Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Histone-lysine N-methyltransferase SUV39H2  

UniProtKB / Swiss-Prot ID :  SUV92_HUMAN

Gene Name (Synonyms) : 
SUV39H2, KMT1B  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (By similarity). Chromosome, centromere (By similarity). Note=Associates with centromeric constitutive heterochromatin (By similarity). 

Protein Function :  Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys- 9' as substrate. 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 cell cycle regulation, transcriptional repression and regulation of telomere length. May participate in regulation of higher order chromatin organization during spermatogenesis. 

Protein Sequence MAAVGAEARGAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVVKDMEYYLVKWKG...
Predicted Secondary Structure CCCCCCHHCCCEEEEEECCHHHHHHHHHHHHCCCCCCCCCCCCHHHHHHHHHHHHHHHCCCEEEEEEEEC...
Protein Variant
LocationDescription
383D -> H (in a breast cancer sample;somatic mutation).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAVGA
---CCCCCC
15.74UniProtKB
Link-
248PhosphothreonineVQKGTQYSL
EECCEECCE
31.22HPRD
Link
303PhosphothreonineNKGITYLFD
CCCCEEEEE
23.88HPRD
Link
303PhosphothreonineNKGITYLFD
CCCCEEEEE
23.88PhosphoELM
Link
310PhosphotyrosineFDLDYESDE
EEECCCCCC
25.32HPRD
Link
310PhosphotyrosineFDLDYESDE
EEECCCCCC
25.32PhosphoELM
Link
316PhosphothreonineSDEFTVDAA
CCCEEEECC
18.54HPRD
Link
316PhosphothreonineSDEFTVDAA
CCCEEEECC
18.54PhosphoELM
Link
381PhosphoserineSGDISSDSI
CCCCCHHHC
32.60HPRD
Link-
381PhosphoserineSGDISSDSI
CCCCCHHHC
32.60PhosphoELM
Link-
381PhosphoserineSGDISSDSI
CCCCCHHHC
32.60Phosphositeplus
Link-
381PhosphoserineSGDISSDSI
CCCCCHHHC
32.60SysPTM
Link-
381Phosphoserine.SGDISSDSI
CCCCCHHHC
32.60UniProtKB
Link-
382PhosphoserineGDISSDSID
CCCCHHHCC
35.39HPRD
Link-
382PhosphoserineGDISSDSID
CCCCHHHCC
35.39PhosphoELM
Link-
382PhosphoserineGDISSDSID
CCCCHHHCC
35.39SysPTM
Link-
382Phosphoserine.GDISSDSID
CCCCHHHCC
35.39UniProtKB
Link-
384PhosphoserineISSDSIDHS
CCHHHCCCC
31.68HPRD
Link-
384PhosphoserineISSDSIDHS
CCHHHCCCC
31.68PhosphoELM
Link-
384PhosphoserineISSDSIDHS
CCHHHCCCC
31.68Phosphositeplus
Link-
384PhosphoserineISSDSIDHS
CCHHHCCCC
31.68SysPTM
Link-
384Phosphoserine.ISSDSIDHS
CCHHHCCCC
31.68UniProtKB
Link-
388PhosphoserineSIDHSPAKK
HCCCCCCHH
23.86HPRD
Link-
388PhosphoserineSIDHSPAKK
HCCCCCCHH
23.86PhosphoELM
Link-
388PhosphoserineSIDHSPAKK
HCCCCCCHH
23.86Phosphositeplus
Link-
388PhosphoserineSIDHSPAKK
HCCCCCCHH
23.86SysPTM
Link-
388Phosphoserine.SIDHSPAKK
HCCCCCCHH
23.86UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CGBP1_HUMANphysical interactionEBI-735944
intact16169070
UB2V2_HUMANphysical interactionEBI-737747
intact16169070
CGBP1_HUMANyeast 2-hybridHPRD:07580HPRD16169070
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-381; SER-384 AND SER-388, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-381; SER-384 AND SER-388, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381; SER-382; SER-384AND SER-388, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures