DCAF5_HUMAN
ID DCAF5_HUMAN Reviewed; 942 AA.
AC Q96JK2; B2RN31; G3V4J7; O60559; Q8N3V3; Q8N3V5;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=DDB1- and CUL4-associated factor 5;
DE AltName: Full=Breakpoint cluster region protein 2;
DE Short=BCRP2;
DE AltName: Full=WD repeat-containing protein 22;
GN Name=DCAF5; Synonyms=BCRG2, KIAA1824, WDR22;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 262-942, AND TISSUE SPECIFICITY.
RC TISSUE=Uterine leiomyoma;
RX PubMed=9740667; DOI=10.1006/geno.1998.5406;
RA Lynch R.A., Piper M., Bankier A., Bhugra B., Surti U., Liu J., Buckler A.,
RA Dear P.H., Menon A.G.;
RT "Genomic and functional map of the chromosome 14 t(12;14) breakpoint
RT cluster region in uterine leiomyoma.";
RL Genomics 52:17-26(1998).
RN [6]
RP FUNCTION, INTERACTION WITH DDB1 AND CUL4A, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010;
RA Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.;
RT "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is
RT required for S phase destruction of the replication factor Cdt1.";
RL Mol. Cell 23:709-721(2006).
RN [7]
RP FUNCTION.
RX PubMed=16964240; DOI=10.1038/nature05175;
RA Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.;
RT "Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase
RT machinery.";
RL Nature 443:590-593(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648 AND SER-651, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645; SER-648 AND SER-794, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3
CC ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367,
CC ECO:0000269|PubMed:16964240}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DDB1 and CUL4A. {ECO:0000269|PubMed:16949367}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96JK2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96JK2-2; Sequence=VSP_010386;
CC Name=3;
CC IsoId=Q96JK2-3; Sequence=VSP_055647;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9740667}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC08965.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB47453.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB058727; BAB47453.1; ALT_INIT; mRNA.
DR EMBL; AL391262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL831932; CAD38589.1; -; mRNA.
DR EMBL; AL831823; CAD38537.2; -; mRNA.
DR EMBL; CH471061; EAW80981.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW80983.1; -; Genomic_DNA.
DR EMBL; BC136632; AAI36633.1; -; mRNA.
DR EMBL; AF044774; AAC08965.1; ALT_FRAME; mRNA.
DR CCDS; CCDS32106.1; -. [Q96JK2-1]
DR CCDS; CCDS61480.1; -. [Q96JK2-2]
DR CCDS; CCDS61481.1; -. [Q96JK2-3]
DR RefSeq; NP_001271135.1; NM_001284206.1. [Q96JK2-3]
DR RefSeq; NP_001271136.1; NM_001284207.1. [Q96JK2-2]
DR RefSeq; NP_003852.1; NM_003861.2. [Q96JK2-1]
DR RefSeq; XP_016877223.1; XM_017021734.1. [Q96JK2-2]
DR RefSeq; XP_016877224.1; XM_017021735.1. [Q96JK2-2]
DR PDB; 3I89; X-ray; 3.00 A; B=13-25.
DR PDBsum; 3I89; -.
DR AlphaFoldDB; Q96JK2; -.
DR SMR; Q96JK2; -.
DR BioGRID; 114343; 92.
DR DIP; DIP-48763N; -.
DR IntAct; Q96JK2; 38.
DR MINT; Q96JK2; -.
DR STRING; 9606.ENSP00000341351; -.
DR iPTMnet; Q96JK2; -.
DR PhosphoSitePlus; Q96JK2; -.
DR BioMuta; DCAF5; -.
DR DMDM; 47606200; -.
DR EPD; Q96JK2; -.
DR jPOST; Q96JK2; -.
DR MassIVE; Q96JK2; -.
DR MaxQB; Q96JK2; -.
DR PaxDb; Q96JK2; -.
DR PeptideAtlas; Q96JK2; -.
DR PRIDE; Q96JK2; -.
DR ProteomicsDB; 33252; -.
DR ProteomicsDB; 76975; -. [Q96JK2-1]
DR ProteomicsDB; 76976; -. [Q96JK2-2]
DR Antibodypedia; 54896; 17 antibodies from 9 providers.
DR DNASU; 8816; -.
DR Ensembl; ENST00000341516.10; ENSP00000341351.5; ENSG00000139990.18. [Q96JK2-1]
DR Ensembl; ENST00000554215.5; ENSP00000451551.1; ENSG00000139990.18. [Q96JK2-2]
DR Ensembl; ENST00000556847.5; ENSP00000452052.1; ENSG00000139990.18. [Q96JK2-2]
DR Ensembl; ENST00000557386.5; ENSP00000451845.1; ENSG00000139990.18. [Q96JK2-3]
DR GeneID; 8816; -.
DR KEGG; hsa:8816; -.
DR MANE-Select; ENST00000341516.10; ENSP00000341351.5; NM_003861.3; NP_003852.1.
DR UCSC; uc001xkp.4; human. [Q96JK2-1]
DR CTD; 8816; -.
DR DisGeNET; 8816; -.
DR GeneCards; DCAF5; -.
DR HGNC; HGNC:20224; DCAF5.
DR HPA; ENSG00000139990; Low tissue specificity.
DR MIM; 603812; gene.
DR neXtProt; NX_Q96JK2; -.
DR OpenTargets; ENSG00000139990; -.
DR PharmGKB; PA165478844; -.
DR VEuPathDB; HostDB:ENSG00000139990; -.
DR eggNOG; KOG4227; Eukaryota.
DR GeneTree; ENSGT00950000182900; -.
DR HOGENOM; CLU_018663_0_0_1; -.
DR InParanoid; Q96JK2; -.
DR OMA; AGMREDP; -.
DR OrthoDB; 335761at2759; -.
DR PhylomeDB; Q96JK2; -.
DR TreeFam; TF320710; -.
DR PathwayCommons; Q96JK2; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q96JK2; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 8816; 23 hits in 1118 CRISPR screens.
DR ChiTaRS; DCAF5; human.
DR EvolutionaryTrace; Q96JK2; -.
DR GenomeRNAi; 8816; -.
DR Pharos; Q96JK2; Tdark.
DR PRO; PR:Q96JK2; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q96JK2; protein.
DR Bgee; ENSG00000139990; Expressed in secondary oocyte and 182 other tissues.
DR ExpressionAtlas; Q96JK2; baseline and differential.
DR Genevisible; Q96JK2; HS.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR045151; DCAF8.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15574; PTHR15574; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..942
FT /note="DDB1- and CUL4-associated factor 5"
FT /id="PRO_0000051369"
FT REPEAT 51..91
FT /note="WD 1"
FT REPEAT 99..139
FT /note="WD 2"
FT REPEAT 140..180
FT /note="WD 3"
FT REPEAT 185..225
FT /note="WD 4"
FT REPEAT 277..317
FT /note="WD 5"
FT REPEAT 331..370
FT /note="WD 6"
FT REGION 449..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 500
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80T85"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80T85"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80T85"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80T85"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80T85"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_010386"
FT VAR_SEQ 132
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_055647"
FT CONFLICT 149
FT /note="S -> F (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="Y -> H (in Ref. 5; AAC08965)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="N -> D (in Ref. 5; AAC08965)"
FT /evidence="ECO:0000305"
FT CONFLICT 836..841
FT /note="RLHPRP -> TLHLS (in Ref. 5; AAC08965)"
FT /evidence="ECO:0000305"
FT HELIX 14..18
FT /evidence="ECO:0007829|PDB:3I89"
FT TURN 19..23
FT /evidence="ECO:0007829|PDB:3I89"
SQ SEQUENCE 942 AA; 103963 MW; 3C627BA3FB2DC522 CRC64;
MKRRAGLGGS MRSVVGFLSQ RGLHGDPLLT QDFQRRRLRG CRNLYKKDLL GHFGCVNAIE
FSNNGGQWLV SGGDDRRVLL WHMEQAIHSR VKPIQLKGEH HSNIFCLAFN SGNTKVFSGG
NDEQVILHDV ESSETLDVFA HEDAVYGLSV SPVNDNIFAS SSDDGRVLIW DIRESPHGEP
FCLANYPSAF HSVMFNPVEP RLLATANSKE GVGLWDIRKP QSSLLRYGGN LSLQSAMSVR
FNSNGTQLLA LRRRLPPVLY DIHSRLPVFQ FDNQGYFNSC TMKSCCFAGD RDQYILSGSD
DFNLYMWRIP ADPEAGGIGR VVNGAFMVLK GHRSIVNQVR FNPHTYMICS SGVEKIIKIW
SPYKQPGCTG DLDGRIEDDS RCLYTHEEYI SLVLNSGSGL SHDYANQSVQ EDPRMMAFFD
SLVRREIEGW SSDSDSDLSE STILQLHAGV SERSGYTDSE SSASLPRSPP PTVDESADNA
FHLGPLRVTT TNTVASTPPT PTCEDAASRQ QRLSALRRYQ DKRLLALSNE SDSEENVCEV
ELDTDLFPRP RSPSPEDESS SSSSSSSSED EEELNERRAS TWQRNAMRRR QKTTREDKPS
APIKPTNTYI GEDNYDYPQI KVDDLSSSPT SSPERSTSTL EIQPSRASPT SDIESVERKI
YKAYKWLRYS YISYSNNKDG ETSLVTGEAD EGRAGTSHKD NPAPSSSKEA CLNIAMAQRN
QDLPPEGCSK DTFKEETPRT PSNGPGHEHS SHAWAEVPEG TSQDTGNSGS VEHPFETKKL
NGKALSSRAE EPPSPPVPKA SGSTLNSGSG NCPRTQSDDS EERSLETICA NHNNGRLHPR
PPHPHNNGQN LGELEVVAYS SPGHSDTDRD NSSLTGTLLH KDCCGSEMAC ETPNAGTRED
PTDTPATDSS RAVHGHSGLK RQRIELEDTD SENSSSEKKL KT
