CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024685
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cullin-3 
Protein Synonyms/Alias
  
Gene Name
 Cul3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
235NSASVYIKKVEARINacetylation[1]
262STEEPIVKVVERELIubiquitination[2]
651LTKEPKSKEIESGHIacetylation[1]
742LPSPVVIKKRIEGLIacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional Description
 Core component of multiple cullin-RING-based BCR (BTB- CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the BCR complex depends on the BTB domain-containing protein as the substrate recognition component. BCR(KLHL42) is involved in ubiquitination of KATNA1. BCR(SPOP) is involved in ubiquitination of BMI1/PCGF4, BRMS1, H2AFY and DAXX, GLI2 and GLI3. Can also form a cullin-RING- based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL; these complexes have lower ubiquitin ligase activity. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on mitotic chromosomes and thereby coordinates faithful mitotic progression and completion of cytokinesis. BCR(KLHL12) is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B). BCR(KLHL3) acts as a regulator of ion transport in the distal nephron; possibly by mediating ubiquitination of SLC12A3/NCC. The BCR(KLHL21) E3 ubiquitin ligase complex regulates localization of the chromosomal passenger complex (CPC) from chromosomes to the spindle midzone in anaphase and mediates the ubiquitination of AURKB. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. Involved in ubiquitination of cyclin E and of cyclin D1 (in vitro) thus involved in regulation of G1/S transition (By similarity). Involved in the ubiquitination of KEAP1, ENC1 and KLHL41. 
Sequence Annotation
 MOD_RES 450 450 Phosphoserine (By similarity).
 CROSSLNK 712 712 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Complete proteome; ER-Golgi transport; Golgi apparatus; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Transport; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 768 AA 
Protein Sequence
MSNLSKGTGS RKDTKMRIRA FPMTMDEKYV NSIWDLLKNA IQEIQRKNNS GLSFEELYRN 60
AYTMVLHKHG EKLYTGLREV VTEHLINKVR EDVLNSLNNN FLQTLNQAWN DHQTAMVMIR 120
DILMYMDRVY VQQNNVENVY NLGLIIFRDQ VVRYGCIRDH LRQTLLDMIA RERKGEVVDR 180
GAIRNACQML MILGLEGRSV YEEDFEAPFL EMSAEFFQME SQKFLAENSA SVYIKKVEAR 240
INEEIERVMH CLDKSTEEPI VKVVERELIS KHMKTIVEME NSGLVHMLKN GKTEDLACMY 300
KLFSRVPNGL KTMCECMSSY LREQGKALVS EEGEGKNPVD YIQGLLDLKS RFDRFLQESF 360
NNDRLFKQTI AGDFEYFLNL NSRSPEYLSL FIDDKLKKGV KGLTEQEVET ILDKAMVLFR 420
FMQEKDVFER YYKQHLARRL LTNKSVSDDS EKNMISKLKT ECGCQFTSKL EGMFRDMSIS 480
NTTMDEFRQH LQATGVSLGG VDLTVRVLTT GYWPTQSATP KCNIPPAPRH AFEIFRRFYL 540
AKHSGRQLTL QHHMGSADLN ATFYGPVKKE DGSEVGVGGA QVTGSNTRKH ILQVSTFQMT 600
ILMLFNNREK YTFEEIQQET DIPERELVRA LQSLACGKPT QRVLTKEPKS KEIESGHIFT 660
VNDQFTSKLH RVKIQTVAAK QGESDPERKE TRQKVDDDRK HEIEAAIVRI MKSRKKMQHN 720
VLVAEVTQQL KARFLPSPVV IKKRIEGLIE REYLARTPED RKVYTYVA 768 
Gene Ontology
 GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
 GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005827; C:polar microtubule; IEA:Compara.
 GO:0031208; F:POZ domain binding; ISS:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:Compara.
 GO:0016477; P:cell migration; IEA:Compara.
 GO:0048208; P:COPII vesicle coating; ISS:UniProtKB.
 GO:0008054; P:cyclin catabolic process; IEA:Compara.
 GO:0000910; P:cytokinesis; IEA:Compara.
 GO:0040016; P:embryonic cleavage; ISS:UniProtKB.
 GO:0007369; P:gastrulation; IEA:Compara.
 GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
 GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:Compara.
 GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
 GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
 GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
 GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
 GO:0017145; P:stem cell division; ISS:UniProtKB.
 GO:0043149; P:stress fiber assembly; IEA:Compara.
 GO:0001831; P:trophectodermal cellular morphogenesis; IEA:Compara.
 GO:0016055; P:Wnt receptor signaling pathway; IEA:Compara. 
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