CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010400
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Immunoglobulin-binding protein 1 
Protein Synonyms/Alias
 B-cell signal transduction molecule alpha 4; Protein alpha-4; CD79a-binding protein 1; Protein phosphatase 2/4/6 regulatory subunit; Renal carcinoma antigen NY-REN-16 
Gene Name
 IGBP1 
Gene Synonyms/Alias
 IBP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
44IVQEKVFKGLDLLEKubiquitination[1, 2, 3, 4, 5]
91FQGALTMKQVNPSKRubiquitination[3, 5]
176EHRLSAMKSAVESGQubiquitination[6]
241RQERPPVKPFILTRNacetylation[5, 7, 8]
241RQERPPVKPFILTRNubiquitination[1, 2, 3, 4]
253TRNMAQAKVFGAGYPubiquitination[1, 4]
287LPDQGIAKAAPEEFRubiquitination[3, 6]
295AAPEEFRKAAQQQEEubiquitination[6]
Reference
 [1] 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]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
 Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits. 
Sequence Annotation
 REPEAT 46 60 UIM.
 REGION 98 202 Interaction with PPP2CA.
 REGION 225 290 Interaction with MID1.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 241 241 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; B-cell activation; Chaperone; Complete proteome; Cytoplasm; Mental retardation; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 339 AA 
Protein Sequence
MAAEDELQLP RLPELFETGR QLLDEVEVAT EPAGSRIVQE KVFKGLDLLE KAAEMLSQLD 60
LFSRNEDLEE IASTDLKYLL VPAFQGALTM KQVNPSKRLD HLQRAREHFI NYLTQCHCYH 120
VAEFELPKTM NNSAENHTAN SSMAYPSLVA MASQRQAKIQ RYKQKKELEH RLSAMKSAVE 180
SGQADDERVR EYYLLHLQRW IDISLEEIES IDQEIKILRE RDSSREASTS NSSRQERPPV 240
KPFILTRNMA QAKVFGAGYP SLPTMTVSDW YEQHRKYGAL PDQGIAKAAP EEFRKAAQQQ 300
EEQEEKEEED DEQTLHRARE WDDWKDTHPR GYGNRQNMG 339 
Gene Ontology
 GO:0005737; C:cytoplasm; NAS:UniProtKB.
 GO:0008601; F:protein phosphatase type 2A regulator activity; IDA:UniProtKB.
 GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
 GO:0035308; P:negative regulation of protein dephosphorylation; IEA:Compara.
 GO:0032873; P:negative regulation of stress-activated MAPK cascade; IMP:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
 GO:0035306; P:positive regulation of dephosphorylation; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0060632; P:regulation of microtubule-based movement; IMP:UniProtKB.
 GO:0070555; P:response to interleukin-1; IMP:UniProtKB.
 GO:0034612; P:response to tumor necrosis factor; IMP:UniProtKB.
 GO:0007165; P:signal transduction; NAS:UniProtKB. 
Interpro
 IPR007304; TAP42-like. 
Pfam
 PF04177; TAP42 
SMART
  
PROSITE
 PS50330; UIM 
PRINTS