UniProt Accession

 SUV91_HUMAN; O43463; B2R6E8; Q53G60; Q6FHK6 

Genbank Protein ID

 AF019968; CR541746; AK223071; AK312547; AF196970; CH471224; BC006238 

Genbank Nucleotide ID

 AAB92224.1; CAG46546.1; BAD96791.1; BAG35445.1; EAW50756.1; AAH06238.1 

Protein Name

 Histone-lysine N-methyltransferase SUV39H1 

Protein Synonyms/Alias

 Histone H3-K9 methyltransferase 1; H3-K9-HMTase 1; Lysine N-methyltransferase 1A; Position-effect variegation 3-9 homolog; Suppressor of variegation 3-9 homolog 1; Su(var)3-9 homolog 1 

Gene Name

 SUV39H1 

Gene Synonyms/Alias

 KMT1A; SUV39H 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MAENLKGCSVCCK	ubiquitination	[1, 2, 3]
37	CPALGISKRNLYDFE	ubiquitination	[2]
87	LKCVRILKQFHKDLE	ubiquitination	[2]
123	NYLVQKAKQRRALRR	ubiquitination	[2]
138	WEQELNAKRSHLGRI	ubiquitination	[1, 2, 4, 5]

Reference

 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 

Functional Description

 Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys- 9' as substrate. Also weakly methylates histone H1 (in vitro). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone- modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. 

Sequence Annotation

 DOMAIN 43 101 Chromo.
 DOMAIN 179 240 Pre-SET.
 DOMAIN 243 366 SET.
 DOMAIN 396 412 Post-SET.
 REGION 1 89 Interaction with SIRT1.
 REGION 255 377 Mediates interaction with MECOM (By
 MOD_RES 266 266 N6-acetyllysine.
 MOD_RES 391 391 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Cell cycle; Centromere; Chromatin regulator; Chromosome; Complete proteome; Differentiation; Host-virus interaction; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; Repressor; rRNA processing; S-adenosyl-L-methionine; Transcription; Transcription regulation; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 412 AA 

Protein Sequence

Gene Ontology

 GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
 GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
 GO:0000794; C:condensed nuclear chromosome; TAS:ProtInc.
 GO:0033553; C:rDNA heterochromatin; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; TAS:ProtInc.
 GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0000183; P:chromatin silencing at rDNA; IDA:UniProtKB.
 GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 IPR023780; Chromo_domain.
 IPR000953; Chromo_domain/shadow.
 IPR016197; Chromodomain-like.
 IPR023779; Chromodomain_CS.
 IPR011381; Histone_H3-K9_MeTrfase.
 IPR003616; Post-SET_dom.
 IPR007728; Pre-SET_dom.
 IPR003606; Pre-SET_Zn-bd_sub.
 IPR001214; SET_dom. 

Pfam

 PF00385; Chromo
 PF05033; Pre-SET
 PF00856; SET 

SMART

 SM00298; CHROMO
 SM00508; PostSET
 SM00468; PreSET
 SM00317; SET 

PROSITE

 PS00598; CHROMO_1
 PS50013; CHROMO_2
 PS50868; POST_SET
 PS50867; PRE_SET
 PS51579; SAM_MT43_SUVAR39_3
 PS50280; SET 

PRINTS