CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005773
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cellular retinoic acid-binding protein 2 
Protein Synonyms/Alias
 Cellular retinoic acid-binding protein II; CRABP-II 
Gene Name
 CRABP2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
21ENFEELLKVLGVNVMubiquitination[1, 2]
31GVNVMLRKIAVAAASubiquitination[1, 2]
39IAVAAASKPAVEIKQubiquitination[1, 2, 3]
45SKPAVEIKQEGDTFYubiquitination[1, 2]
83TVDGRPCKSLVKWESubiquitination[4, 5]
87RPCKSLVKWESENKMubiquitination[1]
102VCEQKLLKGEGPKTSubiquitination[1, 3]
Reference
 [1] 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]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] 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]
 [4] 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]
 [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
 Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors. 
Sequence Annotation
 REGION 133 135 Retinoic acid binding.
 MOTIF 21 31 Nuclear localization signal.
 CROSSLNK 102 102 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Endoplasmic reticulum; Isopeptide bond; Nucleus; Reference proteome; Retinol-binding; Transport; Ubl conjugation; Vitamin A. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 138 AA 
Protein Sequence
MPNFSGNWKI IRSENFEELL KVLGVNVMLR KIAVAAASKP AVEIKQEGDT FYIKTSTTVR 60
TTEINFKVGE EFEEQTVDGR PCKSLVKWES ENKMVCEQKL LKGEGPKTSW TRELTNDGEL 120
ILTMTADDVV CTRVYVRE 138 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0016918; F:retinal binding; IEA:UniProtKB-KW.
 GO:0001972; F:retinoic acid binding; IEA:Compara.
 GO:0005501; F:retinoid binding; TAS:ProtInc.
 GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
 GO:0005215; F:transporter activity; IEA:InterPro.
 GO:0035115; P:embryonic forelimb morphogenesis; IEA:Compara.
 GO:0008544; P:epidermis development; TAS:ProtInc.
 GO:0006355; P:regulation of transcription, DNA-dependent; TAS:ProtInc.
 GO:0042573; P:retinoic acid metabolic process; IEA:Compara.
 GO:0007165; P:signal transduction; TAS:ProtInc. 
Interpro
 IPR012674; Calycin.
 IPR011038; Calycin-like.
 IPR000463; Fatty_acid-bd.
 IPR000566; Lipocln_cytosolic_FA-bd_dom. 
Pfam
 PF00061; Lipocalin 
SMART
  
PROSITE
 PS00214; FABP 
PRINTS
 PR00178; FATTYACIDBP.