CUL4A
entrez
8451
canonical
uniprot
Q13619
canonical
ensembl
ENSG00000139842
resolver
ensp
ENSP00000322132
resolver
ensp
ENSP00000364589
resolver
ensp
ENSP00000364590
resolver
ensp
ENSP00000389118
resolver
ensp
ENSP00000480367
resolver
ensp
ENSP00000481782
resolver
enst
ENST00000326335
resolver
enst
ENST00000488558
resolver
genesymbol
CUL4A
resolver
hgnc
HGNC:2554
resolver
uniprot
A0A087WWN2
resolver
uniprot
A0A0A0MR50
resolver
uniprot
A2A2W2
resolver
uniprot
O75834
resolver
uniprot
Q589T6
resolver
uniprot
Q5TC62
resolver
uniprot
Q6UP08
resolver
uniprot
Q9UP17
resolver
uniprot_entry
A0A087WWN2_HUMAN
resolver
uniprot_entry
A0A0A0MR50_HUMAN
resolver
uniprot_entry
CUL4A_HUMAN
resolver
uniprot_sec
A2A2W2
resolver
uniprot_sec
O75834
resolver
uniprot_sec
Q589T6
resolver
uniprot_sec
Q5TC62
resolver
uniprot_sec
Q6UP08
resolver
uniprot_sec
Q9UP17
resolver
amino_acid_sequence
MADEAPRKGSFSALVGRTNGLTKPAALAAAPAKPGGAGGSKKLVIKNFRDRPRLPDNYTQDTWRKLHEAVRAVQSSTSIRYNLEELYQAVENLCSHKVSPMLYKQLRQACEDHVQAQILPFREDSLDSVLFLKKINTCWQDHCRQMIMIRSIFLFLDRTYVLQNSTLPSIWDMGLELFRTHIISDKMVQSKTIDGILLLIERERSGEAVDRSLLRSLLGMLSDLQVYKDSFELKFLEETNCLYAAEGQRLMQEREVPEYLNHVSKRLEEEGDRVITYLDHSTQKPLIACVEKQLLGEHLTAILQKGLDHLLDENRVPDLAQMYQLFSRVRGGQQALLQHWSEYIKTFGTAIVINPEKDKDMVQDLLDFKDKVDHVIEVCFQKNERFVNLMKESFETFINKRPNKPAELIAKHVDSKLRAGNKEATDEELERTLDKIMILFRFIHGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMVHFKQHMQNQSDSGPIDLTVNILTMGYWPTYTPMEVHLTPEMIKLQEVFKAFYLGKHSGRKLQWQTTLGHAVLKAEFKEGKKEFQVSLFQTLVLLMFNEGDGFSFEEIKMATGIEDSELRRTLQSLACGKARVLIKSPKGKEVEDGDKFIFNGEFKHKLFRIKINQIQMKETVEEQVSTTERVFQDRQYQIDAAIVRIMKMRKTLGHNLLVSELYNQLKFPVKPGDLKKRIESLIDRDYMERDKDNPNQYHYVA
uniprot
proteins
function
FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination of target proteins (PubMed:14578910, PubMed:14739464, PubMed:15448697, PubMed:15548678, PubMed:15811626, PubMed:16678110, PubMed:17041588, PubMed:24209620, PubMed:30166453, PubMed:33854232, PubMed:33854239). As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:14739464, PubMed:15448697, PubMed:15548678, PubMed:15811626, PubMed:16678110, PubMed:17041588, PubMed:24209620). 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 (PubMed:14578910, PubMed:14739464, PubMed:15448697, PubMed:15548678, PubMed:15811626, PubMed:16678110, PubMed:17041588, PubMed:24209620). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component (PubMed:14578910, PubMed:14739464, PubMed:15448697, PubMed:15548678, PubMed:15811626, PubMed:16678110, PubMed:17041588, PubMed:24209620). DCX(DET1-COP1) directs ubiquitination of JUN (PubMed:14739464). DCX(DDB2) directs ubiquitination of XPC (PubMed:15811626). 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 (PubMed:16678110, PubMed:17041588, PubMed:24209620). 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 (PubMed:14578910, PubMed:15448697, PubMed:15548678). DCX(DTL) directs autoubiquitination of DTL (PubMed:23478445). In association with DDB1 and SKP2 probably is involved in ubiquitination of CDKN1B/p27kip (PubMed:16537899). Is involved in ubiquitination of HOXA9 (PubMed:14609952). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). The DCX(ERCC8) complex (also named CSA complex) plays a role in transcription-coupled repair (TCR) (PubMed:12732143, PubMed:32355176, PubMed:38316879). 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 (PubMed:29779948). 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) (PubMed:33854232, PubMed:33854239). 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 (PubMed:30166453). With CUL4B, contributes to ribosome biogenesis (PubMed:26711351). {ECO:0000269|PubMed:12732143, ECO:0000269|PubMed:14578910, ECO:0000269|PubMed:14609952, ECO:0000269|PubMed:14739464, ECO:0000269|PubMed:15448697, ECO:0000269|PubMed:15548678, ECO:0000269|PubMed:15811626, ECO:0000269|PubMed:16537899, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:17041588, ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:24209620, ECO:0000269|PubMed:26431207, ECO:0000269|PubMed:26711351, ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:30166453, ECO:0000269|PubMed:32355176, ECO:0000269|PubMed:33854232, ECO:0000269|PubMed:33854239}.
uniprot
proteins
mass_dalton
87680
uniprot
proteins
mutagenesis
MUTAGEN 86..90; /note="LYQAV->AAAAA: Largely reduces interaction with DDB1; abolishes interaction with DDB2."; /evidence="ECO:0000269|PubMed:16482215, ECO:0000269|PubMed:17079684"; MUTAGEN 139..142; /note="WQDH->AADA: Largely reduces interaction with DDB1; abolishes interaction with DDB2."; /evidence="ECO:0000269|PubMed:16482215, ECO:0000269|PubMed:17079684
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:14609952, ECO:0000269|PubMed:15448697, ECO:0000269|PubMed:15548678, ECO:0000269|PubMed:16537899, ECO:0000269|PubMed:23478445, ECO:0000269|PubMed:24209620, ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:30166453, ECO:0000269|PubMed:33854232, ECO:0000269|PubMed:33854239, ECO:0000269|PubMed:38316879}.
uniprot
proteins
post_translational_modification
PTM: Neddylated; required for activity of cullin-RING-based E3 ubiquitin-protein ligase complexes (PubMed:10597293, PubMed:24076655, PubMed:38316879, PubMed:9694792). Deneddylated via its interaction with the COP9 signalosome (CSN) complex (PubMed:10597293, PubMed:24076655, PubMed:9694792). {ECO:0000269|PubMed:10597293, ECO:0000269|PubMed:24076655, ECO:0000269|PubMed:38316879, ECO:0000269|PubMed:9694792}.; PTM: (Microbial infection) Deneddylated by Epstein-Barr virus BPLF1 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
10230407
uniprot
proteins
pubmed
10597293
uniprot
proteins
pubmed
12609982
uniprot
proteins
pubmed
12732143
uniprot
proteins
pubmed
14578910
uniprot
proteins
pubmed
14609952
uniprot
proteins
pubmed
14739464
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15448697
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15548678
uniprot
proteins
pubmed
15811626
uniprot
proteins
pubmed
16482215
uniprot
proteins
pubmed
16537899
uniprot
proteins
pubmed
16678110
uniprot
proteins
pubmed
16949367
uniprot
proteins
pubmed
16964240
uniprot
proteins
pubmed
17041588
uniprot
proteins
pubmed
17079684
uniprot
proteins
pubmed
17254749
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20190741
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22118460
uniprot
proteins
pubmed
22935713
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23201271
uniprot
proteins
pubmed
23478445
uniprot
proteins
pubmed
24076655
uniprot
proteins
pubmed
24209620
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26431207
uniprot
proteins
pubmed
26711351
uniprot
proteins
pubmed
26906416
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29779948
uniprot
proteins
pubmed
30166453
uniprot
proteins
pubmed
32355176
uniprot
proteins
pubmed
33854232
uniprot
proteins
pubmed
33854239
uniprot
proteins
pubmed
38316879
uniprot
proteins
pubmed
8681378
uniprot
proteins
pubmed
9694792
uniprot
proteins
pubmed
9721878
uniprot
proteins
sequence_length
759
uniprot
proteins