DCAF15
entrez
90379
canonical
uniprot
Q66K64
canonical
ensembl
ENSG00000132017
resolver
ensembl
ENSG00000288453
resolver
ensp
ENSP00000254337
resolver
ensp
ENSP00000500158
resolver
ensp
ENSP00000562391
resolver
ensp
ENSP00000562392
resolver
ensp
ENSP00000562393
resolver
ensp
ENSP00000606759
resolver
ensp
ENSP00000606761
resolver
ensp
ENSP00000606763
resolver
enst
ENST00000254337
resolver
enst
ENST00000672437
resolver
genesymbol
DCAF15
resolver
genesymbol_syn
C19orf72
resolver
hgnc
HGNC:25095
resolver
uniprot
B3KS86
resolver
uniprot
Q96DW0
resolver
uniprot
Q9BU31
resolver
uniprot_entry
DCA15_HUMAN
resolver
uniprot_sec
B3KS86
resolver
uniprot_sec
Q96DW0
resolver
uniprot_sec
Q9BU31
resolver
activity_regulation
ACTIVITY REGULATION: Aryl sulfonamide anticancer drugs change the substrate specificity of DCAF15 by acting as a molecular glue that promotes binding between DCAF15 and weak affinity interactors, such as RBM39. {ECO:0000269|PubMed:28302793, ECO:0000269|PubMed:28437394, ECO:0000269|PubMed:31686031, ECO:0000269|PubMed:31819272}.
uniprot
proteins
amino_acid_sequence
MAPSSKSERNSGAGSGGGGPGGAGGKRAAGRRREHVLKQLERVKISGQLSPRLFRKLPPRVCVSLKNIVDEDFLYAGHIFLGFSKCGRYVLSYTSSSGDDDFSFYIYHLYWWEFNVHSKLKLVRQVRLFQDEEIYSDLYLTVCEWPSDASKVIVFGFNTRSANGMLMNMMMMSDENHRDIYVSTVAVPPPGRCAACQDASRAHPGDPNAQCLRHGFMLHTKYQVVYPFPTFQPAFQLKKDQVVLLNTSYSLVACAVSVHSAGDRSFCQILYDHSTCPLAPASPPEPQSPELPPALPSFCPEAAPARSSGSPEPSPAIAKAKEFVADIFRRAKEAKGGVPEEARPALCPGPSGSRCRAHSEPLALCGETAPRDSPPASEAPASEPGYVNYTKLYYVLESGEGTEPEDELEDDKISLPFVVTDLRGRNLRPMRERTAVQGQYLTVEQLTLDFEYVINEVIRHDATWGHQFCSFSDYDIVILEVCPETNQVLINIGLLLLAFPSPTEEGQLRPKTYHTSLKVAWDLNTGIFETVSVGDLTEVKGQTSGSVWSSYRKSCVDMVMKWLVPESSGRYVNRMTNEALHKGCSLKVLADSERYTWIVL
uniprot
proteins
function
FUNCTION: Substrate-recognition component of the DCX(DCAF15) complex, a cullin-4-RING E3 ubiquitin-protein ligase complex that mediates ubiquitination and degradation of target proteins (PubMed:16949367, PubMed:31452512). The DCX(DCAF15) complex acts as a regulator of the natural killer (NK) cells effector functions, possibly by mediating ubiquitination and degradation of cohesin subunits SMC1A and SMC3 (PubMed:31452512). May play a role in the activation of antigen-presenting cells (APC) and their interaction with NK cells (PubMed:31452512). {ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:31452512}.; FUNCTION: Binding of aryl sulfonamide anticancer drugs, such as indisulam (E7070) or E7820, change the substrate specificity of the DCX(DCAF15) complex, leading to promote ubiquitination and degradation of splicing factor RBM39 (PubMed:28302793, PubMed:28437394, PubMed:31452512, PubMed:31693891). RBM39 degradation results in splicing defects and death in cancer cell lines (PubMed:28302793, PubMed:28437394, PubMed:31693891). Aryl sulfonamide anticancer drugs change the substrate specificity of DCAF15 by acting as a molecular glue that promotes binding between DCAF15 and weak affinity interactor RBM39 (PubMed:31686031, PubMed:31819272). Aryl sulfonamide anticancer drugs also promote ubiquitination and degradation of RBM23 and PRPF39 (PubMed:31626998, PubMed:31686031, PubMed:31693891). {ECO:0000269|PubMed:28302793, ECO:0000269|PubMed:28437394, ECO:0000269|PubMed:31452512, ECO:0000269|PubMed:31626998, ECO:0000269|PubMed:31686031, ECO:0000269|PubMed:31693891, ECO:0000269|PubMed:31819272}.
uniprot
proteins
mass_dalton
66463
uniprot
proteins
mutagenesis
MUTAGEN 90; /note="V->D: Abolished interaction with DDB1, DDA1 and RBM39 in presence of indisulam."; /evidence="ECO:0000269|PubMed:31693891"; MUTAGEN 91; /note="L->P: Abolished interaction with DDB1, DDA1 and RBM39 in presence of indisulam."; /evidence="ECO:0000269|PubMed:31693891"; MUTAGEN 112; /note="W->R: Abolished interaction with DDB1, DDA1 and RBM39 in presence of indisulam."; /evidence="ECO:0000269|PubMed:31693891"; MUTAGEN 129; /note="F->S,V: Abolished interaction with DDB1, DDA1 and RBM39 in presence of indisulam."; /evidence="ECO:0000269|PubMed:31693891"; MUTAGEN 182; /note="V->D: Decreased interaction with DDB1, DDA1 and RBM39 in presence of indisulam."; /evidence="ECO:0000269|PubMed:31693891"; MUTAGEN 196; /note="C->Y: Decreased interaction with DDB1, DDA1 and RBM39 in presence of indisulam."; /evidence="ECO:0000269|PubMed:31693891"; MUTAGEN 232; /note="Q->R: Decreased interaction with RBM39 in presence of indisulam, without affecting interaction with DDA1 and DDB1."; /evidence="ECO:0000269|PubMed:31693891"; MUTAGEN 244; /note="L->P: Decreased interaction with DDB1, DDA1 and RBM39 in presence of indisulam."; /evidence="ECO:0000269|PubMed:31693891"; MUTAGEN 392; /note="L->P: Decreased interaction with DDA1 and RBM39 in presence of indisulam."; /evidence="ECO:0000269|PubMed:31693891"; MUTAGEN 420; /note="T->P: Decreased interaction with DDA1 and RBM39 in presence of indisulam."; /evidence="ECO:0000269|PubMed:31693891"; MUTAGEN 444; /note="E->K: Decreased interaction with DDA1 and RBM39 in presence of indisulam."; /evidence="ECO:0000269|PubMed:31693891"; MUTAGEN 453; /note="V->D: Decreased interaction with DDA1 and RBM39 in presence of indisulam."; /evidence="ECO:0000269|PubMed:31693891"; MUTAGEN 475; /note="D->H,N,V: Decreased interaction with RBM39 in presence of indisulam, without affecting interaction with DDA1 and DDB1."; /evidence="ECO:0000269|PubMed:31693891
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:28302793, ECO:0000269|PubMed:28437394, ECO:0000269|PubMed:31452512, ECO:0000269|PubMed:31693891}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16949367
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
28302793
uniprot
proteins
pubmed
28437394
uniprot
proteins
pubmed
28546157
uniprot
proteins
pubmed
31452512
uniprot
proteins
pubmed
31626998
uniprot
proteins
pubmed
31686031
uniprot
proteins
pubmed
31693891
uniprot
proteins
pubmed
31693911
uniprot
proteins
pubmed
31819272
uniprot
proteins
sequence_length
600
uniprot
proteins