Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein virilizer homolog  

UniProtKB / Swiss-Prot ID :  VIR_HUMAN

Gene Name (Synonyms) : 
KIAA1429 MSTP054  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (By similarity). 

Protein Function :  May be involved in mRNA splicing regulation (By similarity). 

Protein Sequence MAVDSAMELLFLDTFKHPSAEQSSHIDVVRFPCVVYINEVRVIPPGVRAHSSLPDNRAYGETSPHTFQLD...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
753I -> V (in dbSNP:rs7814840). VAR_036845
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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
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.---MAVDSA
---
25.73UniProtKB
Link-
36PhosphotyrosinePCVVYINEV
4.24HPRD
Link-
36PhosphotyrosinePCVVYINEV
4.24Phosphositeplus
Link-
105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RPNSKVNTD
46.26Phosphositeplus
Link-
108PhosphothreonineSKVNTDGLV
34.14HPRD
Link-
108PhosphothreonineSKVNTDGLV
34.14Phosphositeplus
Link-
133PhosphoserineDRVISHDRD
19.24HPRD
Link-
133PhosphoserineDRVISHDRD
19.24Phosphositeplus
Link-
138PhosphoserineHDRDSPPPP
39.95HPRD
Link-
138PhosphoserineHDRDSPPPP
39.95Phosphositeplus
Link-
138PhosphoserineHDRDSPPPP
39.95SysPTM
Link-
138Phosphoserine.HDRDSPPPP
39.95UniProtKB
Link-
173PhosphoserineQFNGSPPRP
32.60HPRD
Link-
173PhosphoserineQFNGSPPRP
32.60Phosphositeplus
Link-
173PhosphoserineQFNGSPPRP
32.60SysPTM
Link-
173Phosphoserine.QFNGSPPRP
32.60UniProtKB
Link-
184PhosphothreonineRGPRTPPGP
36.65HPRD
Link-
184PhosphothreonineRGPRTPPGP
36.65Phosphositeplus
Link-
184PhosphothreonineRGPRTPPGP
36.65SysPTM
Link-
184Phosphothreonine.RGPRTPPGP
36.65UniProtKB
Link-
204PhosphoserinePLPVSGDKE
39.06Phosphositeplus
Link-
217PhosphotyrosineHREDYFEPI
12.70Phosphositeplus
Link-
222PhosphoserineFEPISPDRN
31.31HPRD
Link-
222PhosphoserineFEPISPDRN
31.31Phosphositeplus
Link-
222PhosphoserineFEPISPDRN
31.31SysPTM
Link-
222Phosphoserine.FEPISPDRN
31.31UniProtKB
Link-
235PhosphoserineEGQYSDEGE
22.69HPRD
Link-
302PhosphoserineYEQISSDED
31.28HPRD
Link-
303PhosphoserineEQISSDEDG
46.80HPRD
Link-
373Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QGPDKENSG
63.03Phosphositeplus
Link-
576Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HLAEKTSSL
48.37Phosphositeplus
Link-
887Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ENNAKLQEL
53.48Phosphositeplus
Link-
899Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LEPLKNLRF
65.73Phosphositeplus
Link-
914PhosphotyrosineNLIEYVKQN
13.12Phosphositeplus
Link-
1029Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SFEFKDMRV
43.34Phosphositeplus
Link-
1432PhosphoserineSRTMSINAA
16.45HPRD
Link-
1472PhosphoserineDNLDSLLDS
33.72HPRD
Link-
1578PhosphoserineLSEPSSPGR
45.15HPRD
Link-
1578PhosphoserineLSEPSSPGR
45.15Phosphositeplus
Link-
1578PhosphoserineLSEPSSPGR
45.15SysPTM
Link-
1579PhosphoserineSEPSSPGRT
41.93HPRD
Link-
1579PhosphoserineSEPSSPGRT
41.93Phosphositeplus
Link-
1579PhosphoserineSEPSSPGRT
41.93SysPTM
Link-
1579Phosphoserine.SEPSSPGRT
41.93UniProtKB
Link-
1583PhosphothreonineSPGRTKTTK
38.36HPRD
Link-
1583PhosphothreonineSPGRTKTTK
38.36SysPTM
Link-
1647PhosphoserineKQNTSRPPS
50.79HPRD
Link-
1708PhosphothreonineNRFFTPPAS
26.17HPRD
Link-
1708PhosphothreonineNRFFTPPAS
26.17Phosphositeplus
Link-
1708PhosphothreonineNRFFTPPAS
26.17SysPTM
Link-
1708Phosphothreonine.NRFFTPPAS
26.17UniProtKB
Link-
1798PhosphoserineGKFVSGGSG
40.34HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433Z_HUMANphysical interactionMINT-3297021MINT15161933
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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-1579, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1579, 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-1579 AND THR-1708, ANDMASS SPECTROMETRY.
"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-1579, AND MASS SPECTROMETRY.
"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-138 AND SER-1579, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222 AND SER-1579, ANDMASS SPECTROMETRY.
"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-173; THR-184 ANDSER-222, 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