SETD7

SETD7
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1H3I, 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, 5AYF
Identifiers
Aliases	SETD7, KMT7, SET7, SET7/9, SET9, SET domain containing lysine methyltransferase 7, SET domain containing 7, histone lysine methyltransferase
External IDs	OMIM: 606594 MGI: 1920501 HomoloGene: 12741 GeneCards: SETD7
Gene location (Human)
Chr.	Chromosome 4 (human)
End	139,606,699 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	51,468,300 bp
RNA expression pattern
	Top expressed in
	tibialis anterior muscle; ; deltoid muscle; ; quadriceps femoris muscle; ; biceps brachii; ; vastus lateralis muscle; ; synovial joint; ; synovial membrane; ; lactiferous duct; ; saphenous vein; ; pericardium;
	Top expressed in
	triceps brachii muscle; ; temporal muscle; ; sternocleidomastoid muscle; ; ciliary body; ; digastric muscle; ; cerebellar vermis; ; ankle; ; lateral geniculate nucleus; ; iris; ; body of femur;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	methyltransferase activity; transferase activity; p53 binding; chromatin binding; protein-lysine N-methyltransferase activity; protein binding; histone-lysine N-methyltransferase activity;
Cellular component	nucleoplasm; chromosome; nucleolus; nucleus;
Biological process	regulation 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 organization;
	Sources:Amigo / QuickGO
Orthologs
	80854
	73251
	ENSG00000145391
	ENSMUSG00000037111
	Q8WTS6
	Q8VHL1
	NM_001306199; NM_001306200; NM_030648
	NM_080793
	NP_001293128; NP_001293129; NP_085151
	NP_542983
	Wikidata
View/Edit Human	View/Edit Mouse

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

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000145391 - Ensembl, May 2017
1 2 3 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) ]".

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000145391 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid11850410-5] 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.

[pmid11779497-6] 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.

[entrez-7] "SETD7 SET domain containing 7, histone lysine methyltransferase [ Homo sapiens (human) ]".

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References

Further reading