CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031547
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 BRCA2 and CDKN1A-interacting protein 
Protein Synonyms/Alias
  
Gene Name
 BCCIP 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
76NDYDGIKKLLQQLFLubiquitination[1, 2, 3, 4]
107NHIGSVIKGTQCVEQubiquitination[4]
129FCEKNCEKSMVEQLDacetylation[5]
129FCEKNCEKSMVEQLDubiquitination[3, 4, 6]
144KFLNDTTKPVGLLLSubiquitination[1, 2, 3, 4]
171PMYQQLQKELAGAHRubiquitination[3, 4]
201KTFVEAGKNNSKKKPubiquitination[3, 4]
205EAGKNNSKKKPSNKKubiquitination[3]
213KKPSNKKKAALMFANubiquitination[3]
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] 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]
 [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] 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]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
 May promote cell cycle arrest by enhancing the inhibition of CDK2 activity by CDKN1A. May be required for repair of DNA damage by homologous recombination in conjunction with BRCA2. May not be involved in non-homologous end joining (NHEJ) (By similarity). 
Sequence Annotation
  
Keyword
 Cell cycle; Complete proteome; DNA damage; DNA repair; Nucleus; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 262 AA 
Protein Sequence
MASRSKRRAV ESGVPQPPDP PVQRDEEEEK EVENEDEDDD DSDKEKDEED EVIDEEVNIE 60
FEAYSLSDND YDGIKKLLQQ LFLKAPVNTA ELTDLLIQQN HIGSVIKGTQ CVEQIQELVL 120
RFCEKNCEKS MVEQLDKFLN DTTKPVGLLL SERFINVPPQ IALPMYQQLQ KELAGAHRTN 180
KPCGKCYFYL LISKTFVEAG KNNSKKKPSN KKKAALMFAN AEEEFFYEEQ GKPEVLGGPD 240
TRRGLEPVPI QHNGWSVPPV LE 262 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW. 
Interpro
 IPR025602; BCP1_family. 
Pfam
 PF13862; BCIP 
SMART
  
PROSITE
  
PRINTS