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Wikipedia

SETD7

January 01, 1970

Histone-lysine N-methyltransferase SETD7 is an enzyme that in humans is encoded by the SETD7 gene.[5][6][7]

SETD7
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSETD7, KMT7, SET7, SET7/9, SET9, SET domain containing lysine methyltransferase 7, SET domain containing 7, histone lysine methyltransferase
External IDsOMIM: 606594 MGI: 1920501 HomoloGene: 12741 GeneCards: SETD7
Orthologs
SpeciesHumanMouse
Entrez

80854

73251

Ensembl

ENSG00000145391

ENSMUSG00000037111

UniProt

Q8WTS6

Q8VHL1

RefSeq (mRNA)

NM_001306199
NM_001306200
NM_030648

NM_080793

RefSeq (protein)

NP_001293128
NP_001293129
NP_085151

NP_542983

Location (UCSC)Chr 4: 139.5 – 139.61 MbChr 3: 51.42 – 51.47 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000145391 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000037111 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Nishioka K, Chuikov S, Sarma K, Erdjument-Bromage H, Allis CD, Tempst P, Reinberg D (Feb 2002). "Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation". Genes Dev. 16 (4): 479–89. doi:10.1101/gad.967202. PMC 155346. PMID 11850410.
  6. ^ Wang H, Cao R, Xia L, Erdjument-Bromage H, Borchers C, Tempst P, Zhang Y (Jan 2002). "Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase". Mol Cell. 8 (6): 1207–17. doi:10.1016/S1097-2765(01)00405-1. PMID 11779497. S2CID 37879139.
  7. ^ "SETD7 SET domain containing 7, histone lysine methyltransferase [ Homo sapiens (human) ]".

Further reading edit

  • Nagase T, Kikuno R, Hattori A, et al. (2001). "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (6): 347–55. doi:10.1093/dnares/7.6.347. PMID 11214970.
  • Wilson JR, Jing C, Walker PA, et al. (2002). "Crystal structure and functional analysis of the histone methyltransferase SET7/9". Cell. 111 (1): 105–15. doi:10.1016/S0092-8674(02)00964-9. PMID 12372304. S2CID 14727763.
  • Jacobs SA, Harp JM, Devarakonda S, et al. (2002). "The active site of the SET domain is constructed on a knot". Nat. Struct. Biol. 9 (11): 833–8. doi:10.1038/nsb861. PMID 12389038. S2CID 28718612.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Kwon T, Chang JH, Kwak E, et al. (2003). "Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9–AdoMet". EMBO J. 22 (2): 292–303. doi:10.1093/emboj/cdg025. PMC 140100. PMID 12514135.
  • Xiao B, Jing C, Wilson JR, et al. (2003). "Structure and catalytic mechanism of the human histone methyltransferase SET7/9" (PDF). Nature. 421 (6923): 652–6. Bibcode:2003Natur.421..652X. doi:10.1038/nature01378. PMID 12540855. S2CID 4423407.
  • Wysocka J, Myers MP, Laherty CD, et al. (2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes Dev. 17 (7): 896–911. doi:10.1101/gad.252103. PMC 196026. PMID 12670868.
  • Kouskouti A, Scheer E, Staub A, et al. (2004). "Gene-specific modulation of TAF10 function by SET9-mediated methylation". Mol. Cell. 14 (2): 175–82. CiteSeerX 10.1.1.320.8454. doi:10.1016/S1097-2765(04)00182-0. PMID 15099517.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Chuikov S, Kurash JK, Wilson JR, et al. (2004). "Regulation of p53 activity through lysine methylation". Nature. 432 (7015): 353–60. Bibcode:2004Natur.432..353C. doi:10.1038/nature03117. PMID 15525938. S2CID 4398310.
  • Couture JF, Collazo E, Hauk G, Trievel RC (2006). "Structural basis for the methylation site specificity of SET7/9". Nat. Struct. Mol. Biol. 13 (2): 140–6. doi:10.1038/nsmb1045. PMID 16415881. S2CID 38483056.
  • Hayakawa T, Ohtani Y, Hayakawa N, et al. (2007). "RBP2 is an MRG15 complex component and down-regulates intragenic histone H3 lysine 4 methylation". Genes Cells. 12 (6): 811–26. doi:10.1111/j.1365-2443.2007.01089.x. PMID 17573780. S2CID 10003129.


 

This article on a gene on human chromosome 4 is a stub. You can help Wikipedia by expanding it.

January 01, 1970
setd7, histone, lysine, methyltransferase, enzyme, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes1h3i, 1mt6, 1muf, 1n6a, 1n6c, 1o9s, 1xqh, 2f69, 3cbm, 3cbo, 3cbp, 3m53, 3m54, 3m55, 3m56, 3m57, 3m58, 3m59, 3m5a, 3os. Histone lysine N methyltransferase SETD7 is an enzyme that in humans is encoded by the SETD7 gene 5 6 7 SETD7Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes1H3I 1MT6 1MUF 1N6A 1N6C 1O9S 1XQH 2F69 3CBM 3CBO 3CBP 3M53 3M54 3M55 3M56 3M57 3M58 3M59 3M5A 3OS5 3VUZ 3VV0 4E47 4J7F 4J8O 4JDS 4JLG 5EG2 5AYFIdentifiersAliasesSETD7 KMT7 SET7 SET7 9 SET9 SET domain containing lysine methyltransferase 7 SET domain containing 7 histone lysine methyltransferaseExternal IDsOMIM 606594 MGI 1920501 HomoloGene 12741 GeneCards SETD7Gene location Human Chr Chromosome 4 human 1 Band4q31 1Start139 495 941 bp 1 End139 606 699 bp 1 Gene location Mouse Chr Chromosome 3 mouse 2 Band3 3 CStart51 422 740 bp 2 End51 468 300 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed intibialis anterior muscledeltoid musclequadriceps femoris musclebiceps brachiivastus lateralis musclesynovial jointsynovial membranelactiferous ductsaphenous veinpericardiumTop expressed intriceps brachii muscletemporal musclesternocleidomastoid muscleciliary bodydigastric musclecerebellar vermisanklelateral geniculate nucleusirisbody of femurMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionmethyltransferase activity transferase activity p53 binding chromatin binding protein lysine N methyltransferase activity protein binding histone lysine N methyltransferase activityCellular componentnucleoplasm chromosome nucleolus nucleusBiological processregulation of transcription DNA templated peptidyl lysine monomethylation transcription DNA templated cellular response to DNA damage stimulus positive regulation of transcription DNA templated peptidyl lysine methylation methylation heterochromatin organization peptidyl lysine dimethylation histone lysine methylation response to ethanol regulation of histone H3 K9 methylation chromatin organizationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez8085473251EnsemblENSG00000145391ENSMUSG00000037111UniProtQ8WTS6Q8VHL1RefSeq mRNA NM 001306199NM 001306200NM 030648NM 080793RefSeq protein NP 001293128NP 001293129NP 085151NP 542983Location UCSC Chr 4 139 5 139 61 MbChr 3 51 42 51 47 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseReferences edit a b c GRCh38 Ensembl release 89 ENSG00000145391 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000037111 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Nishioka K Chuikov S Sarma K Erdjument Bromage H Allis CD Tempst P Reinberg D Feb 2002 Set9 a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation Genes Dev 16 4 479 89 doi 10 1101 gad 967202 PMC 155346 PMID 11850410 Wang H Cao R Xia L Erdjument Bromage H Borchers C Tempst P Zhang Y Jan 2002 Purification and functional characterization of a histone H3 lysine 4 specific methyltransferase Mol Cell 8 6 1207 17 doi 10 1016 S1097 2765 01 00405 1 PMID 11779497 S2CID 37879139 SETD7 SET domain containing 7 histone lysine methyltransferase Homo sapiens human Further reading editNagase T Kikuno R Hattori A et al 2001 Prediction of the coding sequences of unidentified human genes XIX The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro DNA Res 7 6 347 55 doi 10 1093 dnares 7 6 347 PMID 11214970 Wilson JR Jing C Walker PA et al 2002 Crystal structure and functional analysis of the histone methyltransferase SET7 9 Cell 111 1 105 15 doi 10 1016 S0092 8674 02 00964 9 PMID 12372304 S2CID 14727763 Jacobs SA Harp JM Devarakonda S et al 2002 The active site of the SET domain is constructed on a knot Nat Struct Biol 9 11 833 8 doi 10 1038 nsb861 PMID 12389038 S2CID 28718612 Strausberg RL Feingold EA Grouse LH et al 2003 Generation and initial analysis of more than 15 000 full length human and mouse cDNA sequences Proc Natl Acad Sci U S A 99 26 16899 903 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Kwon T Chang JH Kwak E et al 2003 Mechanism of histone lysine methyl transfer revealed by the structure of SET7 9 AdoMet EMBO J 22 2 292 303 doi 10 1093 emboj cdg025 PMC 140100 PMID 12514135 Xiao B Jing C Wilson JR et al 2003 Structure and catalytic mechanism of the human histone methyltransferase SET7 9 PDF Nature 421 6923 652 6 Bibcode 2003Natur 421 652X doi 10 1038 nature01378 PMID 12540855 S2CID 4423407 Wysocka J Myers MP Laherty CD et al 2003 Human Sin3 deacetylase and trithorax related Set1 Ash2 histone H3 K4 methyltransferase are tethered together selectively by the cell proliferation factor HCF 1 Genes Dev 17 7 896 911 doi 10 1101 gad 252103 PMC 196026 PMID 12670868 Kouskouti A Scheer E Staub A et al 2004 Gene specific modulation of TAF10 function by SET9 mediated methylation Mol Cell 14 2 175 82 CiteSeerX 10 1 1 320 8454 doi 10 1016 S1097 2765 04 00182 0 PMID 15099517 Gerhard DS Wagner L Feingold EA et al 2004 The Status Quality and Expansion of the NIH Full Length cDNA Project The Mammalian Gene Collection MGC Genome Res 14 10B 2121 7 doi 10 1101 gr 2596504 PMC 528928 PMID 15489334 Chuikov S Kurash JK Wilson JR et al 2004 Regulation of p53 activity through lysine methylation Nature 432 7015 353 60 Bibcode 2004Natur 432 353C doi 10 1038 nature03117 PMID 15525938 S2CID 4398310 Couture JF Collazo E Hauk G Trievel RC 2006 Structural basis for the methylation site specificity of SET7 9 Nat Struct Mol Biol 13 2 140 6 doi 10 1038 nsmb1045 PMID 16415881 S2CID 38483056 Hayakawa T Ohtani Y Hayakawa N et al 2007 RBP2 is an MRG15 complex component and down regulates intragenic histone H3 lysine 4 methylation Genes Cells 12 6 811 26 doi 10 1111 j 1365 2443 2007 01089 x PMID 17573780 S2CID 10003129 nbsp This article on a gene on human chromosome 4 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title SETD7 amp oldid 1142701736, wikipedia, wiki, book, books, library,

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