Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 07:25, 19 November 2007 (UTC)
[edit]Proteins without matches (7)
[edit]Proteins with a High Potential Match (6)
[edit]Redirected Proteins (12)
[edit]Manual Inspection (Page not found) (13)
[edit]
Protein Status Grid - Date: 07:25, 19 November 2007 (UTC)
[edit]Vebose Log - Date: 07:25, 19 November 2007 (UTC)
[edit]- INFO: Beginning work on APLP2... {November 18, 2007 10:59:22 PM PST}
- SEARCH REDIRECT: Control Box Found: APLP2 {November 18, 2007 10:59:59 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:00:02 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:00:02 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:00:02 PM PST}
- UPDATED: Updated protein page: APLP2 {November 18, 2007 11:00:08 PM PST}
- INFO: Beginning work on ASS1... {November 18, 2007 11:00:09 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:00:35 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_ASS1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2nz2.
| PDB = {{PDB2|2nz2}}
| Name = Argininosuccinate synthetase 1
| HGNCid = 758
| Symbol = ASS1
| AltSymbols =; ASS; CTLN1
| OMIM = 603470
| ECnumber =
| Homologene = 6899
| MGIid = 88090
| GeneAtlas_image1 = PBB_GE_ASS1_207076_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004055 |text = argininosuccinate synthase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000050 |text = urea cycle}} {{GNF_GO|id=GO:0006526 |text = arginine biosynthetic process}} {{GNF_GO|id=GO:0008652 |text = amino acid biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 445
| Hs_Ensembl = ENSG00000130707
| Hs_RefseqProtein = NP_000041
| Hs_RefseqmRNA = NM_000050
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 132310137
| Hs_GenLoc_end = 132366482
| Hs_Uniprot = P00966
| Mm_EntrezGene = 11898
| Mm_Ensembl = ENSMUSG00000076441
| Mm_RefseqmRNA = NM_007494
| Mm_RefseqProtein = NP_031520
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 31292216
| Mm_GenLoc_end = 31342681
| Mm_Uniprot = Q3UEJ7
}}
}}
'''Argininosuccinate synthetase 1''', also known as '''ASS1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ASS1 argininosuccinate synthetase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=445| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene catalyzes the penultimate step of the arginine biosynthetic pathway. There are approximately 10 to 14 copies of this gene including the pseudogenes scattered across the human genome, among which the one located on chromosome 9 appears to be the only functional gene for argininosuccinate synthetase. Mutations in the chromosome 9 copy of ASS cause citrullinemia. Two transcript variants encoding the same protein have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ASS1 argininosuccinate synthetase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=445| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Beaudet AL, O'Brien WE, Bock HG, ''et al.'' |title=The human argininosuccinate synthetase locus and citrullinemia. |journal=Adv. Hum. Genet. |volume=15 |issue= |pages= 161-96, 291-2 |year= 1986 |pmid= 3513483 |doi= }}
*{{cite journal | author=Ikeda S |title=[Recent advances of the treatment in metabolic disorders] |journal=Rinsho Shinkeigaku |volume=40 |issue= 12 |pages= 1264-6 |year= 2001 |pmid= 11464474 |doi= }}
*{{cite journal | author=Carritt B, Goldfarb PS, Hooper ML, Slack C |title=Chromosome assignment of a human gene for argininosuccinate synthetase expression in Chinese hamsterxhuman somatic cell hybrids. |journal=Exp. Cell Res. |volume=106 |issue= 1 |pages= 71-8 |year= 1977 |pmid= 852520 |doi= }}
*{{cite journal | author=Carritt B |title=Somatic cell genetic evidence for the presence of a gene for citrullinemia on human chromosome 9. |journal=Cytogenet. Cell Genet. |volume=19 |issue= 1 |pages= 44-8 |year= 1977 |pmid= 891260 |doi= }}
*{{cite journal | author=Dhanakoti SN, Brosnan ME, Herzberg GR, Brosnan JT |title=Cellular and subcellular localization of enzymes of arginine metabolism in rat kidney. |journal=Biochem. J. |volume=282 ( Pt 2) |issue= |pages= 369-75 |year= 1992 |pmid= 1312326 |doi= }}
*{{cite journal | author=Wakui H, Komatsuda A, Itoh H, ''et al.'' |title=Renal argininosuccinate synthetase: purification, immunohistochemical localization, and elastin-binding property. |journal=Ren. Physiol. Biochem. |volume=15 |issue= 1 |pages= 1-9 |year= 1992 |pmid= 1372742 |doi= }}
*{{cite journal | author=Kobayashi K, Rosenbloom C, Beaudet AL, O'Brien WE |title=Additional mutations in argininosuccinate synthetase causing citrullinemia. |journal=Mol. Biol. Med. |volume=8 |issue= 1 |pages= 95-100 |year= 1991 |pmid= 1943692 |doi= }}
*{{cite journal | author=Kobayashi K, Jackson MJ, Tick DB, ''et al.'' |title=Heterogeneity of mutations in argininosuccinate synthetase causing human citrullinemia. |journal=J. Biol. Chem. |volume=265 |issue= 19 |pages= 11361-7 |year= 1990 |pmid= 2358466 |doi= }}
*{{cite journal | author=Isashiki Y, Noda T, Kobayashi K, ''et al.'' |title=Identification of essential arginine residue(s) for Mg-ATP binding of human argininosuccinate synthetase. |journal=Protein Seq. Data Anal. |volume=2 |issue= 4 |pages= 283-7 |year= 1989 |pmid= 2788888 |doi= }}
*{{cite journal | author=Jinno Y, Nomiyama H, Matuo S, ''et al.'' |title=Structure of the 5' end region of the human argininosuccinate synthetase gene. |journal=J. Inherit. Metab. Dis. |volume=8 |issue= 3 |pages= 157-9 |year= 1987 |pmid= 3027451 |doi= }}
*{{cite journal | author=Freytag SO, Beaudet AL, Bock HG, O'Brien WE |title=Molecular structure of the human argininosuccinate synthetase gene: occurrence of alternative mRNA splicing. |journal=Mol. Cell. Biol. |volume=4 |issue= 10 |pages= 1978-84 |year= 1985 |pmid= 6095035 |doi= }}
*{{cite journal | author=Bock HG, Su TS, O'Brien WE, Beaudet AL |title=Sequence for human argininosuccinate synthetase cDNA. |journal=Nucleic Acids Res. |volume=11 |issue= 18 |pages= 6505-12 |year= 1983 |pmid= 6194510 |doi= }}
*{{cite journal | author=Freytag SO, Bock HG, Beaudet AL, O'Brien WE |title=Molecular structures of human argininosuccinate synthetase pseudogenes. Evolutionary and mechanistic implications. |journal=J. Biol. Chem. |volume=259 |issue= 5 |pages= 3160-6 |year= 1984 |pmid= 6321498 |doi= }}
*{{cite journal | author=Kobayashi K, Kakinoki H, Fukushige T, ''et al.'' |title=Nature and frequency of mutations in the argininosuccinate synthetase gene that cause classical citrullinemia. |journal=Hum. Genet. |volume=96 |issue= 4 |pages= 454-63 |year= 1995 |pmid= 7557970 |doi= }}
*{{cite journal | author=Kobayashi K, Shaheen N, Terazono H, Saheki T |title=Mutations in argininosuccinate synthetase mRNA of Japanese patients, causing classical citrullinemia. |journal=Am. J. Hum. Genet. |volume=55 |issue= 6 |pages= 1103-12 |year= 1994 |pmid= 7977368 |doi= }}
*{{cite journal | author=Shaheen N, Kobayashi K, Terazono H, ''et al.'' |title=Characterization of human wild-type and mutant argininosuccinate synthetase proteins expressed in bacterial cells. |journal=Enzyme Protein |volume=48 |issue= 5-6 |pages= 251-64 |year= 1996 |pmid= 8792870 |doi= }}
*{{cite journal | author=Gress TM, Müller-Pillasch F, Geng M, ''et al.'' |title=A pancreatic cancer-specific expression profile. |journal=Oncogene |volume=13 |issue= 8 |pages= 1819-30 |year= 1996 |pmid= 8895530 |doi= }}
*{{cite journal | author=Ji H, Reid GE, Moritz RL, ''et al.'' |title=A two-dimensional gel database of human colon carcinoma proteins. |journal=Electrophoresis |volume=18 |issue= 3-4 |pages= 605-13 |year= 1997 |pmid= 9150948 |doi= 10.1002/elps.1150180344 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GSR... {November 18, 2007 11:00:35 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:00:59 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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_GSR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bwc.
| PDB = {{PDB2|1bwc}}, {{PDB2|1dnc}}, {{PDB2|1gra}}, {{PDB2|1grb}}, {{PDB2|1gre}}, {{PDB2|1grf}}, {{PDB2|1grg}}, {{PDB2|1grt}}, {{PDB2|1gsn}}, {{PDB2|1k4q}}, {{PDB2|1xan}}, {{PDB2|2aaq}}, {{PDB2|2gh5}}, {{PDB2|2grt}}, {{PDB2|3grs}}, {{PDB2|3grt}}, {{PDB2|4gr1}}, {{PDB2|4grt}}, {{PDB2|5grt}}
| Name = Glutathione reductase
| HGNCid = 4623
| Symbol = GSR
| AltSymbols =; MGC78522
| OMIM = 138300
| ECnumber =
| Homologene = 531
| MGIid = 95804
| GeneAtlas_image1 = PBB_GE_GSR_205770_at_tn.png
| Function = {{GNF_GO|id=GO:0004362 |text = glutathione-disulfide reductase activity}} {{GNF_GO|id=GO:0015036 |text = disulfide oxidoreductase activity}} {{GNF_GO|id=GO:0050660 |text = FAD binding}} {{GNF_GO|id=GO:0050661 |text = NADP binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006749 |text = glutathione metabolic process}} {{GNF_GO|id=GO:0045454 |text = cell redox homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2936
| Hs_Ensembl = ENSG00000104687
| Hs_RefseqProtein = NP_000628
| Hs_RefseqmRNA = NM_000637
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 30656549
| Hs_GenLoc_end = 30704894
| Hs_Uniprot = P00390
| Mm_EntrezGene = 14782
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_010344
| Mm_RefseqProtein = NP_034474
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Glutathione reductase''', also known as '''GSR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GSR glutathione reductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2936| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sinet PM, Bresson JL, Couturier J, ''et al.'' |title=[Possible localization of the glutathione reductase (EC 1.6.4.2) on the 8p21 band] |journal=Ann. Genet. |volume=20 |issue= 1 |pages= 13-7 |year= 1977 |pmid= 302667 |doi= }}
*{{cite journal | author=Krohne-Ehrich G, Schirmer RH, Untucht-Grau R |title=Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide. |journal=Eur. J. Biochem. |volume=80 |issue= 1 |pages= 65-71 |year= 1978 |pmid= 923580 |doi= }}
*{{cite journal | author=Loos H, Roos D, Weening R, Houwerzijl J |title=Familial deficiency of glutathione reductase in human blood cells. |journal=Blood |volume=48 |issue= 1 |pages= 53-62 |year= 1976 |pmid= 947404 |doi= }}
*{{cite journal | author=Tutic M, Lu XA, Schirmer RH, Werner D |title=Cloning and sequencing of mammalian glutathione reductase cDNA. |journal=Eur. J. Biochem. |volume=188 |issue= 3 |pages= 523-8 |year= 1990 |pmid= 2185014 |doi= }}
*{{cite journal | author=Palmer EJ, MacManus JP, Mutus B |title=Inhibition of glutathione reductase by oncomodulin. |journal=Arch. Biochem. Biophys. |volume=277 |issue= 1 |pages= 149-54 |year= 1990 |pmid= 2306116 |doi= }}
*{{cite journal | author=Arnold HH, Heinze H |title=Treatment of human peripheral lymphocytes with concanavalin A activates expression of glutathione reductase. |journal=FEBS Lett. |volume=267 |issue= 2 |pages= 189-92 |year= 1990 |pmid= 2379581 |doi= }}
*{{cite journal | author=Karplus PA, Schulz GE |title=Refined structure of glutathione reductase at 1.54 A resolution. |journal=J. Mol. Biol. |volume=195 |issue= 3 |pages= 701-29 |year= 1987 |pmid= 3656429 |doi= }}
*{{cite journal | author=Pai EF, Schulz GE |title=The catalytic mechanism of glutathione reductase as derived from x-ray diffraction analyses of reaction intermediates. |journal=J. Biol. Chem. |volume=258 |issue= 3 |pages= 1752-7 |year= 1983 |pmid= 6822532 |doi= }}
*{{cite journal | author=Krauth-Siegel RL, Blatterspiel R, Saleh M, ''et al.'' |title=Glutathione reductase from human erythrocytes. The sequences of the NADPH domain and of the interface domain. |journal=Eur. J. Biochem. |volume=121 |issue= 2 |pages= 259-67 |year= 1982 |pmid= 7060551 |doi= }}
*{{cite journal | author=Thieme R, Pai EF, Schirmer RH, Schulz GE |title=Three-dimensional structure of glutathione reductase at 2 A resolution. |journal=J. Mol. Biol. |volume=152 |issue= 4 |pages= 763-82 |year= 1982 |pmid= 7334521 |doi= }}
*{{cite journal | author=Huang J, Philbert MA |title=Distribution of glutathione and glutathione-related enzyme systems in mitochondria and cytosol of cultured cerebellar astrocytes and granule cells. |journal=Brain Res. |volume=680 |issue= 1-2 |pages= 16-22 |year= 1995 |pmid= 7663973 |doi= }}
*{{cite journal | author=Savvides SN, Karplus PA |title=Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor. |journal=J. Biol. Chem. |volume=271 |issue= 14 |pages= 8101-7 |year= 1996 |pmid= 8626496 |doi= }}
*{{cite journal | author=Nordhoff A, Tziatzios C, van den Broek JA, ''et al.'' |title=Denaturation and reactivation of dimeric human glutathione reductase--an assay for folding inhibitors. |journal=Eur. J. Biochem. |volume=245 |issue= 2 |pages= 273-82 |year= 1997 |pmid= 9151953 |doi= }}
*{{cite journal | author=Stoll VS, Simpson SJ, Krauth-Siegel RL, ''et al.'' |title=Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. |journal=Biochemistry |volume=36 |issue= 21 |pages= 6437-47 |year= 1997 |pmid= 9174360 |doi= 10.1021/bi963074p }}
*{{cite journal | author=Becker K, Savvides SN, Keese M, ''et al.'' |title=Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers. |journal=Nat. Struct. Biol. |volume=5 |issue= 4 |pages= 267-71 |year= 1998 |pmid= 9546215 |doi= }}
*{{cite journal | author=Kelner MJ, Montoya MA |title=Structural organization of the human glutathione reductase gene: determination of correct cDNA sequence and identification of a mitochondrial leader sequence. |journal=Biochem. Biophys. Res. Commun. |volume=269 |issue= 2 |pages= 366-8 |year= 2000 |pmid= 10708558 |doi= 10.1006/bbrc.2000.2267 }}
*{{cite journal | author=Qanungo S, Mukherjea M |title=Ontogenic profile of some antioxidants and lipid peroxidation in human placental and fetal tissues. |journal=Mol. Cell. Biochem. |volume=215 |issue= 1-2 |pages= 11-9 |year= 2001 |pmid= 11204445 |doi= }}
*{{cite journal | author=Berry Y, Truscott RJ |title=The presence of a human UV filter within the lens represents an oxidative stress. |journal=Exp. Eye Res. |volume=72 |issue= 4 |pages= 411-21 |year= 2001 |pmid= 11273669 |doi= 10.1006/exer.2000.0970 }}
*{{cite journal | author=Rhie G, Shin MH, Seo JY, ''et al.'' |title=Aging- and photoaging-dependent changes of enzymic and nonenzymic antioxidants in the epidermis and dermis of human skin in vivo. |journal=J. Invest. Dermatol. |volume=117 |issue= 5 |pages= 1212-7 |year= 2001 |pmid= 11710935 |doi= 10.1046/j.0022-202x.2001.01469.x }}
*{{cite journal | author=Zatorska A, Józwiak Z |title=Involvement of glutathione and glutathione-related enzymes in the protection of normal and trisomic human fibroblasts against daunorubicin. |journal=Cell Biol. Int. |volume=26 |issue= 5 |pages= 383-91 |year= 2003 |pmid= 12095224 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GTF2F2... {November 18, 2007 11:00:59 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:01:25 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
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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_GTF2F2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bby.
| PDB = {{PDB2|1bby}}, {{PDB2|1f3u}}, {{PDB2|2bby}}
| Name = General transcription factor IIF, polypeptide 2, 30kDa
| HGNCid = 4653
| Symbol = GTF2F2
| AltSymbols =; BTF4; TFIIF; RAP30; TF2F2
| OMIM = 189969
| ECnumber =
| Homologene = 37884
| MGIid = 1915955
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004386 |text = helicase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016251 |text = general RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005674 |text = transcription factor TFIIF complex}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006367 |text = transcription initiation from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006368 |text = RNA elongation from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2963
| Hs_Ensembl = ENSG00000188342
| Hs_RefseqProtein = NP_004119
| Hs_RefseqmRNA = NM_004128
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 44592650
| Hs_GenLoc_end = 44756237
| Hs_Uniprot = P13984
| Mm_EntrezGene = 68705
| Mm_Ensembl = ENSMUSG00000067995
| Mm_RefseqmRNA = NM_026816
| Mm_RefseqProtein = NP_081092
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 74631517
| Mm_GenLoc_end = 74745016
| Mm_Uniprot = Q3UMJ4
}}
}}
'''General transcription factor IIF, polypeptide 2, 30kDa''', also known as '''GTF2F2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GTF2F2 general transcription factor IIF, polypeptide 2, 30kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2963| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kato H, Sumimoto H, Pognonec P, ''et al.'' |title=HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors. |journal=Genes Dev. |volume=6 |issue= 4 |pages= 655-66 |year= 1992 |pmid= 1559613 |doi= }}
*{{cite journal | author=Horikoshi M, Fujita H, Wang J, ''et al.'' |title=Nucleotide and amino acid sequence of RAP30. |journal=Nucleic Acids Res. |volume=19 |issue= 19 |pages= 5436 |year= 1991 |pmid= 1840667 |doi= }}
*{{cite journal | author=Sopta M, Burton ZF, Greenblatt J |title=Structure and associated DNA-helicase activity of a general transcription initiation factor that binds to RNA polymerase II. |journal=Nature |volume=341 |issue= 6241 |pages= 410-4 |year= 1989 |pmid= 2477704 |doi= 10.1038/341410a0 }}
*{{cite journal | author=Sopta M, Carthew RW, Greenblatt J |title=Isolation of three proteins that bind to mammalian RNA polymerase II. |journal=J. Biol. Chem. |volume=260 |issue= 18 |pages= 10353-60 |year= 1985 |pmid= 3860504 |doi= }}
*{{cite journal | author=Tan S, Aso T, Conaway RC, Conaway JW |title=Roles for both the RAP30 and RAP74 subunits of transcription factor IIF in transcription initiation and elongation by RNA polymerase II. |journal=J. Biol. Chem. |volume=269 |issue= 41 |pages= 25684-91 |year= 1994 |pmid= 7929273 |doi= }}
*{{cite journal | author=Heng HH, Xiao H, Shi XM, ''et al.'' |title=Genes encoding general initiation factors for RNA polymerase II transcription are dispersed in the human genome. |journal=Hum. Mol. Genet. |volume=3 |issue= 1 |pages= 61-4 |year= 1994 |pmid= 8162052 |doi= }}
*{{cite journal | author=Yonaha M, Aso T, Kobayashi Y, ''et al.'' |title=Domain structure of a human general transcription initiation factor, TFIIF. |journal=Nucleic Acids Res. |volume=21 |issue= 2 |pages= 273-9 |year= 1993 |pmid= 8441635 |doi= }}
*{{cite journal | author=Tang H, Sun X, Reinberg D, Ebright RH |title=Protein-protein interactions in eukaryotic transcription initiation: structure of the preinitiation complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 3 |pages= 1119-24 |year= 1996 |pmid= 8577725 |doi= }}
*{{cite journal | author=Martin ML, Lieberman PM, Curran T |title=Fos-Jun dimerization promotes interaction of the basic region with TFIIE-34 and TFIIF. |journal=Mol. Cell. Biol. |volume=16 |issue= 5 |pages= 2110-8 |year= 1996 |pmid= 8628277 |doi= }}
*{{cite journal | author=Fang SM, Burton ZF |title=RNA polymerase II-associated protein (RAP) 74 binds transcription factor (TF) IIB and blocks TFIIB-RAP30 binding. |journal=J. Biol. Chem. |volume=271 |issue= 20 |pages= 11703-9 |year= 1996 |pmid= 8662660 |doi= }}
*{{cite journal | author=Dubrovskaya V, Lavigne AC, Davidson I, ''et al.'' |title=Distinct domains of hTAFII100 are required for functional interaction with transcription factor TFIIF beta (RAP30) and incorporation into the TFIID complex. |journal=EMBO J. |volume=15 |issue= 14 |pages= 3702-12 |year= 1996 |pmid= 8758937 |doi= }}
*{{cite journal | author=Rowlands JC, McEwan IJ, Gustafsson JA |title=Trans-activation by the human aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator proteins: direct interactions with basal transcription factors. |journal=Mol. Pharmacol. |volume=50 |issue= 3 |pages= 538-48 |year= 1996 |pmid= 8794892 |doi= }}
*{{cite journal | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605-10 |year= 1996 |pmid= 8849451 |doi= }}
*{{cite journal | author=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. |journal=Nature |volume=384 |issue= 6607 |pages= 375-8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 }}
*{{cite journal | author=Kojima S, Kobayashi A, Gotoh O, ''et al.'' |title=Transcriptional activation domain of human BTEB2, a GC box-binding factor. |journal=J. Biochem. |volume=121 |issue= 2 |pages= 389-96 |year= 1997 |pmid= 9089417 |doi= }}
*{{cite journal | author=Cujec TP, Cho H, Maldonado E, ''et al.'' |title=The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 1817-23 |year= 1997 |pmid= 9121429 |doi= }}
*{{cite journal | author=McEwan IJ, Gustafsson J |title=Interaction of the human androgen receptor transactivation function with the general transcription factor TFIIF. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 16 |pages= 8485-90 |year= 1997 |pmid= 9238003 |doi= }}
*{{cite journal | author=Newberry EP, Latifi T, Battaile JT, Towler DA |title=Structure-function analysis of Msx2-mediated transcriptional suppression. |journal=Biochemistry |volume=36 |issue= 34 |pages= 10451-62 |year= 1997 |pmid= 9265625 |doi= 10.1021/bi971008x }}
*{{cite journal | author=Liang G, Hai T |title=Characterization of human activating transcription factor 4, a transcriptional activator that interacts with multiple domains of cAMP-responsive element-binding protein (CREB)-binding protein. |journal=J. Biol. Chem. |volume=272 |issue= 38 |pages= 24088-95 |year= 1997 |pmid= 9295363 |doi= }}
*{{cite journal | author=Okamoto T, Yamamoto S, Watanabe Y, ''et al.'' |title=Analysis of the role of TFIIE in transcriptional regulation through structure-function studies of the TFIIEbeta subunit. |journal=J. Biol. Chem. |volume=273 |issue= 31 |pages= 19866-76 |year= 1998 |pmid= 9677423 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HOXB7... {November 18, 2007 11:01:26 PM PST}
- SEARCH REDIRECT: Control Box Found: HOXB7 {November 18, 2007 11:02:10 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:02:12 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:02:12 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:02:12 PM PST}
- UPDATED: Updated protein page: HOXB7 {November 18, 2007 11:02:20 PM PST}
- INFO: Beginning work on HPX... {November 18, 2007 11:02:20 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:02:39 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 = Hemopexin
| HGNCid = 5171
| Symbol = HPX
| AltSymbols =;
| OMIM = 142290
| ECnumber =
| Homologene = 511
| MGIid = 105112
| GeneAtlas_image1 = PBB_GE_HPX_39763_at_tn.png
| GeneAtlas_image2 = PBB_GE_HPX_210013_at_tn.png
| Function = {{GNF_GO|id=GO:0005488 |text = binding}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0015232 |text = heme transporter activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006879 |text = cellular iron ion homeostasis}} {{GNF_GO|id=GO:0015886 |text = heme transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3263
| Hs_Ensembl = ENSG00000110169
| Hs_RefseqProtein = NP_000604
| Hs_RefseqmRNA = NM_000613
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 6408858
| Hs_GenLoc_end = 6418830
| Hs_Uniprot = P02790
| Mm_EntrezGene = 15458
| Mm_Ensembl = ENSMUSG00000030895
| Mm_RefseqmRNA = NM_017371
| Mm_RefseqProtein = NP_059067
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 105465432
| Mm_GenLoc_end = 105473917
| Mm_Uniprot = Q3UKP2
}}
}}
'''Hemopexin''', also known as '''HPX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HPX hemopexin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3263| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Piccard H, Van den Steen PE, Opdenakker G |title=Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins. |journal=J. Leukoc. Biol. |volume=81 |issue= 4 |pages= 870-92 |year= 2007 |pmid= 17185359 |doi= 10.1189/jlb.1006629 }}
*{{cite journal | author=Morgan WT, Muller-Eberhard U, Lamola AA |title=Interaction of rabbit hemopexin with bilirubin. |journal=Biochim. Biophys. Acta |volume=532 |issue= 1 |pages= 57-64 |year= 1978 |pmid= 620056 |doi= }}
*{{cite journal | author=Liu HM, Atack JR, Rapoport SI |title=Immunohistochemical localization of intracellular plasma proteins in the human central nervous system. |journal=Acta Neuropathol. |volume=78 |issue= 1 |pages= 16-21 |year= 1989 |pmid= 2735186 |doi= }}
*{{cite journal | author=Smith A, Tatum FM, Muster P, ''et al.'' |title=Importance of ligand-induced conformational changes in hemopexin for receptor-mediated heme transport. |journal=J. Biol. Chem. |volume=263 |issue= 11 |pages= 5224-9 |year= 1988 |pmid= 2833500 |doi= }}
*{{cite journal | author=Altruda F, Poli V, Restagno G, Silengo L |title=Structure of the human hemopexin gene and evidence for intron-mediated evolution. |journal=J. Mol. Evol. |volume=27 |issue= 2 |pages= 102-8 |year= 1988 |pmid= 2842511 |doi= }}
*{{cite journal | author=Altruda F, Poli V, Restagno G, ''et al.'' |title=The primary structure of human hemopexin deduced from cDNA sequence: evidence for internal, repeating homology. |journal=Nucleic Acids Res. |volume=13 |issue= 11 |pages= 3841-59 |year= 1985 |pmid= 2989777 |doi= }}
*{{cite journal | author=Taketani S, Kohno H, Naitoh Y, Tokunaga R |title=Isolation of the hemopexin receptor from human placenta. |journal=J. Biol. Chem. |volume=262 |issue= 18 |pages= 8668-71 |year= 1987 |pmid= 3036819 |doi= }}
*{{cite journal | author=Law ML, Cai GY, Hartz JA, ''et al.'' |title=The hemopexin gene maps to the same location as the beta-globin gene cluster on human chromosome 11. |journal=Genomics |volume=3 |issue= 1 |pages= 48-52 |year= 1989 |pmid= 3220477 |doi= }}
*{{cite journal | author=Morgan WT, Alam J, Deaciuc V, ''et al.'' |title=Interaction of hemopexin with Sn-protoporphyrin IX, an inhibitor of heme oxygenase. Role for hemopexin in hepatic uptake of Sn-protoporphyrin IX and induction of mRNA for heme oxygenase. |journal=J. Biol. Chem. |volume=263 |issue= 17 |pages= 8226-31 |year= 1988 |pmid= 3372522 |doi= }}
*{{cite journal | author=Takahashi N, Takahashi Y, Putnam FW |title=Complete amino acid sequence of human hemopexin, the heme-binding protein of serum. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 1 |pages= 73-7 |year= 1985 |pmid= 3855550 |doi= }}
*{{cite journal | author=Takahashi N, Takahashi Y, Putnam FW |title=Structure of human hemopexin: O-glycosyl and N-glycosyl sites and unusual clustering of tryptophan residues. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 7 |pages= 2021-5 |year= 1984 |pmid= 6371807 |doi= }}
*{{cite journal | author=Frantíková V, Borvák J, Kluh I, Morávek L |title=Amino acid sequence of the N-terminal region of human hemopexin. |journal=FEBS Lett. |volume=178 |issue= 2 |pages= 213-6 |year= 1985 |pmid= 6510521 |doi= }}
*{{cite journal | author=Smith A, Alam J, Escriba PV, Morgan WT |title=Regulation of heme oxygenase and metallothionein gene expression by the heme analogs, cobalt-, and tin-protoporphyrin. |journal=J. Biol. Chem. |volume=268 |issue= 10 |pages= 7365-71 |year= 1993 |pmid= 8463269 |doi= }}
*{{cite journal | author=Morris CM, Candy JM, Edwardson JA, ''et al.'' |title=Evidence for the localization of haemopexin immunoreactivity in neurones in the human brain. |journal=Neurosci. Lett. |volume=149 |issue= 2 |pages= 141-4 |year= 1993 |pmid= 8474687 |doi= }}
*{{cite journal | author=Hrkal Z, Kuzelová K, Muller-Eberhard U, Stern R |title=Hyaluronan-binding properties of human serum hemopexin. |journal=FEBS Lett. |volume=383 |issue= 1-2 |pages= 72-4 |year= 1996 |pmid= 8612795 |doi= }}
*{{cite journal | author=Hunt RC, Hunt DM, Gaur N, Smith A |title=Hemopexin in the human retina: protection of the retina against heme-mediated toxicity. |journal=J. Cell. Physiol. |volume=168 |issue= 1 |pages= 71-80 |year= 1996 |pmid= 8647924 |doi= 10.1002/(SICI)1097-4652(199607)168:1<71::AID-JCP9>3.0.CO;2-5 }}
*{{cite journal | author=Miller YI, Smith A, Morgan WT, Shaklai N |title=Role of hemopexin in protection of low-density lipoprotein against hemoglobin-induced oxidation. |journal=Biochemistry |volume=35 |issue= 40 |pages= 13112-7 |year= 1996 |pmid= 8855948 |doi= 10.1021/bi960737u }}
*{{cite journal | author=Grinberg LN, O'Brien PJ, Hrkal Z |title=The effects of heme-binding proteins on the peroxidative and catalatic activities of hemin. |journal=Free Radic. Biol. Med. |volume=27 |issue= 1-2 |pages= 214-9 |year= 1999 |pmid= 10443938 |doi= }}
*{{cite journal | author=Nakajima S, Moriyama T, Hayashi H, ''et al.'' |title=Hemopexin as a carrier protein of tumor-localizing Ga-metalloporphyrin-ATN-2. |journal=Cancer Lett. |volume=149 |issue= 1-2 |pages= 221-6 |year= 2000 |pmid= 10737728 |doi= }}
*{{cite journal | author=Shipulina N, Smith A, Morgan WT |title=Heme binding by hemopexin: evidence for multiple modes of binding and functional implications. |journal=J. Protein Chem. |volume=19 |issue= 3 |pages= 239-48 |year= 2001 |pmid= 10981817 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HTR1B... {November 18, 2007 11:02:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:03:18 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 = 5-hydroxytryptamine (serotonin) receptor 1B
| HGNCid = 5287
| Symbol = HTR1B
| AltSymbols =; 5-HT1B; 5-HT1DB; HTR1D2; HTR1DB; S12
| OMIM = 182131
| ECnumber =
| Homologene = 669
| MGIid = 96274
| GeneAtlas_image1 = PBB_GE_HTR1B_210799_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004993 |text = serotonin receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007187 |text = G-protein signaling, coupled to cyclic nucleotide second messenger}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3351
| Hs_Ensembl = ENSG00000135312
| Hs_RefseqProtein = NP_000854
| Hs_RefseqmRNA = NM_000863
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 78228641
| Hs_GenLoc_end = 78229900
| Hs_Uniprot = P28222
| Mm_EntrezGene = 15551
| Mm_Ensembl = ENSMUSG00000049511
| Mm_RefseqmRNA = NM_010482
| Mm_RefseqProtein = NP_034612
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 81428110
| Mm_GenLoc_end = 81429270
| Mm_Uniprot = Q0VES5
}}
}}
'''5-hydroxytryptamine (serotonin) receptor 1B''', also known as '''HTR1B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HTR1B 5-hydroxytryptamine (serotonin) receptor 1B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3351| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Olivier B, van Oorschot R |title=5-HT1B receptors and aggression: a review. |journal=Eur. J. Pharmacol. |volume=526 |issue= 1-3 |pages= 207-17 |year= 2006 |pmid= 16310769 |doi= 10.1016/j.ejphar.2005.09.066 }}
*{{cite journal | author=Hamblin MW, Metcalf MA, McGuffin RW, Karpells S |title=Molecular cloning and functional characterization of a human 5-HT1B serotonin receptor: a homologue of the rat 5-HT1B receptor with 5-HT1D-like pharmacological specificity. |journal=Biochem. Biophys. Res. Commun. |volume=184 |issue= 2 |pages= 752-9 |year= 1992 |pmid= 1315531 |doi= }}
*{{cite journal | author=Veldman SA, Bienkowski MJ |title=Cloning and pharmacological characterization of a novel human 5-hydroxytryptamine1D receptor subtype. |journal=Mol. Pharmacol. |volume=42 |issue= 3 |pages= 439-44 |year= 1992 |pmid= 1328844 |doi= }}
*{{cite journal | author=Jin H, Oksenberg D, Ashkenazi A, ''et al.'' |title=Characterization of the human 5-hydroxytryptamine1B receptor. |journal=J. Biol. Chem. |volume=267 |issue= 9 |pages= 5735-8 |year= 1992 |pmid= 1348246 |doi= }}
*{{cite journal | author=Demchyshyn L, Sunahara RK, Miller K, ''et al.'' |title=A human serotonin 1D receptor variant (5HT1D beta) encoded by an intronless gene on chromosome 6. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 12 |pages= 5522-6 |year= 1992 |pmid= 1351684 |doi= }}
*{{cite journal | author=Levy FO, Gudermann T, Perez-Reyes E, ''et al.'' |title=Molecular cloning of a human serotonin receptor (S12) with a pharmacological profile resembling that of the 5-HT1D subtype. |journal=J. Biol. Chem. |volume=267 |issue= 11 |pages= 7553-62 |year= 1992 |pmid= 1559993 |doi= }}
*{{cite journal | author=Weinshank RL, Zgombick JM, Macchi MJ, ''et al.'' |title=Human serotonin 1D receptor is encoded by a subfamily of two distinct genes: 5-HT1D alpha and 5-HT1D beta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 8 |pages= 3630-4 |year= 1992 |pmid= 1565658 |doi= }}
*{{cite journal | author=Mochizuki D, Yuyama Y, Tsujita R, ''et al.'' |title=Cloning and expression of the human 5-HT1B-type receptor gene. |journal=Biochem. Biophys. Res. Commun. |volume=185 |issue= 2 |pages= 517-23 |year= 1992 |pmid= 1610347 |doi= }}
*{{cite journal | author=Nöthen MM, Erdmann J, Shimron-Abarbanell D, Propping P |title=Identification of genetic variation in the human serotonin 1D beta receptor gene. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 2 |pages= 1194-200 |year= 1995 |pmid= 7802650 |doi= }}
*{{cite journal | author=Ng GY, George SR, Zastawny RL, ''et al.'' |title=Human serotonin1B receptor expression in Sf9 cells: phosphorylation, palmitoylation, and adenylyl cyclase inhibition. |journal=Biochemistry |volume=32 |issue= 43 |pages= 11727-33 |year= 1993 |pmid= 8218242 |doi= }}
*{{cite journal | author=Bouchelet I, Cohen Z, Case B, ''et al.'' |title=Differential expression of sumatriptan-sensitive 5-hydroxytryptamine receptors in human trigeminal ganglia and cerebral blood vessels. |journal=Mol. Pharmacol. |volume=50 |issue= 2 |pages= 219-23 |year= 1996 |pmid= 8700126 |doi= }}
*{{cite journal | author=Sanders AR, Cao Q, Taylor J, ''et al.'' |title=Genetic diversity of the human serotonin receptor 1B (HTR1B) gene. |journal=Genomics |volume=72 |issue= 1 |pages= 1-14 |year= 2001 |pmid= 11247661 |doi= 10.1006/geno.2000.6411 }}
*{{cite journal | author=Varnäs K, Hall H, Bonaventure P, Sedvall G |title=Autoradiographic mapping of 5-HT(1B) and 5-HT(1D) receptors in the post mortem human brain using [(3)H]GR 125743. |journal=Brain Res. |volume=915 |issue= 1 |pages= 47-57 |year= 2001 |pmid= 11578619 |doi= }}
*{{cite journal | author=Salim K, Fenton T, Bacha J, ''et al.'' |title=Oligomerization of G-protein-coupled receptors shown by selective co-immunoprecipitation. |journal=J. Biol. Chem. |volume=277 |issue= 18 |pages= 15482-5 |year= 2002 |pmid= 11854302 |doi= 10.1074/jbc.M201539200 }}
*{{cite journal | author=Hasegawa Y, Higuchi S, Matsushita S, Miyaoka H |title=Association of a polymorphism of the serotonin 1B receptor gene and alcohol dependence with inactive aldehyde dehydrogenase-2. |journal=Journal of neural transmission (Vienna, Austria : 1996) |volume=109 |issue= 4 |pages= 513-21 |year= 2002 |pmid= 11956970 |doi= 10.1007/s007020200042 }}
*{{cite journal | author=Hawi Z, Dring M, Kirley A, ''et al.'' |title=Serotonergic system and attention deficit hyperactivity disorder (ADHD): a potential susceptibility locus at the 5-HT(1B) receptor gene in 273 nuclear families from a multi-centre sample. |journal=Mol. Psychiatry |volume=7 |issue= 7 |pages= 718-25 |year= 2003 |pmid= 12192616 |doi= 10.1038/sj.mp.4001048 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Huang YY, Oquendo MA, Friedman JM, ''et al.'' |title=Substance abuse disorder and major depression are associated with the human 5-HT1B receptor gene (HTR1B) G861C polymorphism. |journal=Neuropsychopharmacology |volume=28 |issue= 1 |pages= 163-9 |year= 2003 |pmid= 12496953 |doi= 10.1038/sj.npp.1300000 }}
*{{cite journal | author=Quist JF, Barr CL, Schachar R, ''et al.'' |title=The serotonin 5-HT1B receptor gene and attention deficit hyperactivity disorder. |journal=Mol. Psychiatry |volume=8 |issue= 1 |pages= 98-102 |year= 2003 |pmid= 12556913 |doi= 10.1038/sj.mp.4001244 }}
*{{cite journal | author=Sinha R, Cloninger CR, Parsian A |title=Linkage disequilibrium and haplotype analysis between serotonin receptor 1B gene variations and subtypes of alcoholism. |journal=Am. J. Med. Genet. B Neuropsychiatr. Genet. |volume=121 |issue= 1 |pages= 83-8 |year= 2003 |pmid= 12898580 |doi= 10.1002/ajmg.b.20064 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IFNA2... {November 18, 2007 11:03:18 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:03:50 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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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_IFNA2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1itf.
| PDB = {{PDB2|1itf}}, {{PDB2|1rh2}}, {{PDB2|2hym}}
| Name = Interferon, alpha 2
| HGNCid = 5423
| Symbol = IFNA2
| AltSymbols =; IFNA; INFA2; MGC125764; MGC125765
| OMIM = 147562
| ECnumber =
| Homologene = 86655
| MGIid =
| GeneAtlas_image1 = PBB_GE_IFNA2_211338_at_tn.png
| Function = {{GNF_GO|id=GO:0005132 |text = interferon-alpha/beta receptor binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0009615 |text = response to virus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3440
| Hs_Ensembl = ENSG00000188379
| Hs_RefseqProtein = NP_000596
| Hs_RefseqmRNA = NM_000605
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 21374253
| Hs_GenLoc_end = 21375387
| Hs_Uniprot = P01563
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Interferon, alpha 2''', also known as '''IFNA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IFNA2 interferon, alpha 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3440| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Conti L, Fantuzzi L, Del Cornò M, ''et al.'' |title=Immunomodulatory effects of the HIV-1 gp120 protein on antigen presenting cells: implications for AIDS pathogenesis. |journal=Immunobiology |volume=209 |issue= 1-2 |pages= 99-115 |year= 2005 |pmid= 15481145 |doi= }}
*{{cite journal | author=Capobianchi MR, Ankel H, Ameglio F, ''et al.'' |title=Recombinant glycoprotein 120 of human immunodeficiency virus is a potent interferon inducer. |journal=AIDS Res. Hum. Retroviruses |volume=8 |issue= 5 |pages= 575-9 |year= 1992 |pmid= 1381203 |doi= }}
*{{cite journal | author=Olopade OI, Bohlander SK, Pomykala H, ''et al.'' |title=Mapping of the shortest region of overlap of deletions of the short arm of chromosome 9 associated with human neoplasia. |journal=Genomics |volume=14 |issue= 2 |pages= 437-43 |year= 1992 |pmid= 1385305 |doi= }}
*{{cite journal | author=Flores I, Mariano TM, Pestka S |title=Human interferon omega (omega) binds to the alpha/beta receptor. |journal=J. Biol. Chem. |volume=266 |issue= 30 |pages= 19875-7 |year= 1991 |pmid= 1834641 |doi= }}
*{{cite journal | author=Tyring SK, Cauda R, Tumbarello M, ''et al.'' |title=Synthetic peptides corresponding to sequences in HIV envelope gp41 and gp120 enhance in vitro production of interleukin-1 and tumor necrosis factor but depress production of interferon-alpha, interferon-gamma and interleukin-2. |journal=Viral Immunol. |volume=4 |issue= 1 |pages= 33-42 |year= 1991 |pmid= 1905933 |doi= }}
*{{cite journal | author=Adolf GR, Kalsner I, Ahorn H, ''et al.'' |title=Natural human interferon-alpha 2 is O-glycosylated. |journal=Biochem. J. |volume=276 ( Pt 2) |issue= |pages= 511-8 |year= 1991 |pmid= 2049076 |doi= }}
*{{cite journal | author=Stine KC, Bolognesi D, Weinhold KJ |title=Cytokine augmentation of human immunodeficiency virus type 1 (HIV-1) gp120-specific cellular cytotoxicity. |journal=Journal of biological response modifiers |volume=8 |issue= 5 |pages= 501-10 |year= 1989 |pmid= 2552026 |doi= }}
*{{cite journal | author=Oliver G, Balbás P, Valle F, ''et al.'' |title=[Cloning of human leukocyte interferon cDNA and a strategy for its production in E. coli] |journal=Rev. Latinoam. Microbiol. |volume=27 |issue= 2 |pages= 141-50 |year= 1986 |pmid= 3906813 |doi= }}
*{{cite journal | author=Streuli M, Nagata S, Weissmann C |title=At least three human type alpha interferons: structure of alpha 2. |journal=Science |volume=209 |issue= 4463 |pages= 1343-7 |year= 1980 |pmid= 6158094 |doi= }}
*{{cite journal | author=Allen G, Fantes KH |title=A family of structural genes for human lymphoblastoid (leukocyte-type) interferon. |journal=Nature |volume=287 |issue= 5781 |pages= 408-11 |year= 1981 |pmid= 6159537 |doi= }}
*{{cite journal | author=Goeddel DV, Yelverton E, Ullrich A, ''et al.'' |title=Human leukocyte interferon produced by E. coli is biologically active. |journal=Nature |volume=287 |issue= 5781 |pages= 411-6 |year= 1981 |pmid= 6159538 |doi= }}
*{{cite journal | author=Wetzel R |title=Assignment of the disulphide bonds of leukocyte interferon. |journal=Nature |volume=289 |issue= 5798 |pages= 606-7 |year= 1981 |pmid= 6162107 |doi= }}
*{{cite journal | author=Goeddel DV, Leung DW, Dull TJ, ''et al.'' |title=The structure of eight distinct cloned human leukocyte interferon cDNAs. |journal=Nature |volume=290 |issue= 5801 |pages= 20-6 |year= 1981 |pmid= 6163083 |doi= }}
*{{cite journal | author=Maeda S, McCandliss R, Gross M, ''et al.'' |title=Construction and identification of bacterial plasmids containing nucleotide sequence for human leukocyte interferon. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=77 |issue= 12 |pages= 7010-3 |year= 1981 |pmid= 6164056 |doi= }}
*{{cite journal | author=Lawn RM, Gross M, Houck CM, ''et al.'' |title=DNA sequence of a major human leukocyte interferon gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=78 |issue= 9 |pages= 5435-9 |year= 1982 |pmid= 6170983 |doi= }}
*{{cite journal | author=Weber H, Weissmann C |title=Formation of genes coding for hybrid proteins by recombination between related, cloned genes in E. coli. |journal=Nucleic Acids Res. |volume=11 |issue= 16 |pages= 5661-9 |year= 1983 |pmid= 6310510 |doi= }}
*{{cite journal | author=Ameglio F, Capobianchi MR, Castilletti C, ''et al.'' |title=Recombinant gp120 induces IL-10 in resting peripheral blood mononuclear cells; correlation with the induction of other cytokines. |journal=Clin. Exp. Immunol. |volume=95 |issue= 3 |pages= 455-8 |year= 1994 |pmid= 7511078 |doi= }}
*{{cite journal | author=Ankel H, Capobianchi MR, Castilletti C, Dianzani F |title=Interferon induction by HIV glycoprotein 120: role of the V3 loop. |journal=Virology |volume=205 |issue= 1 |pages= 34-43 |year= 1994 |pmid= 7526537 |doi= 10.1006/viro.1994.1617 }}
*{{cite journal | author=Nair MP, Chadha KC, Stadler I, ''et al.'' |title=Differential effects of human immunodeficiency virus type 1 envelope protein gp120 on interferon production by mononuclear cells from adults and neonates. |journal=Clin. Diagn. Lab. Immunol. |volume=2 |issue= 4 |pages= 434-8 |year= 1995 |pmid= 7583919 |doi= }}
*{{cite journal | author=Lee N, Ni D, Brissette R, ''et al.'' |title=Interferon-alpha 2 variants in the human genome. |journal=J. Interferon Cytokine Res. |volume=15 |issue= 4 |pages= 341-9 |year= 1995 |pmid= 7627809 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ITK... {November 18, 2007 11:03:50 PM PST}
- SEARCH REDIRECT: Control Box Found: ITK (gene) {November 18, 2007 11:04:26 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:04:28 PM PST}
- SKIP SUMMARY: SKIPPING Summary, No Errors. {November 18, 2007 11:04:28 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:04:28 PM PST}
- UPDATED: Updated protein page: ITK (gene) {November 18, 2007 11:04:34 PM PST}
- INFO: Beginning work on KLKB1... {November 18, 2007 11:04:34 PM PST}
- SEARCH REDIRECT: Control Box Found: KLKB1 {November 18, 2007 11:04:56 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:04:57 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:04:57 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:04:57 PM PST}
- UPDATED: Updated protein page: KLKB1 {November 18, 2007 11:05:07 PM PST}
- INFO: Beginning work on LHB... {November 18, 2007 11:05:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:05:33 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Luteinizing hormone beta polypeptide
| HGNCid = 6584
| Symbol = LHB
| AltSymbols =; CGB4; LSH-B; hLHB
| OMIM = 152780
| ECnumber =
| Homologene = 81806
| MGIid = 96782
| GeneAtlas_image1 = PBB_GE_LHB_214471_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007530 |text = sex determination}} {{GNF_GO|id=GO:0008584 |text = male gonad development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3972
| Hs_Ensembl = ENSG00000104826
| Hs_RefseqProtein = NP_000885
| Hs_RefseqmRNA = NM_000894
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 54211049
| Hs_GenLoc_end = 54212159
| Hs_Uniprot = P01229
| Mm_EntrezGene = 16866
| Mm_Ensembl = ENSMUSG00000038194
| Mm_RefseqmRNA = NM_008497
| Mm_RefseqProtein = NP_032523
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 45288988
| Mm_GenLoc_end = 45289896
| Mm_Uniprot = Q3UUG9
}}
}}
'''Luteinizing hormone beta polypeptide''', also known as '''LHB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LHB luteinizing hormone beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3972| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the glycoprotein hormone beta chain family and encodes the beta subunit of luteinizing hormone (LH). Glycoprotein hormones are heterodimers consisting of a common alpha subunit and an unique beta subunit which confers biological specificity. LH is expressed in the pituitary gland and promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids. The genes for the beta chains of chorionic gonadotropin and for luteinizing hormone are contiguous on chromosome 19q13.3. Mutations in this gene are associated with hypogonadism which is characterized by infertility and pseudohermaphroditism.<ref name="entrez">{{cite web | title = Entrez Gene: LHB luteinizing hormone beta polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3972| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sairam MR, Li CH |title=Human pituitary lutropin. Isolation, properties, and the complete amino acid sequence of the beta-subunit. |journal=Biochim. Biophys. Acta |volume=412 |issue= 1 |pages= 70-81 |year= 1976 |pmid= 1191677 |doi= }}
*{{cite journal | author=Keutmann HT, Hua QX, Weiss MA |title=Structure of a receptor-binding fragment from human luteinizing hormone beta-subunit determined by [1H]- and [15N]nuclear magnetic resonance spectroscopy. |journal=Mol. Endocrinol. |volume=6 |issue= 6 |pages= 904-13 |year= 1992 |pmid= 1495492 |doi= }}
*{{cite journal | author=Weiss J, Axelrod L, Whitcomb RW, ''et al.'' |title=Hypogonadism caused by a single amino acid substitution in the beta subunit of luteinizing hormone. |journal=N. Engl. J. Med. |volume=326 |issue= 3 |pages= 179-83 |year= 1992 |pmid= 1727547 |doi= }}
*{{cite journal | author=Weisshaar G, Hiyama J, Renwick AG, Nimtz M |title=NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin. |journal=Eur. J. Biochem. |volume=195 |issue= 1 |pages= 257-68 |year= 1991 |pmid= 1991473 |doi= }}
*{{cite journal | author=Jameson JL, Lindell CM, Habener JF |title=Evolution of different transcriptional start sites in the human luteinizing hormone and chorionic gonadotropin beta-subunit genes. |journal=DNA |volume=5 |issue= 3 |pages= 227-34 |year= 1986 |pmid= 2424697 |doi= }}
*{{cite journal | author=Keutmann HT, Charlesworth MC, Mason KA, ''et al.'' |title=A receptor-binding region in human choriogonadotropin/lutropin beta subunit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 7 |pages= 2038-42 |year= 1987 |pmid= 3470775 |doi= }}
*{{cite journal | author=Shome B, Parlow AF |title=The primary structure of the hormone-specific, beta subunit of human pituitary luteinizing hormone (hLH). |journal=J. Clin. Endocrinol. Metab. |volume=36 |issue= 3 |pages= 618-21 |year= 1973 |pmid= 4685398 |doi= }}
*{{cite journal | author=Closset J, Hennen G, Lequin RM |title=Human luteinizing hormone. The amino acid sequence of the subunit. |journal=FEBS Lett. |volume=29 |issue= 2 |pages= 97-100 |year= 1973 |pmid= 4719207 |doi= }}
*{{cite journal | author=Talmadge K, Vamvakopoulos NC, Fiddes JC |title=Evolution of the genes for the beta subunits of human chorionic gonadotropin and luteinizing hormone. |journal=Nature |volume=307 |issue= 5946 |pages= 37-40 |year= 1984 |pmid= 6690982 |doi= }}
*{{cite journal | author=Beitins IZ, Axelrod L, Ostrea T, ''et al.'' |title=Hypogonadism in a male with an immunologically active, biologically inactive luteinizing hormone: characterization of the abnormal hormone. |journal=J. Clin. Endocrinol. Metab. |volume=52 |issue= 6 |pages= 1143-9 |year= 1981 |pmid= 6785294 |doi= }}
*{{cite journal | author=Berger P, Kranewitter W, Madersbacher S, ''et al.'' |title=Eutopic production of human chorionic gonadotropin beta (hCG beta) and luteinizing hormone beta (hLH beta) in the human testis. |journal=FEBS Lett. |volume=343 |issue= 3 |pages= 229-33 |year= 1994 |pmid= 7513655 |doi= }}
*{{cite journal | author=Keutmann HT, Rubin DA |title=A subunit interaction site in human luteinizing hormone: identification by photoaffinity cross-linking. |journal=Endocrinology |volume=132 |issue= 3 |pages= 1305-12 |year= 1993 |pmid= 7679977 |doi= }}
*{{cite journal | author=Herrlich A, Kühn B, Grosse R, ''et al.'' |title=Involvement of Gs and Gi proteins in dual coupling of the luteinizing hormone receptor to adenylyl cyclase and phospholipase C. |journal=J. Biol. Chem. |volume=271 |issue= 28 |pages= 16764-72 |year= 1996 |pmid= 8663226 |doi= }}
*{{cite journal | author=Muyan M, Furuhashi M, Sugahara T, Boime I |title=The carboxy-terminal region of the beta-subunits of luteinizing hormone and chorionic gonadotropin differentially influence secretion and assembly of the heterodimers. |journal=Mol. Endocrinol. |volume=10 |issue= 12 |pages= 1678-87 |year= 1997 |pmid= 8961276 |doi= }}
*{{cite journal | author=Roy AC, Liao WX, Chen Y, ''et al.'' |title=Identification of seven novel mutations in LH beta-subunit gene by SSCP. |journal=Mol. Cell. Biochem. |volume=165 |issue= 2 |pages= 151-3 |year= 1997 |pmid= 8979264 |doi= }}
*{{cite journal | author=Liao WX, Roy AC, Chan C, ''et al.'' |title=A new molecular variant of luteinizing hormone associated with female infertility. |journal=Fertil. Steril. |volume=69 |issue= 1 |pages= 102-6 |year= 1998 |pmid= 9457942 |doi= }}
*{{cite journal | author=O'Connor JF, Kovalevskaya G, Birken S, ''et al.'' |title=The expression of the urinary forms of human luteinizing hormone beta fragment in various populations as assessed by a specific immunoradiometric assay. |journal=Hum. Reprod. |volume=13 |issue= 4 |pages= 826-35 |year= 1998 |pmid= 9619532 |doi= }}
*{{cite journal | author=Takahashi K, Kurioka H, Ozaki T, ''et al.'' |title=Increased prevalence of luteinizing hormone beta-subunit variant in Japanese infertility patients. |journal=Hum. Reprod. |volume=13 |issue= 12 |pages= 3338-44 |year= 1999 |pmid= 9886510 |doi= }}
*{{cite journal | author=Elter K, Erel CT, Cine N, ''et al.'' |title=Role of the mutations Trp8 => Arg and Ile15 => Thr of the human luteinizing hormone beta-subunit in women with polycystic ovary syndrome. |journal=Fertil. Steril. |volume=71 |issue= 3 |pages= 425-30 |year= 1999 |pmid= 10065776 |doi= }}
*{{cite journal | author=Jiang M, Pakarinen P, Zhang FP, ''et al.'' |title=A common polymorphic allele of the human luteinizing hormone beta-subunit gene: additional mutations and differential function of the promoter sequence. |journal=Hum. Mol. Genet. |volume=8 |issue= 11 |pages= 2037-46 |year= 1999 |pmid= 10484773 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MAPK10... {November 18, 2007 11:13:29 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:14:16 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 = PBB_Protein_MAPK10_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jnk.
| PDB = {{PDB2|1jnk}}, {{PDB2|1pmn}}, {{PDB2|1pmq}}, {{PDB2|1pmu}}, {{PDB2|1pmv}}, {{PDB2|1ukh}}, {{PDB2|1uki}}, {{PDB2|2b1p}}, {{PDB2|2exc}}, {{PDB2|2g01}}, {{PDB2|2gmx}}, {{PDB2|2h96}}, {{PDB2|2no3}}, {{PDB2|2o0u}}, {{PDB2|2o2u}}, {{PDB2|2ok1}}
| Name = Mitogen-activated protein kinase 10
| HGNCid = 6872
| Symbol = MAPK10
| AltSymbols =; FLJ12099; FLJ33785; JNK3; JNK3A; MGC50974; PRKM10; p493F12; p54bSAPK
| OMIM = 602897
| ECnumber =
| Homologene = 56439
| MGIid = 1346863
| GeneAtlas_image1 = PBB_GE_MAPK10_204813_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:0004708 |text = MAP kinase kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007254 |text = JNK cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5602
| Hs_Ensembl = ENSG00000109339
| Hs_RefseqProtein = NP_002744
| Hs_RefseqmRNA = NM_002753
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 87156656
| Hs_GenLoc_end = 87511051
| Hs_Uniprot = P53779
| Mm_EntrezGene = 26414
| Mm_Ensembl = ENSMUSG00000046709
| Mm_RefseqmRNA = NM_176970
| Mm_RefseqProtein = NP_795944
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 103152671
| Mm_GenLoc_end = 103451575
| Mm_Uniprot = Q8C9D4
}}
}}
'''Mitogen-activated protein kinase 10''', also known as '''MAPK10''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAPK10 mitogen-activated protein kinase 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5602| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the 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 protein is a neuronal-specific form of c-Jun N-terminal kinases (JNKs). Through its phosphorylation and nuclear localization, this kinase plays regulatory roles in the signaling pathways during neuronal apoptosis. Beta-arrestin 2, a receptor-regulated MAP kinase scaffold protein, is found to interact with, and stimulate the phosphorylation of this kinase by MAP kinase kinase 4 (MKK4). Cyclin-dependent kianse 5 can phosphorylate, and inhibit the activity of this kinase, which may be important in preventing neuronal apoptosis. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: MAPK10 mitogen-activated protein kinase 10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5602| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{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=Pulverer BJ, Kyriakis JM, Avruch J, ''et al.'' |title=Phosphorylation of c-jun mediated by MAP kinases. |journal=Nature |volume=353 |issue= 6345 |pages= 670-4 |year= 1991 |pmid= 1922387 |doi= 10.1038/353670a0 }}
*{{cite journal | author=Mohit AA, Martin JH, Miller CA |title=p493F12 kinase: a novel MAP kinase expressed in a subset of neurons in the human nervous system. |journal=Neuron |volume=14 |issue= 1 |pages= 67-78 |year= 1995 |pmid= 7826642 |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=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=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=Yang DD, Kuan CY, Whitmarsh AJ, ''et al.'' |title=Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene. |journal=Nature |volume=389 |issue= 6653 |pages= 865-70 |year= 1997 |pmid= 9349820 |doi= 10.1038/39899 }}
*{{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=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=Xie X, Gu Y, Fox T, ''et al.'' |title=Crystal structure of JNK3: a kinase implicated in neuronal apoptosis. |journal=Structure |volume=6 |issue= 8 |pages= 983-91 |year= 1998 |pmid= 9739089 |doi= }}
*{{cite journal | author= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097-108 |year= 1999 |pmid= 9847074 |doi= }}
*{{cite journal | author=Koyano S, Ito M, Takamatsu N, ''et al.'' |title=A novel Jun N-terminal kinase (JNK)-binding protein that enhances the activation of JNK by MEK kinase 1 and TGF-beta-activated kinase 1. |journal=FEBS Lett. |volume=457 |issue= 3 |pages= 385-8 |year= 1999 |pmid= 10471813 |doi= }}
*{{cite journal | author=Ito M, Yoshioka K, Akechi M, ''et al.'' |title=JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathway. |journal=Mol. Cell. Biol. |volume=19 |issue= 11 |pages= 7539-48 |year= 1999 |pmid= 10523642 |doi= }}
*{{cite journal | author=Kelkar N, Gupta S, Dickens M, Davis RJ |title=Interaction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3. |journal=Mol. Cell. Biol. |volume=20 |issue= 3 |pages= 1030-43 |year= 2000 |pmid= 10629060 |doi= }}
*{{cite journal | author=Lisnock J, Griffin P, Calaycay J, ''et al.'' |title=Activation of JNK3 alpha 1 requires both MKK4 and MKK7: kinetic characterization of in vitro phosphorylated JNK3 alpha 1. |journal=Biochemistry |volume=39 |issue= 11 |pages= 3141-8 |year= 2000 |pmid= 10715136 |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=Pouysségur J |title=Signal transduction. An arresting start for MAPK. |journal=Science |volume=290 |issue= 5496 |pages= 1515-8 |year= 2000 |pmid= 11185509 |doi= }}
*{{cite journal | author=Habelhah H, Shah K, Huang L, ''et al.'' |title=ERK phosphorylation drives cytoplasmic accumulation of hnRNP-K and inhibition of mRNA translation. |journal=Nat. Cell Biol. |volume=3 |issue= 3 |pages= 325-30 |year= 2001 |pmid= 11231586 |doi= 10.1038/35060131 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MARCKS... {November 18, 2007 11:05:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:06:11 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- 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 = Myristoylated alanine-rich protein kinase C substrate
| HGNCid = 6759
| Symbol = MARCKS
| AltSymbols =; 80K-L; FLJ14368; FLJ90045; MACS; MRACKS; PKCSL; PRKCSL
| OMIM = 177061
| ECnumber =
| Homologene = 40623
| MGIid = 96907
| GeneAtlas_image1 = PBB_GE_MARCKS_201669_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MARCKS_201668_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_MARCKS_201670_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0051015 |text = actin filament binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005813 |text = centrosome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005938 |text = cell cortex}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}} {{GNF_GO|id=GO:0042585 |text = germinal vesicle}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4082
| Hs_Ensembl = ENSG00000155130
| Hs_RefseqProtein = NP_002347
| Hs_RefseqmRNA = NM_002356
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 114285234
| Hs_GenLoc_end = 114291341
| Hs_Uniprot = P29966
| Mm_EntrezGene = 17118
| Mm_Ensembl = ENSMUSG00000069662
| Mm_RefseqmRNA = NM_008538
| Mm_RefseqProtein = NP_032564
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 36824237
| Mm_GenLoc_end = 36828330
| Mm_Uniprot = Q05BL6
}}
}}
'''Myristoylated alanine-rich protein kinase C substrate''', also known as '''MARCKS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MARCKS myristoylated alanine-rich protein kinase C substrate| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4082| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a substrate for protein kinase C. It is localized to the plasma membrane and is an actin filament crosslinking protein. Phosphorylation by protein kinase C or binding to calcium-calmodulin inhibits its association with actin and with the plasma membrane, leading to its presence in the cytoplasm. The protein is thought to be involved in cell motility, phagocytosis, membrane trafficking and mitogenesis.<ref name="entrez">{{cite web | title = Entrez Gene: MARCKS myristoylated alanine-rich protein kinase C substrate| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4082| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Blackshear PJ |title=The MARCKS family of cellular protein kinase C substrates. |journal=J. Biol. Chem. |volume=268 |issue= 3 |pages= 1501-4 |year= 1993 |pmid= 8420923 |doi= }}
*{{cite journal | author=Aderem A |title=The MARCKS family of protein kinase-C substrates. |journal=Biochem. Soc. Trans. |volume=23 |issue= 3 |pages= 587-91 |year= 1996 |pmid= 8566422 |doi= }}
*{{cite journal | author=Herget T, Brooks SF, Broad S, Rozengurt E |title=Relationship between the major protein kinase C substrates acidic 80-kDa protein-kinase-C substrate (80K) and myristoylated alanine-rich C-kinase substrate (MARCKS). Members of a gene family or equivalent genes in different species. |journal=Eur. J. Biochem. |volume=209 |issue= 1 |pages= 7-14 |year= 1992 |pmid= 1396720 |doi= }}
*{{cite journal | author=Sakai K, Hirai M, Kudoh J, ''et al.'' |title=Molecular cloning and chromosomal mapping of a cDNA encoding human 80K-L protein: major substrate for protein kinase C. |journal=Genomics |volume=14 |issue= 1 |pages= 175-8 |year= 1992 |pmid= 1427823 |doi= }}
*{{cite journal | author=Hartwig JH, Thelen M, Rosen A, ''et al.'' |title=MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin. |journal=Nature |volume=356 |issue= 6370 |pages= 618-22 |year= 1992 |pmid= 1560845 |doi= 10.1038/356618a0 }}
*{{cite journal | author=Harlan DM, Graff JM, Stumpo DJ, ''et al.'' |title=The human myristoylated alanine-rich C kinase substrate (MARCKS) gene (MACS). Analysis of its gene product, promoter, and chromosomal localization. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14399-405 |year= 1991 |pmid= 1860846 |doi= }}
*{{cite journal | author=Graff JM, Stumpo DJ, Blackshear PJ |title=Characterization of the phosphorylation sites in the chicken and bovine myristoylated alanine-rich C kinase substrate protein, a prominent cellular substrate for protein kinase C. |journal=J. Biol. Chem. |volume=264 |issue= 20 |pages= 11912-9 |year= 1989 |pmid= 2473066 |doi= }}
*{{cite journal | author=Herget T, Oehrlein SA, Pappin DJ, ''et al.'' |title=The myristoylated alanine-rich C-kinase substrate (MARCKS) is sequentially phosphorylated by conventional, novel and atypical isotypes of protein kinase C. |journal=Eur. J. Biochem. |volume=233 |issue= 2 |pages= 448-57 |year= 1995 |pmid= 7588787 |doi= }}
*{{cite journal | author=Taniguchi H, Manenti S, Suzuki M, Titani K |title=Myristoylated alanine-rich C kinase substrate (MARCKS), a major protein kinase C substrate, is an in vivo substrate of proline-directed protein kinase(s). A mass spectroscopic analysis of the post-translational modifications. |journal=J. Biol. Chem. |volume=269 |issue= 28 |pages= 18299-302 |year= 1994 |pmid= 8034575 |doi= }}
*{{cite journal | author=Rao PH, Murty VV, Gaidano G, ''et al.'' |title=Subregional mapping of 8 single copy loci to chromosome 6 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=66 |issue= 4 |pages= 272-3 |year= 1994 |pmid= 8162705 |doi= }}
*{{cite journal | author=Taniguchi H, Manenti S |title=Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids. |journal=J. Biol. Chem. |volume=268 |issue= 14 |pages= 9960-3 |year= 1993 |pmid= 8486722 |doi= }}
*{{cite journal | author=Palmer RH, Schönwasser DC, Rahman D, ''et al.'' |title=PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |journal=FEBS Lett. |volume=378 |issue= 3 |pages= 281-5 |year= 1996 |pmid= 8557118 |doi= }}
*{{cite journal | author=Swierczynski SL, Blackshear PJ |title=Myristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine-rich protein kinase C substrate protein in intact cells. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 23424-30 |year= 1996 |pmid= 8798548 |doi= }}
*{{cite journal | author=Spizz G, Blackshear PJ |title=Identification and characterization of cathepsin B as the cellular MARCKS cleaving enzyme. |journal=J. Biol. Chem. |volume=272 |issue= 38 |pages= 23833-42 |year= 1997 |pmid= 9295331 |doi= }}
*{{cite journal | author=Qi Q, Rajala RV, Anderson W, ''et al.'' |title=Molecular cloning, genomic organization, and biochemical characterization of myristoyl-CoA:protein N-myristoyltransferase from Arabidopsis thaliana. |journal=J. Biol. Chem. |volume=275 |issue= 13 |pages= 9673-83 |year= 2000 |pmid= 10734119 |doi= }}
*{{cite journal | author=Jin Cho S, La M, Ahn JK, ''et al.'' |title=Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation. |journal=Biochem. Biophys. Res. Commun. |volume=283 |issue= 2 |pages= 273-7 |year= 2001 |pmid= 11327693 |doi= 10.1006/bbrc.2001.4773 }}
*{{cite journal | author=Li Y, Martin LD, Spizz G, Adler KB |title=MARCKS protein is a key molecule regulating mucin secretion by human airway epithelial cells in vitro. |journal=J. Biol. Chem. |volume=276 |issue= 44 |pages= 40982-90 |year= 2001 |pmid= 11533058 |doi= 10.1074/jbc.M105614200 }}
*{{cite journal | author=Rauch ME, Ferguson CG, Prestwich GD, Cafiso DS |title=Myristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayers. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 14068-76 |year= 2002 |pmid= 11825894 |doi= 10.1074/jbc.M109572200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MLLT7... {November 18, 2007 11:06:11 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:06:40 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_MLLT7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e17.
| PDB = {{PDB2|1e17}}
| Name = Myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 7
| HGNCid = 7139
| Symbol = MLLT7
| AltSymbols =; AFX; AFX1; FOXO4; MGC120490
| OMIM = 300033
| ECnumber =
| Homologene = 4342
| MGIid = 1891915
| GeneAtlas_image1 = PBB_GE_MLLT7_205451_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0008134 |text = transcription factor binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0000080 |text = G1 phase of mitotic cell cycle}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0007095 |text = mitotic cell cycle G2/M transition DNA damage checkpoint}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007519 |text = striated muscle development}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0008286 |text = insulin receptor signaling pathway}} {{GNF_GO|id=GO:0016525 |text = negative regulation of angiogenesis}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}} {{GNF_GO|id=GO:0051151 |text = negative regulation of smooth muscle cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4303
| Hs_Ensembl = ENSG00000184481
| Hs_RefseqProtein = NP_005929
| Hs_RefseqmRNA = NM_005938
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 70232772
| Hs_GenLoc_end = 70240110
| Hs_Uniprot = P98177
| Mm_EntrezGene = 54601
| Mm_Ensembl = ENSMUSG00000042903
| Mm_RefseqmRNA = XM_983128
| Mm_RefseqProtein = XP_988222
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 97457308
| Mm_GenLoc_end = 97461957
| Mm_Uniprot = Q9WVH3
}}
}}
'''Myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 7''', also known as '''MLLT7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MLLT7 myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4303| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Parry P, Wei Y, Evans G |title=Cloning and characterization of the t(X;11) breakpoint from a leukemic cell line identify a new member of the forkhead gene family. |journal=Genes Chromosomes Cancer |volume=11 |issue= 2 |pages= 79-84 |year= 1995 |pmid= 7529552 |doi= }}
*{{cite journal | author=Borkhardt A, Repp R, Haas OA, ''et al.'' |title=Cloning and characterization of AFX, the gene that fuses to MLL in acute leukemias with a t(X;11)(q13;q23). |journal=Oncogene |volume=14 |issue= 2 |pages= 195-202 |year= 1997 |pmid= 9010221 |doi= 10.1038/sj.onc.1200814 }}
*{{cite journal | author=Peters U, Haberhausen G, Kostrzewa M, ''et al.'' |title=AFX1 and p54nrb: fine mapping, genomic structure, and exclusion as candidate genes of X-linked dystonia parkinsonism. |journal=Hum. Genet. |volume=100 |issue= 5-6 |pages= 569-72 |year= 1997 |pmid= 9341872 |doi= }}
*{{cite journal | author=Kops GJ, de Ruiter ND, De Vries-Smits AM, ''et al.'' |title=Direct control of the Forkhead transcription factor AFX by protein kinase B. |journal=Nature |volume=398 |issue= 6728 |pages= 630-4 |year= 1999 |pmid= 10217147 |doi= 10.1038/19328 }}
*{{cite journal | author=Takaishi H, Konishi H, Matsuzaki H, ''et al.'' |title=Regulation of nuclear translocation of forkhead transcription factor AFX by protein kinase B. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 21 |pages= 11836-41 |year= 1999 |pmid= 10518537 |doi= }}
*{{cite journal | author=Medema RH, Kops GJ, Bos JL, Burgering BM |title=AFX-like Forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1. |journal=Nature |volume=404 |issue= 6779 |pages= 782-7 |year= 2000 |pmid= 10783894 |doi= 10.1038/35008115 }}
*{{cite journal | author=Furuyama T, Nakazawa T, Nakano I, Mori N |title=Identification of the differential distribution patterns of mRNAs and consensus binding sequences for mouse DAF-16 homologues. |journal=Biochem. J. |volume=349 |issue= Pt 2 |pages= 629-34 |year= 2001 |pmid= 10880363 |doi= }}
*{{cite journal | author=Weigelt J, Climent I, Dahlman-Wright K, Wikström M |title=1H, 13C and 15N resonance assignments of the DNA binding domain of the human forkhead transcription factor AFX. |journal=J. Biomol. NMR |volume=17 |issue= 2 |pages= 181-2 |year= 2000 |pmid= 10921784 |doi= }}
*{{cite journal | author=Nasrin N, Ogg S, Cahill CM, ''et al.'' |title=DAF-16 recruits the CREB-binding protein coactivator complex to the insulin-like growth factor binding protein 1 promoter in HepG2 cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 19 |pages= 10412-7 |year= 2000 |pmid= 10973497 |doi= 10.1073/pnas.190326997 }}
*{{cite journal | author=Brownawell AM, Kops GJ, Macara IG, Burgering BM |title=Inhibition of nuclear import by protein kinase B (Akt) regulates the subcellular distribution and activity of the forkhead transcription factor AFX. |journal=Mol. Cell. Biol. |volume=21 |issue= 10 |pages= 3534-46 |year= 2001 |pmid= 11313479 |doi= 10.1128/MCB.21.10.3534-3546.2001 }}
*{{cite journal | author=Weigelt J, Climent I, Dahlman-Wright K, Wikström M |title=Solution structure of the DNA binding domain of the human forkhead transcription factor AFX (FOXO4). |journal=Biochemistry |volume=40 |issue= 20 |pages= 5861-9 |year= 2001 |pmid= 11352721 |doi= }}
*{{cite journal | author=Schuur ER, Loktev AV, Sharma M, ''et al.'' |title=Ligand-dependent interaction of estrogen receptor-alpha with members of the forkhead transcription factor family. |journal=J. Biol. Chem. |volume=276 |issue= 36 |pages= 33554-60 |year= 2001 |pmid= 11435445 |doi= 10.1074/jbc.M105555200 }}
*{{cite journal | author=De Ruiter ND, Burgering BM, Bos JL |title=Regulation of the Forkhead transcription factor AFX by Ral-dependent phosphorylation of threonines 447 and 451. |journal=Mol. Cell. Biol. |volume=21 |issue= 23 |pages= 8225-35 |year= 2001 |pmid= 11689711 |doi= 10.1128/MCB.21.23.8225-8235.2001 }}
*{{cite journal | author=Tang TT, Dowbenko D, Jackson A, ''et al.'' |title=The forkhead transcription factor AFX activates apoptosis by induction of the BCL-6 transcriptional repressor. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 14255-65 |year= 2002 |pmid= 11777915 |doi= 10.1074/jbc.M110901200 }}
*{{cite journal | author=Yang Z, Whelan J, Babb R, Bowen BR |title=An mRNA splice variant of the AFX gene with altered transcriptional activity. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8068-75 |year= 2002 |pmid= 11779849 |doi= 10.1074/jbc.M106091200 }}
*{{cite journal | author=Kops GJ, Medema RH, Glassford J, ''et al.'' |title=Control of cell cycle exit and entry by protein kinase B-regulated forkhead transcription factors. |journal=Mol. Cell. Biol. |volume=22 |issue= 7 |pages= 2025-36 |year= 2002 |pmid= 11884591 |doi= }}
*{{cite journal | author=So CW, Cleary ML |title=MLL-AFX requires the transcriptional effector domains of AFX to transform myeloid progenitors and transdominantly interfere with forkhead protein function. |journal=Mol. Cell. Biol. |volume=22 |issue= 18 |pages= 6542-52 |year= 2002 |pmid= 12192052 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Tang TT, Lasky LA |title=The forkhead transcription factor FOXO4 induces the down-regulation of hypoxia-inducible factor 1 alpha by a von Hippel-Lindau protein-independent mechanism. |journal=J. Biol. Chem. |volume=278 |issue= 32 |pages= 30125-35 |year= 2003 |pmid= 12761217 |doi= 10.1074/jbc.M302042200 }}
*{{cite journal | author=Crossley LJ |title=Neutrophil activation by fMLP regulates FOXO (forkhead) transcription factors by multiple pathways, one of which includes the binding of FOXO to the survival factor Mcl-1. |journal=J. Leukoc. Biol. |volume=74 |issue= 4 |pages= 583-92 |year= 2003 |pmid= 12960271 |doi= 10.1189/jlb.0103020 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NONO... {November 18, 2007 11:06:40 PM PST}
- SEARCH REDIRECT: Control Box Found: NONO {November 18, 2007 11:07:11 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:07:12 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:07:12 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:07:12 PM PST}
- UPDATED: Updated protein page: NONO {November 18, 2007 11:08:37 PM PST}
- INFO: Beginning work on NOX4... {November 18, 2007 11:17:56 PM PST}
- SEARCH REDIRECT: Control Box Found: NOX4 {November 18, 2007 11:18:26 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:18:29 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:18:29 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:18:29 PM PST}
- UPDATED: Updated protein page: NOX4 {November 18, 2007 11:18:35 PM PST}
- INFO: Beginning work on P2RY2... {November 18, 2007 11:09:15 PM PST}
- SEARCH REDIRECT: Control Box Found: P2RY2 {November 18, 2007 11:09:53 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:09:57 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:09:57 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:09:57 PM PST}
- UPDATED: Updated protein page: P2RY2 {November 18, 2007 11:10:03 PM PST}
- INFO: Beginning work on PIAS4... {November 18, 2007 11:18:35 PM PST}
- SEARCH REDIRECT: Control Box Found: PIAS4 {November 18, 2007 11:19:08 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:19:11 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:19:11 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:19:11 PM PST}
- UPDATED: Updated protein page: PIAS4 {November 18, 2007 11:19:17 PM PST}
- INFO: Beginning work on PLA2G1B... {November 18, 2007 11:10:03 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:10:38 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 = Phospholipase A2, group IB (pancreas)
| HGNCid = 9030
| Symbol = PLA2G1B
| AltSymbols =; MGC119834; MGC119835; PLA2; PLA2A; PPLA2
| OMIM = 172410
| ECnumber =
| Homologene = 715
| MGIid = 101842
| GeneAtlas_image1 = PBB_GE_PLA2G1B_206311_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004623 |text = phospholipase A2 activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006644 |text = phospholipid metabolic process}} {{GNF_GO|id=GO:0007015 |text = actin filament organization}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0016042 |text = lipid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5319
| Hs_Ensembl = ENSG00000170890
| Hs_RefseqProtein = NP_000919
| Hs_RefseqmRNA = NM_000928
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 119244298
| Hs_GenLoc_end = 119249975
| Hs_Uniprot = P04054
| Mm_EntrezGene = 18778
| Mm_Ensembl = ENSMUSG00000029522
| Mm_RefseqmRNA = NM_011107
| Mm_RefseqProtein = NP_035237
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 115727265
| Mm_GenLoc_end = 115735716
| Mm_Uniprot = Q9Z0Y2
}}
}}
'''Phospholipase A2, group IB (pancreas)''', also known as '''PLA2G1B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PLA2G1B phospholipase A2, group IB (pancreas)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5319| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Phospholipase A2 (EC 3.1.1.4) catalyzes the release of fatty acids from glycero-3-phosphocholines. The best known varieties are the digestive enzymes secreted as zymogens by the pancreas of mammals. Sequences of pancreatic PLA2 enzymes from a variety of mammals have been reported. One striking feature of these enzymes is their close homology to venom phospholipases of snakes. Other forms of PLA2 have been isolated from brain, liver, lung, spleen, intestine, macrophages, leukocytes, erythrocytes, inflammatory exudates, chondrocytes, and platelets (Seilhamer et al., 1986) .[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: PLA2G1B phospholipase A2, group IB (pancreas)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5319| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Dennis EA |title=Diversity of group types, regulation, and function of phospholipase A2. |journal=J. Biol. Chem. |volume=269 |issue= 18 |pages= 13057-60 |year= 1994 |pmid= 8175726 |doi= }}
*{{cite journal | author=Schröder HC, Perovic S, Kavsan V, ''et al.'' |title=Mechanisms of prionSc- and HIV-1 gp120 induced neuronal cell death. |journal=Neurotoxicology |volume=19 |issue= 4-5 |pages= 683-8 |year= 1998 |pmid= 9745929 |doi= }}
*{{cite journal | author=Sapirstein A, Bonventre JV |title=Phospholipases A2 in ischemic and toxic brain injury. |journal=Neurochem. Res. |volume=25 |issue= 5 |pages= 745-53 |year= 2000 |pmid= 10905638 |doi= }}
*{{cite journal | author=Svensson CI, Yaksh TL |title=The spinal phospholipase-cyclooxygenase-prostanoid cascade in nociceptive processing. |journal=Annu. Rev. Pharmacol. Toxicol. |volume=42 |issue= |pages= 553-83 |year= 2002 |pmid= 11807183 |doi= 10.1146/annurev.pharmtox.42.092401.143905 }}
*{{cite journal | author=Clark MA, Ozgür LE, Conway TM, ''et al.'' |title=Cloning of a phospholipase A2-activating protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 12 |pages= 5418-22 |year= 1991 |pmid= 2052621 |doi= }}
*{{cite journal | author=Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK |title=Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung. |journal=DNA |volume=5 |issue= 6 |pages= 519-27 |year= 1987 |pmid= 3028739 |doi= }}
*{{cite journal | author=Verheij HM, Westerman J, Sternby B, De Haas GH |title=The complete primary structure of phospholipase A2 from human pancreas. |journal=Biochim. Biophys. Acta |volume=747 |issue= 1-2 |pages= 93-9 |year= 1983 |pmid= 6349696 |doi= }}
*{{cite journal | author=Sternby B, Akerström B |title=Immunoreactive pancreatic colipase, lipase and phospholipase A2 in human plasma and urine from healthy individuals. |journal=Biochim. Biophys. Acta |volume=789 |issue= 2 |pages= 164-9 |year= 1984 |pmid= 6477929 |doi= }}
*{{cite journal | author=Grataroli R, Dijkman R, Dutilh CE, ''et al.'' |title=Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region. |journal=Eur. J. Biochem. |volume=122 |issue= 1 |pages= 111-7 |year= 1982 |pmid= 7060561 |doi= }}
*{{cite journal | author=Rönkkö S |title=Immunohistochemical localization of phospholipase A2 in human and bovine male reproductive organs. |journal=Comp. Biochem. Physiol. B, Biochem. Mol. Biol. |volume=110 |issue= 3 |pages= 503-9 |year= 1995 |pmid= 7584826 |doi= }}
*{{cite journal | author=Lilja I, Smedh K, Olaison G, ''et al.'' |title=Phospholipase A2 gene expression and activity in histologically normal ileal mucosa and in Crohn's ileitis. |journal=Gut |volume=37 |issue= 3 |pages= 380-5 |year= 1995 |pmid= 7590434 |doi= }}
*{{cite journal | author=Ancian P, Lambeau G, Mattéi MG, Lazdunski M |title=The human 180-kDa receptor for secretory phospholipases A2. Molecular cloning, identification of a secreted soluble form, expression, and chromosomal localization. |journal=J. Biol. Chem. |volume=270 |issue= 15 |pages= 8963-70 |year= 1995 |pmid= 7721806 |doi= }}
*{{cite journal | author=Chen J, Engle SJ, Seilhamer JJ, Tischfield JA |title=Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2. |journal=J. Biol. Chem. |volume=269 |issue= 4 |pages= 2365-8 |year= 1994 |pmid= 8300559 |doi= }}
*{{cite journal | author=Gispert S, Twells R, Orozco G, ''et al.'' |title=Chromosomal assignment of the second locus for autosomal dominant cerebellar ataxia (SCA2) to chromosome 12q23-24.1. |journal=Nat. Genet. |volume=4 |issue= 3 |pages= 295-9 |year= 1993 |pmid= 8358438 |doi= 10.1038/ng0793-295 }}
*{{cite journal | author=Cupillard L, Koumanov K, Mattéi MG, ''et al.'' |title=Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2. |journal=J. Biol. Chem. |volume=272 |issue= 25 |pages= 15745-52 |year= 1997 |pmid= 9188469 |doi= }}
*{{cite journal | author=Mavoungou E, Georges-Courbot MC, Poaty-Mavoungou V, ''et al.'' |title=HIV and SIV envelope glycoproteins induce phospholipase A2 activation in human and macaque lymphocytes. |journal=J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. |volume=16 |issue= 1 |pages= 1-9 |year= 1997 |pmid= 9377118 |doi= }}
*{{cite journal | author= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097-108 |year= 1999 |pmid= 9847074 |doi= }}
*{{cite journal | author=Sartipy P, Bondjers G, Hurt-Camejo E |title=Phospholipase A2 type II binds to extracellular matrix biglycan: modulation of its activity on LDL by colocalization in glycosaminoglycan matrixes. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=18 |issue= 12 |pages= 1934-41 |year= 1999 |pmid= 9848887 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PPP1CC... {November 18, 2007 11:10:38 PM PST}
- SEARCH REDIRECT: Control Box Found: PPP1CC {November 18, 2007 11:12:44 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:12:45 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:12:45 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:12:45 PM PST}
- UPDATED: Updated protein page: PPP1CC {November 18, 2007 11:12:51 PM PST}
- INFO: Beginning work on PPP5C... {November 18, 2007 11:12:51 PM PST}
- SEARCH REDIRECT: Control Box Found: PPP5C {November 18, 2007 11:13:21 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:13:23 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:13:23 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:13:23 PM PST}
- UPDATED: Updated protein page: PPP5C {November 18, 2007 11:13:29 PM PST}
- INFO: Beginning work on PSMB3... {November 18, 2007 11:14:16 PM PST}
- SEARCH REDIRECT: Control Box Found: PSMB3 {November 18, 2007 11:14:40 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:14:41 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:14:41 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:14:41 PM PST}
- UPDATED: Updated protein page: PSMB3 {November 18, 2007 11:14:54 PM PST}
- INFO: Beginning work on PSMD5... {November 18, 2007 11:14:54 PM PST}
- SEARCH REDIRECT: Control Box Found: PSMD5 {November 18, 2007 11:15:17 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:15:20 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:15:20 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:15:20 PM PST}
- UPDATED: Updated protein page: PSMD5 {November 18, 2007 11:15:30 PM PST}
- INFO: Beginning work on RARG... {November 18, 2007 11:15:30 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:17:56 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RARG_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dsz.
| PDB = {{PDB2|1dsz}}, {{PDB2|1exa}}, {{PDB2|1exx}}, {{PDB2|1fcx}}, {{PDB2|1fcy}}, {{PDB2|1fcz}}, {{PDB2|1fd0}}, {{PDB2|1hra}}, {{PDB2|2lbd}}, {{PDB2|3lbd}}, {{PDB2|4lbd}}
| Name = Retinoic acid receptor, gamma
| HGNCid = 9866
| Symbol = RARG
| AltSymbols =; NR1B3; RARC
| OMIM = 180190
| ECnumber =
| Homologene = 20263
| MGIid = 97858
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0003708 |text = retinoic acid receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005667 |text = transcription factor complex}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0043065 |text = positive regulation of apoptosis}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0048048 |text = embryonic eye morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5916
| Hs_Ensembl =
| Hs_RefseqProtein = XP_945931
| Hs_RefseqmRNA = XM_940838
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 19411
| Mm_Ensembl = ENSMUSG00000001288
| Mm_RefseqmRNA = NM_001042727
| Mm_RefseqProtein = NP_001036192
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 102062974
| Mm_GenLoc_end = 102085313
| Mm_Uniprot = Q3UG86
}}
}}
'''Retinoic acid receptor, gamma''', also known as '''RARG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RARG retinoic acid receptor, gamma| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5916| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Leid M, Kastner P, Lyons R, ''et al.'' |title=Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently. |journal=Cell |volume=68 |issue= 2 |pages= 377-95 |year= 1992 |pmid= 1310259 |doi= }}
*{{cite journal | author=Vollberg TM, Nervi C, George MD, ''et al.'' |title=Retinoic acid receptors as regulators of human epidermal keratinocyte differentiation. |journal=Mol. Endocrinol. |volume=6 |issue= 5 |pages= 667-76 |year= 1992 |pmid= 1318502 |doi= }}
*{{cite journal | author=Lehmann JM, Zhang XK, Pfahl M |title=RAR gamma 2 expression is regulated through a retinoic acid response element embedded in Sp1 sites. |journal=Mol. Cell. Biol. |volume=12 |issue= 7 |pages= 2976-85 |year= 1992 |pmid= 1320193 |doi= }}
*{{cite journal | author=Mattei MG, Rivière M, Krust A, ''et al.'' |title=Chromosomal assignment of retinoic acid receptor (RAR) genes in the human, mouse, and rat genomes. |journal=Genomics |volume=10 |issue= 4 |pages= 1061-9 |year= 1991 |pmid= 1655630 |doi= }}
*{{cite journal | author=Lehmann JM, Hoffmann B, Pfahl M |title=Genomic organization of the retinoic acid receptor gamma gene. |journal=Nucleic Acids Res. |volume=19 |issue= 3 |pages= 573-8 |year= 1991 |pmid= 1849262 |doi= }}
*{{cite journal | author=Kastner P, Krust A, Mendelsohn C, ''et al.'' |title=Murine isoforms of retinoic acid receptor gamma with specific patterns of expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 7 |pages= 2700-4 |year= 1990 |pmid= 2157210 |doi= }}
*{{cite journal | author=Giguère V, Shago M, Zirngibl R, ''et al.'' |title=Identification of a novel isoform of the retinoic acid receptor gamma expressed in the mouse embryo. |journal=Mol. Cell. Biol. |volume=10 |issue= 5 |pages= 2335-40 |year= 1990 |pmid= 2157970 |doi= }}
*{{cite journal | author=Ishikawa T, Umesono K, Mangelsdorf DJ, ''et al.'' |title=A functional retinoic acid receptor encoded by the gene on human chromosome 12. |journal=Mol. Endocrinol. |volume=4 |issue= 6 |pages= 837-44 |year= 1990 |pmid= 2172793 |doi= }}
*{{cite journal | author=Krust A, Kastner P, Petkovich M, ''et al.'' |title=A third human retinoic acid receptor, hRAR-gamma. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 14 |pages= 5310-4 |year= 1989 |pmid= 2546152 |doi= }}
*{{cite journal | author=Renaud JP, Rochel N, Ruff M, ''et al.'' |title=Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid. |journal=Nature |volume=378 |issue= 6558 |pages= 681-9 |year= 1996 |pmid= 7501014 |doi= 10.1038/378681a0 }}
*{{cite journal | author=Zhou L, Pang J, Munroe DG, Lau C |title=A human retinoic acid receptor gamma isoform is homologous to the murine retinoic acid receptor gamma 7. |journal=Nucleic Acids Res. |volume=21 |issue= 10 |pages= 2520 |year= 1993 |pmid= 7685085 |doi= }}
*{{cite journal | author=Zitnik RJ, Kotloff RM, Latifpour J, ''et al.'' |title=Retinoic acid inhibition of IL-1-induced IL-6 production by human lung fibroblasts. |journal=J. Immunol. |volume=152 |issue= 3 |pages= 1419-27 |year= 1994 |pmid= 8301142 |doi= }}
*{{cite journal | author=Botling J, Castro DS, Oberg F, ''et al.'' |title=Retinoic acid receptor/retinoid X receptor heterodimers can be activated through both subunits providing a basis for synergistic transactivation and cellular differentiation. |journal=J. Biol. Chem. |volume=272 |issue= 14 |pages= 9443-9 |year= 1997 |pmid= 9083083 |doi= }}
*{{cite journal | author=Lømo J, Smeland EB, Ulven S, ''et al.'' |title=RAR-, not RXR, ligands inhibit cell activation and prevent apoptosis in B-lymphocytes. |journal=J. Cell. Physiol. |volume=175 |issue= 1 |pages= 68-77 |year= 1998 |pmid= 9491782 |doi= 10.1002/(SICI)1097-4652(199804)175:1<68::AID-JCP8>3.0.CO;2-A }}
*{{cite journal | author=Klaholz BP, Renaud JP, Mitschler A, ''et al.'' |title=Conformational adaptation of agonists to the human nuclear receptor RAR gamma. |journal=Nat. Struct. Biol. |volume=5 |issue= 3 |pages= 199-202 |year= 1998 |pmid= 9501913 |doi= }}
*{{cite journal | author=Zhang ZP, Gambone CJ, Gabriel JL, ''et al.'' |title=Arg278, but not Lys229 or Lys236, plays an important role in the binding of retinoic acid by retinoic acid receptor gamma. |journal=J. Biol. Chem. |volume=273 |issue= 51 |pages= 34016-21 |year= 1999 |pmid= 9852056 |doi= }}
*{{cite journal | author=Yang C, Zhou D, Chen S |title=Modulation of aromatase expression in the breast tissue by ERR alpha-1 orphan receptor. |journal=Cancer Res. |volume=58 |issue= 24 |pages= 5695-700 |year= 1999 |pmid= 9865725 |doi= }}
*{{cite journal | author=Nagpal S, Ghosn C, DiSepio D, ''et al.'' |title=Retinoid-dependent recruitment of a histone H1 displacement activity by retinoic acid receptor. |journal=J. Biol. Chem. |volume=274 |issue= 32 |pages= 22563-8 |year= 1999 |pmid= 10428834 |doi= }}
*{{cite journal | author=Egea PF, Mitschler A, Rochel N, ''et al.'' |title=Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid. |journal=EMBO J. |volume=19 |issue= 11 |pages= 2592-601 |year= 2000 |pmid= 10835357 |doi= 10.1093/emboj/19.11.2592 }}
*{{cite journal | author=Boudjelal M, Voorhees JJ, Fisher GJ |title=Retinoid signaling is attenuated by proteasome-mediated degradation of retinoid receptors in human keratinocyte HaCaT cells. |journal=Exp. Cell Res. |volume=274 |issue= 1 |pages= 130-7 |year= 2002 |pmid= 11855864 |doi= 10.1006/excr.2001.5450 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC11A2... {November 18, 2007 11:08:37 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:09:15 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| 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 = Solute carrier family 11 (proton-coupled divalent metal ion transporters), member 2
| HGNCid = 10908
| Symbol = SLC11A2
| AltSymbols =; DMT1; DCT1; FLJ37416; NRAMP2
| OMIM = 600523
| ECnumber =
| Homologene = 55471
| MGIid = 1345279
| GeneAtlas_image1 = PBB_GE_SLC11A2_203123_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SLC11A2_203124_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_SLC11A2_203125_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005381 |text = iron ion transmembrane transporter activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0015087 |text = cobalt ion transmembrane transporter activity}}
| Component = {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0010008 |text = endosome membrane}} {{GNF_GO|id=GO:0012505 |text = endomembrane system}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006824 |text = cobalt ion transport}} {{GNF_GO|id=GO:0006826 |text = iron ion transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4891
| Hs_Ensembl = ENSG00000110911
| Hs_RefseqProtein = NP_000608
| Hs_RefseqmRNA = NM_000617
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 49659585
| Hs_GenLoc_end = 49706434
| Hs_Uniprot = P49281
| Mm_EntrezGene = 18174
| Mm_Ensembl = ENSMUSG00000023030
| Mm_RefseqmRNA = NM_008732
| Mm_RefseqProtein = NP_032758
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 100215936
| Mm_GenLoc_end = 100252189
| Mm_Uniprot = Q3UFV5
}}
}}
'''Solute carrier family 11 (proton-coupled divalent metal ion transporters), member 2''', also known as '''SLC11A2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC11A2 solute carrier family 11 (proton-coupled divalent metal ion transporters), member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4891| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Vidal S, Belouchi AM, Cellier M, ''et al.'' |title=Cloning and characterization of a second human NRAMP gene on chromosome 12q13. |journal=Mamm. Genome |volume=6 |issue= 4 |pages= 224-30 |year= 1995 |pmid= 7613023 |doi= }}
*{{cite journal | author=Fleming MD, Trenor CC, Su MA, ''et al.'' |title=Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene. |journal=Nat. Genet. |volume=16 |issue= 4 |pages= 383-6 |year= 1997 |pmid= 9241278 |doi= 10.1038/ng0897-383 }}
*{{cite journal | author=Kishi F, Tabuchi M |title=Complete nucleotide sequence of human NRAMP2 cDNA. |journal=Mol. Immunol. |volume=34 |issue= 12-13 |pages= 839-42 |year= 1998 |pmid= 9464519 |doi= }}
*{{cite journal | author=Lee PL, Gelbart T, West C, ''et al.'' |title=The human Nramp2 gene: characterization of the gene structure, alternative splicing, promoter region and polymorphisms. |journal=Blood Cells Mol. Dis. |volume=24 |issue= 2 |pages= 199-215 |year= 1998 |pmid= 9642100 |doi= 10.1006/bcmd.1998.0186 }}
*{{cite journal | author=Kishi F, Tabuchi M |title=Human natural resistance-associated macrophage protein 2: gene cloning and protein identification. |journal=Biochem. Biophys. Res. Commun. |volume=251 |issue= 3 |pages= 775-83 |year= 1998 |pmid= 9790986 |doi= 10.1006/bbrc.1998.9415 }}
*{{cite journal | author=Tabuchi M, Yoshimori T, Yamaguchi K, ''et al.'' |title=Human NRAMP2/DMT1, which mediates iron transport across endosomal membranes, is localized to late endosomes and lysosomes in HEp-2 cells. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22220-8 |year= 2000 |pmid= 10751401 |doi= 10.1074/jbc.M001478200 }}
*{{cite journal | author=Griffiths WJ, Kelly AL, Smith SJ, Cox TM |title=Localization of iron transport and regulatory proteins in human cells. |journal=QJM : monthly journal of the Association of Physicians |volume=93 |issue= 9 |pages= 575-87 |year= 2000 |pmid= 10984552 |doi= }}
*{{cite journal | author=Georgieff MK, Wobken JK, Welle J, ''et al.'' |title=Identification and localization of divalent metal transporter-1 (DMT-1) in term human placenta. |journal=Placenta |volume=21 |issue= 8 |pages= 799-804 |year= 2001 |pmid= 11095929 |doi= 10.1053/plac.2000.0566 }}
*{{cite journal | author=Tallkvist J, Bowlus CL, Lönnerdal B |title=DMT1 gene expression and cadmium absorption in human absorptive enterocytes. |journal=Toxicol. Lett. |volume=122 |issue= 2 |pages= 171-7 |year= 2001 |pmid= 11439223 |doi= }}
*{{cite journal | author=Sharp P, Tandy S, Yamaji S, ''et al.'' |title=Rapid regulation of divalent metal transporter (DMT1) protein but not mRNA expression by non-haem iron in human intestinal Caco-2 cells. |journal=FEBS Lett. |volume=510 |issue= 1-2 |pages= 71-6 |year= 2002 |pmid= 11755534 |doi= }}
*{{cite journal | author=Umbreit JN, Conrad ME, Hainsworth LN, Simovich M |title=The ferrireductase paraferritin contains divalent metal transporter as well as mobilferrin. |journal=Am. J. Physiol. Gastrointest. Liver Physiol. |volume=282 |issue= 3 |pages= G534-9 |year= 2002 |pmid= 11842004 |doi= 10.1152/ajpgi.00199.2001 }}
*{{cite journal | author=Simovich MJ, Conrad ME, Umbreit JN, ''et al.'' |title=Cellular location of proteins related to iron absorption and transport. |journal=Am. J. Hematol. |volume=69 |issue= 3 |pages= 164-70 |year= 2002 |pmid= 11891802 |doi= }}
*{{cite journal | author=Rolfs A, Bonkovsky HL, Kohlroser JG, ''et al.'' |title=Intestinal expression of genes involved in iron absorption in humans. |journal=Am. J. Physiol. Gastrointest. Liver Physiol. |volume=282 |issue= 4 |pages= G598-607 |year= 2002 |pmid= 11897618 |doi= 10.1152/ajpgi.00371.2001 }}
*{{cite journal | author=Wang X, Ghio AJ, Yang F, ''et al.'' |title=Iron uptake and Nramp2/DMT1/DCT1 in human bronchial epithelial cells. |journal=Am. J. Physiol. Lung Cell Mol. Physiol. |volume=282 |issue= 5 |pages= L987-95 |year= 2002 |pmid= 11943663 |doi= 10.1152/ajplung.00253.2001 }}
*{{cite journal | author=I Bannon D, Portnoy ME, Olivi L, ''et al.'' |title=Uptake of lead and iron by divalent metal transporter 1 in yeast and mammalian cells. |journal=Biochem. Biophys. Res. Commun. |volume=295 |issue= 4 |pages= 978-84 |year= 2002 |pmid= 12127992 |doi= }}
*{{cite journal | author=Zoller H, Decristoforo C, Weiss G |title=Erythroid 5-aminolevulinate synthase, ferrochelatase and DMT1 expression in erythroid progenitors: differential pathways for erythropoietin and iron-dependent regulation. |journal=Br. J. Haematol. |volume=118 |issue= 2 |pages= 619-26 |year= 2002 |pmid= 12139757 |doi= }}
*{{cite journal | author=Hubert N, Hentze MW |title=Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 19 |pages= 12345-50 |year= 2002 |pmid= 12209011 |doi= 10.1073/pnas.192423399 }}
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}}
{{refend}}
{{protein-stub}}
end log.
