DCAF6_HUMAN
ID DCAF6_HUMAN Reviewed; 860 AA.
AC Q58WW2; A2A295; B4DNB8; Q7L8I0; Q8IXH3; Q8TB19;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=DDB1- and CUL4-associated factor 6;
DE AltName: Full=Androgen receptor complex-associated protein;
DE Short=ARCAP;
DE AltName: Full=IQ motif and WD repeat-containing protein 1;
DE AltName: Full=Nuclear receptor interaction protein;
DE Short=NRIP;
GN Name=DCAF6; Synonyms=IQWD1; ORFNames=MSTP055;
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), FUNCTION, INTERACTION WITH NR3C1
RP AND AR, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15784617; DOI=10.1074/jbc.m412169200;
RA Tsai T.C., Lee Y.L., Hsiao W.C., Tsao Y.P., Chen S.L.;
RT "NRIP, a novel nuclear receptor interaction protein, enhances the
RT transcriptional activity of nuclear receptors.";
RL J. Biol. Chem. 280:20000-20009(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Chang T.-J., Lui W.-Y., Hsia C.-Y., Huang K.-T., Huang M.-H., Lai C.,
RA King K.-L., Chau G.-Y., Chi C.-W., Li A.F.-Y.;
RT "ARCAP, a novel androgen receptor coactivator, modulates the proliferation
RT of hepatoma cells.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Heart;
RA Zhao B., Xu Y.Y., Liu Y.Q., Wang X.Y., Liu B., Ye J., Song L., Zhao Y.,
RA Cao H.Q., Zhao X.W., Gao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y.,
RA Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Heart;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 329-860 (ISOFORM 1), AND VARIANT
RP ALA-547.
RC TISSUE=B-cell;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 355-860 (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [9]
RP FUNCTION, INTERACTION WITH DDB1; CUL4A AND CUL4B, AND IDENTIFICATION BY
RP 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336 AND SER-657, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336 AND SER-657, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-649; THR-654 AND
RP SER-657, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336 AND SER-657, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; THR-654 AND SER-657, 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: Ligand-dependent coactivator of nuclear receptors. Enhance
CC transcriptional activity of the nuclear receptors NR3C1 and AR. May
CC function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein
CC ligase complex. {ECO:0000269|PubMed:15784617,
CC ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:16964240}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with the nuclear receptors NR3C1 and AR in the
CC presence of ligand. Interacts with DDB1, CUL4A and CUL4B.
CC {ECO:0000269|PubMed:15784617, ECO:0000269|PubMed:16949367}.
CC -!- INTERACTION:
CC Q58WW2; Q9UHL9: GTF2IRD1; NbExp=2; IntAct=EBI-2559044, EBI-372530;
CC Q58WW2; Q99750: MDFI; NbExp=3; IntAct=EBI-2559044, EBI-724076;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15784617}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q58WW2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q58WW2-2; Sequence=VSP_028019;
CC Name=3;
CC IsoId=Q58WW2-3; Sequence=VSP_028020, VSP_028021;
CC Name=4;
CC IsoId=Q58WW2-4; Sequence=VSP_043312, VSP_028020, VSP_028021;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and testis.
CC Expressed to a lesser degree in heart, prostate, and adrenal gland.
CC {ECO:0000269|PubMed:15784617}.
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DR EMBL; AY766164; AAX09330.1; -; mRNA.
DR EMBL; DQ768089; ABG76793.1; -; mRNA.
DR EMBL; AF116725; AAO15301.1; -; mRNA.
DR EMBL; AK297847; BAG60180.1; -; mRNA.
DR EMBL; Z97876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL033531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL033532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90809.1; -; Genomic_DNA.
DR EMBL; BC025262; AAH25262.2; -; mRNA.
DR EMBL; AL136738; CAB66672.2; -; mRNA.
DR CCDS; CCDS1267.2; -. [Q58WW2-2]
DR CCDS; CCDS30933.1; -. [Q58WW2-1]
DR CCDS; CCDS55657.1; -. [Q58WW2-3]
DR CCDS; CCDS55658.1; -. [Q58WW2-4]
DR RefSeq; NP_001017977.1; NM_001017977.2. [Q58WW2-1]
DR RefSeq; NP_001185885.1; NM_001198956.1. [Q58WW2-3]
DR RefSeq; NP_001185886.1; NM_001198957.1. [Q58WW2-4]
DR RefSeq; NP_060912.2; NM_018442.3. [Q58WW2-2]
DR PDB; 3I7O; X-ray; 2.80 A; B=9-21.
DR PDBsum; 3I7O; -.
DR AlphaFoldDB; Q58WW2; -.
DR SMR; Q58WW2; -.
DR BioGRID; 120933; 108.
DR DIP; DIP-44678N; -.
DR IntAct; Q58WW2; 37.
DR MINT; Q58WW2; -.
DR STRING; 9606.ENSP00000356814; -.
DR iPTMnet; Q58WW2; -.
DR PhosphoSitePlus; Q58WW2; -.
DR BioMuta; DCAF6; -.
DR DMDM; 74755134; -.
DR EPD; Q58WW2; -.
DR jPOST; Q58WW2; -.
DR MassIVE; Q58WW2; -.
DR MaxQB; Q58WW2; -.
DR PaxDb; Q58WW2; -.
DR PeptideAtlas; Q58WW2; -.
DR PRIDE; Q58WW2; -.
DR ProteomicsDB; 62628; -. [Q58WW2-1]
DR ProteomicsDB; 62629; -. [Q58WW2-2]
DR ProteomicsDB; 62630; -. [Q58WW2-3]
DR ProteomicsDB; 62631; -. [Q58WW2-4]
DR Antibodypedia; 34346; 154 antibodies from 26 providers.
DR DNASU; 55827; -.
DR Ensembl; ENST00000312263.10; ENSP00000311949.6; ENSG00000143164.16. [Q58WW2-1]
DR Ensembl; ENST00000367840.4; ENSP00000356814.3; ENSG00000143164.16. [Q58WW2-3]
DR Ensembl; ENST00000367843.7; ENSP00000356817.3; ENSG00000143164.16. [Q58WW2-2]
DR Ensembl; ENST00000432587.6; ENSP00000396238.2; ENSG00000143164.16. [Q58WW2-4]
DR GeneID; 55827; -.
DR KEGG; hsa:55827; -.
DR MANE-Select; ENST00000367840.4; ENSP00000356814.3; NM_001198956.2; NP_001185885.1. [Q58WW2-3]
DR UCSC; uc001gev.5; human. [Q58WW2-1]
DR CTD; 55827; -.
DR DisGeNET; 55827; -.
DR GeneCards; DCAF6; -.
DR HGNC; HGNC:30002; DCAF6.
DR HPA; ENSG00000143164; Group enriched (skeletal muscle, tongue).
DR MIM; 610494; gene.
DR neXtProt; NX_Q58WW2; -.
DR OpenTargets; ENSG00000143164; -.
DR PharmGKB; PA165751150; -.
DR VEuPathDB; HostDB:ENSG00000143164; -.
DR eggNOG; KOG1310; Eukaryota.
DR eggNOG; KOG1334; Eukaryota.
DR GeneTree; ENSGT00950000182900; -.
DR InParanoid; Q58WW2; -.
DR OMA; HIYSFDI; -.
DR OrthoDB; 1270484at2759; -.
DR PhylomeDB; Q58WW2; -.
DR TreeFam; TF326071; -.
DR PathwayCommons; Q58WW2; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q58WW2; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 55827; 38 hits in 1117 CRISPR screens.
DR ChiTaRS; DCAF6; human.
DR EvolutionaryTrace; Q58WW2; -.
DR GenomeRNAi; 55827; -.
DR Pharos; Q58WW2; Tbio.
DR PRO; PR:Q58WW2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q58WW2; protein.
DR Bgee; ENSG00000143164; Expressed in skeletal muscle tissue of rectus abdominis and 204 other tissues.
DR ExpressionAtlas; Q58WW2; baseline and differential.
DR Genevisible; Q58WW2; 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:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR045151; DCAF8.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
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; 2.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..860
FT /note="DDB1- and CUL4-associated factor 6"
FT /id="PRO_0000304401"
FT REPEAT 49..88
FT /note="WD 1"
FT REPEAT 92..133
FT /note="WD 2"
FT REPEAT 139..179
FT /note="WD 3"
FT REPEAT 189..229
FT /note="WD 4"
FT REPEAT 251..290
FT /note="WD 5"
FT DOMAIN 676..705
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REPEAT 718..756
FT /note="WD 6"
FT REPEAT 759..798
FT /note="WD 7"
FT REGION 288..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 654
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC22"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DC22"
FT VAR_SEQ 54..84
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043312"
FT VAR_SEQ 459
FT /note="S -> SDSPSSVVNKQLGSMSLDEQQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_028019"
FT VAR_SEQ 459
FT /note="S -> SEFLRGPEIALLRKRLQQLRLKKAEQQRQQELAAHTQQQPSTSDQSS
FT HEGSSQDPHASDSPSSVVNKQLGSMSLDEQQ (in isoform 3 and isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_028020"
FT VAR_SEQ 675
FT /note="D -> DRFNIRGTTIGDRIM (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_028021"
FT VARIANT 547
FT /note="V -> A (in dbSNP:rs11558511)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035020"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:3I7O"
SQ SEQUENCE 860 AA; 96292 MW; 8C7602D635DAF124 CRC64;
MSRGGSYPHL LWDVRKRSLG LEDPSRLRSR YLGRREFIQR LKLEATLNVH DGCVNTICWN
DTGEYILSGS DDTKLVISNP YSRKVLTTIR SGHRANIFSA KFLPCTNDKQ IVSCSGDGVI
FYTNVEQDAE TNRQCQFTCH YGTTYEIMTV PNDPYTFLSC GEDGTVRWFD TRIKTSCTKE
DCKDDILINC RRAATSVAIC PPIPYYLAVG CSDSSVRIYD RRMLGTRATG NYAGRGTTGM
VARFIPSHLN NKSCRVTSLC YSEDGQEILV SYSSDYIYLF DPKDDTAREL KTPSAEERRE
ELRQPPVKRL RLRGDWSDTG PRARPESERE RDGEQSPNVS LMQRMSDMLS RWFEEASEVA
QSNRGRGRSR PRGGTSQSDI STLPTVPSSP DLEVSETAME VDTPAEQFLQ PSTSSTMSAQ
AHSTSSPTES PHSTPLLSSP DSEQRQSVEA SGHHTHHQSD NNNEKLSPKP GTGEPVLSLH
YSTEGTTTST IKLNFTDEWS SIASSSRGIG SHCKSEGQEE SFVPQSSVQP PEGDSETKAP
EESSEDVTKY QEGVSAENPV ENHINITQSD KFTAKPLDSN SGERNDLNLD RSCGVPEESA
SSEKAKEPET SDQTSTESAT NENNTNPEPQ FQTEATGPSA HEETSTRDSA LQDTDDSDDD
PVLIPGARYR AGPGDRRSAV ARIQEFFRRR KERKEMEELD TLNIRRPLVK MVYKGHRNSR
TMIKEANFWG ANFVMSGSDC GHIFIWDRHT AEHLMLLEAD NHVVNCLQPH PFDPILASSG
IDYDIKIWSP LEESRIFNRK LADEVITRNE LMLEETRNTI TVPASFMLRM LASLNHIRAD
RLEGDRSEGS GQENENEDEE
