CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012173
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cullin-4B 
Protein Synonyms/Alias
 CUL-4B 
Gene Name
 CUL4B 
Gene Synonyms/Alias
 KIAA0695 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
58PTSAKKRKLNSSSSSubiquitination[1]
158TSQQQQLKNKSILISubiquitination[1]
219YTDETWQKLKEAVEAubiquitination[1]
258KISANLYKQLRQICEubiquitination[2, 3, 4]
341AHIISDQKVQNKTIDubiquitination[1]
403LYAAEGQKLMQEREVubiquitination[2, 4]
513VINPEKDKTMVQELLubiquitination[2, 4]
558FINKRPNKPAELIAKubiquitination[1]
570IAKYVDSKLRAGNKEubiquitination[5]
600IFRFIYGKDVFEAFYubiquitination[2, 4]
608DVFEAFYKKDLAKRLubiquitination[1, 2, 4]
609VFEAFYKKDLAKRLLubiquitination[5]
619AKRLLVGKSASVDAEubiquitination[5]
650SKLEGMFKDMELSKDubiquitination[2, 3, 4]
709VKLQEIFKTFYLGKHubiquitination[2, 4]
789LQSLACGKARVLAKNubiquitination[5]
829KINQIQMKETVEEQAubiquitination[1]
862VRIMKMRKTLSHNLLubiquitination[2, 4]
882NQLKFPVKPADLKKRubiquitination[1]
903RDYMERDKENPNQYNubiquitination[1]
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] 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]
 [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] 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] 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] 
Functional Description
 Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation- induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8. 
Sequence Annotation
 MOTIF 55 58 Nuclear localization signal.
 MOD_RES 49 49 Phosphothreonine.
 MOD_RES 53 53 Phosphoserine.
 MOD_RES 146 146 Phosphoserine.
 MOD_RES 193 193 Phosphoserine.
 CROSSLNK 859 859 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Alternative splicing; Cell cycle; Complete proteome; Disease mutation; DNA damage; DNA repair; Isopeptide bond; Mental retardation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 913 AA 
Protein Sequence
MMSQSSGSGD GNDDEATTSK DGGFSSPSPS AAAAAQEVRS ATDGNTSTTP PTSAKKRKLN 60
SSSSSSSNSS NEREDFDSTS SSSSTPPLQP RDSASPSTSS FCLGVSVAAS SHVPIQKKLR 120
FEDTLEFVGF DAKMAEESSS SSSSSSPTAA TSQQQQLKNK SILISSVASV HHANGLAKSS 180
TTVSSFANSK PGSAKKLVIK NFKDKPKLPE NYTDETWQKL KEAVEAIQNS TSIKYNLEEL 240
YQAVENLCSY KISANLYKQL RQICEDHIKA QIHQFREDSL DSVLFLKKID RCWQNHCRQM 300
IMIRSIFLFL DRTYVLQNSM LPSIWDMGLE LFRAHIISDQ KVQNKTIDGI LLLIERERNG 360
EAIDRSLLRS LLSMLSDLQI YQDSFEQRFL EETNRLYAAE GQKLMQEREV PEYLHHVNKR 420
LEEEADRLIT YLDQTTQKSL IATVEKQLLG EHLTAILQKG LNNLLDENRI QDLSLLYQLF 480
SRVRGGVQVL LQQWIEYIKA FGSTIVINPE KDKTMVQELL DFKDKVDHII DICFLKNEKF 540
INAMKEAFET FINKRPNKPA ELIAKYVDSK LRAGNKEATD EELEKMLDKI MIIFRFIYGK 600
DVFEAFYKKD LAKRLLVGKS ASVDAEKSML SKLKHECGAA FTSKLEGMFK DMELSKDIMI 660
QFKQYMQNQN VPGNIELTVN ILTMGYWPTY VPMEVHLPPE MVKLQEIFKT FYLGKHSGRK 720
LQWQSTLGHC VLKAEFKEGK KELQVSLFQT LVLLMFNEGE EFSLEEIKQA TGIEDGELRR 780
TLQSLACGKA RVLAKNPKGK DIEDGDKFIC NDDFKHKLFR IKINQIQMKE TVEEQASTTE 840
RVFQDRQYQI DAAIVRIMKM RKTLSHNLLV SEVYNQLKFP VKPADLKKRI ESLIDRDYME 900
RDKENPNQYN YIA 913 
Gene Ontology
 GO:0031465; C:Cul4B-RING ubiquitin ligase complex; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0007049; P:cell cycle; NAS:UniProtKB.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0045732; P:positive regulation of protein catabolic process; IEA:Compara.
 GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 IPR016157; Cullin_CS.
 IPR016158; Cullin_homology.
 IPR001373; Cullin_N.
 IPR019559; Cullin_neddylation_domain.
 IPR016159; Cullin_repeat-like_dom.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF00888; Cullin
 PF10557; Cullin_Nedd8 
SMART
 SM00182; CULLIN
 SM00884; Cullin_Nedd8 
PROSITE
 PS01256; CULLIN_1
 PS50069; CULLIN_2 
PRINTS