WDR3_HUMAN
ID WDR3_HUMAN Reviewed; 943 AA.
AC Q9UNX4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=WD repeat-containing protein 3;
GN Name=WDR3;
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].
RX PubMed=10395803; DOI=10.1006/geno.1999.5858;
RA Claudio J.O., Liew C.-C., Ma J., Heng H.H.Q., Stewart A.K., Hawley R.G.;
RT "Cloning and expression analysis of a novel WD repeat gene, WDR3, mapping
RT to 1p12-p13.";
RL Genomics 59:85-89(1999).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240 AND SER-241, 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 [5]
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 [6]
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 [7]
RP 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257 AND SER-726, 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 [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-474 AND LYS-529, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the WD repeat WDR3/UTP12 family. {ECO:0000305}.
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DR EMBL; AF083217; AAD45865.1; -; mRNA.
DR CCDS; CCDS898.1; -.
DR RefSeq; NP_006775.1; NM_006784.2.
DR PDB; 7MQ8; EM; 3.60 A; LQ=1-943.
DR PDB; 7MQ9; EM; 3.87 A; LQ=1-943.
DR PDB; 7MQA; EM; 2.70 A; LQ=1-943.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; Q9UNX4; -.
DR SMR; Q9UNX4; -.
DR BioGRID; 116092; 144.
DR IntAct; Q9UNX4; 35.
DR MINT; Q9UNX4; -.
DR STRING; 9606.ENSP00000308179; -.
DR iPTMnet; Q9UNX4; -.
DR PhosphoSitePlus; Q9UNX4; -.
DR SwissPalm; Q9UNX4; -.
DR BioMuta; WDR3; -.
DR DMDM; 12230773; -.
DR SWISS-2DPAGE; Q9UNX4; -.
DR EPD; Q9UNX4; -.
DR jPOST; Q9UNX4; -.
DR MassIVE; Q9UNX4; -.
DR MaxQB; Q9UNX4; -.
DR PaxDb; Q9UNX4; -.
DR PeptideAtlas; Q9UNX4; -.
DR PRIDE; Q9UNX4; -.
DR ProteomicsDB; 85340; -.
DR Antibodypedia; 33896; 95 antibodies from 21 providers.
DR DNASU; 10885; -.
DR Ensembl; ENST00000349139.6; ENSP00000308179.4; ENSG00000065183.16.
DR GeneID; 10885; -.
DR KEGG; hsa:10885; -.
DR MANE-Select; ENST00000349139.6; ENSP00000308179.4; NM_006784.3; NP_006775.1.
DR UCSC; uc010oxe.2; human.
DR CTD; 10885; -.
DR DisGeNET; 10885; -.
DR GeneCards; WDR3; -.
DR HGNC; HGNC:12755; WDR3.
DR HPA; ENSG00000065183; Low tissue specificity.
DR MIM; 604737; gene.
DR neXtProt; NX_Q9UNX4; -.
DR OpenTargets; ENSG00000065183; -.
DR PharmGKB; PA37359; -.
DR VEuPathDB; HostDB:ENSG00000065183; -.
DR eggNOG; KOG0306; Eukaryota.
DR GeneTree; ENSGT00940000153859; -.
DR HOGENOM; CLU_005318_0_1_1; -.
DR InParanoid; Q9UNX4; -.
DR OMA; GHQSEVR; -.
DR OrthoDB; 459903at2759; -.
DR PhylomeDB; Q9UNX4; -.
DR TreeFam; TF300427; -.
DR PathwayCommons; Q9UNX4; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9UNX4; -.
DR BioGRID-ORCS; 10885; 765 hits in 1088 CRISPR screens.
DR GeneWiki; WDR3; -.
DR GenomeRNAi; 10885; -.
DR Pharos; Q9UNX4; Tbio.
DR PRO; PR:Q9UNX4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UNX4; protein.
DR Bgee; ENSG00000065183; Expressed in cervix squamous epithelium and 206 other tissues.
DR ExpressionAtlas; Q9UNX4; baseline and differential.
DR Genevisible; Q9UNX4; HS.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0034388; C:Pwp2p-containing subcomplex of 90S preribosome; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030515; F:snoRNA binding; IBA:GO_Central.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 4.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR007148; SSU_processome_Utp12.
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 Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF04003; Utp12; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 9.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation; WD repeat.
FT CHAIN 1..943
FT /note="WD repeat-containing protein 3"
FT /id="PRO_0000051347"
FT REPEAT 21..60
FT /note="WD 1"
FT REPEAT 63..102
FT /note="WD 2"
FT REPEAT 105..144
FT /note="WD 3"
FT REPEAT 147..186
FT /note="WD 4"
FT REPEAT 189..228
FT /note="WD 5"
FT REPEAT 277..316
FT /note="WD 6"
FT REPEAT 413..451
FT /note="WD 7"
FT REPEAT 453..493
FT /note="WD 8"
FT REPEAT 494..533
FT /note="WD 9"
FT REPEAT 547..586
FT /note="WD 10"
FT REPEAT 589..630
FT /note="WD 11"
FT REPEAT 631..670
FT /note="WD 12"
FT REPEAT 673..712
FT /note="WD 13"
FT REGION 326..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 474
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 529
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 234
FT /note="P -> A (in dbSNP:rs3738420)"
FT /id="VAR_033809"
SQ SEQUENCE 943 AA; 106099 MW; 316A151738D91AD7 CRC64;
MGLTKQYLRY VASAVFGVIG SQKGNIVFVT LRGEKGRYVA VPACEHVFIW DLRKGEKILI
LQGLKQEVTC LCPSPDGLHL AVGYEDGSIR IFSLLSGEGN VTFNGHKAAI TTLKYDQLGG
RLASGSKDTD IIVWDVINES GLYRLKGHKD AITQALFLRE KNLLVTSGKD TMVKWWDLDT
QHCFKTMVGH RTEVWGLVLL SEEKRLITGA SDSELRVWDI AYLQEIEDPE EPDPKKIKGS
SPGIQDTLEA EDGAFETDEA PEDRILSCRK AGSIMREGRD RVVNLAVDKT GRILACHGTD
SVLELFCILS KKEIQKKMDK KMKKARKKAK LHSSKGEEED PEVNVEMSLQ DEIQRVTNIK
TSAKIKSFDL IHSPHGELKA VFLLQNNLVE LYSLNPSLPT PQPVRTSRIT IGGHRSDVRT
LSFSSDNIAV LSAAADSIKI WNRSTLQCIR TMTCEYALCS FFVPGDRQVV IGTKTGKLQL
YDLASGNLLE TIDAHDGALW SMSLSPDQRG FVTGGADKSV KFWDFELVKD ENSTQKRLSV
KQTRTLQLDE DVLCVSYSPN QKLLAVSLLD CTVKIFYVDT LKFFLSLYGH KLPVICMDIS
HDGALIATGS ADRNVKIWGL DFGDCHKSLF AHDDSVMYLQ FVPKSHLFFT AGKDHKIKQW
DADKFEHIQT LEGHHQEIWC LAVSPSGDYV VSSSHDKSLR LWERTREPLI LEEEREMERE
AEYEESVAKE DQPAVPGETQ GDSYFTGKKT IETVKAAERI MEAIELYREE TAKMKEHKAI
CKAAGKEVPL PSNPILMAYG SISPSAYVLE IFKGIKSSEL EESLLVLPFS YVPDILKLFN
EFIQLGSDVE LICRCLFFLL RIHFGQITSN QMLVPVIEKL RETTISKVSQ VRDVIGFNMA
GLDYLKRECE AKSEVMFFAD ATSHLEEKKR KRKKREKLIL TLT
