Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Interferon regulatory factor 2-binding protein 2  

UniProtKB / Swiss-Prot ID :  I2BP2_HUMAN

Gene Name (Synonyms) : 
IRF2BP2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. 

Protein Function :  Acts as a transcriptional corepressor in a IRF2- dependent manner; this repression is not mediated by histone deacetylase activities. Represses the NFAT1-dependent transactivation of NFAT-responsive promoters. Acts as a coactivator of VEGFA expression in cardiac and skeletal muscle. 

Protein Sequence MAAAVAVAAASRRQSCYLCDLPRMPWAMIWDFTEPVCRGCVNYEGADRVEFVIETARQLKRAHGCFPEGR...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
254A -> V (in dbSNP:rs11502). VAR_042503
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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.---MAAAVA
---
12.25UniProtKB
Link-
71PhosphoserinePEGRSPPGA
46.43Phosphositeplus
Link-
175PhosphoserineLNRQSPNPR
24.33HPRD
Link-
175PhosphoserineLNRQSPNPR
24.33Phosphositeplus
Link-
175Phosphoserine.LNRQSPNPR
24.33UniProtKB
Link-
240PhosphoserineKRPASVSSS
25.80HPRD
Link-
240PhosphoserineKRPASVSSS
25.80Phosphositeplus
Link-
242PhosphoserinePASVSSSAA
18.97HPRD
Link-
242PhosphoserinePASVSSSAA
18.97Phosphositeplus
Link-
243PhosphoserineASVSSSAAV
23.11Phosphositeplus
Link-
244PhosphoserineSVSSSAAVE
16.85Phosphositeplus
Link-
272PhosphoserineGPADSLSTA
26.73HPRD
Link-
318PhosphoserineQHGHSGPFE
53.40HPRD
Link-
318PhosphoserineQHGHSGPFE
53.40Phosphositeplus
Link-
323PhosphoserineGPFESKFKK
43.71HPRD
Link-
323PhosphoserineGPFESKFKK
43.71Phosphositeplus
Link-
360PhosphoserineKRKPSPEPE
44.95HPRD
Link-
360PhosphoserineKRKPSPEPE
44.95Phosphositeplus
Link-
360PhosphoserineKRKPSPEPE
44.95SysPTM
Link-
360Phosphoserine.KRKPSPEPE
44.95UniProtKB
Link-
381PhosphoserineQPWLSTSTE
19.22HPRD
Link-
392PhosphothreonineKIPMTPTSS
20.33Phosphositeplus
Link-
392Phosphothreonine.KIPMTPTSS
20.33UniProtKB
Link-
396PhosphoserineTPTSSFVSP
31.95HPRD
Link-
396PhosphoserineTPTSSFVSP
31.95SysPTM
Link-
404PhosphothreoninePPPPTASPH
45.61HPRD
Link-
406PhosphoserinePPTASPHSN
26.14HPRD
Link-
406PhosphoserinePPTASPHSN
26.14Phosphositeplus
Link-
412PhosphothreonineHSNRTTPPE
48.15HPRD
Link-
413PhosphothreonineSNRTTPPEA
33.34HPRD
Link-
423PhosphoserineQNGQSPMAA
20.31HPRD
Link-
441PhosphoserineGSHASKDAN
26.16HPRD
Link-
455PhosphoserineTRRNSNSPP
36.55HPRD
Link-
455PhosphoserineTRRNSNSPP
36.55Phosphositeplus
Link-
455PhosphoserineTRRNSNSPP
36.55SysPTM
Link-
455Phosphoserine.TRRNSNSPP
36.55UniProtKB
Link-
457PhosphoserineRNSNSPPSP
37.70HPRD
Link-
457PhosphoserineRNSNSPPSP
37.70Phosphositeplus
Link-
457PhosphoserineRNSNSPPSP
37.70SysPTM
Link-
457Phosphoserine.RNSNSPPSP
37.70UniProtKB
Link-
460PhosphoserineNSPPSPSSM
40.58HPRD
Link-
460PhosphoserineNSPPSPSSM
40.58Phosphositeplus
Link-
460PhosphoserineNSPPSPSSM
40.58SysPTM
Link-
460Phosphoserine.NSPPSPSSM
40.58UniProtKB
Link-
462PhosphoserinePPSPSSMNQ
46.70HPRD
Link-
462PhosphoserinePPSPSSMNQ
46.70SysPTM
Link-
462Phosphoserine.PPSPSSMNQ
46.70UniProtKB
Link-
463PhosphoserinePSPSSMNQR
25.74HPRD
Link-
495Caspase cleavage aspartic acidASLPDSSLA
57.03Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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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-455; SER-457; SER-460 AND SER-462, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Identification of a phosphorylation-dependent nuclear localizationmotif in interferon regulatory factor 2 binding protein 2.";
Teng A.C., Al-Montashiri N.A., Cheng B.L., Lou P., Ozmizrak P.,Chen H.H., Stewart A.F.;
PLoS ONE 6:E24100-E24100(2011).
Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND PHOSPHORYLATIONAT SER-360.
"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-175; SER-360; SER-455;SER-457 AND SER-460, AND MASS 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-455; SER-457; SER-460 AND SER-462, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND MASSSPECTROMETRY.
"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-360; THR-392 ANDSER-457, 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