From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
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 methyltransferaseExternal IDs
OMIM :
606594 ;
MGI :
1920501 ;
HomoloGene :
12741 ;
GeneCards :
SETD7 ;
OMA :
SETD7 - orthologs
RNA expression pattern
Bgee
Human
Mouse (ortholog)
Top expressed in tibialis anterior muscle deltoid muscle cardiac muscle tissue of right atrium myocardium of left ventricle skin of arm quadriceps femoris muscle Skeletal muscle tissue of rectus abdominis biceps brachii vastus lateralis muscle Skeletal muscle tissue of biceps brachii
Top expressed in triceps brachii muscle temporal muscle sternocleidomastoid muscle ciliary body digastric muscle lobe of cerebellum cerebellar vermis ankle lateral geniculate nucleus epithelium of lens
More reference expression data
BioGPS
Wikidata
Histone-lysine N-methyltransferase SETD7 is an
enzyme that in humans is encoded by the SETD7
gene .
[5]
[6]
[7]
References
^
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
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 .
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
