CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016943
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Interferon regulatory factor 2-binding protein 1 
Protein Synonyms/Alias
 IRF-2-binding protein 1; IRF-2BP1; Probable E3 ubiquitin-protein ligase IRF2BP1 
Gene Name
 IRF2BP1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
198LFGSDFEKEKQQRNAubiquitination[1]
200GSDFEKEKQQRNADCubiquitination[1]
227EEWHGRPKAVREQLLubiquitination[1]
247APFNVRFKKDHGLVGubiquitination[1, 2]
306DALREPGKALASSGFubiquitination[1, 2]
314ALASSGFKYLEYERRubiquitination[1, 2, 3, 4, 5]
438EALGHSPKDPGGGGGubiquitination[3, 5]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 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. 
Sequence Annotation
 ZN_FING 503 550 RING-type; degenerate.
 REGION 503 550 Cys-rich.
 MOD_RES 66 66 Phosphoserine.
 MOD_RES 125 125 Phosphoserine.
 MOD_RES 186 186 Phosphoserine.
 MOD_RES 384 384 Phosphoserine.
 MOD_RES 421 421 Phosphoserine.
 MOD_RES 436 436 Phosphoserine.
 MOD_RES 453 453 Phosphoserine.
 MOD_RES 457 457 Phosphoserine.  
Keyword
 Coiled coil; Complete proteome; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 584 AA 
Protein Sequence
MASVQASRRQ WCYLCDLPKM PWAMVWDFSE AVCRGCVNFE GADRIELLID AARQLKRSHV 60
LPEGRSPGPP ALKHPATKDL AAAAAQGPQL PPPQAQPQPS GTGGGVSGQD RYDRATSSGR 120
LPLPSPALEY TLGSRLANGL GREEAVAEGA RRALLGSMPG LMPPGLLAAA VSGLGSRGLT 180
LAPGLSPARP LFGSDFEKEK QQRNADCLAE LNEAMRGRAE EWHGRPKAVR EQLLALSACA 240
PFNVRFKKDH GLVGRVFAFD ATARPPGYEF ELKLFTEYPC GSGNVYAGVL AVARQMFHDA 300
LREPGKALAS SGFKYLEYER RHGSGEWRQL GELLTDGVRS FREPAPAEAL PQQYPEPAPA 360
ALCGPPPRAP SRNLAPTPRR RKASPEPEGE AAGKMTTEEQ QQRHWVAPGG PYSAETPGVP 420
SPIAALKNVA EALGHSPKDP GGGGGPVRAG GASPAASSTA QPPTQHRLVA RNGEAEVSPT 480
AGAEAVSGGG SGTGATPGAP LCCTLCRERL EDTHFVQCPS VPGHKFCFPC SREFIKAQGP 540
AGEVYCPSGD KCPLVGSSVP WAFMQGEIAT ILAGDIKVKK ERDP 584 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR022750; Interferon_reg_fac2-bd1_2_Znf.
 IPR018957; Znf_C3HC4_RING-type. 
Pfam
 PF11261; IRF-2BP1_2
 PF00097; zf-C3HC4 
SMART
  
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS