CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019651
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein cereblon 
Protein Synonyms/Alias
  
Gene Name
 CRBN 
Gene Synonyms/Alias
 AD-006 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
43QDSKEAKKPNIINFDubiquitination[1, 2, 3]
116MVRNLIQKDRTFAVLubiquitination[2]
166AIGRQRFKVLELRTQubiquitination[1, 2, 3]
211KCQIFPSKPVSREDQubiquitination[2]
222REDQCSYKWWQKYQKubiquitination[2]
226CSYKWWQKYQKRKFHubiquitination[2]
269REWDENLKDDSLPSNubiquitination[4]
300VLRIQLLKIGSAIQRubiquitination[1, 2, 3, 5]
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] 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]
 [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]
 [4] 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]
 [5] 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
Functional Description
 Component of some DCX (DDB1-CUL4-X-box) E3 protein ligase complex, a complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins and is required for limb outgrowth and expression of the fibroblast growth factor FGF8. In the complex, may act as a substrate receptor. Regulates the assembly and neuronal surface expression of large-conductance calcium-activated potassium channels in brain regions involved in memory and learning via its interaction with KCNT1. 
Sequence Annotation
 DOMAIN 80 317 Lon.
 REGION 339 442 Thalidomide-binding.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Membrane; Mental retardation; Nucleus; Reference proteome; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 442 AA 
Protein Sequence
MAGEGDQQDA AHNMGNHLPL LPAESEEEDE MEVEDQDSKE AKKPNIINFD TSLPTSHTYL 60
GADMEEFHGR TLHDDDSCQV IPVLPQVMMI LIPGQTLPLQ LFHPQEVSMV RNLIQKDRTF 120
AVLAYSNVQE REAQFGTTAE IYAYREEQDF GIEIVKVKAI GRQRFKVLEL RTQSDGIQQA 180
KVQILPECVL PSTMSAVQLE SLNKCQIFPS KPVSREDQCS YKWWQKYQKR KFHCANLTSW 240
PRWLYSLYDA ETLMDRIKKQ LREWDENLKD DSLPSNPIDF SYRVAACLPI DDVLRIQLLK 300
IGSAIQRLRC ELDIMNKCTS LCCKQCQETE ITTKNEIFSL SLCGPMAAYV NPHGYVHETL 360
TVYKACNLNL IGRPSTEHSW FPGYAWTVAQ CKICASHIGW KFTATKKDMS PQKFWGLTRS 420
ALLPTIPDTE DEISPDKVIL CL 442 
Gene Ontology
 GO:0031464; C:Cul4A-RING ubiquitin ligase complex; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
 GO:0034766; P:negative regulation of ion transmembrane transport; IEA:Compara.
 GO:0032463; P:negative regulation of protein homooligomerization; IEA:Compara.
 GO:0090073; P:positive regulation of protein homodimerization activity; IEA:Compara.
 GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
 GO:0016567; P:protein ubiquitination; IMP:UniProtKB. 
Interpro
 IPR003111; Pept_S16_N.
 IPR015947; PUA-like_domain. 
Pfam
 PF02190; LON 
SMART
 SM00464; LON 
PROSITE
  
PRINTS