DCA10_HUMAN
ID DCA10_HUMAN Reviewed; 559 AA.
AC Q5QP82; A4VCJ5; Q32NE2; Q8N2Q5; Q96ET5; Q9BTQ5; Q9H5P6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=DDB1- and CUL4-associated factor 10;
DE AltName: Full=WD repeat-containing protein 32;
GN Name=DCAF10; Synonyms=WDR32;
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 GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 298-559 (ISOFORM 2).
RC TISSUE=Ovary, Skin, and Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-559.
RC TISSUE=Embryo, and Ileal mucosa;
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 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [8]
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-92 AND SER-349, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-92, 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).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-134, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3
CC ubiquitin-protein ligase complex. {ECO:0000269|PubMed:16949367}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DDB1. {ECO:0000269|PubMed:16949367}.
CC -!- INTERACTION:
CC Q5QP82; Q969G2: LHX4; NbExp=3; IntAct=EBI-723230, EBI-2865388;
CC Q5QP82-2; O60260-5: PRKN; NbExp=3; IntAct=EBI-10983996, EBI-21251460;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5QP82-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5QP82-2; Sequence=VSP_028513;
CC -!- SIMILARITY: Belongs to the WD repeat DCAF10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI08687.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15574.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC11043.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL138752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58263.1; -; Genomic_DNA.
DR EMBL; BC003520; AAH03520.2; -; mRNA.
DR EMBL; BC011959; AAH11959.2; -; mRNA.
DR EMBL; BC108686; AAI08687.1; ALT_INIT; mRNA.
DR EMBL; BC139834; AAI39835.1; -; mRNA.
DR EMBL; AK026854; BAB15574.1; ALT_INIT; mRNA.
DR EMBL; AK074532; BAC11043.1; ALT_INIT; mRNA.
DR CCDS; CCDS6613.2; -. [Q5QP82-1]
DR RefSeq; NP_001273739.1; NM_001286810.1.
DR RefSeq; NP_077321.3; NM_024345.4. [Q5QP82-1]
DR RefSeq; XP_005251634.1; XM_005251577.3. [Q5QP82-2]
DR AlphaFoldDB; Q5QP82; -.
DR SMR; Q5QP82; -.
DR BioGRID; 122612; 119.
DR IntAct; Q5QP82; 40.
DR MINT; Q5QP82; -.
DR STRING; 9606.ENSP00000366953; -.
DR iPTMnet; Q5QP82; -.
DR PhosphoSitePlus; Q5QP82; -.
DR BioMuta; DCAF10; -.
DR DMDM; 74762212; -.
DR EPD; Q5QP82; -.
DR jPOST; Q5QP82; -.
DR MassIVE; Q5QP82; -.
DR MaxQB; Q5QP82; -.
DR PaxDb; Q5QP82; -.
DR PeptideAtlas; Q5QP82; -.
DR PRIDE; Q5QP82; -.
DR ProteomicsDB; 63640; -. [Q5QP82-1]
DR ProteomicsDB; 63641; -. [Q5QP82-2]
DR Antibodypedia; 12056; 97 antibodies from 20 providers.
DR DNASU; 79269; -.
DR Ensembl; ENST00000377724.8; ENSP00000366953.3; ENSG00000122741.16. [Q5QP82-1]
DR GeneID; 79269; -.
DR KEGG; hsa:79269; -.
DR MANE-Select; ENST00000377724.8; ENSP00000366953.3; NM_024345.5; NP_077321.3.
DR UCSC; uc004aao.5; human. [Q5QP82-1]
DR CTD; 79269; -.
DR GeneCards; DCAF10; -.
DR HGNC; HGNC:23686; DCAF10.
DR HPA; ENSG00000122741; Low tissue specificity.
DR neXtProt; NX_Q5QP82; -.
DR OpenTargets; ENSG00000122741; -.
DR PharmGKB; PA165585713; -.
DR VEuPathDB; HostDB:ENSG00000122741; -.
DR eggNOG; KOG0264; Eukaryota.
DR eggNOG; KOG4155; Eukaryota.
DR GeneTree; ENSGT00390000012666; -.
DR InParanoid; Q5QP82; -.
DR OMA; EFQEGTP; -.
DR OrthoDB; 1068414at2759; -.
DR PhylomeDB; Q5QP82; -.
DR TreeFam; TF323434; -.
DR PathwayCommons; Q5QP82; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q5QP82; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 79269; 14 hits in 1119 CRISPR screens.
DR ChiTaRS; DCAF10; human.
DR GenomeRNAi; 79269; -.
DR Pharos; Q5QP82; Tdark.
DR PRO; PR:Q5QP82; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5QP82; protein.
DR Bgee; ENSG00000122741; Expressed in sperm and 187 other tissues.
DR ExpressionAtlas; Q5QP82; baseline and differential.
DR Genevisible; Q5QP82; HS.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR039085; DCA10.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR14588; PTHR14588; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methylation; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..559
FT /note="DDB1- and CUL4-associated factor 10"
FT /id="PRO_0000306833"
FT REPEAT 166..205
FT /note="WD 1"
FT REPEAT 209..247
FT /note="WD 2"
FT REPEAT 251..290
FT /note="WD 3"
FT REPEAT 296..335
FT /note="WD 4"
FT REPEAT 408..448
FT /note="WD 5"
FT REPEAT 470..508
FT /note="WD 6"
FT REPEAT 526..559
FT /note="WD 7"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..61
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AKB9"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AKB9"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 134
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 352..388
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028513"
FT CONFLICT 309
FT /note="D -> G (in Ref. 4; BAC11043)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="K -> N (in Ref. 3; AAH03520)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="C -> W (in Ref. 4; BAB15574)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 60582 MW; 583B5A781ADAED38 CRC64;
MFPFGPHSPG GDGSAGAGAE EPTPHEGQAA ATGPPSPLHP GADATHPPPP ARSPRRPGAP
SLSPAPRSGE LGLPGAPESS TASAPGEPSP PSPPCRRPGP DCRAKSRGRH GLGAGLGGPG
ARLFGWLKER SLGRGLFVDP ARDNFRTMTS LYGSIHPADS VYLSTRTHGA VFNLEYSPDG
SVLTVACEQT EVLLFDPISS KHIKTLSEAH EDCVNNIRFL DNRLFATCSD DTTIALWDLR
KLNTKVCTLH GHTSWVKNIE YDTNTRLLVT SGFDGNVIIW DTNRYTEDGC PHKKFFHTRF
LMRMRLTPDC SKMLISTSSG YLLILHDLDL TKSLEVGSYP ILRARRTTSS SDLTTSSSSS
GPRVSGSPCH HSDSNSSEKH MSRASQREGV SPRNSLEVVT PEVLGESDHG NCITSLQLHP
KGWATLLRCS SNSDDEECTC VYEFQEGAPV RPVSPRCSLR LTHYIEEANV GRGYIKELCF
SPDGRMISSP HGYGIRLLGF DKQCSELVDC LPKEASPLRV IRSLYSHNDV VLTTKFSPTH
CQIASGCLSG RVSLYQPKF
