SUV91_HUMAN - dbPTM
SUV91_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SUV91_HUMAN
UniProt AC O43463
Protein Name Histone-lysine N-methyltransferase SUV39H1
Gene Name SUV39H1
Organism Homo sapiens (Human).
Sequence Length 412
Subcellular Localization Nucleus. Nucleus lamina. Nucleus, nucleoplasm. 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. 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. 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 MAENLKGCSVCCKSSWNQLQDLCRLAKLSCPALGISKRNLYDFEVEYLCDYKKIREQEYYLVKWRGYPDSESTWEPRQNLKCVRILKQFHKDLERELLRRHHRSKTPRHLDPSLANYLVQKAKQRRALRRWEQELNAKRSHLGRITVENEVDLDGPPRAFVYINEYRVGEGITLNQVAVGCECQDCLWAPTGGCCPGASLHKFAYNDQGQVRLRAGLPIYECNSRCRCGYDCPNRVVQKGIRYDLCIFRTDDGRGWGVRTLEKIRKNSFVMEYVGEIITSEEAERRGQIYDRQGATYLFDLDYVEDVYTVDAAYYGNISHFVNHSCDPNLQVYNVFIDNLDERLPRIAFFATRTIRAGEELTFDYNMQVDPVDMESTRMDSNFGLAGLPGSPKKRVRIECKCGTESCRKYLF
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
6Ubiquitination--MAENLKGCSVCCK
--CCCCCCCCCEECC		70.2522505724
13UbiquitinationKGCSVCCKSSWNQLQ
CCCCEECCCCHHHHH		42.2629967540
37UbiquitinationCPALGISKRNLYDFE
CCCCCCCCCCCCEEE		43.30-
48UbiquitinationYDFEVEYLCDYKKIR
CEEEEEEEECCHHHH		0.83-
63UbiquitinationEQEYYLVKWRGYPDS
CCEEEEEEECCCCCC		28.6929967540
70PhosphorylationKWRGYPDSESTWEPR
EECCCCCCCCCCCCC		29.01-
74UbiquitinationYPDSESTWEPRQNLK
CCCCCCCCCCCCCHH		23.9129967540
81UbiquitinationWEPRQNLKCVRILKQ
CCCCCCHHHHHHHHH		37.9329967540
87UbiquitinationLKCVRILKQFHKDLE
HHHHHHHHHHHHHHH		48.8529967540
91UbiquitinationRILKQFHKDLERELL
HHHHHHHHHHHHHHH		66.3629967540
92UbiquitinationILKQFHKDLERELLR
HHHHHHHHHHHHHHH		45.2329967540
98UbiquitinationKDLERELLRRHHRSK
HHHHHHHHHHHHHCC		3.76-
98UbiquitinationKDLERELLRRHHRSK
HHHHHHHHHHHHHCC		3.7629967540
102UbiquitinationRELLRRHHRSKTPRH
HHHHHHHHHCCCCCC		33.6229967540
104PhosphorylationLLRRHHRSKTPRHLD
HHHHHHHCCCCCCCC		36.2023898821
105MethylationLRRHHRSKTPRHLDP
HHHHHHCCCCCCCCH		63.61126257621
106PhosphorylationRRHHRSKTPRHLDPS
HHHHHCCCCCCCCHH		27.1423898821
113PhosphorylationTPRHLDPSLANYLVQ
CCCCCCHHHHHHHHH		39.5223898821
117PhosphorylationLDPSLANYLVQKAKQ
CCHHHHHHHHHHHHH		11.5723898821
121UbiquitinationLANYLVQKAKQRRAL
HHHHHHHHHHHHHHH		50.5021906983
123UbiquitinationNYLVQKAKQRRALRR
HHHHHHHHHHHHHHH		51.9122817900
123MethylationNYLVQKAKQRRALRR
HHHHHHHHHHHHHHH		51.91126257623
132UbiquitinationRRALRRWEQELNAKR
HHHHHHHHHHHHHCH		32.1621963094
132UbiquitinationRRALRRWEQELNAKR
HHHHHHHHHHHHHCH		32.16-
134UbiquitinationALRRWEQELNAKRSH
HHHHHHHHHHHCHHC		32.2622817900
134UbiquitinationALRRWEQELNAKRSH
HHHHHHHHHHHCHHC		32.26-
138UbiquitinationWEQELNAKRSHLGRI
HHHHHHHCHHCCCCE		54.0523000965
146PhosphorylationRSHLGRITVENEVDL
HHCCCCEEEECEECC		22.02-
149UbiquitinationLGRITVENEVDLDGP
CCCEEEECEECCCCC		50.7023000965
162PhosphorylationGPPRAFVYINEYRVG
CCCCEEEEEEEEEEC		7.5029496907
214MethylationDQGQVRLRAGLPIYE
CCCCEEEECCCCEEE		18.9530995317
224PhosphorylationLPIYECNSRCRCGYD
CCEEEECCCCCCCCC		44.4020068231
260PhosphorylationGRGWGVRTLEKIRKN
CCCCCHHCHHHHHCC		36.5429083192
266AcetylationRTLEKIRKNSFVMEY
HCHHHHHCCCCHHHE		61.4918004385
297PhosphorylationYDRQGATYLFDLDYV
CCCCCCEEEEECCCE		12.58-
381PhosphorylationMESTRMDSNFGLAGL
HHHCCCCCCCCCCCC		25.3923927012
391PhosphorylationGLAGLPGSPKKRVRI
CCCCCCCCCCCCEEE		31.4429255136
402PhosphorylationRVRIECKCGTESCRK
CEEEEEECCCHHHHH		14.2532645325
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 SUV91_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
266KAcetylation

18004385
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 SUV91_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBX5_HUMANCBX5physical
16189514
RUNX1_HUMANRUNX1physical
12917624
DNM3A_HUMANDNMT3Aphysical
12711675
RBL1_HUMANRBL1physical
12588981
RBL2_HUMANRBL2physical
12588981
RB_HUMANRB1physical
11484059
RB_HUMANRB1physical
11533237
MTMR5_HUMANSBF1physical
10848615
MTMR5_HUMANSBF1genetic
10848615
CBX1_HUMANCBX1physical
10202156
CBX5_MOUSECbx5physical
12565857
HDAC1_HUMANHDAC1physical
11788710
HDAC2_HUMANHDAC2physical
11788710
HDAC3_HUMANHDAC3physical
11788710
RBBP4_HUMANRBBP4physical
11788710
RBBP7_HUMANRBBP7physical
11788710
CABIN_HUMANCABIN1physical
17172641
GFI1B_HUMANGFI1Bphysical
16688220
RUNX1_HUMANRUNX1physical
16652147
RUNX3_HUMANRUNX3physical
16652147
EVI1_HUMANMECOMphysical
18655152
VIGLN_HUMANHDLBPphysical
18648073
EVI1_HUMANMECOMphysical
18619962
H31_HUMANHIST1H3Aphysical
16449642
H31_HUMANHIST1H3Aphysical
16409643
ESCO2_HUMANESCO2physical
18501190
CBX4_HUMANCBX4physical
12101246
EPC2_XENLAepc2physical
12101246
TAL1_HUMANTAL1physical
15677454
DNM3B_HUMANDNMT3Bphysical
15120635
SMAD5_HUMANSMAD5physical
15107829
SIR1_HUMANSIRT1physical
18004385
BC11B_HUMANBCL11Bphysical
17245431
ESCO1_HUMANESCO1physical
20331966
CBX4_HUMANCBX4physical
22078878
RUNX2_HUMANRUNX2physical
22537242
UHRF1_HUMANUHRF1physical
22330138
CTNB1_HUMANCTNNB1physical
21726809
CDC73_HUMANCDC73physical
21726809
KDM1A_HUMANKDM1Aphysical
23455924
ANM6_HUMANPRMT6physical
23455924
CBX5_HUMANCBX5physical
25416956
HOOK2_HUMANHOOK2physical
25416956
CEP70_HUMANCEP70physical
25416956
LZTS2_HUMANLZTS2physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
ESR1_HUMANESR1physical
24101509
SUV91_HUMANSUV39H1physical
24101509
H33_HUMANH3F3Aphysical
17172641
H31_HUMANHIST1H3Aphysical
16858404
DAXX_HUMANDAXXphysical
26340527
MAGC1_HUMANMAGEC1physical
28514442
UBP34_HUMANUSP34physical
28514442
MCAF1_HUMANATF7IPphysical
28514442
MCMBP_HUMANMCMBPphysical
28514442
ENKD1_HUMANENKD1physical
28514442
CBX5_HUMANCBX5physical
28514442
ZN644_HUMANZNF644physical
28514442
UBP24_HUMANUSP24physical
28514442
SETB1_HUMANSETDB1physical
28514442
M1IP1_HUMANMID1IP1physical
28514442
ABRX2_HUMANFAM175Bphysical
28514442
USP9X_HUMANUSP9Xphysical
28514442
PHLP_HUMANPDCLphysical
28514442
DDI2_HUMANDDI2physical
28514442
EHMT2_HUMANEHMT2physical
28514442
UBP7_HUMANUSP7physical
26971997
MDM2_HUMANMDM2physical
26971997
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 SUV91_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"SIRT1 regulates the histone methyl-transferase SUV39H1 duringheterochromatin formation.";
Vaquero A., Scher M., Erdjument-Bromage H., Tempst P., Serrano L.,Reinberg D.;
Nature 450:440-444(2007).
Cited for: FUNCTION, CATALYTIC ACTIVITY, ACETYLATION AT LYS-266, MUTAGENESIS OFLYS-266, AND SUBCELLULAR LOCATION.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, 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-391, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND MASSSPECTROMETRY.

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