CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011967
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 
Protein Synonyms/Alias
  
Gene Name
 BNIP2 
Gene Synonyms/Alias
 NIP2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
174KTTEVIRKGSITEYTubiquitination[1]
186EYTAAEEKEDGRRWRubiquitination[1]
207QDHRVDMKAIEPYKKubiquitination[1]
214KAIEPYKKVISHGGYubiquitination[1]
281NGATTRRKMPSLGWLubiquitination[1, 2]
290PSLGWLRKCYQQIDRubiquitination[1]
329TRPFISSKFSQKIRYubiquitination[1, 2, 3]
333ISSKFSQKIRYVFNLubiquitination[1]
368VDQELNGKQDEPKNEubiquitination[1]
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] 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] 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
 Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins. 
Sequence Annotation
 DOMAIN 147 304 CRAL-TRIO.
 MOD_RES 114 114 Phosphoserine.  
Keyword
 Alternative splicing; Apoptosis; Complete proteome; Cytoplasm; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 314 AA 
Protein Sequence
MEPCPSSAPP PFYPGVGEVA GLRWFSIYDQ RPSWYRTKKL GLLDIGSLDY QEFVVDIESR 60
LRMEGVELKE EWQDEDFPIP LPEDDSIEAD ILAITGPEDQ PGSLEVNGNK VRKKLMAPDI 120
SLTLDPSDGS VLSDDLDESG EIDLDGLDTP SENSNEFEWE DDLPKPKTTE VIRKGSITEY 180
TAAEEKEDGR RWRMFRIGEQ DHRVDMKAIE PYKKVISHGG YYGDGLNAIV VFAVCFMPES 240
SQPNYRYLMD NLFKYVIGTL ELLVAENYMI VYLNGATTRR KMPSLGWLRK CYQQIDRRLR 300
KNLKSLIIVH PSWFIRTLLA VTRPFISSKF SQKIRYVFNL AELAELVPME YVGIPECIKQ 360
VDQELNGKQD EPKNEQ 376 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005635; C:nuclear envelope; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; TAS:UniProtKB.
 GO:0005096; F:GTPase activator activity; TAS:ProtInc.
 GO:0006915; P:apoptotic process; IPI:MGI.
 GO:0042692; P:muscle cell differentiation; TAS:Reactome.
 GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
 GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome. 
Interpro
 IPR022181; Bcl2-/adenovirus-E1B.
 IPR001251; CRAL-TRIO_dom. 
Pfam
 PF12496; BNIP2 
SMART
 SM00516; SEC14 
PROSITE
 PS50191; CRAL_TRIO 
PRINTS