtlas_image1 = PBB_GE_EPHB2_209588_at_tn.png
| GeneAtlas_image2 = PBB_GE_EPHB2_209589_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_EPHB2_210651_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005003 |text = ephrin receptor activity}} {{GNF_GO|id=GO:0005005 |text = transmembrane-ephrin receptor activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008046 |text = axon guidance receptor activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0045202 |text = synapse}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007411 |text = axon guidance}} {{GNF_GO|id=GO:0007612 |text = learning}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0048168 |text = regulation of neuronal synaptic plasticity}} {{GNF_GO|id=GO:0048170 |text = positive regulation of long-term neuronal synaptic plasticity}} {{GNF_GO|id=GO:0050770 |text = regulation of axonogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2048
| Hs_Ensembl = ENSG00000133216
| Hs_RefseqProtein = NP_004433
| Hs_RefseqmRNA = NM_004442
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 22910045
| Hs_GenLoc_end = 23114405
| Hs_Uniprot = P29323
| Mm_EntrezGene = 13844
| Mm_Ensembl = ENSMUSG00000028664
| Mm_RefseqmRNA = NM_010142
| Mm_RefseqProtein = NP_034272
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 135925688
| Mm_GenLoc_end = 136108032
| Mm_Uniprot = Q6GTQ7
}}
}}
'''EPH receptor B2''', also known as '''EPHB2''', 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 = Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by this gene is a receptor for ephrin-B family members.<ref>{{cite web | title = Entrez Gene: EPHB2 EPH receptor B2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2048| accessdate = }}</ref>
}}
==References==
{{reflist}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GFAP... {November 14, 2007 3:35:19 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:35:55 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
}}
<!-- 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 = Glial fibrillary acidic protein
| HGNCid = 4235
| Symbol = GFAP
| AltSymbols =; FLJ45472
| OMIM = 137780
| ECnumber =
| Homologene = 1554
| MGIid = 95697
| GeneAtlas_image1 = PBB_GE_GFAP_203540_at_tn.png
| Function = {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005882 |text = intermediate filament}}
| Process = {{GNF_GO|id=GO:0045103 |text = intermediate filament-based process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2670
| Hs_Ensembl = ENSG00000131095
| Hs_RefseqProtein = NP_002046
| Hs_RefseqmRNA = NM_002055
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 40338521
| Hs_GenLoc_end = 40348388
| Hs_Uniprot = P14136
| Mm_EntrezGene = 14580
| Mm_Ensembl = ENSMUSG00000020932
| Mm_RefseqmRNA = NM_010277
| Mm_RefseqProtein = NP_034407
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 102703437
| Mm_GenLoc_end = 102713221
| Mm_Uniprot = A0MTM0
}}
}}
'''Glial fibrillary acidic protein''', also known as '''GFAP''', 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 one of the major intermediate filament proteins of mature astrocytes. It is used as a marker to distinguish astrocytes from other glial cells during development. Mutations in this gene cause Alexander disease, a rare disorder of astrocytes in the central nervous system. An additional transcript variant has been described, but its full length sequence has not been determined.<ref>{{cite web | title = Entrez Gene: GFAP glial fibrillary acidic protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2670| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Garbuglia M, Verzini M, Sorci G, ''et al.'' |title=The calcium-modulated proteins, S100A1 and S100B, as potential regulators of the dynamics of type III intermediate filaments. |journal=Braz. J. Med. Biol. Res. |volume=32 |issue= 10 |pages= 1177-85 |year= 2000 |pmid= 10510252 |doi= }}
*{{cite journal | author=Quaranta MG, Mattioli B, Giordani L, Viora M |title=The immunoregulatory effects of HIV-1 Nef on dendritic cells and the pathogenesis of AIDS. |journal=FASEB J. |volume=20 |issue= 13 |pages= 2198-208 |year= 2006 |pmid= 17077296 |doi= 10.1096/fj.06-6260rev }}
*{{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=Kumanishi T, Usui H, Ichikawa T, ''et al.'' |title=Human glial fibrillary acidic protein (GFAP): molecular cloning of the complete cDNA sequence and chromosomal localization (chromosome 17) of the GFAP gene. |journal=Acta Neuropathol. |volume=83 |issue= 6 |pages= 569-78 |year= 1992 |pmid= 1636374 |doi= }}
*{{cite journal | author=Bongcam-Rudloff E, Nistér M, Betsholtz C, ''et al.'' |title=Human glial fibrillary acidic protein: complementary DNA cloning, chromosome localization, and messenger RNA expression in human glioma cell lines of various phenotypes. |journal=Cancer Res. |volume=51 |issue= 5 |pages= 1553-60 |year= 1991 |pmid= 1847665 |doi= }}
*{{cite journal | author=Besnard F, Brenner M, Nakatani Y, ''et al.'' |title=Multiple interacting sites regulate astrocyte-specific transcription of the human gene for glial fibrillary acidic protein. |journal=J. Biol. Chem. |volume=266 |issue= 28 |pages= 18877-83 |year= 1991 |pmid= 1918004 |doi= }}
*{{cite journal | author=Tokui T, Yamauchi T, Yano T, ''et al.'' |title=Ca2(+)-calmodulin-dependent protein kinase II phosphorylates various types of non-epithelial intermediate filament proteins. |journal=Biochem. Biophys. Res. Commun. |volume=169 |issue= 3 |pages= 896-904 |year= 1990 |pmid= 2114109 |doi= }}
*{{cite journal | author=Inagaki M, Gonda Y, Nishizawa K, ''et al.'' |title=Phosphorylation sites linked to glial filament disassembly in vitro locate in a non-alpha-helical head domain. |journal=J. Biol. Chem. |volume=265 |issue= 8 |pages= 4722-9 |year= 1990 |pmid= 2155236 |doi= }}
*{{cite journal | author=Brenner M, Lampel K, Nakatani Y, ''et al.'' |title=Characterization of human cDNA and genomic clones for glial fibrillary acidic protein. |journal=Brain Res. Mol. Brain Res. |volume=7 |issue= 4 |pages= 277-86 |year= 1990 |pmid= 2163003 |doi= }}
*{{cite journal | author=Shoeman RL, Höner B, Stoller TJ, ''et al.'' |title=Human immunodeficiency virus type 1 protease cleaves the intermediate filament proteins vimentin, desmin, and glial fibrillary acidic protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 16 |pages= 6336-40 |year= 1990 |pmid= 2201025 |doi= }}
*{{cite journal | author=Nakatani Y, Brenner M, Freese E |title=An RNA polymerase II promoter containing sequences upstream and downstream from the RNA startpoint that direct initiation of transcription from the same site. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 11 |pages= 4289-93 |year= 1990 |pmid= 2349237 |doi= }}
*{{cite journal | author=Reeves SA, Helman LJ, Allison A, Israel MA |title=Molecular cloning and primary structure of human glial fibrillary acidic protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 13 |pages= 5178-82 |year= 1989 |pmid= 2740350 |doi= }}
*{{cite journal | author=Duguid JR, Bohmont CW, Liu NG, Tourtellotte WW |title=Changes in brain gene expression shared by scrapie and Alzheimer disease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 18 |pages= 7260-4 |year= 1989 |pmid= 2780570 |doi= }}
*{{cite journal | author=Tsujimura K, Tanaka J, Ando S, ''et al.'' |title=Identification of phosphorylation sites on glial fibrillary acidic protein for cdc2 kinase and Ca(2+)-calmodulin-dependent protein kinase II. |journal=J. Biochem. |volume=116 |issue= 2 |pages= 426-34 |year= 1995 |pmid= 7822264 |doi= }}
*{{cite journal | author=Bernardo A, Patrizio M, Levi G, Petrucci TC |title=Human immunodeficiency virus protein gp120 interferes with beta-adrenergic receptor-mediated protein phosphorylation in cultured rat cortical astrocytes. |journal=Cell. Mol. Neurobiol. |volume=14 |issue= 2 |pages= 159-73 |year= 1995 |pmid= 7842474 |doi= }}
*{{cite journal | author=Hatch N, Sarid J |title=Glial fibrillary acidic protein transcriptional regulation is independent of a TFIID-binding downstream initiator sequence. |journal=J. Neurochem. |volume=63 |issue= 6 |pages= 2003-9 |year= 1994 |pmid= 7964717 |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=Pulliam L, West D, Haigwood N, Swanson RA |title=HIV-1 envelope gp120 alters astrocytes in human brain cultures. |journal=AIDS Res. Hum. Retroviruses |volume=9 |issue= 5 |pages= 439-44 |year= 1993 |pmid= 8318270 |doi= }}
*{{cite journal | author=Levi G, Patrizio M, Bernardo A, ''et al.'' |title=Human immunodeficiency virus coat protein gp120 inhibits the beta-adrenergic regulation of astroglial and microglial functions. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 4 |pages= 1541-5 |year= 1993 |pmid= 8381971 |doi= }}
*{{cite journal | author=Kosako H, Amano M, Yanagida M, ''et al.'' |title=Phosphorylation of glial fibrillary acidic protein at the same sites by cleavage furrow kinase and Rho-associated kinase. |journal=J. Biol. Chem. |volume=272 |issue= 16 |pages= 10333-6 |year= 1997 |pmid= 9099667 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GLA... {November 14, 2007 3:35:55 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:36:24 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 = PBB_Protein_GLA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1r46.
| PDB = {{PDB2|1r46}}, {{PDB2|1r47}}
| Name = Galactosidase, alpha
| HGNCid = 4296
| Symbol = GLA
| AltSymbols =; GALA
| OMIM = 301500
| ECnumber =
| Homologene = 55441
| MGIid = 1347344
| GeneAtlas_image1 = PBB_GE_GLA_214430_at_tn.png
| Function = {{GNF_GO|id=GO:0004553 |text = hydrolase activity, hydrolyzing O-glycosyl compounds}} {{GNF_GO|id=GO:0004557 |text = alpha-galactosidase activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0043169 |text = cation binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}}
| Process = {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0009311 |text = oligosaccharide metabolic process}} {{GNF_GO|id=GO:0045019 |text = negative regulation of nitric oxide biosynthetic process}} {{GNF_GO|id=GO:0046479 |text = glycosphingolipid catabolic process}} {{GNF_GO|id=GO:0051001 |text = negative regulation of nitric-oxide synthase activity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2717
| Hs_Ensembl = ENSG00000102393
| Hs_RefseqProtein = NP_000160
| Hs_RefseqmRNA = NM_000169
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 100539453
| Hs_GenLoc_end = 100549607
| Hs_Uniprot = P06280
| Mm_EntrezGene = 11605
| Mm_Ensembl = ENSMUSG00000031266
| Mm_RefseqmRNA = NM_013463
| Mm_RefseqProtein = NP_038491
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 129934521
| Mm_GenLoc_end = 129947287
| Mm_Uniprot = Q3TLY5
}}
}}
'''Galactosidase, alpha''', also known as '''GLA''', 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 homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. This enzyme predominantly hydrolyzes ceramide trihexoside, and it can catalyze the hydrolysis of melibiose into galactose and glucose. A variety of mutations in this gene affect the synthesis, processing, and stability of this enzyme, which causes Fabry disease, a rare lysosomal storage disorder that results from a failure to catabolize alpha-D-galactosyl glycolipid moieties.<ref>{{cite web | title = Entrez Gene: GLA galactosidase, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2717| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Eng CM, Desnick RJ |title=Molecular basis of Fabry disease: mutations and polymorphisms in the human alpha-galactosidase A gene. |journal=Hum. Mutat. |volume=3 |issue= 2 |pages= 103-11 |year= 1994 |pmid= 7911050 |doi= 10.1002/humu.1380030204 }}
*{{cite journal | author=Caillaud C, Poenaru L |title=[Gaucher's and Fabry's diseases: biochemical and genetic aspects] |journal=J. Soc. Biol. |volume=196 |issue= 2 |pages= 135-40 |year= 2002 |pmid= 12360742 |doi= }}
*{{cite journal | author=Germain DP |title=[Fabry's disease (alpha-galactosidase-A deficiency): physiopathology, clinical signs, and genetic aspects] |journal=J. Soc. Biol. |volume=196 |issue= 2 |pages= 161-73 |year= 2002 |pmid= 12360745 |doi= }}
*{{cite journal | author=Schaefer E, Mehta A, Gal A |title=Genotype and phenotype in Fabry disease: analysis of the Fabry Outcome Survey. |journal=Acta paediatrica (Oslo, Norway : 1992). Supplement |volume=94 |issue= 447 |pages= 87-92; discussion 79 |year= 2005 |pmid= 15895718 |doi= }}
*{{cite journal | author=Levin M |title=Fabry disease. |journal=Drugs Today |volume=42 |issue= 1 |pages= 65-70 |year= 2006 |pmid= 16511611 |doi= 10.1358/dot.2006.42.1.957357 }}
*{{cite journal | author=Lidove O, Joly D, Barbey F, ''et al.'' |title=Clinical results of enzyme replacement therapy in Fabry disease: a comprehensive review of literature. |journal=Int. J. Clin. Pract. |volume=61 |issue= 2 |pages= 293-302 |year= 2007 |pmid= 17263716 |doi= 10.1111/j.1742-1241.2006.01237.x }}
*{{cite journal | author=Dean KJ, Sweeley CC |title=Studies on human liver alpha-galactosidases. I. Purification of alpha-galactosidase A and its enzymatic properties with glycolipid and oligosaccharide substrates. |journal=J. Biol. Chem. |volume=254 |issue= 20 |pages= 9994-10000 |year= 1979 |pmid= 39940 |doi= }}
*{{cite journal | author=Ishii S, Sakuraba H, Suzuki Y |title=Point mutations in the upstream region of the alpha-galactosidase A gene exon 6 in an atypical variant of Fabry disease. |journal=Hum. Genet. |volume=89 |issue= 1 |pages= 29-32 |year= 1992 |pmid= 1315715 |doi= }}
*{{cite journal | author=Ioannou YA, Bishop DF, Desnick RJ |title=Overexpression of human alpha-galactosidase A results in its intracellular aggregation, crystallization in lysosomes, and selective secretion. |journal=J. Cell Biol. |volume=119 |issue= 5 |pages= 1137-50 |year= 1992 |pmid= 1332979 |doi= }}
*{{cite journal | author=von Scheidt W, Eng CM, Fitzmaurice TF, ''et al.'' |title=An atypical variant of Fabry's disease with manifestations confined to the myocardium. |journal=N. Engl. J. Med. |volume=324 |issue= 6 |pages= 395-9 |year= 1991 |pmid= 1846223 |doi= }}
*{{cite journal | author=Koide T, Ishiura M, Iwai K, ''et al.'' |title=A case of Fabry's disease in a patient with no alpha-galactosidase A activity caused by a single amino acid substitution of Pro-40 by Ser. |journal=FEBS Lett. |volume=259 |issue= 2 |pages= 353-6 |year= 1990 |pmid= 2152885 |doi= }}
*{{cite journal | author=Kornreich R, Bishop DF, Desnick RJ |title=Alpha-galactosidase A gene rearrangements causing Fabry disease. Identification of short direct repeats at breakpoints in an Alu-rich gene. |journal=J. Biol. Chem. |volume=265 |issue= 16 |pages= 9319-26 |year= 1990 |pmid= 2160973 |doi= }}
*{{cite journal | author=Sakuraba H, Oshima A, Fukuhara Y, ''et al.'' |title=Identification of point mutations in the alpha-galactosidase A gene in classical and atypical hemizygotes with Fabry disease. |journal=Am. J. Hum. Genet. |volume=47 |issue= 5 |pages= 784-9 |year= 1990 |pmid= 2171331 |doi= }}
*{{cite journal | author=Bernstein HS, Bishop DF, Astrin KH, ''et al.'' |title=Fabry disease: six gene rearrangements and an exonic point mutation in the alpha-galactosidase gene. |journal=J. Clin. Invest. |volume=83 |issue= 4 |pages= 1390-9 |year= 1989 |pmid= 2539398 |doi= }}
*{{cite journal | author=Kornreich R, Desnick RJ, Bishop DF |title=Nucleotide sequence of the human alpha-galactosidase A gene. |journal=Nucleic Acids Res. |volume=17 |issue= 8 |pages= 3301-2 |year= 1989 |pmid= 2542896 |doi= }}
*{{cite journal | author=Bishop DF, Kornreich R, Desnick RJ |title=Structural organization of the human alpha-galactosidase A gene: further evidence for the absence of a 3' untranslated region. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 11 |pages= 3903-7 |year= 1988 |pmid= 2836863 |doi= }}
*{{cite journal | author=Quinn M, Hantzopoulos P, Fidanza V, Calhoun DH |title=A genomic clone containing the promoter for the gene encoding the human lysosomal enzyme, alpha-galactosidase A. |journal=Gene |volume=58 |issue= 2-3 |pages= 177-88 |year= 1988 |pmid= 2892762 |doi= }}
*{{cite journal | author=Bishop DF, Calhoun DH, Bernstein HS, ''et al.'' |title=Human alpha-galactosidase A: nucleotide sequence of a cDNA clone encoding the mature enzyme. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 13 |pages= 4859-63 |year= 1986 |pmid= 3014515 |doi= }}
*{{cite journal | author=Lemansky P, Bishop DF, Desnick RJ, ''et al.'' |title=Synthesis and processing of alpha-galactosidase A in human fibroblasts. Evidence for different mutations in Fabry disease. |journal=J. Biol. Chem. |volume=262 |issue= 5 |pages= 2062-5 |year= 1987 |pmid= 3029062 |doi= }}
*{{cite journal | author=Tsuji S, Martin BM, Kaslow DC, ''et al.'' |title=Signal sequence and DNA-mediated expression of human lysosomal alpha-galactosidase A. |journal=Eur. J. Biochem. |volume=165 |issue= 2 |pages= 275-80 |year= 1987 |pmid= 3036505 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HMGA1... {November 14, 2007 3:36:24 PM PST}
- SEARCH REDIRECT: Control Box Found: HMGA1 {November 14, 2007 3:37:05 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 3:37:08 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 3:37:08 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 3:37:08 PM PST}
- UPDATED: Updated protein page: HMGA1 {November 14, 2007 3:37:16 PM PST}
- INFO: Beginning work on HNRPA1... {November 14, 2007 3:37:16 PM PST}
- SEARCH REDIRECT: Control Box Found: HNRPA1 {November 14, 2007 3:37:49 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 3:37:50 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 3:37:50 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 3:37:50 PM PST}
- UPDATED: Updated protein page: HNRPA1 {November 14, 2007 3:37:56 PM PST}
- INFO: Beginning work on HSF1... {November 14, 2007 3:37:56 PM PST}
- SEARCH REDIRECT: Control Box Found: HSF1 {November 14, 2007 3:38:23 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 3:38:26 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 3:38:26 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 3:38:26 PM PST}
- UPDATED: Updated protein page: HSF1 {November 14, 2007 3:38:32 PM PST}
- INFO: Beginning work on ID1... {November 14, 2007 3:38:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:39:16 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Inhibitor of DNA binding 1, dominant negative helix-loop-helix protein
| HGNCid = 5360
| Symbol = ID1
| AltSymbols =; ID
| OMIM = 600349
| ECnumber =
| Homologene = 1631
| MGIid = 96396
| GeneAtlas_image1 = PBB_GE_ID1_208937_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0030509 |text = BMP signaling pathway}} {{GNF_GO|id=GO:0043433 |text = negative regulation of transcription factor activity}} {{GNF_GO|id=GO:0045765 |text = regulation of angiogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3397
| Hs_Ensembl = ENSG00000125968
| Hs_RefseqProtein = NP_002156
| Hs_RefseqmRNA = NM_002165
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 29656747
| Hs_GenLoc_end = 29657979
| Hs_Uniprot = P41134
| Mm_EntrezGene = 15901
| Mm_Ensembl = ENSMUSG00000042745
| Mm_RefseqmRNA = NM_010495
| Mm_RefseqProtein = NP_034625
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 152427715
| Mm_GenLoc_end = 152428851
| Mm_Uniprot = Q6GTZ3
}}
}}
'''Inhibitor of DNA binding 1, dominant negative helix-loop-helix protein''', also known as '''ID1''', 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 helix-loop-helix (HLH) protein that can form heterodimers with members of the basic HLH family of transcription factors. The encoded protein has no DNA binding activity and therefore can inhibit the DNA binding and transcriptional activation ability of basic HLH proteins with which it interacts. This protein may play a role in cell growth, senescence, and differentiation. Two transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: ID1 inhibitor of DNA binding 1, dominant negative helix-loop-helix protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3397| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Zhu W, Dahmen J, Bulfone A, ''et al.'' |title=Id gene expression during development and molecular cloning of the human Id-1 gene. |journal=Brain Res. Mol. Brain Res. |volume=30 |issue= 2 |pages= 312-26 |year= 1995 |pmid= 7637581 |doi= }}
*{{cite journal | author=Deed RW, Jasiok M, Norton JD |title=Nucleotide sequence of the cDNA encoding human helix-loop-helix Id-1 protein: identification of functionally conserved residues common to Id proteins. |journal=Biochim. Biophys. Acta |volume=1219 |issue= 1 |pages= 160-2 |year= 1994 |pmid= 8086456 |doi= }}
*{{cite journal | author=Hara E, Yamaguchi T, Nojima H, ''et al.'' |title=Id-related genes encoding helix-loop-helix proteins are required for G1 progression and are repressed in senescent human fibroblasts. |journal=J. Biol. Chem. |volume=269 |issue= 3 |pages= 2139-45 |year= 1994 |pmid= 8294468 |doi= }}
*{{cite journal | author=Mathew S, Chen W, Murty VV, ''et al.'' |title=Chromosomal assignment of human ID1 and ID2 genes. |journal=Genomics |volume=30 |issue= 2 |pages= 385-7 |year= 1996 |pmid= 8586447 |doi= 10.1006/geno.1995.0037 }}
*{{cite journal | author=Nehlin JO, Hara E, Kuo WL, ''et al.'' |title=Genomic organization, sequence, and chromosomal localization of the human helix-loop-helix Id1 gene. |journal=Biochem. Biophys. Res. Commun. |volume=231 |issue= 3 |pages= 628-34 |year= 1997 |pmid= 9070860 |doi= 10.1006/bbrc.1997.6152 }}
*{{cite journal | author=Anand G, Yin X, Shahidi AK, ''et al.'' |title=Novel regulation of the helix-loop-helix protein Id1 by S5a, a subunit of the 26 S proteasome. |journal=J. Biol. Chem. |volume=272 |issue= 31 |pages= 19140-51 |year= 1997 |pmid= 9235903 |doi= }}
*{{cite journal | author=Langlands K, Yin X, Anand G, Prochownik EV |title=Differential interactions of Id proteins with basic-helix-loop-helix transcription factors. |journal=J. Biol. Chem. |volume=272 |issue= 32 |pages= 19785-93 |year= 1997 |pmid= 9242638 |doi= }}
*{{cite journal | author=Yates PR, Atherton GT, Deed RW, ''et al.'' |title=Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors. |journal=EMBO J. |volume=18 |issue= 4 |pages= 968-76 |year= 1999 |pmid= 10022839 |doi= 10.1093/emboj/18.4.968 }}
*{{cite journal | author=Outinen PA, Sood SK, Pfeifer SI, ''et al.'' |title=Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells. |journal=Blood |volume=94 |issue= 3 |pages= 959-67 |year= 1999 |pmid= 10419887 |doi= }}
*{{cite journal | author=Langlands K, Down GA, Kealey T |title=Id proteins are dynamically expressed in normal epidermis and dysregulated in squamous cell carcinoma. |journal=Cancer Res. |volume=60 |issue= 21 |pages= 5929-33 |year= 2000 |pmid= 11085505 |doi= }}
*{{cite journal | author=Ohtani N, Zebedee Z, Huot TJ, ''et al.'' |title=Opposing effects of Ets and Id proteins on p16INK4a expression during cellular senescence. |journal=Nature |volume=409 |issue= 6823 |pages= 1067-70 |year= 2001 |pmid= 11234019 |doi= 10.1038/35059131 }}
*{{cite journal | author=Suzuki H, Fukunishi Y, Kagawa I, ''et al.'' |title=Protein-protein interaction panel using mouse full-length cDNAs. |journal=Genome Res. |volume=11 |issue= 10 |pages= 1758-65 |year= 2001 |pmid= 11591653 |doi= 10.1101/gr.180101 }}
*{{cite journal | author=Korchynskyi O, ten Dijke P |title=Identification and functional characterization of distinct critically important bone morphogenetic protein-specific response elements in the Id1 promoter. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 4883-91 |year= 2002 |pmid= 11729207 |doi= 10.1074/jbc.M111023200 }}
*{{cite journal | author=Jögi A, Persson P, Grynfeld A, ''et al.'' |title=Modulation of basic helix-loop-helix transcription complex formation by Id proteins during neuronal differentiation. |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 9118-26 |year= 2002 |pmid= 11756408 |doi= 10.1074/jbc.M107713200 }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal | author=Singh J, Murata K, Itahana Y, Desprez PY |title=Constitutive expression of the Id-1 promoter in human metastatic breast cancer cells is linked with the loss of NF-1/Rb/HDAC-1 transcription repressor complex. |journal=Oncogene |volume=21 |issue= 12 |pages= 1812-22 |year= 2002 |pmid= 11896613 |doi= 10.1038/sj.onc.1205252 }}
*{{cite journal | author=Liu CJ, Ding B, Wang H, Lengyel P |title=The MyoD-inducible p204 protein overcomes the inhibition of myoblast differentiation by Id proteins. |journal=Mol. Cell. Biol. |volume=22 |issue= 9 |pages= 2893-905 |year= 2002 |pmid= 11940648 |doi= }}
*{{cite journal | author=Ouyang XS, Wang X, Ling MT, ''et al.'' |title=Id-1 stimulates serum independent prostate cancer cell proliferation through inactivation of p16(INK4a)/pRB pathway. |journal=Carcinogenesis |volume=23 |issue= 5 |pages= 721-5 |year= 2002 |pmid= 12016143 |doi= }}
*{{cite journal | author=Ling MT, Wang X, Tsao SW, Wong YC |title=Down-regulation of Id-1 expression is associated with TGF beta 1-induced growth arrest in prostate epithelial cells. |journal=Biochim. Biophys. Acta |volume=1570 |issue= 3 |pages= 145-52 |year= 2002 |pmid= 12020803 |doi= }}
*{{cite journal | author=Wang X, Xu K, Ling MT, ''et al.'' |title=Evidence of increased Id-1 expression and its role in cell proliferation in nasopharyngeal carcinoma cells. |journal=Mol. Carcinog. |volume=35 |issue= 1 |pages= 42-9 |year= 2002 |pmid= 12203366 |doi= 10.1002/mc.10072 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on KHDRBS1... {November 14, 2007 3:45:09 PM PST}
- SEARCH REDIRECT: Control Box Found: KHDRBS1 {November 14, 2007 3:45:44 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 3:45:46 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 3:45:46 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 3:45:46 PM PST}
- UPDATED: Updated protein page: KHDRBS1 {November 14, 2007 3:45:53 PM PST}
- INFO: Beginning work on MAP2K4... {November 14, 2007 3:44:16 PM PST}
- SEARCH REDIRECT: Control Box Found: MAP2K4 {November 14, 2007 3:45:00 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 3:45:02 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 3:45:02 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 3:45:02 PM PST}
- UPDATED: Updated protein page: MAP2K4 {November 14, 2007 3:45:09 PM PST}
- INFO: Beginning work on MAPK9... {November 14, 2007 3:41:23 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:42:25 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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| 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 = Mitogen-activated protein kinase 9
| HGNCid = 6886
| Symbol = MAPK9
| AltSymbols =; JNK-55; JNK2; JNK2A; JNK2ALPHA; JNK2B; JNK2BETA; PRKM9; p54aSAPK
| OMIM = 602896
| ECnumber =
| Homologene = 55685
| MGIid = 1346862
| GeneAtlas_image1 = PBB_GE_MAPK9_203218_at_tn.png
| GeneAtlas_image2 = PBB_GE_MAPK9_210570_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004705 |text = JUN kinase activity}} {{GNF_GO|id=GO:0004707 |text = MAP kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006950 |text = response to stress}} {{GNF_GO|id=GO:0007254 |text = JNK cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5601
| Hs_Ensembl = ENSG00000050748
| Hs_RefseqProtein = NP_002743
| Hs_RefseqmRNA = NM_002752
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 179595388
| Hs_GenLoc_end = 179640218
| Hs_Uniprot = P45984
| Mm_EntrezGene = 26420
| Mm_Ensembl = ENSMUSG00000020366
| Mm_RefseqmRNA = NM_016961
| Mm_RefseqProtein = NP_058657
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 49690177
| Mm_GenLoc_end = 49729834
| Mm_Uniprot = Q5NCK7
}}
}}
'''Mitogen-activated protein kinase 9''', also known as '''MAPK9''', 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 MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase targets specific transcription factors, and thus mediates immediate-early gene expression in response to various cell stimuli. It is most closely related to MAPK8, both of which are involved in UV radiation induced apoptosis, thought to be related to the cytochrome c-mediated cell death pathway. This gene and MAPK8 are also known as c-Jun N-terminal kinases. This kinase blocks the ubiquitination of tumor suppressor p53, and thus it increases the stability of p53 in nonstressed cells. Studies of this gene's mouse counterpart suggest a key role in T-cell differentiation. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.<ref>{{cite web | title = Entrez Gene: MAPK9 mitogen-activated protein kinase 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5601| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Davis RJ |title=Signal transduction by the JNK group of MAP kinases. |journal=Cell |volume=103 |issue= 2 |pages= 239-52 |year= 2000 |pmid= 11057897 |doi= }}
*{{cite journal | author=Freedman BD, Liu QH, Del Corno M, Collman RG |title=HIV-1 gp120 chemokine receptor-mediated signaling in human macrophages. |journal=Immunol. Res. |volume=27 |issue= 2-3 |pages= 261-76 |year= 2004 |pmid= 12857973 |doi= }}
*{{cite journal | author=Lee C, Liu QH, Tomkowicz B, ''et al.'' |title=Macrophage activation through CCR5- and CXCR4-mediated gp120-elicited signaling pathways. |journal=J. Leukoc. Biol. |volume=74 |issue= 5 |pages= 676-82 |year= 2004 |pmid= 12960231 |doi= 10.1189/jlb.0503206 }}
*{{cite journal | author=Denys H, Desmet R, Stragier M, ''et al.'' |title=Cystitis emphysematosa. |journal=Acta urologica Belgica |volume=45 |issue= 4 |pages= 327-31 |year= 1978 |pmid= 602896 |doi= }}
*{{cite journal | author=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=Livingstone C, Patel G, Jones N |title=ATF-2 contains a phosphorylation-dependent transcriptional activation domain. |journal=EMBO J. |volume=14 |issue= 8 |pages= 1785-97 |year= 1995 |pmid= 7737129 |doi= }}
*{{cite journal | author=Sluss HK, Barrett T, Dérijard B, Davis RJ |title=Signal transduction by tumor necrosis factor mediated by JNK protein kinases. |journal=Mol. Cell. Biol. |volume=14 |issue= 12 |pages= 8376-84 |year= 1994 |pmid= 7969172 |doi= }}
*{{cite journal | author=Kallunki T, Su B, Tsigelny I, ''et al.'' |title=JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation. |journal=Genes Dev. |volume=8 |issue= 24 |pages= 2996-3007 |year= 1995 |pmid= 8001819 |doi= }}
*{{cite journal | author=Gille H, Strahl T, Shaw PE |title=Activation of ternary complex factor Elk-1 by stress-activated protein kinases. |journal=Curr. Biol. |volume=5 |issue= 10 |pages= 1191-200 |year= 1996 |pmid= 8548291 |doi= }}
*{{cite journal | author=Chu Y, Solski PA, Khosravi-Far R, ''et al.'' |title=The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation. |journal=J. Biol. Chem. |volume=271 |issue= 11 |pages= 6497-501 |year= 1996 |pmid= 8626452 |doi= }}
*{{cite journal | author=Bocco JL, Bahr A, Goetz J, ''et al.'' |title=In vivo association of ATFa with JNK/SAP kinase activities. |journal=Oncogene |volume=12 |issue= 9 |pages= 1971-80 |year= 1996 |pmid= 8649858 |doi= }}
*{{cite journal | author=Gupta S, Barrett T, Whitmarsh AJ, ''et al.'' |title=Selective interaction of JNK protein kinase isoforms with transcription factors. |journal=EMBO J. |volume=15 |issue= 11 |pages= 2760-70 |year= 1996 |pmid= 8654373 |doi= }}
*{{cite journal | author=Kallunki T, Deng T, Hibi M, Karin M |title=c-Jun can recruit JNK to phosphorylate dimerization partners via specific docking interactions. |journal=Cell |volume=87 |issue= 5 |pages= 929-39 |year= 1997 |pmid= 8945519 |doi= }}
*{{cite journal | author=Jabado N, Pallier A, Jauliac S, ''et al.'' |title=gp160 of HIV or anti-CD4 monoclonal antibody ligation of CD4 induces inhibition of JNK and ERK-2 activities in human peripheral CD4+ T lymphocytes. |journal=Eur. J. Immunol. |volume=27 |issue= 2 |pages= 397-404 |year= 1997 |pmid= 9045910 |doi= }}
*{{cite journal | author=Janknecht R, Hunter T |title=Convergence of MAP kinase pathways on the ternary complex factor Sap-1a. |journal=EMBO J. |volume=16 |issue= 7 |pages= 1620-7 |year= 1997 |pmid= 9130707 |doi= 10.1093/emboj/16.7.1620 }}
*{{cite journal | author=Fukunaga R, Hunter T |title=MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. |journal=EMBO J. |volume=16 |issue= 8 |pages= 1921-33 |year= 1997 |pmid= 9155018 |doi= 10.1093/emboj/16.8.1921 }}
*{{cite journal | author=Chow CW, Rincón M, Cavanagh J, ''et al.'' |title=Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway. |journal=Science |volume=278 |issue= 5343 |pages= 1638-41 |year= 1997 |pmid= 9374467 |doi= }}
*{{cite journal | author=Hu MC, Qiu WR, Wang YP |title=JNK1, JNK2 and JNK3 are p53 N-terminal serine 34 kinases. |journal=Oncogene |volume=15 |issue= 19 |pages= 2277-87 |year= 1997 |pmid= 9393873 |doi= 10.1038/sj.onc.1201401 }}
*{{cite journal | author=Lannuzel A, Barnier JV, Hery C, ''et al.'' |title=Human immunodeficiency virus type 1 and its coat protein gp120 induce apoptosis and activate JNK and ERK mitogen-activated protein kinases in human neurons. |journal=Ann. Neurol. |volume=42 |issue= 6 |pages= 847-56 |year= 1998 |pmid= 9403476 |doi= 10.1002/ana.410420605 }}
*{{cite journal | author=Fuchs SY, Xie B, Adler V, ''et al.'' |title=c-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factors. |journal=J. Biol. Chem. |volume=272 |issue= 51 |pages= 32163-8 |year= 1998 |pmid= 9405416 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MYH9... {November 14, 2007 3:39:54 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:40:39 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 = Myosin, heavy chain 9, non-muscle
| HGNCid = 7579
| Symbol = MYH9
| AltSymbols =; DFNA17; EPSTS; FTNS; MGC104539; MHA; NMHC-II-A; NMMHCA
| OMIM = 160775
| ECnumber =
| Homologene = 68257
| MGIid = 107717
| GeneAtlas_image1 = PBB_GE_MYH9_211926_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000146 |text = microfilament motor activity}} {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003774 |text = motor activity}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0043495 |text = protein anchor}} {{GNF_GO|id=GO:0051015 |text = actin filament binding}}
| Component = {{GNF_GO|id=GO:0001725 |text = stress fiber}} {{GNF_GO|id=GO:0001726 |text = ruffle}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005826 |text = contractile ring}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005913 |text = cell-cell adherens junction}} {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0016459 |text = myosin complex}} {{GNF_GO|id=GO:0032154 |text = cleavage furrow}}
| Process = {{GNF_GO|id=GO:0000904 |text = cellular morphogenesis during differentiation}} {{GNF_GO|id=GO:0000910 |text = cytokinesis}} {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0006509 |text = membrane protein ectodomain proteolysis}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007605 |text = sensory perception of sound}} {{GNF_GO|id=GO:0008360 |text = regulation of cell shape}} {{GNF_GO|id=GO:0015031 |text = protein transport}} {{GNF_GO|id=GO:0016337 |text = cell-cell adhesion}} {{GNF_GO|id=GO:0030048 |text = actin filament-based movement}} {{GNF_GO|id=GO:0030220 |text = platelet formation}} {{GNF_GO|id=GO:0030224 |text = monocyte differentiation}} {{GNF_GO|id=GO:0031532 |text = actin cytoskeleton reorganization}} {{GNF_GO|id=GO:0043534 |text = blood vessel endothelial cell migration}} {{GNF_GO|id=GO:0050900 |text = leukocyte migration}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4627
| Hs_Ensembl = ENSG00000100345
| Hs_RefseqProtein = NP_002464
| Hs_RefseqmRNA = NM_002473
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 35007273
| Hs_GenLoc_end = 35113958
| Hs_Uniprot = P35579
| Mm_EntrezGene = 17886
| Mm_Ensembl = ENSMUSG00000022443
| Mm_RefseqmRNA = NM_181327
| Mm_RefseqProtein = NP_851844
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 77587843
| Mm_GenLoc_end = 77669360
| Mm_Uniprot = O89055
}}
}}
'''Myosin, heavy chain 9, non-muscle''', also known as '''MYH9''', 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=Starr R, Offer G |title=The interaction of C-protein with heavy meromyosin and subfragment-2. |journal=Biochem. J. |volume=171 |issue= 3 |pages= 813-6 |year= 1978 |pmid= 352343 |doi= }}
*{{cite journal | author=Lee CL, Atassi MZ |title=Enzymic and immunochemical properties of lysozyme. Accurate definition of the antigenic site around the disulphide bridge 30-115 (site 3) by 'surface-simulation' synthesis. |journal=Biochem. J. |volume=167 |issue= 3 |pages= 571-81 |year= 1978 |pmid= 603622 |doi= }}
*{{cite journal | author=Tweed WA, Phua WT, Chong KY, ''et al.'' |title=Large tidal volume ventilation improves pulmonary gas exchange during lower abdominal surgery in Trendelenburg's position. |journal=Canadian journal of anaesthesia = Journal canadien d'anesthésie |volume=38 |issue= 8 |pages= 989-95 |year= 1992 |pmid= 1752022 |doi= }}
*{{cite journal | author=Simons M, Wang M, McBride OW, ''et al.'' |title=Human nonmuscle myosin heavy chains are encoded by two genes located on different chromosomes. |journal=Circ. Res. |volume=69 |issue= 2 |pages= 530-9 |year= 1991 |pmid= 1860190 |doi= }}
*{{cite journal | author=Toothaker LE, Gonzalez DA, Tung N, ''et al.'' |title=Cellular myosin heavy chain in human leukocytes: isolation of 5' cDNA clones, characterization of the protein, chromosomal localization, and upregulation during myeloid differentiation. |journal=Blood |volume=78 |issue= 7 |pages= 1826-33 |year= 1991 |pmid= 1912569 |doi= }}
*{{cite journal | author=Saez CG, Myers JC, Shows TB, Leinwand LA |title=Human nonmuscle myosin heavy chain mRNA: generation of diversity through alternative polyadenylylation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 3 |pages= 1164-8 |year= 1990 |pmid= 1967836 |doi= }}
*{{cite journal | author=Moos C, Feng IN |title=Effect of C-protein on actomyosin ATPase. |journal=Biochim. Biophys. Acta |volume=632 |issue= 2 |pages= 141-9 |year= 1980 |pmid= 6448079 |doi= }}
*{{cite journal | author=Obermann WM, Plessmann U, Weber K, Fürst DO |title=Purification and biochemical characterization of myomesin, a myosin-binding and titin-binding protein, from bovine skeletal muscle. |journal=Eur. J. Biochem. |volume=233 |issue= 1 |pages= 110-5 |year= 1995 |pmid= 7588733 |doi= }}
*{{cite journal | author=Maupin P, Phillips CL, Adelstein RS, Pollard TD |title=Differential localization of myosin-II isozymes in human cultured cells and blood cells. |journal=J. Cell. Sci. |volume=107 ( Pt 11) |issue= |pages= 3077-90 |year= 1995 |pmid= 7699007 |doi= }}
*{{cite journal | author=Bement WM, Hasson T, Wirth JA, ''et al.'' |title=Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6549-53 |year= 1994 |pmid= 8022818 |doi= }}
*{{cite journal | author=Eilertsen KJ, Kazmierski ST, Keller TC |title=Cellular titin localization in stress fibers and interaction with myosin II filaments in vitro. |journal=J. Cell Biol. |volume=126 |issue= 5 |pages= 1201-10 |year= 1994 |pmid= 8063857 |doi= }}
*{{cite journal | author=Shoeman RL, Sachse C, Höner B, ''et al.'' |title=Cleavage of human and mouse cytoskeletal and sarcomeric proteins by human immunodeficiency virus type 1 protease. Actin, desmin, myosin, and tropomyosin. |journal=Am. J. Pathol. |volume=142 |issue= 1 |pages= 221-30 |year= 1993 |pmid= 8424456 |doi= }}
*{{cite journal | author=Lalwani AK, Linthicum FH, Wilcox ER, ''et al.'' |title=A five-generation family with late-onset progressive hereditary hearing impairment due to cochleosaccular degeneration. |journal=Audiol. Neurootol. |volume=2 |issue= 3 |pages= 139-54 |year= 1998 |pmid= 9390828 |doi= }}
*{{cite journal | author=Ford HL, Silver DL, Kachar B, ''et al.'' |title=Effect of Mts1 on the structure and activity of nonmuscle myosin II. |journal=Biochemistry |volume=36 |issue= 51 |pages= 16321-7 |year= 1998 |pmid= 9405067 |doi= 10.1021/bi971182l }}
*{{cite journal | author=Obermann WM, van der Ven PF, Steiner F, ''et al.'' |title=Mapping of a myosin-binding domain and a regulatory phosphorylation site in M-protein, a structural protein of the sarcomeric M band. |journal=Mol. Biol. Cell |volume=9 |issue= 4 |pages= 829-40 |year= 1998 |pmid= 9529381 |doi= }}
*{{cite journal | author=Dunham I, Shimizu N, Roe BA, ''et al.'' |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489-95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 }}
*{{cite journal | author=Miyamoto CA, Fischman DA, Reinach FC |title=The interface between MyBP-C and myosin: site-directed mutagenesis of the CX myosin-binding domain of MyBP-C. |journal=J. Muscle Res. Cell. Motil. |volume=20 |issue= 7 |pages= 703-15 |year= 2000 |pmid= 10672519 |doi= }}
*{{cite journal | author=Sajid M, Hu Z, Lele M, Stouffer GA |title=Protein complexes involving alpha v beta 3 integrins, nonmuscle myosin heavy chain-A, and focal adhesion kinase from in thrombospondin-treated smooth muscle cells. |journal=J. Investig. Med. |volume=48 |issue= 3 |pages= 190-7 |year= 2000 |pmid= 10822899 |doi= }}
*{{cite journal | author=Husi H, Ward MA, Choudhary JS, ''et al.'' |title=Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. |journal=Nat. Neurosci. |volume=3 |issue= 7 |pages= 661-9 |year= 2000 |pmid= 10862698 |doi= 10.1038/76615 }}
*{{cite journal | author=Kelley MJ, Jawien W, Lin A, ''et al.'' |title=Autosomal dominant macrothrombocytopenia with leukocyte inclusions (May-Hegglin anomaly) is linked to chromosome 22q12-13. |journal=Hum. Genet. |volume=106 |issue= 5 |pages= 557-64 |year= 2000 |pmid= 10914687 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NQO1... {November 14, 2007 3:32:08 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:32:49 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_NQO1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1d4a.
| PDB = {{PDB2|1d4a}}, {{PDB2|1dxo}}, {{PDB2|1gg5}}, {{PDB2|1h66}}, {{PDB2|1h69}}, {{PDB2|1kbo}}, {{PDB2|1kbq}}, {{PDB2|1qbg}}, {{PDB2|2f1o}}
| Name = NAD(P)H dehydrogenase, quinone 1
| HGNCid = 2874
| Symbol = NQO1
| AltSymbols =; DHQU; DIA4; DTD; NMOR1; NMORI; QR1
| OMIM = 125860
| ECnumber =
| Homologene = 695
| MGIid = 103187
| GeneAtlas_image1 = PBB_GE_NQO1_201468_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NQO1_201467_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_NQO1_210519_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003955 |text = NAD(P)H dehydrogenase (quinone) activity}} {{GNF_GO|id=GO:0004128 |text = cytochrome-b5 reductase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006805 |text = xenobiotic metabolic process}} {{GNF_GO|id=GO:0006809 |text = nitric oxide biosynthetic process}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}} {{GNF_GO|id=GO:0007271 |text = synaptic transmission, cholinergic}} {{GNF_GO|id=GO:0009636 |text = response to toxin}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1728
| Hs_Ensembl = ENSG00000181019
| Hs_RefseqProtein = NP_000894
| Hs_RefseqmRNA = NM_000903
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 68300808
| Hs_GenLoc_end = 68318034
| Hs_Uniprot = P15559
| Mm_EntrezGene = 18104
| Mm_Ensembl = ENSMUSG00000003849
| Mm_RefseqmRNA = NM_008706
| Mm_RefseqProtein = NP_032732
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 110277948
| Mm_GenLoc_end = 110282145
| Mm_Uniprot = Q542Y0
}}
}}
'''NAD(P)H dehydrogenase, quinone 1''', also known as '''NQO1''', 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 NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. This FAD-binding protein forms homodimers and reduces quinones to hydroquinones. This protein's enzymatic activity prevents the one electron reduction of quinones that results in the production of radical species. Mutations in this gene have been associated with tardive dyskinesia (TD), an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer. Altered expression of this protein has been seen in many tumors and is also associated with Alzheimer's disease (AD). Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref>{{cite web | title = Entrez Gene: NQO1 NAD(P)H dehydrogenase, quinone 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1728| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Vasiliou V, Ross D, Nebert DW |title=Update of the NAD(P)H:quinone oxidoreductase (NQO) gene family. |journal=Hum. Genomics |volume=2 |issue= 5 |pages= 329-35 |year= 2006 |pmid= 16595077 |doi= }}
*{{cite journal | author=Li Y, Jaiswal AK |title=Regulation of human NAD(P)H:quinone oxidoreductase gene. Role of AP1 binding site contained within human antioxidant response element. |journal=J. Biol. Chem. |volume=267 |issue= 21 |pages= 15097-104 |year= 1992 |pmid= 1340765 |doi= }}
*{{cite journal | author=Jaiswal AK |title=Human NAD(P)H:quinone oxidoreductase (NQO1) gene structure and induction by dioxin. |journal=Biochemistry |volume=30 |issue= 44 |pages= 10647-53 |year= 1991 |pmid= 1657151 |doi= }}
*{{cite journal | author=Traver RD, Horikoshi T, Danenberg KD, ''et al.'' |title=NAD(P)H:quinone oxidoreductase gene expression in human colon carcinoma cells: characterization of a mutation which modulates DT-diaphorase activity and mitomycin sensitivity. |journal=Cancer Res. |volume=52 |issue= 4 |pages= 797-802 |year= 1992 |pmid= 1737339 |doi= }}
*{{cite journal | author=Chen LZ, Harris PC, Apostolou S, ''et al.'' |title=A refined physical map of the long arm of human chromosome 16. |journal=Genomics |volume=10 |issue= 2 |pages= 308-12 |year= 1991 |pmid= 2071140 |doi= }}
*{{cite journal | author=Jaiswal AK, McBride OW, Adesnik M, Nebert DW |title=Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase. cDNA sequence and localization of gene to chromosome 16. |journal=J. Biol. Chem. |volume=263 |issue= 27 |pages= 13572-8 |year= 1988 |pmid= 2843525 |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=Rothman N, Smith MT, Hayes RB, ''et al.'' |title=Benzene poisoning, a risk factor for hematological malignancy, is associated with the NQO1 609C-->T mutation and rapid fractional excretion of chlorzoxazone. |journal=Cancer Res. |volume=57 |issue= 14 |pages= 2839-42 |year= 1997 |pmid= 9230185 |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=Smiley JF, Levey AI, Mesulam MM |title=Infracortical interstitial cells concurrently expressing m2-muscarinic receptors, acetylcholinesterase and nicotinamide adenine dinucleotide phosphate-diaphorase in the human and monkey cerebral cortex. |journal=Neuroscience |volume=84 |issue= 3 |pages= 755-69 |year= 1998 |pmid= 9579781 |doi= }}
*{{cite journal | author=Moran JL, Siegel D, Ross D |title=A potential mechanism underlying the increased susceptibility of individuals with a polymorphism in NAD(P)H:quinone oxidoreductase 1 (NQO1) to benzene toxicity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 14 |pages= 8150-5 |year= 1999 |pmid= 10393963 |doi= }}
*{{cite journal | author=Kristiansen OP, Larsen ZM, Johannesen J, ''et al.'' |title=No linkage of P187S polymorphism in NAD(P)H: quinone oxidoreductase (NQO1/DIA4) and type 1 diabetes in the Danish population. DIEGG and DSGD. Danish IDDM Epidemiology and Genetics Group and The Danish Study Group of Diabetes in Childhood. |journal=Hum. Mutat. |volume=14 |issue= 1 |pages= 67-70 |year= 1999 |pmid= 10447260 |doi= 10.1002/(SICI)1098-1004(1999)14:1<67::AID-HUMU8>3.0.CO;2-5 }}
*{{cite journal | author=Eliasson M, Boström M, DePierre JW |title=Levels and subcellular distributions of detoxifying enzymes in the ovarian corpus luteum of the pregnant and non-pregnant pig. |journal=Biochem. Pharmacol. |volume=58 |issue= 8 |pages= 1287-92 |year= 1999 |pmid= 10487530 |doi= }}
*{{cite journal | author=Skelly JV, Sanderson MR, Suter DA, ''et al.'' |title=Crystal structure of human DT-diaphorase: a model for interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954). |journal=J. Med. Chem. |volume=42 |issue= 21 |pages= 4325-30 |year= 1999 |pmid= 10543876 |doi= }}
*{{cite journal | author=Faig M, Bianchet MA, Talalay P, ''et al.'' |title=Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3177-82 |year= 2000 |pmid= 10706635 |doi= 10.1073/pnas.050585797 }}
*{{cite journal | author=Harada S, Fujii C, Hayashi A, Ohkoshi N |title=An association between idiopathic Parkinson's disease and polymorphisms of phase II detoxification enzymes: glutathione S-transferase M1 and quinone oxidoreductase 1 and 2. |journal=Biochem. Biophys. Res. Commun. |volume=288 |issue= 4 |pages= 887-92 |year= 2001 |pmid= 11688992 |doi= 10.1006/bbrc.2001.5868 }}
*{{cite journal | author=Siegel D, Ryder J, Ross D |title=NAD(P)H: quinone oxidoreductase 1 expression in human bone marrow endothelial cells. |journal=Toxicol. Lett. |volume=125 |issue= 1-3 |pages= 93-8 |year= 2001 |pmid= 11701227 |doi= }}
*{{cite journal | author=Anwar A, Siegel D, Kepa JK, Ross D |title=Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 14060-7 |year= 2002 |pmid= 11821413 |doi= 10.1074/jbc.M111576200 }}
*{{cite journal | author=Winski SL, Koutalos Y, Bentley DL, Ross D |title=Subcellular localization of NAD(P)H:quinone oxidoreductase 1 in human cancer cells. |journal=Cancer Res. |volume=62 |issue= 5 |pages= 1420-4 |year= 2002 |pmid= 11888914 |doi= }}
*{{cite journal | author=Begleiter A, Lange L |title=Lack of NQO1 induction in human tumor cells is not due to changes in the promoter region of the gene. |journal=Int. J. Oncol. |volume=20 |issue= 4 |pages= 835-8 |year= 2002 |pmid= 11894133 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NR5A1... {November 14, 2007 3:34:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:35:19 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_NR5A1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ymt.
| PDB = {{PDB2|1ymt}}, {{PDB2|1yow}}, {{PDB2|1yp0}}, {{PDB2|1zdt}}, {{PDB2|2a66}}, {{PDB2|2ff0}}
| Name = Nuclear receptor subfamily 5, group A, member 1
| HGNCid = 7983
| Symbol = NR5A1
| AltSymbols =; AD4BP; ELP; FTZ1; FTZF1; SF-1; SF1
| OMIM = 184757
| ECnumber =
| Homologene = 3638
| MGIid = 1346833
| GeneAtlas_image1 = PBB_GE_NR5A1_210333_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004879 |text = ligand-dependent nuclear receptor activity}} {{GNF_GO|id=GO:0005496 |text = steroid binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0016439 |text = tRNA-pseudouridine synthase 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:0001553 |text = luteinization}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007538 |text = primary sex determination}} {{GNF_GO|id=GO:0008406 |text = gonad development}} {{GNF_GO|id=GO:0008584 |text = male gonad development}} {{GNF_GO|id=GO:0009888 |text = tissue development}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0030325 |text = adrenal gland development}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0050810 |text = regulation of steroid biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2516
| Hs_Ensembl = ENSG00000136931
| Hs_RefseqProtein = NP_004950
| Hs_RefseqmRNA = NM_004959
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 126283337
| Hs_GenLoc_end = 126309530
| Hs_Uniprot = Q13285
| Mm_EntrezGene = 26423
| Mm_Ensembl = ENSMUSG00000026751
| Mm_RefseqmRNA = NM_139051
| Mm_RefseqProtein = NP_620639
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 38514636
| Mm_GenLoc_end = 38536513
| Mm_Uniprot = P97782
}}
}}
'''Nuclear receptor subfamily 5, group A, member 1''', also known as '''NR5A1''', 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=Morohashi KI, Omura T |title=Ad4BP/SF-1, a transcription factor essential for the transcription of steroidogenic cytochrome P450 genes and for the establishment of the reproductive function. |journal=FASEB J. |volume=10 |issue= 14 |pages= 1569-77 |year= 1997 |pmid= 9002548 |doi= }}
*{{cite journal | author=Parker KL, Schimmer BP |title=Steroidogenic factor 1: a key determinant of endocrine development and function. |journal=Endocr. Rev. |volume=18 |issue= 3 |pages= 361-77 |year= 1997 |pmid= 9183568 |doi= }}
*{{cite journal | author=Achermann JC, Meeks JJ, Jameson JL |title=Phenotypic spectrum of mutations in DAX-1 and SF-1. |journal=Mol. Cell. Endocrinol. |volume=185 |issue= 1-2 |pages= 17-25 |year= 2003 |pmid= 11738790 |doi= }}
*{{cite journal | author=Ozisik G, Achermann JC, Jameson JL |title=The role of SF1 in adrenal and reproductive function: insight from naturally occurring mutations in humans. |journal=Mol. Genet. Metab. |volume=76 |issue= 2 |pages= 85-91 |year= 2003 |pmid= 12083805 |doi= }}
*{{cite journal | author=Jameson JL |title=Of mice and men: The tale of steroidogenic factor-1. |journal=J. Clin. Endocrinol. Metab. |volume=89 |issue= 12 |pages= 5927-9 |year= 2005 |pmid= 15579738 |doi= 10.1210/jc.2004-2047 }}
*{{cite journal | author=de-Souza BF, Lin L, Achermann JC |title=Steroidogenic factor-1 (SF-1) and its relevance to pediatric endocrinology. |journal=Pediatric endocrinology reviews : PER |volume=3 |issue= 4 |pages= 359-64 |year= 2006 |pmid= 16816804 |doi= }}
*{{cite journal | author=Sadovsky Y, Crawford PA, Woodson KG, ''et al.'' |title=Mice deficient in the orphan receptor steroidogenic factor 1 lack adrenal glands and gonads but express P450 side-chain-cleavage enzyme in the placenta and have normal embryonic serum levels of corticosteroids. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 24 |pages= 10939-43 |year= 1995 |pmid= 7479914 |doi= }}
*{{cite journal | author=Sasano H, Shizawa S, Suzuki T, ''et al.'' |title=Ad4BP in the human adrenal cortex and its disorders. |journal=J. Clin. Endocrinol. Metab. |volume=80 |issue= 8 |pages= 2378-80 |year= 1995 |pmid= 7629233 |doi= }}
*{{cite journal | author=Taketo M, Parker KL, Howard TA, ''et al.'' |title=Homologs of Drosophila Fushi-Tarazu factor 1 map to mouse chromosome 2 and human chromosome 9q33. |journal=Genomics |volume=25 |issue= 2 |pages= 565-7 |year= 1995 |pmid= 7789992 |doi= }}
*{{cite journal | author=Shen WH, Moore CC, Ikeda Y, ''et al.'' |title=Nuclear receptor steroidogenic factor 1 regulates the müllerian inhibiting substance gene: a link to the sex determination cascade. |journal=Cell |volume=77 |issue= 5 |pages= 651-61 |year= 1994 |pmid= 8205615 |doi= }}
*{{cite journal | author=Oba K, Yanase T, Nomura M, ''et al.'' |title=Structural characterization of human Ad4bp (SF-1) gene. |journal=Biochem. Biophys. Res. Commun. |volume=226 |issue= 1 |pages= 261-7 |year= 1996 |pmid= 8806624 |doi= }}
*{{cite journal | author=Asa SL, Bamberger AM, Cao B, ''et al.'' |title=The transcription activator steroidogenic factor-1 is preferentially expressed in the human pituitary gonadotroph. |journal=J. Clin. Endocrinol. Metab. |volume=81 |issue= 6 |pages= 2165-70 |year= 1996 |pmid= 8964846 |doi= }}
*{{cite journal | author=Bamberger AM, Ezzat S, Cao B, ''et al.'' |title=Expression of steroidogenic factor-1 (SF-1) mRNA and protein in the human placenta. |journal=Mol. Hum. Reprod. |volume=2 |issue= 6 |pages= 457-61 |year= 1997 |pmid= 9238716 |doi= }}
*{{cite journal | author=Crawford PA, Polish JA, Ganpule G, Sadovsky Y |title=The activation function-2 hexamer of steroidogenic factor-1 is required, but not sufficient for potentiation by SRC-1. |journal=Mol. Endocrinol. |volume=11 |issue= 11 |pages= 1626-35 |year= 1998 |pmid= 9328345 |doi= }}
*{{cite journal | author=Nachtigal MW, Hirokawa Y, Enyeart-VanHouten DL, ''et al.'' |title=Wilms' tumor 1 and Dax-1 modulate the orphan nuclear receptor SF-1 in sex-specific gene expression. |journal=Cell |volume=93 |issue= 3 |pages= 445-54 |year= 1998 |pmid= 9590178 |doi= }}
*{{cite journal | author=De Santa Barbara P, Bonneaud N, Boizet B, ''et al.'' |title=Direct interaction of SRY-related protein SOX9 and steroidogenic factor 1 regulates transcription of the human anti-Müllerian hormone gene. |journal=Mol. Cell. Biol. |volume=18 |issue= 11 |pages= 6653-65 |year= 1998 |pmid= 9774680 |doi= }}
*{{cite journal | author=Hammer GD, Krylova I, Zhang Y, ''et al.'' |title=Phosphorylation of the nuclear receptor SF-1 modulates cofactor recruitment: integration of hormone signaling in reproduction and stress. |journal=Mol. Cell |volume=3 |issue= 4 |pages= 521-6 |year= 1999 |pmid= 10230405 |doi= }}
*{{cite journal | author=Achermann JC, Ito M, Ito M, ''et al.'' |title=A mutation in the gene encoding steroidogenic factor-1 causes XY sex reversal and adrenal failure in humans. |journal=Nat. Genet. |volume=22 |issue= 2 |pages= 125-6 |year= 1999 |pmid= 10369247 |doi= 10.1038/9629 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on POLR2B... {November 14, 2007 3:40:39 PM PST}
- SEARCH REDIRECT: Control Box Found: POLR2B {November 14, 2007 3:41:14 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 3:41:16 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 3:41:16 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 3:41:16 PM PST}
- UPDATED: Updated protein page: POLR2B {November 14, 2007 3:41:23 PM PST}
- INFO: Beginning work on PRL... {November 14, 2007 3:42:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:42:51 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PRL_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1n9d.
| PDB = {{PDB2|1n9d}}, {{PDB2|1rw5}}
| Name = Prolactin
| HGNCid = 9445
| Symbol = PRL
| AltSymbols =;
| OMIM = 176760
| ECnumber =
| Homologene = 732
| MGIid = 97762
| GeneAtlas_image1 = PBB_GE_PRL_205445_at_tn.png
| Function = {{GNF_GO|id=GO:0005148 |text = prolactin receptor binding}} {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007516 |text = hemocyte development}} {{GNF_GO|id=GO:0007565 |text = female pregnancy}} {{GNF_GO|id=GO:0007595 |text = lactation}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5617
| Hs_Ensembl = ENSG00000172179
| Hs_RefseqProtein = NP_000939
| Hs_RefseqmRNA = NM_000948
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 22395459
| Hs_GenLoc_end = 22405709
| Hs_Uniprot = P01236
| Mm_EntrezGene = 19109
| Mm_Ensembl = ENSMUSG00000021342
| Mm_RefseqmRNA = NM_011164
| Mm_RefseqProtein = NP_035294
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 27065042
| Mm_GenLoc_end = 27072657
| Mm_Uniprot = Q3TT66
}}
}}
'''Prolactin''', also known as '''PRL''', 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=Bole-Feysot C, Goffin V, Edery M, ''et al.'' |title=Prolactin (PRL) and its receptor: actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice. |journal=Endocr. Rev. |volume=19 |issue= 3 |pages= 225-68 |year= 1998 |pmid= 9626554 |doi= }}
*{{cite journal | author=Tansey MJ, Schlechte JA |title=Pituitary production of prolactin and prolactin-suppressing drugs. |journal=Lupus |volume=10 |issue= 10 |pages= 660-4 |year= 2002 |pmid= 11721691 |doi= }}
*{{cite journal | author=Montgomery DW |title=Prolactin production by immune cells. |journal=Lupus |volume=10 |issue= 10 |pages= 665-75 |year= 2002 |pmid= 11721692 |doi= }}
*{{cite journal | author=Stevens A, Ray DW, Worthington J, Davis JR |title=Polymorphisms of the human prolactin gene--implications for production of lymphocyte prolactin and systemic lupus erythematosus. |journal=Lupus |volume=10 |issue= 10 |pages= 676-83 |year= 2002 |pmid= 11721693 |doi= }}
*{{cite journal | author=Buckley AR |title=Prolactin, a lymphocyte growth and survival factor. |journal=Lupus |volume=10 |issue= 10 |pages= 684-90 |year= 2002 |pmid= 11721694 |doi= }}
*{{cite journal | author=Yu-Lee L |title=Stimulation of interferon regulatory factor-1 by prolactin. |journal=Lupus |volume=10 |issue= 10 |pages= 691-9 |year= 2002 |pmid= 11721695 |doi= }}
*{{cite journal | author=Welniak LA, Richards SM, Murphy WJ |title=Effects of prolactin on hematopoiesis. |journal=Lupus |volume=10 |issue= 10 |pages= 700-5 |year= 2002 |pmid= 11721696 |doi= }}
*{{cite journal | author=Hooghe R, Dogusan Z, Martens N, ''et al.'' |title=Effects of prolactin on signal transduction and gene expression: possible relevance for systemic lupus erythematosus. |journal=Lupus |volume=10 |issue= 10 |pages= 719-27 |year= 2002 |pmid= 11721698 |doi= }}
*{{cite journal | author=Matera L, Mori M, Galetto A |title=Effect of prolactin on the antigen presenting function of monocyte-derived dendritic cells. |journal=Lupus |volume=10 |issue= 10 |pages= 728-34 |year= 2002 |pmid= 11721699 |doi= }}
*{{cite journal | author=Jara LJ, Vera-Lastra O, Miranda JM, ''et al.'' |title=Prolactin in human systemic lupus erythematosus. |journal=Lupus |volume=10 |issue= 10 |pages= 748-56 |year= 2002 |pmid= 11721702 |doi= }}
*{{cite journal | author=Blanco-Favela F, Chavez-Rueda K, Leaños-Miranda A |title=Analysis of anti-prolactin autoantibodies in systemic lupus erythematosus. |journal=Lupus |volume=10 |issue= 10 |pages= 757-61 |year= 2002 |pmid= 11721703 |doi= }}
*{{cite journal | author=Méndez I, Cariño C, Díaz L |title=[Prolactin in the immunological system: synthesis and biological effects] |journal=Rev. Invest. Clin. |volume=57 |issue= 3 |pages= 447-56 |year= 2005 |pmid= 16187706 |doi= }}
*{{cite journal | author=Farquhar MG, Reid JJ, Daniell LW |title=Intracellular transport and packaging of prolactin: a quantitative electron microscope autoradiographic study of mammotrophs dissociated from rat pituitaries. |journal=Endocrinology |volume=102 |issue= 1 |pages= 296-311 |year= 1979 |pmid= 743954 |doi= }}
*{{cite journal | author=Shome B, Parlow AF |title=Human pituitary prolactin (hPRL): the entire linear amino acid sequence. |journal=J. Clin. Endocrinol. Metab. |volume=45 |issue= 5 |pages= 1112-5 |year= 1978 |pmid= 925136 |doi= }}
*{{cite journal | author=Jacobs JW, Niall HD |title=High sensitivity automated sequence determination of polypeptides. |journal=J. Biol. Chem. |volume=250 |issue= 10 |pages= 3629-36 |year= 1975 |pmid= 1126929 |doi= }}
*{{cite journal | author=Maddox PR, Jones DL, Mansel RE |title=Bioactive and immunoactive prolactin levels after TRH-stimulation in the sera of normal women. |journal=Horm. Metab. Res. |volume=24 |issue= 4 |pages= 181-4 |year= 1992 |pmid= 1601394 |doi= }}
*{{cite journal | author=DiMattia GE, Gellersen B, Duckworth ML, Friesen HG |title=Human prolactin gene expression. The use of an alternative noncoding exon in decidua and the IM-9-P3 lymphoblast cell line. |journal=J. Biol. Chem. |volume=265 |issue= 27 |pages= 16412-21 |year= 1990 |pmid= 1697858 |doi= }}
*{{cite journal | author=Gellersen B, Kempf R |title=Human prolactin gene expression: positive correlation between site-specific methylation and gene activity in a set of human lymphoid cell lines. |journal=Mol. Endocrinol. |volume=4 |issue= 12 |pages= 1874-86 |year= 1991 |pmid= 1707126 |doi= }}
*{{cite journal | author=Hiraoka Y, Tatsumi K, Shiozawa M, ''et al.'' |title=A placenta-specific 5' non-coding exon of human prolactin. |journal=Mol. Cell. Endocrinol. |volume=75 |issue= 1 |pages= 71-80 |year= 1991 |pmid= 2050267 |doi= }}
*{{cite journal | author=Evans AM, Petersen JW, Sekhon GS, DeMars R |title=Mapping of prolactin and tumor necrosis factor-beta genes on human chromosome 6p using lymphoblastoid cell deletion mutants. |journal=Somat. Cell Mol. Genet. |volume=15 |issue= 3 |pages= 203-13 |year= 1989 |pmid= 2567059 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RELB... {November 14, 2007 3:42:52 PM PST}
- SEARCH REDIRECT: Control Box Found: RELB {November 14, 2007 3:43:19 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 3:43:20 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 3:43:20 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 3:43:20 PM PST}
- UPDATED: Updated protein page: RELB {November 14, 2007 3:43:26 PM PST}
- INFO: Beginning work on SELL... {November 14, 2007 3:43:26 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 3:44:16 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 = Selectin L (lymphocyte adhesion molecule 1)
| HGNCid = 10720
| Symbol = SELL
| AltSymbols =; CD62L; LAM-1; LAM1; LECAM1; LNHR; LSEL; LYAM1; Leu-8; Lyam-1; PLNHR; TQ1; hLHRc
| OMIM = 153240
| ECnumber =
| Homologene = 539
| MGIid = 98279
| GeneAtlas_image1 = PBB_GE_SELL_204563_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6402
| Hs_Ensembl = ENSG00000188404
| Hs_RefseqProtein = NP_000646
| Hs_RefseqmRNA = NM_000655
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 167926432
| Hs_GenLoc_end = 167947463
| Hs_Uniprot = P14151
| Mm_EntrezGene = 20343
| Mm_Ensembl = ENSMUSG00000026581
| Mm_RefseqmRNA = NM_011346
| Mm_RefseqProtein = NP_035476
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 165899728
| Mm_GenLoc_end = 165909011
| Mm_Uniprot = Q3TA36
}}
}}
'''Selectin L (lymphocyte adhesion molecule 1)''', also known as '''SELL''', 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 = SELL is a cell surface component that is a member of a family of adhesion/homing receptors which play important roles in leukocyte-endothelial cell interactions. The molecule is composed of multiple domains: one homologous to lectins, one to epidermal growth factor, and two to the consensus repeat units found in C3/C4 binding proteins.<ref>{{cite web | title = Entrez Gene: SELL selectin L (lymphocyte adhesion molecule 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6402| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ryan US, Worthington RE |title=Cell-cell contact mechanisms. |journal=Curr. Opin. Immunol. |volume=4 |issue= 1 |pages= 33-7 |year= 1992 |pmid= 1375831 |doi= }}
*{{cite journal | author=Nicholson IC |title=CD62L (L-selectin). |journal=J. Biol. Regul. Homeost. Agents |volume=16 |issue= 2 |pages= 144-6 |year= 2003 |pmid= 12144128 |doi= }}
*{{cite journal | author=Ivetic A, Ridley AJ |title=The telling tail of L-selectin. |journal=Biochem. Soc. Trans. |volume=32 |issue= Pt 6 |pages= 1118-21 |year= 2005 |pmid= 15506984 |doi= 10.1042/BST0321118 }}
*{{cite journal | author=Lasky LA, Singer MS, Dowbenko D, ''et al.'' |title=An endothelial ligand for L-selectin is a novel mucin-like molecule. |journal=Cell |volume=69 |issue= 6 |pages= 927-38 |year= 1992 |pmid= 1376638 |doi= }}
*{{cite journal | author=Ord DC, Ernst TJ, Zhou LJ, ''et al.'' |title=Structure of the gene encoding the human leukocyte adhesion molecule-1 (TQ1, Leu-8) of lymphocytes and neutrophils. |journal=J. Biol. Chem. |volume=265 |issue= 14 |pages= 7760-7 |year= 1990 |pmid= 1692315 |doi= }}
*{{cite journal | author=Bevilacqua M, Butcher E, Furie B, ''et al.'' |title=Selectins: a family of adhesion receptors. |journal=Cell |volume=67 |issue= 2 |pages= 233 |year= 1991 |pmid= 1717161 |doi= }}
*{{cite journal | author=Tedder TF, Isaacs CM, Ernst TJ, ''et al.'' |title=Isolation and chromosomal localization of cDNAs encoding a novel human lymphocyte cell surface molecule, LAM-1. Homology with the mouse lymphocyte homing receptor and other human adhesion proteins. |journal=J. Exp. Med. |volume=170 |issue= 1 |pages= 123-33 |year= 1989 |pmid= 2473156 |doi= }}
*{{cite journal | author=Camerini D, James SP, Stamenkovic I, Seed B |title=Leu-8/TQ1 is the human equivalent of the Mel-14 lymph node homing receptor. |journal=Nature |volume=342 |issue= 6245 |pages= 78-82 |year= 1989 |pmid= 2509939 |doi= 10.1038/342078a0 }}
*{{cite journal | author=Bowen BR, Nguyen T, Lasky LA |title=Characterization of a human homologue of the murine peripheral lymph node homing receptor. |journal=J. Cell Biol. |volume=109 |issue= 1 |pages= 421-7 |year= 1989 |pmid= 2663882 |doi= }}
*{{cite journal | author=Siegelman MH, Weissman IL |title=Human homologue of mouse lymph node homing receptor: evolutionary conservation at tandem cell interaction domains. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 14 |pages= 5562-6 |year= 1989 |pmid= 2664786 |doi= }}
*{{cite journal | author=Bajorath J, Aruffo A |title=A template for generation and comparison of three-dimensional selectin models. |journal=Biochem. Biophys. Res. Commun. |volume=216 |issue= 3 |pages= 1018-23 |year= 1995 |pmid= 7488174 |doi= 10.1006/bbrc.1995.2722 }}
*{{cite journal | author=Dianzani U, Bragardo M, Buonfiglio D, ''et al.'' |title=Modulation of CD4 lateral interaction with lymphocyte surface molecules induced by HIV-1 gp120. |journal=Eur. J. Immunol. |volume=25 |issue= 5 |pages= 1306-11 |year= 1995 |pmid= 7539755 |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=Brenner B, Gulbins E, Schlottmann K, ''et al.'' |title=L-selectin activates the Ras pathway via the tyrosine kinase p56lck. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 26 |pages= 15376-81 |year= 1997 |pmid= 8986819 |doi= }}
*{{cite journal | author=Zöllner O, Lenter MC, Blanks JE, ''et al.'' |title=L-selectin from human, but not from mouse neutrophils binds directly to E-selectin. |journal=J. Cell Biol. |volume=136 |issue= 3 |pages= 707-16 |year= 1997 |pmid= 9024699 |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=Prakobphol A, Thomsson KA, Hansson GC, ''et al.'' |title=Human low-molecular-weight salivary mucin expresses the sialyl lewisx determinant and has L-selectin ligand activity. |journal=Biochemistry |volume=37 |issue= 14 |pages= 4916-27 |year= 1998 |pmid= 9538010 |doi= 10.1021/bi972612a }}
*{{cite journal | author=Sassetti C, Tangemann K, Singer MS, ''et al.'' |title=Identification of podocalyxin-like protein as a high endothelial venule ligand for L-selectin: parallels to CD34. |journal=J. Exp. Med. |volume=187 |issue= 12 |pages= 1965-75 |year= 1998 |pmid= 9625756 |doi= }}
*{{cite journal | author=Malhotra R, Ward M, Sim RB, Bird MI |title=Identification of human complement Factor H as a ligand for L-selectin. |journal=Biochem. J. |volume=341 ( Pt 1) |issue= |pages= 61-9 |year= 1999 |pmid= 10377245 |doi= }}
}}
{{refend}}
{{protein-stub}}
end log.
