SUV92_HUMAN - dbPTM
SUV92_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SUV92_HUMAN
UniProt AC Q9H5I1
Protein Name Histone-lysine N-methyltransferase SUV39H2
Gene Name SUV39H2
Organism Homo sapiens (Human).
Sequence Length 410
Subcellular Localization Nucleus. Chromosome, centromere. Associates with centromeric constitutive heterochromatin..
Protein Description 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. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation..
Protein Sequence MAAVGAEARGAWCVPCLVSLDTLQELCRKEKLTCKSIGITKRNLNNYEVEYLCDYKVVKDMEYYLVKWKGWPDSTNTWEPLQNLKCPLLLQQFSNDKHNYLSQVKKGKAITPKDNNKTLKPAIAEYIVKKAKQRIALQRWQDELNRRKNHKGMIFVENTVDLEGPPSDFYYINEYKPAPGISLVNEATFGCSCTDCFFQKCCPAEAGVLLAYNKNQQIKIPPGTPIYECNSRCQCGPDCPNRIVQKGTQYSLCIFRTSNGRGWGVKTLVKIKRMSFVMEYVGEVITSEEAERRGQFYDNKGITYLFDLDYESDEFTVDAARYGNVSHFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTINAGEELTFDYQMKGSGDISSDSIDHSPAKKRVRTVCKCGAVTCRGYLN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAAVGAEAR
------CCCCCCCCC		15.74-
41AcetylationCKSIGITKRNLNNYE
CCEECCCCCCCCCCE		37.0525953088
45UbiquitinationGITKRNLNNYEVEYL
CCCCCCCCCCEEEEE		53.2229967540
53UbiquitinationNYEVEYLCDYKVVKD
CCEEEEEEEEEEECC		5.4229967540
63PhosphorylationKVVKDMEYYLVKWKG
EEECCCEEEEEEECC		8.7522985185
69UbiquitinationEYYLVKWKGWPDSTN
EEEEEEECCCCCCCC		45.4333845483
85MethylationWEPLQNLKCPLLLQQ
CHHHHCCCCCHHHHH		41.16115980297
97AcetylationLQQFSNDKHNYLSQV
HHHHCCCCCCCHHHH		37.6926051181
105UbiquitinationHNYLSQVKKGKAITP
CCCHHHHCCCCCCCC		48.4429967540
111PhosphorylationVKKGKAITPKDNNKT
HCCCCCCCCCCCCCC		29.1924719451
113UbiquitinationKGKAITPKDNNKTLK
CCCCCCCCCCCCCCC		65.5229967540
118PhosphorylationTPKDNNKTLKPAIAE
CCCCCCCCCCHHHHH		41.98-
120AcetylationKDNNKTLKPAIAEYI
CCCCCCCCHHHHHHH		37.3226051181
129AcetylationAIAEYIVKKAKQRIA
HHHHHHHHHHHHHHH		37.1426051181
129UbiquitinationAIAEYIVKKAKQRIA
HHHHHHHHHHHHHHH		37.1433845483
148PhosphorylationQDELNRRKNHKGMIF
HHHHHHHHCCCCEEE		61.2332645325
208PhosphorylationCCPAEAGVLLAYNKN
HCCCCCCEEEEEECC		5.2232645325
248PhosphorylationNRIVQKGTQYSLCIF
CCCEECCCCEEEEEE		31.2220068231
250PhosphorylationIVQKGTQYSLCIFRT
CEECCCCEEEEEEEC		11.9320068231
251PhosphorylationVQKGTQYSLCIFRTS
EECCCCEEEEEEECC		13.6220068231
303PhosphorylationFYDNKGITYLFDLDY
CCCCCCEEEEEECCC		23.8818669648
310PhosphorylationTYLFDLDYESDEFTV
EEEEECCCCCCCEEE		25.3218669648
316PhosphorylationDYESDEFTVDAARYG
CCCCCCEEEEHHHHC		18.5418669648
328PhosphorylationRYGNVSHFVNHSCDP
HHCCHHHHHCCCCCC		4.6032645325
377PhosphorylationFDYQMKGSGDISSDS
ECEEECCCCCCCCCC		27.9828176443
381PhosphorylationMKGSGDISSDSIDHS
ECCCCCCCCCCCCCC		32.6029255136
382PhosphorylationKGSGDISSDSIDHSP
CCCCCCCCCCCCCCC		35.3929255136
384PhosphorylationSGDISSDSIDHSPAK
CCCCCCCCCCCCCCH		31.6829255136
388PhosphorylationSSDSIDHSPAKKRVR
CCCCCCCCCCHHHHC		23.8629255136
396PhosphorylationPAKKRVRTVCKCGAV
CCHHHHCCEEECCCE		27.65-
404PhosphorylationVCKCGAVTCRGYLN-
EEECCCEEECCCCC-		8.92-
408PhosphorylationGAVTCRGYLN-----
CCEEECCCCC-----		5.45-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SUV92_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SUV92_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SUV92_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMAD5_HUMANSMAD5physical
15107829
RASF1_HUMANRASSF1physical
21900206
GANP_HUMANMCM3APphysical
21900206
SHC1_HUMANSHC1physical
21900206
CEP70_HUMANCEP70physical
21900206
LRIF1_HUMANLRIF1physical
21900206
FA20C_HUMANFAM20Cphysical
21900206
EHMT1_HUMANEHMT1physical
26186194
EHMT2_HUMANEHMT2physical
26186194
AP4E1_HUMANAP4E1physical
26186194
CBX1_HUMANCBX1physical
26186194
CBX5_HUMANCBX5physical
26186194
SYNC_HUMANNARSphysical
26186194
ZN644_HUMANZNF644physical
26186194
AP4E1_HUMANAP4E1physical
28514442
CBX5_HUMANCBX5physical
28514442
ZN644_HUMANZNF644physical
28514442
EHMT2_HUMANEHMT2physical
28514442
EHMT1_HUMANEHMT1physical
28514442
AP4S1_HUMANAP4S1physical
28514442
ACTBL_HUMANACTBL2physical
28514442
CBX1_HUMANCBX1physical
28514442
AP4M1_HUMANAP4M1physical
28514442
ANDR_HUMANARphysical
28042025
MAGAB_HUMANMAGEA11physical
28042025
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SUV92_HUMAN

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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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