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   10-FEB-2021, entry version 166.
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   SMR; Q96JK2; -.
DR   BioGRID; 114343; 58.
DR   DIP; DIP-48763N; -.
DR   IntAct; Q96JK2; 34.
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; 15 antibodies.
DR   Ensembl; ENST00000341516; ENSP00000341351; ENSG00000139990. [Q96JK2-1]
DR   Ensembl; ENST00000554215; ENSP00000451551; ENSG00000139990. [Q96JK2-2]
DR   Ensembl; ENST00000556847; ENSP00000452052; ENSG00000139990. [Q96JK2-2]
DR   Ensembl; ENST00000557386; ENSP00000451845; ENSG00000139990. [Q96JK2-3]
DR   GeneID; 8816; -.
DR   KEGG; hsa:8816; -.
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:ENSG00000139990.17; -.
DR   eggNOG; KOG4227; Eukaryota.
DR   GeneTree; ENSGT00950000182900; -.
DR   HOGENOM; CLU_018663_0_0_1; -.
DR   InParanoid; Q96JK2; -.
DR   OMA; RPSHPHN; -.
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; 6 hits in 874 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 216 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:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.130.10.10; -; 3.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
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   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:0000244|PubMed:24275569"
FT   MOD_RES         648
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569"
FT   MOD_RES         651
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332"
FT   MOD_RES         794
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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:0000244|PDB:3I89"
FT   TURN            19..23
FT                   /evidence="ECO:0000244|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
//