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 1  

UniProtKB / Swiss-Prot ID :  I2BP1_HUMAN

Gene Name (Synonyms) : 
IRF2BP1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Acts as a transcriptional corepressor in a IRF2- dependent manner; this repression is not mediated by histone deacetylase activities. May act as an E3 ligase towards JDP2, enhancing its polyubiquitination. Represses ATF2-dependent transcriptional activation. 

Protein Sequence MASVQASRRQWCYLCDLPKMPWAMVWDFSEAVCRGCVNFEGADRIELLIDAARQLKRSHVLPEGRSPGPP...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
24M -> I (in dbSNP:rs11550349). VAR_042502
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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.---MASVQA
---
20.57UniProtKB
Link-
66PhosphoserinePEGRSPGPP
45.10HPRD
Link-
66PhosphoserinePEGRSPGPP
45.10Phosphositeplus
Link-
66PhosphoserinePEGRSPGPP
45.10SysPTM
Link-
66Phosphoserine.PEGRSPGPP
45.10UniProtKB
Link-
125PhosphoserineLPLPSPALE
30.41Phosphositeplus
Link-
125Phosphoserine.LPLPSPALE
30.41UniProtKB
Link-
130PhosphotyrosinePALEYTLGS
14.23Phosphositeplus
Link-
186PhosphoserineAPGLSPARP
23.56HPRD
Link-
186PhosphoserineAPGLSPARP
23.56Phosphositeplus
Link-
186PhosphoserineAPGLSPARP
23.56SysPTM
Link-
186Phosphoserine.APGLSPARP
23.56UniProtKB
Link-
268PhosphotyrosineRPPGYEFEL
24.18Phosphositeplus
Link-
314Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SSGFKYLEY
53.07Phosphositeplus
Link-
384PhosphoserineRRKASPEPE
32.60HPRD
Link-
384PhosphoserineRRKASPEPE
32.60Phosphositeplus
Link-
384PhosphoserineRRKASPEPE
32.60SysPTM
Link-
421PhosphoserinePGVPSPIAA
26.91HPRD
Link-
421PhosphoserinePGVPSPIAA
26.91Phosphositeplus
Link-
421PhosphoserinePGVPSPIAA
26.91SysPTM
Link-
421Phosphoserine.PGVPSPIAA
26.91UniProtKB
Link-
436PhosphoserineALGHSPKDP
31.67HPRD
Link-
436PhosphoserineALGHSPKDP
31.67Phosphositeplus
Link-
436PhosphoserineALGHSPKDP
31.67SysPTM
Link-
436Phosphoserine.ALGHSPKDP
31.67UniProtKB
Link-
438Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GHSPKDPGG
78.54Phosphositeplus
Link-
453PhosphoserineAGGASPAAS
20.53HPRD
Link-
453PhosphoserineAGGASPAAS
20.53Phosphositeplus
Link-
453PhosphoserineAGGASPAAS
20.53SysPTM
Link-
453Phosphoserine.AGGASPAAS
20.53UniProtKB
Link-
457PhosphoserineSPAASSTAQ
30.26HPRD
Link-
457PhosphoserineSPAASSTAQ
30.26Phosphositeplus
Link-
457PhosphoserineSPAASSTAQ
30.26SysPTM
Link-
457Phosphoserine.SPAASSTAQ
30.26UniProtKB
Link-
491PhosphoserineSGGGSGTGA
36.13HPRD
Link-
493PhosphothreonineGGSGTGATP
25.91HPRD
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, AND MASS SPECTROMETRY.
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-125 AND SER-436, 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-421; SER-436 ANDSER-453, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-453, ANDMASS SPECTROMETRY.
"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-66; SER-186; SER-421;SER-436; SER-453 AND SER-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