DCAF7_HUMAN
ID DCAF7_HUMAN Reviewed; 342 AA.
AC P61962; B4E039; D3DU14; O15491; Q9DAE4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=DDB1- and CUL4-associated factor 7;
DE AltName: Full=WD repeat-containing protein 68;
DE AltName: Full=WD repeat-containing protein An11 homolog;
GN Name=DCAF7; Synonyms=HAN11, WDR68;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9192870; DOI=10.1101/gad.11.11.1422;
RA de Vetten N., Quattrocchio F., Mol J., Koes R.;
RT "The an11 locus controlling flower pigmentation in petunia encodes a novel
RT WD-repeat protein conserved in yeast, plants, and animals.";
RL Genes Dev. 11:1422-1434(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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 [6]
RP INTERACTION WITH DYRK1A AND DYRK1B.
RX PubMed=14593110; DOI=10.1074/jbc.m301769200;
RA Skurat A.V., Dietrich A.D.;
RT "Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family
RT protein kinases.";
RL J. Biol. Chem. 279:2490-2498(2004).
RN [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH DIAPH1 AND DYRK1A, AND FUNCTION.
RX PubMed=16887337; DOI=10.1016/j.jdermsci.2006.06.001;
RA Morita K., Lo Celso C., Spencer-Dene B., Zouboulis C.C., Watt F.M.;
RT "HAN11 binds mDia1 and controls GLI1 transcriptional activity.";
RL J. Dermatol. Sci. 44:11-20(2006).
RN [8]
RP FUNCTION, INTERACTION WITH DDB1, AND IDENTIFICATION BY MASS 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 [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 INTERACTION WITH ZNF703, AND SUBCELLULAR LOCATION.
RX PubMed=21328542; DOI=10.1002/emmm.201100121;
RA Sircoulomb F., Nicolas N., Ferrari A., Finetti P., Bekhouche I.,
RA Rousselet E., Lonigro A., Adelaide J., Baudelet E., Esteyries S.,
RA Wicinski J., Audebert S., Charafe-Jauffret E., Jacquemier J., Lopez M.,
RA Borg J.P., Sotiriou C., Popovici C., Bertucci F., Birnbaum D.,
RA Chaffanet M., Ginestier C.;
RT "ZNF703 gene amplification at 8p12 specifies luminal B breast cancer.";
RL EMBO Mol. Med. 3:153-166(2011).
RN [11]
RP INTERACTION WITH HADV5 E1A.
RX PubMed=23864635; DOI=10.1128/jvi.00786-13;
RA Cohen M.J., Yousef A.F., Massimi P., Fonseca G.J., Todorovic B., Pelka P.,
RA Turnell A.S., Banks L., Mymryk J.S.;
RT "Dissection of the C-terminal region of E1A redefines the roles of CtBP and
RT other cellular targets in oncogenic transformation.";
RL J. Virol. 87:10348-10355(2013).
CC -!- FUNCTION: Involved in craniofacial development. Acts upstream of the
CC EDN1 pathway and is required for formation of the upper jaw equivalent,
CC the palatoquadrate. The activity required for EDN1 pathway function
CC differs between the first and second arches (By similarity). Associates
CC with DIAPH1 and controls GLI1 transcriptional activity. Could be
CC involved in normal and disease skin development. May function as a
CC substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.
CC {ECO:0000250, ECO:0000269|PubMed:16887337,
CC ECO:0000269|PubMed:16949367}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DYRK1A, DYRK1B and DIAPH1. Interacts with DDB1.
CC Interacts with ZNF703. Interacts with human adenovirus 5 E1A protein
CC (PubMed:23864635). {ECO:0000269|PubMed:14593110,
CC ECO:0000269|PubMed:16887337, ECO:0000269|PubMed:16949367,
CC ECO:0000269|PubMed:21328542, ECO:0000269|PubMed:23864635}.
CC -!- INTERACTION:
CC P61962; Q86V38: ATN1; NbExp=3; IntAct=EBI-359808, EBI-11954292;
CC P61962; P55212: CASP6; NbExp=3; IntAct=EBI-359808, EBI-718729;
CC P61962; Q13627: DYRK1A; NbExp=8; IntAct=EBI-359808, EBI-1053596;
CC P61962; Q9Y463: DYRK1B; NbExp=5; IntAct=EBI-359808, EBI-634187;
CC P61962; Q9H2X6: HIPK2; NbExp=10; IntAct=EBI-359808, EBI-348345;
CC P61962; P42858: HTT; NbExp=10; IntAct=EBI-359808, EBI-466029;
CC P61962; Q92876: KLK6; NbExp=3; IntAct=EBI-359808, EBI-2432309;
CC P61962; P13473-2: LAMP2; NbExp=3; IntAct=EBI-359808, EBI-21591415;
CC P61962; Q13233: MAP3K1; NbExp=7; IntAct=EBI-359808, EBI-49776;
CC P61962; O60260-5: PRKN; NbExp=3; IntAct=EBI-359808, EBI-21251460;
CC P61962; Q13148: TARDBP; NbExp=3; IntAct=EBI-359808, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Overexpression of DIAHP1
CC or active RHOA causes translocation from the nucleus to cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61962-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61962-2; Sequence=VSP_054015;
CC -!- SIMILARITY: Belongs to the WD repeat DCAF7 family. {ECO:0000305}.
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DR EMBL; U94747; AAC18913.1; -; mRNA.
DR EMBL; AK303212; BAG64301.1; -; mRNA.
DR EMBL; AC113554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94305.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94306.1; -; Genomic_DNA.
DR EMBL; BC001264; AAH01264.1; -; mRNA.
DR CCDS; CCDS74127.1; -. [P61962-1]
DR RefSeq; NP_005819.3; NM_005828.4. [P61962-1]
DR AlphaFoldDB; P61962; -.
DR SMR; P61962; -.
DR BioGRID; 115532; 278.
DR DIP; DIP-40363N; -.
DR IntAct; P61962; 197.
DR MINT; P61962; -.
DR STRING; 9606.ENSP00000483236; -.
DR iPTMnet; P61962; -.
DR PhosphoSitePlus; P61962; -.
DR SwissPalm; P61962; -.
DR BioMuta; DCAF7; -.
DR DMDM; 48428729; -.
DR EPD; P61962; -.
DR jPOST; P61962; -.
DR MassIVE; P61962; -.
DR MaxQB; P61962; -.
DR PaxDb; P61962; -.
DR PeptideAtlas; P61962; -.
DR PRIDE; P61962; -.
DR ProteomicsDB; 5647; -.
DR ProteomicsDB; 57346; -. [P61962-1]
DR Antibodypedia; 9425; 185 antibodies from 26 providers.
DR DNASU; 10238; -.
DR Ensembl; ENST00000415273.2; ENSP00000403920.2; ENSG00000136485.16. [P61962-2]
DR Ensembl; ENST00000431926.7; ENSP00000402312.2; ENSG00000136485.16. [P61962-1]
DR Ensembl; ENST00000614556.5; ENSP00000483236.1; ENSG00000136485.16. [P61962-1]
DR Ensembl; ENST00000686337.1; ENSP00000508930.1; ENSG00000136485.16. [P61962-1]
DR Ensembl; ENST00000690417.1; ENSP00000509006.1; ENSG00000136485.16. [P61962-1]
DR GeneID; 10238; -.
DR KEGG; hsa:10238; -.
DR MANE-Select; ENST00000614556.5; ENSP00000483236.1; NM_005828.5; NP_005819.3.
DR UCSC; uc010wpn.5; human. [P61962-1]
DR CTD; 10238; -.
DR DisGeNET; 10238; -.
DR GeneCards; DCAF7; -.
DR HGNC; HGNC:30915; DCAF7.
DR HPA; ENSG00000136485; Low tissue specificity.
DR MIM; 605973; gene.
DR neXtProt; NX_P61962; -.
DR OpenTargets; ENSG00000136485; -.
DR PharmGKB; PA165431770; -.
DR VEuPathDB; HostDB:ENSG00000136485; -.
DR eggNOG; KOG0290; Eukaryota.
DR GeneTree; ENSGT00390000006939; -.
DR HOGENOM; CLU_013694_0_0_1; -.
DR InParanoid; P61962; -.
DR OMA; INQIQWG; -.
DR OrthoDB; 750776at2759; -.
DR PhylomeDB; P61962; -.
DR TreeFam; TF106135; -.
DR PathwayCommons; P61962; -.
DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; P61962; -.
DR SIGNOR; P61962; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 10238; 78 hits in 346 CRISPR screens.
DR ChiTaRS; DCAF7; human.
DR GeneWiki; WDR68; -.
DR GenomeRNAi; 10238; -.
DR Pharos; P61962; Tbio.
DR PRO; PR:P61962; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P61962; protein.
DR Bgee; ENSG00000136485; Expressed in ventricular zone and 203 other tissues.
DR ExpressionAtlas; P61962; baseline and differential.
DR Genevisible; P61962; HS.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:FlyBase.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045159; DCAF7-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19919; PTHR19919; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..342
FT /note="DDB1- and CUL4-associated factor 7"
FT /id="PRO_0000051425"
FT REPEAT 6..52
FT /note="WD 1"
FT REPEAT 60..100
FT /note="WD 2"
FT REPEAT 108..150
FT /note="WD 3"
FT REPEAT 165..206
FT /note="WD 4"
FT REPEAT 213..252
FT /note="WD 5"
FT REPEAT 257..296
FT /note="WD 6"
FT REPEAT 303..342
FT /note="WD 7"
FT VAR_SEQ 47..246
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054015"
SQ SEQUENCE 342 AA; 38926 MW; 794CC69A45D0CC7C CRC64;
MSLHGKRKEI YKYEAPWTVY AMNWSVRPDK RFRLALGSFV EEYNNKVQLV GLDEESSEFI
CRNTFDHPYP TTKLMWIPDT KGVYPDLLAT SGDYLRVWRV GETETRLECL LNNNKNSDFC
APLTSFDWNE VDPYLLGTSS IDTTCTIWGL ETGQVLGRVN LVSGHVKTQL IAHDKEVYDI
AFSRAGGGRD MFASVGADGS VRMFDLRHLE HSTIIYEDPQ HHPLLRLCWN KQDPNYLATM
AMDGMEVVIL DVRVPCTPVA RLNNHRACVN GIAWAPHSSC HICTAADDHQ ALIWDIQQMP
RAIEDPILAY TAEGEINNVQ WASTQPDWIA ICYNNCLEIL RV
