DCAF1
entrez
9730
canonical
uniprot
Q9Y4B6
canonical
ensembl
ENSG00000145041
resolver
ensp
ENSP00000393183
resolver
ensp
ENSP00000421724
resolver
ensp
ENSP00000506880
resolver
ensp
ENSP00000525750
resolver
ensp
ENSP00000525751
resolver
ensp
ENSP00000525752
resolver
ensp
ENSP00000596515
resolver
ensp
ENSP00000596516
resolver
ensp
ENSP00000596518
resolver
genesymbol
DCAF1
resolver
genesymbol_syn
KIAA0800
resolver
genesymbol_syn
RIP
resolver
genesymbol_syn
VPRBP
resolver
hgnc
HGNC:30911
resolver
uniprot
Q2YD74
resolver
uniprot
Q8TBD9
resolver
uniprot
Q9HCA1
resolver
uniprot
Q9UG37
resolver
uniprot_entry
DCAF1_HUMAN
resolver
uniprot_sec
Q2YD74
resolver
uniprot_sec
Q8TBD9
resolver
uniprot_sec
Q9HCA1
resolver
uniprot_sec
Q9UG37
resolver
amino_acid_sequence
MTTVVVHVDSKAELTTLLEQWEKEHGSGQDMVPILTRMSQLIEKETEEYRKGDPDPFDDRHPGRADPECMLGHLLRILFKNDDFMNALVNAYVMTSREPPLNTAACRLLLDIMPGLETAVVFQEKEGIVENLFKWAREADQPLRTYSTGLLGGAMENQDIAANYRDENSQLVAIVLRRLRELQLQEVALRQENKRPSPRKLSSEPLLPLDEEAVDMDYGDMAVDVVDGDQEEASGDMEISFHLDSGHKTSSRVNSTTKPEDGGLKKNKSAKQGDRENFRKAKQKLGFSSSDPDRMFVELSNSSWSEMSPWVIGTNYTLYPMTPAIEQRLILQYLTPLGEYQELLPIFMQLGSRELMMFYIDLKQTNDVLLTFEALKHLASLLLHNKFATEFVAHGGVQKLLEIPRPSMAATGVSMCLYYLSYNQDAMERVCMHPHNVLSDVVNYTLWLMECSHASGCCHATMFFSICFSFRAVLELFDRYDGLRRLVNLISTLEILNLEDQGALLSDDEIFASRQTGKHTCMALRKYFEAHLAIKLEQVKQSLQRTEGGILVHPQPPYKACSYTHEQIVEMMEFLIEYGPAQLYWEPAEVFLKLSCVQLLLQLISIACNWKTYYARNDTVRFALDVLAILTVVPKIQLQLAESVDVLDEAGSTVSTVGISIILGVAEGEFFIHDAEIQKSALQIIINCVCGPDNRISSIGKFISGTPRRKLPQNPKSSEHTLAKMWNVVQSNNGIKVLLSLLSIKMPITDADQIRALACKALVGLSRSSTVRQIISKLPLFSSCQIQQLMKEPVLQDKRSDHVKFCKYAAELIERVSGKPLLIGTDVSLARLQKADVVAQSRISFPEKELLLLIRNHLISKGLGETATVLTKEADLPMTAASHSSAFTPVTAAASPVSLPRTPRIANGIATRLGSHAAVGASAPSAPTAHPQPRPPQGPLALPGPSYAGNSPLIGRISFIRERPSPCNGRKIRVLRQKSDHGAYSQSPAIKKQLDRHLPSPPTLDSIITEYLREQHARCKNPVATCPPFSLFTPHQCPEPKQRRQAPINFTSRLNRRASFPKYGGVDGGCFDRHLIFSRFRPISVFREANEDESGFTCCAFSARERFLMLGTCTGQLKLYNVFSGQEEASYNCHNSAITHLEPSRDGSLLLTSATWSQPLSALWGMKSVFDMKHSFTEDHYVEFSKHSQDRVIGTKGDIAHIYDIQTGNKLLTLFNPDLANNYKRNCATFNPTDDLVLNDGVLWDVRSAQAIHKFDKFNMNISGVFHPNGLEVIINTEIWDLRTFHLLHTVPALDQCRVVFNHTGTVMYGAMLQADDEDDLMEERMKSPFGSSFRTFNATDYKPIATIDVKRNIFDLCTDTKDCYLAVIENQGSMDALNMDTVCRLYEVGRQRLAEDEDEEEDQEEEEQEEEDDDEDDDDTDDLDELDTDQLLEAELEEDDNNENAGEDGDNDFSPSDEELANLLEEGEDGEDEDSDADEEVELILGDTDSSDNSDLEDDIILSLNE
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2 (PubMed:23063525). Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525). The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination (By similarity). Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:19287380, PubMed:23362280). The EDVP complex also mediates ubiquitination and degradation of CCP110 (PubMed:28242748, PubMed:34259627). Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription (PubMed:24140421). H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors (PubMed:24140421). Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714). By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity). {ECO:0000250|UniProtKB:Q80TR8, ECO:0000269|PubMed:16964240, ECO:0000269|PubMed:17609381, ECO:0000269|PubMed:17630831, ECO:0000269|PubMed:18332868, ECO:0000269|PubMed:18524771, ECO:0000269|PubMed:18606781, ECO:0000269|PubMed:19287380, ECO:0000269|PubMed:20644714, ECO:0000269|PubMed:22184063, ECO:0000269|PubMed:23063525, ECO:0000269|PubMed:23362280, ECO:0000269|PubMed:24140421, ECO:0000269|PubMed:28242748, ECO:0000269|PubMed:34259627}.; FUNCTION: (Microbial infection) In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. The HIV-1 Vpr protein hijacks the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to promote ubiquitination and degradation of proteins such as TERT and ZIP/ZGPAT. {ECO:0000269|PubMed:17314515, ECO:0000269|PubMed:17559673, ECO:0000269|PubMed:17609381, ECO:0000269|PubMed:17620334, ECO:0000269|PubMed:17626091, ECO:0000269|PubMed:17630831, ECO:0000269|PubMed:18524771, ECO:0000269|PubMed:24116224}.; FUNCTION: (Microbial infection) In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage. {ECO:0000269|PubMed:17314515, ECO:0000269|PubMed:18464893, ECO:0000269|PubMed:19264781, ECO:0000269|PubMed:19923175, ECO:0000269|PubMed:24336198, ECO:0000269|PubMed:29891865, ECO:0000269|PubMed:30297740}.
uniprot
proteins
mass_dalton
169007
uniprot
proteins
mutagenesis
MUTAGEN 194; /note="K->R: Abolishes serine/threonine-protein kinase kinase activity."; /evidence="ECO:0000269|PubMed:24140421"; MUTAGEN 361; /note="D->A: Abolishes serine/threonine-protein kinase kinase activity."; /evidence="ECO:0000269|PubMed:24140421"; MUTAGEN 363; /note="K->A: Abolishes serine/threonine-protein kinase kinase activity."; /evidence="ECO:0000269|PubMed:24140421"; MUTAGEN 1247; /note="R->A: Loss of interaction with DDB1, no effect on interaction with TET3; when associated with A-1283."; /evidence="ECO:0000269|PubMed:24357321"; MUTAGEN 1283; /note="R->A: Loss of interaction with DDB1, no effect on interaction with TET3; when associated with A-1247."; /evidence="ECO:0000269|PubMed:24357321
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
protein_family
VPRBP/DCAF1 family
uniprot
proteins
pubmed
11223251
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16949367
uniprot
proteins
pubmed
16964240
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17314515
uniprot
proteins
pubmed
17559673
uniprot
proteins
pubmed
17609381
uniprot
proteins
pubmed
17620334
uniprot
proteins
pubmed
17626091
uniprot
proteins
pubmed
17630831
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18332868
uniprot
proteins
pubmed
18464893
uniprot
proteins
pubmed
18524771
uniprot
proteins
pubmed
18606781
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19264781
uniprot
proteins
pubmed
19287380
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19838296
uniprot
proteins
pubmed
19923175
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20178741
uniprot
proteins
pubmed
20644714
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22072767
uniprot
proteins
pubmed
22184063
uniprot
proteins
pubmed
23063525
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23362280
uniprot
proteins
pubmed
24116224
uniprot
proteins
pubmed
24140421
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24336198
uniprot
proteins
pubmed
24357321
uniprot
proteins
pubmed
25557551
uniprot
proteins
pubmed
28068668
uniprot
proteins
pubmed
28242748
uniprot
proteins
pubmed
29891865
uniprot
proteins
pubmed
30297740
uniprot
proteins
pubmed
34259627
uniprot
proteins
pubmed
8195203
uniprot
proteins
pubmed
9872452
uniprot
proteins
sequence_length
1507
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11223251}. Nucleus {ECO:0000269|PubMed:20178741}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:28242748, ECO:0000269|PubMed:34259627}. Note=Associated with chromatin in a DDB1-independent and cell cycle-dependent manner: recruited to chromatin as DNA is being replicated and is released from chromatin before mitosis (By similarity). Homogeneous pancellular distribution is observed outside S-phase and a slight cytoplasmic-to-nuclear translocation from early to late S-phase (By similarity). Colocalizes with TET1 and PCNA at replicating heterochromatin during late S phase (By similarity). 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 (By similarity). Localizes to centrosomes following interaction with CEP78 (PubMed:28242748, PubMed:34259627). {ECO:0000250|UniProtKB:Q80TR8, ECO:0000269|PubMed:28242748, ECO:0000269|PubMed:34259627}.
uniprot
proteins