SETD7

From Wikipedia, the free encyclopedia

SET domain containing (lysine methyltransferase) 7

PDB rendering based on 1h3i.

Available structures: 1h3i, 1mt6, 1muf, 1n6a, 1n6c, 1o9s, 1xqh, 2f69

Identifiers

Symbol(s)

SETD7; SET7; FLJ21193; KIAA1717; SET7/9; SET9

External IDs

OMIM: 606594 MGI: 1920501 HomoloGene: 12741

Gene ontology
Molecular Function:	• methyltransferase activity • transferase activity • histone-lysine N-methyltransferase activity
Cellular Component:	• nucleus
Biological Process:	• chromatin modification

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_030648 (mRNA)
NP_085151 (protein)

NM_080793 (mRNA)
NP_542983 (protein)

Location

Chr 4: 140.65 - 140.7 Mb

Chr 3: 51.6 - 51.65 Mb

Pubmed search

[1]

[2]

SET domain containing (lysine methyltransferase) 7, also known as SETD7, is a human gene.^[1]

[edit] References

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

[edit] 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. PMID 11214970.
Wang H, Cao R, Xia L, et al. (2002). "Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase.". Mol. Cell 8 (6): 1207-17. PMID 11779497.
Nishioka K, Chuikov S, Sarma K, et al. (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. PMID 11850410.
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. 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. 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. 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. 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. 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. 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.