CUL4B
entrez
8450
canonical
uniprot
Q13620
canonical
ensembl
ENSG00000158290
resolver
ensp
ENSP00000338919
resolver
ensp
ENSP00000360373
resolver
ensp
ENSP00000360374
resolver
ensp
ENSP00000505084
resolver
enst
ENST00000336592
resolver
genesymbol
CUL4B
resolver
genesymbol_syn
KIAA0695
resolver
hgnc
HGNC:2555
resolver
uniprot
B1APK5
resolver
uniprot
B3KVX4
resolver
uniprot
B7Z5K8
resolver
uniprot
K4DI93
resolver
uniprot
Q6PIE4
resolver
uniprot
Q6UP07
resolver
uniprot
Q7Z673
resolver
uniprot
Q9BY37
resolver
uniprot
Q9UEB7
resolver
uniprot
Q9UED7
resolver
uniprot_entry
CUL4B_HUMAN
resolver
uniprot_entry
K4DI93_HUMAN
resolver
uniprot_sec
B1APK5
resolver
uniprot_sec
B3KVX4
resolver
uniprot_sec
B7Z5K8
resolver
uniprot_sec
Q6PIE4
resolver
uniprot_sec
Q6UP07
resolver
uniprot_sec
Q7Z673
resolver
uniprot_sec
Q9BY37
resolver
uniprot_sec
Q9UEB7
resolver
uniprot_sec
Q9UED7
resolver
amino_acid_sequence
MMSQSSGSGDGNDDEATTSKDGGFSSPSPSAAAAAQEVRSATDGNTSTTPPTSAKKRKLNSSSSSSSNSSNEREDFDSTSSSSSTPPLQPRDSASPSTSSFCLGVSVAASSHVPIQKKLRFEDTLEFVGFDAKMAEESSSSSSSSSPTAATSQQQQLKNKSILISSVASVHHANGLAKSSTTVSSFANSKPGSAKKLVIKNFKDKPKLPENYTDETWQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSYKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRAHIISDQKVQNKTIDGILLLIERERNGEAIDRSLLRSLLSMLSDLQIYQDSFEQRFLEETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIATVEKQLLGEHLTAILQKGLNNLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVINPEKDKTMVQELLDFKDKVDHIIDICFLKNEKFINAMKEAFETFINKRPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVPGNIELTVNILTMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQTLVLLMFNEGEEFSLEEIKQATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETVEEQASTTERVFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLKFPVKPADLKKRIESLIDRDYMERDKENPNQYNYIA
uniprot
proteins
disease_involvement
DISEASE: Intellectual developmental disorder, X-linked, syndromic, Cabezas type (MRXSC) [MIM:300354]: A syndromic form of X-linked intellectual disability characterized by severe intellectual deficit associated with short stature, craniofacial dysmorphism, small testes, muscle wasting in lower legs, kyphosis, joint hyperextensibility, pes cavus, small feet, and abnormalities of the toes. Additional neurologic manifestations include speech delay and impairment, tremor, seizures, gait ataxia, hyperactivity and decreased attention span. {ECO:0000269|PubMed:17236139, ECO:0000269|PubMed:17273978, ECO:0000269|PubMed:19377476, ECO:0000269|PubMed:20002452}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14578910, PubMed:16322693, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948, PubMed:30166453, PubMed:33854232, PubMed:33854239, PubMed:25970626). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460, PubMed:29779948). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:16678110, PubMed:18593899, PubMed:22118460). 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 (PubMed:14578910, PubMed:16678110, PubMed:18593899). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (PubMed:16678110). 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). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (PubMed:16322693, PubMed:19801544). Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (PubMed:18235224). Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (PubMed:18235224). With CUL4A, contributes to ribosome biogenesis (PubMed:26711351). {ECO:0000269|PubMed:14578910, ECO:0000269|PubMed:16322693, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:18235224, ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19801544, ECO:0000269|PubMed:22118460, ECO:0000269|PubMed:25970626, ECO:0000269|PubMed:26711351, ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:30166453, ECO:0000269|PubMed:33854232, ECO:0000269|PubMed:33854239}.
uniprot
proteins
mass_dalton
103982
uniprot
proteins
mutagenesis
MUTAGEN 55..58; /note="Missing: Distributed in cytoplasm. Fails to promote cell proliferation. No binding to KPNA2, KPNA4 and KPNA1."; /evidence="ECO:0000269|PubMed:19801544"; MUTAGEN 55; /note="K->A: No impairment in nuclear localization."; /evidence="ECO:0000269|PubMed:19801544"; MUTAGEN 56; /note="K->A: Disrupts nuclear localization and does not bind KPNA2, KPNA4, KPNA1; when associated with A-57. Disrupts nuclear localization."; /evidence="ECO:0000269|PubMed:19801544"; MUTAGEN 57; /note="R->A: Disrupts nuclear localization and does not bind KPNA2, KPNA4, KPNA1; when associated with A-56. Disrupts nuclear localization."; /evidence="ECO:0000269|PubMed:19801544"; MUTAGEN 58; /note="K->A: No impairment in nuclear localization."; /evidence="ECO:0000269|PubMed:19801544
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:30166453, ECO:0000269|PubMed:33854232, ECO:0000269|PubMed:33854239}.
uniprot
proteins
post_translational_modification
PTM: Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex. {ECO:0000269|PubMed:10597293}.
uniprot
proteins
protein_family
Cullin family
uniprot
proteins
pubmed
10230407
uniprot
proteins
pubmed
10597293
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
12609982
uniprot
proteins
pubmed
14578910
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16322693
uniprot
proteins
pubmed
16678110
uniprot
proteins
pubmed
16949367
uniprot
proteins
pubmed
17041588
uniprot
proteins
pubmed
17236139
uniprot
proteins
pubmed
17273978
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18235224
uniprot
proteins
pubmed
18593899
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19377476
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19801544
uniprot
proteins
pubmed
20002452
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22118460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23201271
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25970626
uniprot
proteins
pubmed
26711351
uniprot
proteins
pubmed
26906416
uniprot
proteins
pubmed
29779948
uniprot
proteins
pubmed
30166453
uniprot
proteins
pubmed
33854232
uniprot
proteins
pubmed
33854239
uniprot
proteins
pubmed
8681378
uniprot
proteins
pubmed
9734811
uniprot
proteins
sequence_length
913
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2A432}. Nucleus {ECO:0000269|PubMed:18593899, ECO:0000269|PubMed:19801544}. Note=More concentrated in nuclei than in cytoplasm in germinal vesicle (GV) stage oocytes, zygotes and the 2-cell stage, but distributed in the cytoplasm at the MII-stage oocytes. {ECO:0000250|UniProtKB:A2A432}.
uniprot
proteins