Cul4a
entrez
99375
canonical
uniprot
Q3TCH7
canonical
ensembl
ENSMUSG00000031446
resolver
ensp
ENSMUSP00000016680
resolver
ensp
ENSMUSP00000331839
resolver
enst
ENSMUST00000016680
resolver
genesymbol
Cul4a
resolver
uniprot
Q3THM3
resolver
uniprot
Q91Z44
resolver
uniprot_entry
CUL4A_MOUSE
resolver
uniprot_sec
Q3THM3
resolver
uniprot_sec
Q91Z44
resolver
amino_acid_sequence
MADEGPRKGSVSALMGRTNGLTKPAALAGGPAKPGGTGGSRKLVIKNFRDRPRLPDNYTQDTWRKLHEAVKAIQSSTSIRYNLEELYQAVENLCSHKVSPTLYKQLRQVCEDHVQAQILPFREDSLDSVLFLKKINTCWQDHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRNHIISDRMVQSKTIDGILLLIGRERSGEAVDRSLLRSLLSMLSDLQVYKDSFELKFLEETNCLYAAEGQRLMQDREVPEYLNHVSKRLEEEADRVITYLDHSTQKPLIACVEKQLLGEHLTAILQKGLEHLLDENRVPDLTQMYQLFSRVKGGQHALLQHWSEYIKTFGTTIVINPEKDKDMVQDLLDFKDKVDHVVEVCFQRNERFINLMKESFETFINKRPNKPAELIAKHVDSKLRAGNKEATDEELERILDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQSAPGPIDLTVNILTMGYWPTYTPMEVHLPPEMVRLQEVFKTFYLGKHSGRKLQWQTTLGHAVLKADFKEGKKEFQVSLFQTLVLLMFNEGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKSPKGKEVEDGDKFIFNADFKHKLFRIKINQIQMKETVEEQVSTTERVFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLKFPVKPGDLKKRIESLIDRDYMERDKDSPNQYHYVA
uniprot
proteins
function
FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination 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 E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. DCX(DET1-COP1) directs ubiquitination of JUN. DCX(DDB2) directs ubiquitination of XPC. DCX(DDB2) ubiquitinates histones H3-H4 and is required for efficient histone deposition during replication-coupled (H3.1) and replication-independent (H3.3) nucleosome assembly, probably by facilitating the transfer of H3 from ASF1A/ASF1B to other chaperones involved in histone deposition. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of p53/TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(DTL) directs autoubiquitination of DTL. In association with DDB1 and SKP2 probably is involved in ubiquitination of CDKN1B/p27kip. Is involved in ubiquitination of HOXA9. The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1. The DCX(ERCC8) complex (also named CSA complex) plays a role in transcription-coupled repair (TCR). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. With CUL4B, contributes to ribosome biogenesis. The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes. {ECO:0000250|UniProtKB:Q13619}.
uniprot
proteins
mass_dalton
87753
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q13619}.
uniprot
proteins
post_translational_modification
PTM: Neddylated; required for activity of cullin-RING-based E3 ubiquitin-protein ligase complexes (By similarity). Deneddylated via its interaction with the COP9 signalosome (CSN) complex (By similarity). {ECO:0000250|UniProtKB:Q13619}.; PTM: (Microbial infection) Deneddylated by murine cytomegalovirus M48 leading to a S-phase-like environment that is required for efficient replication of the viral genome. {ECO:0000269|PubMed:20190741}.
uniprot
proteins
protein_family
Cullin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
20190741
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24357321
uniprot
proteins
sequence_length
759
uniprot
proteins