SETD7

SET domain containing (lysine methyltransferase) 7

PDB rendering based on 1h3i.

Available structures

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, 4J7I, 4J83, 4J8O, 4JDS, 4JLG

Identifiers

SETD7 ; KMT7; SET7; SET7/9; SET9

External IDs

OMIM: 606594 MGI: 1920501 HomoloGene: 12741 IUPHAR: 2703 ChEMBL: 5523 GeneCards: SETD7 Gene

Gene ontology
Molecular function	• p53 binding • protein binding • protein-lysine N-methyltransferase activity • histone-lysine N-methyltransferase activity
Cellular component	• nucleus • chromosome
Biological process	• transcription, DNA-templated • regulation of transcription, DNA-templated • chromatin modification • peptidyl-lysine monomethylation • peptidyl-lysine dimethylation • histone lysine methylation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000145391

ENSMUSG00000037111

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 4:
140.42 – 140.53 Mb

Chr 3:
51.52 – 51.56 Mb

PubMed search

Histone-lysine N-methyltransferase SETD7 is an enzyme that in humans is encoded by the SETD7 gene.^[1]^[2]^[3]

References

↑ 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.
↑ "Entrez Gene: SETD7 SET domain containing (lysine methyltransferase) 7".

Further reading

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.
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.
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. 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". Nature 421 (6923): 652–6. doi:10.1038/nature01378. PMID 12540855.
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. 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. doi:10.1038/nature03117. PMID 15525938.
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.
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.

PDB gallery

1h3i: CRYSTAL STRUCTURE OF THE HISTONE METHYLTRANSFERASE SET7/9

1mt6: Structure of histone H3 K4-specific methyltransferase SET7/9 with AdoHcy

1muf: Structure of histone H3 K4-specific methyltransferase SET7/9

1n6a: Structure of SET7/9

1n6c: Structure of SET7/9

1o9s: CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF THE HUMAN HISTONE METHYLTRANSFERASE SET7/9

1xqh: Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH

2f69: Ternary complex of SET7/9 bound to AdoHcy and a TAF10 peptide