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DDB1- and CUL4-associated factor 7 (WD repeat-containing protein 68) (WD repeat-containing protein An11 homolog)

 DCAF7_HUMAN             Reviewed;         342 AA.
P61962; B4E039; D3DU14; O15491; Q9DAE4;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 1.
23-MAY-2018, entry version 152.
RecName: Full=DDB1- and CUL4-associated factor 7;
AltName: Full=WD repeat-containing protein 68;
AltName: Full=WD repeat-containing protein An11 homolog;
Name=DCAF7; Synonyms=HAN11, WDR68;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=9192870; DOI=10.1101/gad.11.11.1422;
de Vetten N., Quattrocchio F., Mol J., Koes R.;
"The an11 locus controlling flower pigmentation in petunia encodes a
novel WD-repeat protein conserved in yeast, plants, and animals.";
Genes Dev. 11:1422-1434(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH DYRK1A AND DYRK1B.
PubMed=14593110; DOI=10.1074/jbc.M301769200;
Skurat A.V., Dietrich A.D.;
"Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family
protein kinases.";
J. Biol. Chem. 279:2490-2498(2004).
[7]
SUBCELLULAR LOCATION, INTERACTION WITH DIAPH1 AND DYRK1A, AND
FUNCTION.
PubMed=16887337; DOI=10.1016/j.jdermsci.2006.06.001;
Morita K., Lo Celso C., Spencer-Dene B., Zouboulis C.C., Watt F.M.;
"HAN11 binds mDia1 and controls GLI1 transcriptional activity.";
J. Dermatol. Sci. 44:11-20(2006).
[8]
FUNCTION, INTERACTION WITH DDB1, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010;
Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.;
"A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
which is required for S phase destruction of the replication factor
Cdt1.";
Mol. Cell 23:709-721(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
INTERACTION WITH ZNF703, AND SUBCELLULAR LOCATION.
PubMed=21328542; DOI=10.1002/emmm.201100121;
Sircoulomb F., Nicolas N., Ferrari A., Finetti P., Bekhouche I.,
Rousselet E., Lonigro A., Adelaide J., Baudelet E., Esteyries S.,
Wicinski J., Audebert S., Charafe-Jauffret E., Jacquemier J.,
Lopez M., Borg J.P., Sotiriou C., Popovici C., Bertucci F.,
Birnbaum D., Chaffanet M., Ginestier C.;
"ZNF703 gene amplification at 8p12 specifies luminal B breast
cancer.";
EMBO Mol. Med. 3:153-166(2011).
[11]
INTERACTION WITH HADV5 E1A.
PubMed=23864635; DOI=10.1128/JVI.00786-13;
Cohen M.J., Yousef A.F., Massimi P., Fonseca G.J., Todorovic B.,
Pelka P., Turnell A.S., Banks L., Mymryk J.S.;
"Dissection of the C-terminal region of E1A redefines the roles of
CtBP and other cellular targets in oncogenic transformation.";
J. Virol. 87:10348-10355(2013).
-!- FUNCTION: Involved in craniofacial development. Acts upstream of
the EDN1 pathway and is required for formation of the upper jaw
equivalent, the palatoquadrate. The activity required for EDN1
pathway function differs between the first and second arches (By
similarity). Associates with DIAPH1 and controls GLI1
transcriptional activity. Could be involved in normal and disease
skin development. May function as a substrate receptor for CUL4-
DDB1 E3 ubiquitin-protein ligase complex. {ECO:0000250,
ECO:0000269|PubMed:16887337, ECO:0000269|PubMed:16949367}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with DYRK1A, DYRK1B and DIAPH1. Interacts with
DDB1. Interacts with ZNF703. Interacts with human adenovirus 5 E1A
protein (PubMed:23864635). {ECO:0000269|PubMed:14593110,
ECO:0000269|PubMed:16887337, ECO:0000269|PubMed:16949367,
ECO:0000269|PubMed:21328542, ECO:0000269|PubMed:23864635}.
-!- INTERACTION:
Q13627:DYRK1A; NbExp=5; IntAct=EBI-359808, EBI-1053596;
Q9Y463:DYRK1B; NbExp=3; IntAct=EBI-359808, EBI-634187;
Q9H2X6:HIPK2; NbExp=10; IntAct=EBI-359808, EBI-348345;
Q13233:MAP3K1; NbExp=7; IntAct=EBI-359808, EBI-49776;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Overexpression of
DIAHP1 or active RHOA causes translocation from the nucleus to
cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P61962-1; Sequence=Displayed;
Name=2;
IsoId=P61962-2; Sequence=VSP_054015;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the WD repeat DCAF7 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U94747; AAC18913.1; -; mRNA.
EMBL; AK303212; BAG64301.1; -; mRNA.
EMBL; AC113554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94305.1; -; Genomic_DNA.
EMBL; CH471109; EAW94306.1; -; Genomic_DNA.
EMBL; BC001264; AAH01264.1; -; mRNA.
CCDS; CCDS74127.1; -. [P61962-1]
RefSeq; NP_005819.3; NM_005828.4. [P61962-1]
UniGene; Hs.410596; -.
ProteinModelPortal; P61962; -.
BioGrid; 115532; 126.
DIP; DIP-40363N; -.
IntAct; P61962; 116.
MINT; P61962; -.
STRING; 9606.ENSP00000308344; -.
iPTMnet; P61962; -.
PhosphoSitePlus; P61962; -.
DMDM; 48428729; -.
EPD; P61962; -.
MaxQB; P61962; -.
PaxDb; P61962; -.
PeptideAtlas; P61962; -.
PRIDE; P61962; -.
DNASU; 10238; -.
Ensembl; ENST00000415273; ENSP00000403920; ENSG00000136485. [P61962-2]
Ensembl; ENST00000431926; ENSP00000402312; ENSG00000136485. [P61962-1]
Ensembl; ENST00000614556; ENSP00000483236; ENSG00000136485. [P61962-1]
GeneID; 10238; -.
KEGG; hsa:10238; -.
UCSC; uc010wpn.5; human. [P61962-1]
CTD; 10238; -.
DisGeNET; 10238; -.
EuPathDB; HostDB:ENSG00000136485.14; -.
GeneCards; DCAF7; -.
HGNC; HGNC:30915; DCAF7.
HPA; HPA022948; -.
HPA; HPA022962; -.
MIM; 605973; gene.
neXtProt; NX_P61962; -.
OpenTargets; ENSG00000136485; -.
PharmGKB; PA165431770; -.
eggNOG; KOG0290; Eukaryota.
eggNOG; ENOG410XQ78; LUCA.
GeneTree; ENSGT00390000006939; -.
HOGENOM; HOG000260968; -.
HOVERGEN; HBG050497; -.
InParanoid; P61962; -.
KO; K11805; -.
OMA; DSAKPND; -.
OrthoDB; EOG091G08UU; -.
PhylomeDB; P61962; -.
Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
Reactome; R-HSA-8951664; Neddylation.
SignaLink; P61962; -.
UniPathway; UPA00143; -.
ChiTaRS; DCAF7; human.
GeneWiki; WDR68; -.
GenomeRNAi; 10238; -.
PRO; PR:P61962; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000136485; -.
CleanEx; HS_WDR68; -.
ExpressionAtlas; P61962; baseline and differential.
Genevisible; P61962; HS.
GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF00400; WD40; 1.
SMART; SM00320; WD40; 5.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm;
Developmental protein; Nucleus; Reference proteome; Repeat;
Ubl conjugation pathway; WD repeat.
CHAIN 1 342 DDB1- and CUL4-associated factor 7.
/FTId=PRO_0000051425.
REPEAT 6 52 WD 1.
REPEAT 60 100 WD 2.
REPEAT 108 150 WD 3.
REPEAT 165 206 WD 4.
REPEAT 213 252 WD 5.
REPEAT 257 296 WD 6.
REPEAT 303 342 WD 7.
VAR_SEQ 47 246 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054015.
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


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