Full text data of DCAF6
DCAF6
(IQWD1)
[Confidence: low (only semi-automatic identification from reviews)]
DDB1- and CUL4-associated factor 6 (Androgen receptor complex-associated protein; ARCAP; IQ motif and WD repeat-containing protein 1; Nuclear receptor interaction protein; NRIP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DDB1- and CUL4-associated factor 6 (Androgen receptor complex-associated protein; ARCAP; IQ motif and WD repeat-containing protein 1; Nuclear receptor interaction protein; NRIP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q58WW2
ID DCAF6_HUMAN Reviewed; 860 AA.
AC Q58WW2; A2A295; B4DNB8; Q7L8I0; Q8IXH3; Q8TB19;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 26-APR-2005, sequence version 1.
DT 22-JAN-2014, entry version 94.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP NR3C1 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
RT proliferation 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.,
RA Zhao Y., Cao H.Q., Zhao X.W., Gao Y., Liu L.S., Ding J.F., Gao R.L.,
RA Wu Q.Y., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RP VARIANT 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
RT project: 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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
RP 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,
RT which is required for S phase destruction of the replication factor
RT 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
RT ligase machinery.";
RL Nature 443:590-593(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336 AND SER-657, AND
RP MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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
RP AND SER-657, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Ligand-dependent coactivator of nuclear receptors.
CC Enhance transcriptional activity of the nuclear receptors NR3C1
CC and AR. May function as a substrate receptor for CUL4-DDB1 E3
CC ubiquitin-protein ligase complex.
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 -!- SUBCELLULAR LOCATION: Nucleus.
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 Note=No experimental confirmation available;
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and
CC testis. Expressed to a lesser degree in heart, prostate, and
CC adrenal gland.
CC -!- SIMILARITY: Contains 1 IQ domain.
CC -!- SIMILARITY: Contains 7 WD repeats.
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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; CAI20078.1; -; Genomic_DNA.
DR EMBL; AL031287; CAI20078.1; JOINED; Genomic_DNA.
DR EMBL; AL033531; CAI20078.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAI20078.1; JOINED; Genomic_DNA.
DR EMBL; AL033531; CAI22478.1; -; Genomic_DNA.
DR EMBL; AL031287; CAI22478.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAI22478.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAI22478.1; JOINED; Genomic_DNA.
DR EMBL; AL031287; CAI22481.1; -; Genomic_DNA.
DR EMBL; AL033531; CAI22481.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAI22481.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAI22481.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAI22625.1; -; Genomic_DNA.
DR EMBL; AL031287; CAI22625.1; JOINED; Genomic_DNA.
DR EMBL; AL033531; CAI22625.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAI22625.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAM28213.1; -; Genomic_DNA.
DR EMBL; AL031287; CAM28213.1; JOINED; Genomic_DNA.
DR EMBL; AL033531; CAM28213.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAM28213.1; JOINED; Genomic_DNA.
DR EMBL; AL033531; CAM28292.1; -; Genomic_DNA.
DR EMBL; AL031287; CAM28292.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAM28292.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAM28292.1; JOINED; Genomic_DNA.
DR EMBL; AL031287; CAM28293.1; -; Genomic_DNA.
DR EMBL; AL033531; CAM28293.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAM28293.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAM28293.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAM28303.1; -; Genomic_DNA.
DR EMBL; AL031287; CAM28303.1; JOINED; Genomic_DNA.
DR EMBL; AL033531; CAM28303.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAM28303.1; JOINED; Genomic_DNA.
DR EMBL; CH471067; EAW90809.1; -; Genomic_DNA.
DR EMBL; BC025262; AAH25262.2; -; mRNA.
DR EMBL; AL136738; CAB66672.2; -; mRNA.
DR RefSeq; NP_001017977.1; NM_001017977.2.
DR RefSeq; NP_001185885.1; NM_001198956.1.
DR RefSeq; NP_001185886.1; NM_001198957.1.
DR RefSeq; NP_060912.2; NM_018442.3.
DR UniGene; Hs.435741; -.
DR PDB; 3I7O; X-ray; 2.80 A; B=9-21.
DR PDBsum; 3I7O; -.
DR ProteinModelPortal; Q58WW2; -.
DR SMR; Q58WW2; 258-286, 732-791.
DR DIP; DIP-44678N; -.
DR IntAct; Q58WW2; 8.
DR STRING; 9606.ENSP00000356817; -.
DR PhosphoSite; Q58WW2; -.
DR DMDM; 74755134; -.
DR PaxDb; Q58WW2; -.
DR PRIDE; Q58WW2; -.
DR DNASU; 55827; -.
DR Ensembl; ENST00000312263; ENSP00000311949; ENSG00000143164.
DR Ensembl; ENST00000367840; ENSP00000356814; ENSG00000143164.
DR Ensembl; ENST00000367843; ENSP00000356817; ENSG00000143164.
DR Ensembl; ENST00000432587; ENSP00000396238; ENSG00000143164.
DR GeneID; 55827; -.
DR KEGG; hsa:55827; -.
DR UCSC; uc001gew.3; human.
DR CTD; 55827; -.
DR GeneCards; GC01P167905; -.
DR HGNC; HGNC:30002; DCAF6.
DR HPA; HPA030852; -.
DR MIM; 610494; gene.
DR neXtProt; NX_Q58WW2; -.
DR PharmGKB; PA165751150; -.
DR eggNOG; NOG292060; -.
DR HOGENOM; HOG000038027; -.
DR HOVERGEN; HBG054871; -.
DR KO; K11795; -.
DR OMA; RELKGPS; -.
DR OrthoDB; EOG7P5T0B; -.
DR SignaLink; Q58WW2; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; DCAF6; human.
DR EvolutionaryTrace; Q58WW2; -.
DR GenomeRNAi; 55827; -.
DR NextBio; 61026; -.
DR PRO; PR:Q58WW2; -.
DR ArrayExpress; Q58WW2; -.
DR Bgee; Q58WW2; -.
DR CleanEx; HS_IQWD1; -.
DR Genevestigator; Q58WW2; -.
DR GO; GO:0080008; C:Cul4-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IC:UniProtKB.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1 860 DDB1- and CUL4-associated factor 6.
FT /FTId=PRO_0000304401.
FT REPEAT 49 88 WD 1.
FT REPEAT 92 133 WD 2.
FT REPEAT 139 179 WD 3.
FT REPEAT 189 229 WD 4.
FT REPEAT 251 290 WD 5.
FT DOMAIN 676 705 IQ.
FT REPEAT 718 756 WD 6.
FT REPEAT 759 798 WD 7.
FT MOD_RES 336 336 Phosphoserine.
FT MOD_RES 649 649 Phosphoserine.
FT MOD_RES 654 654 Phosphothreonine.
FT MOD_RES 657 657 Phosphoserine.
FT VAR_SEQ 54 84 Missing (in isoform 4).
FT /FTId=VSP_043312.
FT VAR_SEQ 459 459 S -> SDSPSSVVNKQLGSMSLDEQQ (in isoform
FT 2).
FT /FTId=VSP_028019.
FT VAR_SEQ 459 459 S -> SEFLRGPEIALLRKRLQQLRLKKAEQQRQQELAAHT
FT QQQPSTSDQSSHEGSSQDPHASDSPSSVVNKQLGSMSLDEQ
FT Q (in isoform 3 and isoform 4).
FT /FTId=VSP_028020.
FT VAR_SEQ 675 675 D -> DRFNIRGTTIGDRIM (in isoform 3 and
FT isoform 4).
FT /FTId=VSP_028021.
FT VARIANT 547 547 V -> A (in dbSNP:rs11558511).
FT /FTId=VAR_035020.
FT HELIX 10 18
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
//
ID DCAF6_HUMAN Reviewed; 860 AA.
AC Q58WW2; A2A295; B4DNB8; Q7L8I0; Q8IXH3; Q8TB19;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 26-APR-2005, sequence version 1.
DT 22-JAN-2014, entry version 94.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP NR3C1 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
RT proliferation 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.,
RA Zhao Y., Cao H.Q., Zhao X.W., Gao Y., Liu L.S., Ding J.F., Gao R.L.,
RA Wu Q.Y., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RP VARIANT 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
RT project: 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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
RP 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,
RT which is required for S phase destruction of the replication factor
RT 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
RT ligase machinery.";
RL Nature 443:590-593(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336 AND SER-657, AND
RP MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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
RP AND SER-657, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Ligand-dependent coactivator of nuclear receptors.
CC Enhance transcriptional activity of the nuclear receptors NR3C1
CC and AR. May function as a substrate receptor for CUL4-DDB1 E3
CC ubiquitin-protein ligase complex.
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 -!- SUBCELLULAR LOCATION: Nucleus.
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 Note=No experimental confirmation available;
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and
CC testis. Expressed to a lesser degree in heart, prostate, and
CC adrenal gland.
CC -!- SIMILARITY: Contains 1 IQ domain.
CC -!- SIMILARITY: Contains 7 WD repeats.
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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; CAI20078.1; -; Genomic_DNA.
DR EMBL; AL031287; CAI20078.1; JOINED; Genomic_DNA.
DR EMBL; AL033531; CAI20078.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAI20078.1; JOINED; Genomic_DNA.
DR EMBL; AL033531; CAI22478.1; -; Genomic_DNA.
DR EMBL; AL031287; CAI22478.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAI22478.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAI22478.1; JOINED; Genomic_DNA.
DR EMBL; AL031287; CAI22481.1; -; Genomic_DNA.
DR EMBL; AL033531; CAI22481.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAI22481.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAI22481.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAI22625.1; -; Genomic_DNA.
DR EMBL; AL031287; CAI22625.1; JOINED; Genomic_DNA.
DR EMBL; AL033531; CAI22625.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAI22625.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAM28213.1; -; Genomic_DNA.
DR EMBL; AL031287; CAM28213.1; JOINED; Genomic_DNA.
DR EMBL; AL033531; CAM28213.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAM28213.1; JOINED; Genomic_DNA.
DR EMBL; AL033531; CAM28292.1; -; Genomic_DNA.
DR EMBL; AL031287; CAM28292.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAM28292.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAM28292.1; JOINED; Genomic_DNA.
DR EMBL; AL031287; CAM28293.1; -; Genomic_DNA.
DR EMBL; AL033531; CAM28293.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAM28293.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAM28293.1; JOINED; Genomic_DNA.
DR EMBL; AL033532; CAM28303.1; -; Genomic_DNA.
DR EMBL; AL031287; CAM28303.1; JOINED; Genomic_DNA.
DR EMBL; AL033531; CAM28303.1; JOINED; Genomic_DNA.
DR EMBL; Z97876; CAM28303.1; JOINED; Genomic_DNA.
DR EMBL; CH471067; EAW90809.1; -; Genomic_DNA.
DR EMBL; BC025262; AAH25262.2; -; mRNA.
DR EMBL; AL136738; CAB66672.2; -; mRNA.
DR RefSeq; NP_001017977.1; NM_001017977.2.
DR RefSeq; NP_001185885.1; NM_001198956.1.
DR RefSeq; NP_001185886.1; NM_001198957.1.
DR RefSeq; NP_060912.2; NM_018442.3.
DR UniGene; Hs.435741; -.
DR PDB; 3I7O; X-ray; 2.80 A; B=9-21.
DR PDBsum; 3I7O; -.
DR ProteinModelPortal; Q58WW2; -.
DR SMR; Q58WW2; 258-286, 732-791.
DR DIP; DIP-44678N; -.
DR IntAct; Q58WW2; 8.
DR STRING; 9606.ENSP00000356817; -.
DR PhosphoSite; Q58WW2; -.
DR DMDM; 74755134; -.
DR PaxDb; Q58WW2; -.
DR PRIDE; Q58WW2; -.
DR DNASU; 55827; -.
DR Ensembl; ENST00000312263; ENSP00000311949; ENSG00000143164.
DR Ensembl; ENST00000367840; ENSP00000356814; ENSG00000143164.
DR Ensembl; ENST00000367843; ENSP00000356817; ENSG00000143164.
DR Ensembl; ENST00000432587; ENSP00000396238; ENSG00000143164.
DR GeneID; 55827; -.
DR KEGG; hsa:55827; -.
DR UCSC; uc001gew.3; human.
DR CTD; 55827; -.
DR GeneCards; GC01P167905; -.
DR HGNC; HGNC:30002; DCAF6.
DR HPA; HPA030852; -.
DR MIM; 610494; gene.
DR neXtProt; NX_Q58WW2; -.
DR PharmGKB; PA165751150; -.
DR eggNOG; NOG292060; -.
DR HOGENOM; HOG000038027; -.
DR HOVERGEN; HBG054871; -.
DR KO; K11795; -.
DR OMA; RELKGPS; -.
DR OrthoDB; EOG7P5T0B; -.
DR SignaLink; Q58WW2; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; DCAF6; human.
DR EvolutionaryTrace; Q58WW2; -.
DR GenomeRNAi; 55827; -.
DR NextBio; 61026; -.
DR PRO; PR:Q58WW2; -.
DR ArrayExpress; Q58WW2; -.
DR Bgee; Q58WW2; -.
DR CleanEx; HS_IQWD1; -.
DR Genevestigator; Q58WW2; -.
DR GO; GO:0080008; C:Cul4-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IC:UniProtKB.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1 860 DDB1- and CUL4-associated factor 6.
FT /FTId=PRO_0000304401.
FT REPEAT 49 88 WD 1.
FT REPEAT 92 133 WD 2.
FT REPEAT 139 179 WD 3.
FT REPEAT 189 229 WD 4.
FT REPEAT 251 290 WD 5.
FT DOMAIN 676 705 IQ.
FT REPEAT 718 756 WD 6.
FT REPEAT 759 798 WD 7.
FT MOD_RES 336 336 Phosphoserine.
FT MOD_RES 649 649 Phosphoserine.
FT MOD_RES 654 654 Phosphothreonine.
FT MOD_RES 657 657 Phosphoserine.
FT VAR_SEQ 54 84 Missing (in isoform 4).
FT /FTId=VSP_043312.
FT VAR_SEQ 459 459 S -> SDSPSSVVNKQLGSMSLDEQQ (in isoform
FT 2).
FT /FTId=VSP_028019.
FT VAR_SEQ 459 459 S -> SEFLRGPEIALLRKRLQQLRLKKAEQQRQQELAAHT
FT QQQPSTSDQSSHEGSSQDPHASDSPSSVVNKQLGSMSLDEQ
FT Q (in isoform 3 and isoform 4).
FT /FTId=VSP_028020.
FT VAR_SEQ 675 675 D -> DRFNIRGTTIGDRIM (in isoform 3 and
FT isoform 4).
FT /FTId=VSP_028021.
FT VARIANT 547 547 V -> A (in dbSNP:rs11558511).
FT /FTId=VAR_035020.
FT HELIX 10 18
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
//
MIM
610494
*RECORD*
*FIELD* NO
610494
*FIELD* TI
*610494 DDB1- AND CUL4-ASSOCIATED FACTOR 6; DCAF6
;;IQ MOTIF- AND WD REPEATS-CONTAINING 1; IQWD1;;
read moreNUCLEAR RECEPTOR INTERACTION PROTEIN; NRIP;;
HOM-TES-88/94/95
*FIELD* TX
CLONING
By subtractive hybridization to enrich for transcripts highly expressed
in testis, followed by serologic expression screening with antibodies
from a seminoma patient, Tureci et al. (2002) isolated IQWD1, which they
designated HOM-TES-88/94/95. RT-PCR detected ubiquitous expression.
Using androgen receptor (AR; 313700) as bait in a yeast 2-hybrid screen
of a HeLa cell cDNA library, Tsai et al. (2005) cloned IQWD1, which they
called NRIP. The deduced 860-amino acid protein has a calculated
molecular mass of 96 kD. It contains 7 WD40 repeats, 5 of which are
N-terminal and 2 of which are C-terminal following a nuclear
localization signal. Tsai et al. (2005) also identified the mouse Nrip
gene, which shares 86.3% homology with human NRIP. Northern blot
analysis detected highest expression in skeletal muscle and testis, and
weaker expression in heart, prostate, and adrenal gland. NRIP was also
detected in all cancer cell lines examined. Fluorescence-tagged NRIP was
expressed in the nuclei of transfected human embryonic kidney cells.
GENE FUNCTION
Using in vitro pull-down assays of in vitro translated proteins and
immunoprecipitation analysis of exogenously expressed proteins, Tsai et
al. (2005) demonstrated that NRIP interacted directly with AR and
glucocorticoid receptor (GCCR; 138040) in the presence of ligand. NRIP
also enhanced AR- and GCCR-mediated transcriptional activity in a
reporter gene assay in the presence of AR or GCCR ligands.
Downregulation of endogenous NRIP by siRNA reduced the growth rate of a
human prostate carcinoma cell line in the absence of ligand. Tsai et al.
(2005) concluded that NRIP functions as a ligand-dependent coactivator
of nuclear receptors and enhances their transcriptional activity.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DCAF6
gene to chromosome 1 (TMAP RH64705).
*FIELD* RF
1. Tsai, T.-C.; Lee, Y.-L.; Hsiao, W.-C.; Tsao, Y.-P.; Chen, S.-L.
: NRIP, a novel nuclear receptor interaction protein, enhances the
transcriptional activity of nuclear receptors. J. Biol. Chem. 280:
20000-20009, 2005.
2. Tureci, O.; Sahin, U.; Koslowski, M.; Buss, B.; Bell, C.; Ballweber,
P.; Zwick, C.; Eberle, T.; Zuber, M.; Villena-Heinsen, C.; Seitz,
G.; Pfreundschuh, M.: A novel tumour associated leucine zipper protein
targeting to sites of gene transcription and splicing. Oncogene 21:
3879-3888, 2002.
*FIELD* CD
Patricia A. Hartz: 10/16/2006
*FIELD* ED
alopez: 03/27/2012
carol: 1/2/2007
wwang: 10/16/2006
*RECORD*
*FIELD* NO
610494
*FIELD* TI
*610494 DDB1- AND CUL4-ASSOCIATED FACTOR 6; DCAF6
;;IQ MOTIF- AND WD REPEATS-CONTAINING 1; IQWD1;;
read moreNUCLEAR RECEPTOR INTERACTION PROTEIN; NRIP;;
HOM-TES-88/94/95
*FIELD* TX
CLONING
By subtractive hybridization to enrich for transcripts highly expressed
in testis, followed by serologic expression screening with antibodies
from a seminoma patient, Tureci et al. (2002) isolated IQWD1, which they
designated HOM-TES-88/94/95. RT-PCR detected ubiquitous expression.
Using androgen receptor (AR; 313700) as bait in a yeast 2-hybrid screen
of a HeLa cell cDNA library, Tsai et al. (2005) cloned IQWD1, which they
called NRIP. The deduced 860-amino acid protein has a calculated
molecular mass of 96 kD. It contains 7 WD40 repeats, 5 of which are
N-terminal and 2 of which are C-terminal following a nuclear
localization signal. Tsai et al. (2005) also identified the mouse Nrip
gene, which shares 86.3% homology with human NRIP. Northern blot
analysis detected highest expression in skeletal muscle and testis, and
weaker expression in heart, prostate, and adrenal gland. NRIP was also
detected in all cancer cell lines examined. Fluorescence-tagged NRIP was
expressed in the nuclei of transfected human embryonic kidney cells.
GENE FUNCTION
Using in vitro pull-down assays of in vitro translated proteins and
immunoprecipitation analysis of exogenously expressed proteins, Tsai et
al. (2005) demonstrated that NRIP interacted directly with AR and
glucocorticoid receptor (GCCR; 138040) in the presence of ligand. NRIP
also enhanced AR- and GCCR-mediated transcriptional activity in a
reporter gene assay in the presence of AR or GCCR ligands.
Downregulation of endogenous NRIP by siRNA reduced the growth rate of a
human prostate carcinoma cell line in the absence of ligand. Tsai et al.
(2005) concluded that NRIP functions as a ligand-dependent coactivator
of nuclear receptors and enhances their transcriptional activity.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DCAF6
gene to chromosome 1 (TMAP RH64705).
*FIELD* RF
1. Tsai, T.-C.; Lee, Y.-L.; Hsiao, W.-C.; Tsao, Y.-P.; Chen, S.-L.
: NRIP, a novel nuclear receptor interaction protein, enhances the
transcriptional activity of nuclear receptors. J. Biol. Chem. 280:
20000-20009, 2005.
2. Tureci, O.; Sahin, U.; Koslowski, M.; Buss, B.; Bell, C.; Ballweber,
P.; Zwick, C.; Eberle, T.; Zuber, M.; Villena-Heinsen, C.; Seitz,
G.; Pfreundschuh, M.: A novel tumour associated leucine zipper protein
targeting to sites of gene transcription and splicing. Oncogene 21:
3879-3888, 2002.
*FIELD* CD
Patricia A. Hartz: 10/16/2006
*FIELD* ED
alopez: 03/27/2012
carol: 1/2/2007
wwang: 10/16/2006