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_MOUSE

Gene Name (Synonyms) : 
Irf2bp1  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Nucleus (By similarity). 

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 (By similarity). 

Protein Sequence MASVQASRRQWCYLCDLPKMPWAMVWDFSEAVCRGCVNFEGADRIELLIDAARQLKRSHVLPEGRSPGPP...
Predicted Secondary Structure  -
Protein Variant -
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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
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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
66PhosphoserinePEGRSPGPP
45.10Phosphositeplus
Link-
384PhosphoserineRRKASPEPE
32.60Phosphositeplus
Link-
384Phosphoserine.RRKASPEPE
32.60UniProtKB
Link-
421PhosphoserinePGVPSPIAA
26.91Phosphositeplus
Link-
436PhosphoserineALGHSPKDP
31.67Phosphositeplus
Link-
436Phosphoserine.ALGHSPKDP
31.67UniProtKB
Link-
453PhosphoserineAGGASPAAS
20.53Phosphositeplus
Link-
453Phosphoserine.AGGASPAAS
20.53UniProtKB
Link-
457PhosphoserineSPAASSTTQ
30.26Phosphositeplus
Link-
478PhosphoserineEAEVSPTAG
14.19Phosphositeplus
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
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384; SER-436 ANDSER-453, AND MASS SPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures