ID WDR20_HUMAN Reviewed; 569 AA. AC Q8TBZ3; B4DN18; E7EUY8; F8W9S4; G3V2F8; G3V5R0; H0YJJ1; Q86TU2; Q8NCN7; AC Q8WXX2; Q9UF86; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 2. DT 24-JAN-2024, entry version 175. DE RecName: Full=WD repeat-containing protein 20; DE AltName: Full=Protein DMR; GN Name=WDR20; 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 MRNA] (ISOFORM 4). RC TISSUE=Neuroblastoma; RA Li W.B., Gruber C., Jessee J., Polayes D.; RT "Full-length cDNA libraries and normalization."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT RP HIS-159. RC TISSUE=Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-569 (ISOFORM 2). RA Li N., Chen T., Wan T., Zhang W., Cao X.; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 232-569 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND SER-434, 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND IDENTIFICATION BY RP 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 INTERACTION WITH USP12 AND USP46, FUNCTION, AND SUBUNIT. RX PubMed=20147737; DOI=10.1074/jbc.m109.095141; RA Kee Y., Yang K., Cohn M.A., Haas W., Gygi S.P., D'Andrea A.D.; RT "WDR20 regulates activity of the USP12 x UAF1 deubiquitinating enzyme RT complex."; RL J. Biol. Chem. 285:11252-11257(2010). RN [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND IDENTIFICATION BY RP 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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; SER-360; SER-434 AND RP SER-465, AND 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 [14] 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 [15] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-262; TRP-306; RP LEU-464 AND LEU-466. RX PubMed=30466959; DOI=10.1016/j.ejcb.2018.10.003; RA Olazabal-Herrero A., Sendino M., Arganda-Carreras I., Rodriguez J.A.; RT "WDR20 regulates shuttling of the USP12 deubiquitinase complex between the RT plasma membrane, cytoplasm and nucleus."; RL Eur. J. Cell Biol. 98:12-26(2019). RN [16] RP SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF PHE-262 AND TRP-306. RX PubMed=33844468; DOI=10.1111/febs.15875; RA Olazabal-Herrero A., Bilbao-Arribas M., Carlevaris O., Sendino M., RA Varela-Martinez E., Jugo B.M., Berra E., Rodriguez J.A.; RT "The dystrophia myotonica WD repeat-containing protein DMWD and WDR20 RT differentially regulate USP12 deubiquitinase."; RL FEBS J. 288:5943-5963(2021). RN [17] {ECO:0007744|PDB:5K19, ECO:0007744|PDB:5K1C} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH USP12 AND WDR48, RP INTERACTION WITH USP12, FUNCTION, AND MUTAGENESIS OF PHE-262 AND TRP-306. RX PubMed=27373336; DOI=10.1016/j.molcel.2016.05.031; RA Li H., Lim K.S., Kim H., Hinds T.R., Jo U., Mao H., Weller C.E., Sun J., RA Chatterjee C., D'Andrea A.D., Zheng N.; RT "Allosteric activation of ubiquitin-specific proteases by beta-propeller RT proteins UAF1 and WDR20."; RL Mol. Cell 63:249-260(2016). CC -!- FUNCTION: Regulator of deubiquitinating complexes. Activates CC deubiquitinating activity of complexes containing USP12 CC (PubMed:20147737, PubMed:27373336). Anchors at the base of the CC ubiquitin-contacting loop of USP12 and remotely modulates the catalytic CC center of the enzyme (PubMed:27373336). Regulates shuttling of the CC USP12 deubiquitinase complex between the plasma membrane, cytoplasm and CC nucleus (PubMed:30466959). {ECO:0000269|PubMed:20147737, CC ECO:0000269|PubMed:27373336, ECO:0000269|PubMed:30466959}. CC -!- SUBUNIT: Interacts with USP12; promotes translocation of USP12/WDR20 to CC the plasma membrane (PubMed:20147737, PubMed:27373336, CC PubMed:30466959). Component of the USP12/WDR20/WDR48 deubiquitinating CC complex (PubMed:20147737, PubMed:27373336). Interacts with USP46; CC contributes to the cytoplasmic localization of the USP46/WDR20 complex CC (PubMed:20147737). Component of the USP12/DMWD/WDR48 deubiquitinating CC complex (PubMed:33844468). {ECO:0000269|PubMed:20147737, CC ECO:0000269|PubMed:27373336, ECO:0000269|PubMed:30466959, CC ECO:0000269|PubMed:33844468}. CC -!- INTERACTION: CC Q8TBZ3; Q9UN19: DAPP1; NbExp=3; IntAct=EBI-2511486, EBI-3918199; CC Q8TBZ3; O75317: USP12; NbExp=5; IntAct=EBI-2511486, EBI-2511507; CC Q8TBZ3; P62068: USP46; NbExp=6; IntAct=EBI-2511486, EBI-2512753; CC Q8TBZ3-3; P22607: FGFR3; NbExp=3; IntAct=EBI-9089370, EBI-348399; CC Q8TBZ3-3; P06396: GSN; NbExp=3; IntAct=EBI-9089370, EBI-351506; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30466959, CC ECO:0000269|PubMed:33844468}. Nucleus {ECO:0000269|PubMed:30466959, CC ECO:0000269|PubMed:33844468}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Name=1; CC IsoId=Q8TBZ3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8TBZ3-2; Sequence=VSP_024387; CC Name=3; CC IsoId=Q8TBZ3-3; Sequence=VSP_043412, VSP_043413; CC Name=4; CC IsoId=Q8TBZ3-4; Sequence=VSP_045225, VSP_045226; CC Name=5; CC IsoId=Q8TBZ3-5; Sequence=VSP_045226; CC Name=6; CC IsoId=Q8TBZ3-6; Sequence=VSP_045226, VSP_024387; CC Name=7; CC IsoId=Q8TBZ3-7; Sequence=VSP_047065; CC Name=8; CC IsoId=Q8TBZ3-8; Sequence=VSP_047064; CC -!- SEQUENCE CAUTION: CC Sequence=AAL56014.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX248274; CAD62602.1; -; mRNA. DR EMBL; AK297727; BAG60080.1; -; mRNA. DR EMBL; AL133223; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359402; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC028387; AAH28387.1; -; mRNA. DR EMBL; BC030654; AAH30654.1; -; mRNA. DR EMBL; AF327354; AAL56014.1; ALT_INIT; mRNA. DR EMBL; AL133558; CAB63713.1; -; mRNA. DR CCDS; CCDS55942.1; -. [Q8TBZ3-8] DR CCDS; CCDS55943.1; -. [Q8TBZ3-7] DR CCDS; CCDS55944.1; -. [Q8TBZ3-3] DR CCDS; CCDS55945.1; -. [Q8TBZ3-6] DR CCDS; CCDS9968.1; -. [Q8TBZ3-2] DR CCDS; CCDS9969.1; -. [Q8TBZ3-1] DR CCDS; CCDS9970.1; -. [Q8TBZ3-5] DR PIR; T43440; T43440. DR RefSeq; NP_001229343.1; NM_001242414.1. [Q8TBZ3-8] DR RefSeq; NP_001229344.1; NM_001242415.1. [Q8TBZ3-3] DR RefSeq; NP_001229345.1; NM_001242416.1. [Q8TBZ3-6] DR RefSeq; NP_001229346.1; NM_001242417.1. [Q8TBZ3-7] DR RefSeq; NP_001229347.1; NM_001242418.1. DR RefSeq; NP_653175.2; NM_144574.3. [Q8TBZ3-1] DR RefSeq; NP_851808.1; NM_181291.2. [Q8TBZ3-2] DR RefSeq; NP_851825.1; NM_181308.2. [Q8TBZ3-5] DR PDB; 5K19; X-ray; 2.60 A; A/B/C=1-569. DR PDB; 5K1C; X-ray; 3.00 A; C=1-569. DR PDB; 6JLQ; X-ray; 3.10 A; C=279-318. DR PDBsum; 5K19; -. DR PDBsum; 5K1C; -. DR PDBsum; 6JLQ; -. DR AlphaFoldDB; Q8TBZ3; -. DR SMR; Q8TBZ3; -. DR BioGRID; 124884; 89. DR CORUM; Q8TBZ3; -. DR IntAct; Q8TBZ3; 47. DR MINT; Q8TBZ3; -. DR STRING; 9606.ENSP00000395793; -. DR iPTMnet; Q8TBZ3; -. DR PhosphoSitePlus; Q8TBZ3; -. DR BioMuta; WDR20; -. DR DMDM; 143811476; -. DR EPD; Q8TBZ3; -. DR jPOST; Q8TBZ3; -. DR MassIVE; Q8TBZ3; -. DR MaxQB; Q8TBZ3; -. DR PaxDb; 9606-ENSP00000406084; -. DR PeptideAtlas; Q8TBZ3; -. DR ProteomicsDB; 18529; -. DR ProteomicsDB; 30372; -. DR ProteomicsDB; 32621; -. DR ProteomicsDB; 39351; -. DR ProteomicsDB; 74057; -. [Q8TBZ3-1] DR ProteomicsDB; 74058; -. [Q8TBZ3-2] DR ProteomicsDB; 74059; -. [Q8TBZ3-3] DR Pumba; Q8TBZ3; -. DR Antibodypedia; 134; 118 antibodies from 23 providers. DR DNASU; 91833; -. DR Ensembl; ENST00000299135.6; ENSP00000299135.6; ENSG00000140153.18. [Q8TBZ3-8] DR Ensembl; ENST00000322340.9; ENSP00000314209.5; ENSG00000140153.18. [Q8TBZ3-3] DR Ensembl; ENST00000335263.9; ENSP00000335434.5; ENSG00000140153.18. [Q8TBZ3-2] DR Ensembl; ENST00000342702.8; ENSP00000341037.3; ENSG00000140153.18. [Q8TBZ3-1] DR Ensembl; ENST00000454394.2; ENSP00000406084.2; ENSG00000140153.18. [Q8TBZ3-7] DR Ensembl; ENST00000555879.5; ENSP00000452470.1; ENSG00000140153.18. [Q8TBZ3-8] DR Ensembl; ENST00000556511.2; ENSP00000451633.2; ENSG00000140153.18. [Q8TBZ3-5] DR Ensembl; ENST00000556807.1; ENSP00000450636.1; ENSG00000140153.18. [Q8TBZ3-6] DR GeneID; 91833; -. DR KEGG; hsa:91833; -. DR MANE-Select; ENST00000342702.8; ENSP00000341037.3; NM_144574.4; NP_653175.2. DR UCSC; uc001ykz.4; human. [Q8TBZ3-1] DR AGR; HGNC:19667; -. DR CTD; 91833; -. DR DisGeNET; 91833; -. DR GeneCards; WDR20; -. DR HGNC; HGNC:19667; WDR20. DR HPA; ENSG00000140153; Low tissue specificity. DR MIM; 617741; gene. DR neXtProt; NX_Q8TBZ3; -. DR OpenTargets; ENSG00000140153; -. DR PharmGKB; PA134936678; -. DR VEuPathDB; HostDB:ENSG00000140153; -. DR eggNOG; KOG2394; Eukaryota. DR GeneTree; ENSGT00390000007686; -. DR HOGENOM; CLU_120535_0_0_1; -. DR InParanoid; Q8TBZ3; -. DR OrthoDB; 1513505at2759; -. DR PhylomeDB; Q8TBZ3; -. DR TreeFam; TF314961; -. DR PathwayCommons; Q8TBZ3; -. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR SignaLink; Q8TBZ3; -. DR BioGRID-ORCS; 91833; 36 hits in 1173 CRISPR screens. DR ChiTaRS; WDR20; human. DR GenomeRNAi; 91833; -. DR Pharos; Q8TBZ3; Tbio. DR PRO; PR:Q8TBZ3; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q8TBZ3; Protein. DR Bgee; ENSG00000140153; Expressed in secondary oocyte and 174 other cell types or tissues. DR ExpressionAtlas; Q8TBZ3; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0035800; F:deubiquitinase activator activity; IDA:UniProtKB. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR14107; WD REPEAT PROTEIN; 1. DR PANTHER; PTHR14107:SF5; WD REPEAT-CONTAINING PROTEIN 20; 1. DR Pfam; PF00400; WD40; 2. DR SMART; SM00320; WD40; 4. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q8TBZ3; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; WD repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..569 FT /note="WD repeat-containing protein 20" FT /id="PRO_0000051366" FT REPEAT 94..138 FT /note="WD 1" FT REPEAT 139..210 FT /note="WD 2" FT REPEAT 211..252 FT /note="WD 3" FT REPEAT 253..331 FT /note="WD 4" FT REPEAT 332..426 FT /note="WD 5" FT REPEAT 427..523 FT /note="WD 6" FT REPEAT 524..559 FT /note="WD 7" FT REGION 405..445 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 450..468 FT /note="Mediates XPO1-dependent nuclear export of WDR20- FT USP12 complexes" FT /evidence="ECO:0000269|PubMed:30466959" FT COMPBIAS 405..422 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 357 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 432 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 434 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 465 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..9 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_045225" FT VAR_SEQ 84..569 FT /note="AADLSKPIDKRIYKGTQPTCHDFNHLTATAESVSLLVGFSAGQVQLIDPIKK FT ETSKLFNEERLIDKSRVTCVKWVPGSESLFLVAHSSGNMYLYNVEHTCGTTAPHYQLLK FT QGESFAVHTCKSKSTRNPLLKWTVGEGALNEFAFSPDGKFLACVSQDGFLRVFNFDSVE FT LHGTMKSYFGGLLCVCWSPDGKYIVTGGEDDLVTVWSFVDCRVIARGHGHKSWVSVVAF FT DPYTTSVEEGDPMEFSGSDEDFQDLLHFGRDRANSTQSRLSKRNSTDSRPVSVTYRFGS FT VGQDTQLCLWDLTEDILFPHQPLSRARTHTNVMNATSPPAGSNGNSVTTPGNSVPPPLP FT RSNSLPHSAVSNAGSKSSVMDGAIASGVSKFATLSLHDRKERHHEKDHKRNHSMGHISS FT KSSDKLNLVTKTKTDPAKTLGTPLCPRMEDVPLLEPLICKKIAHERLTVLIFLEDCIVT FT ACQEGFICTWGRPGKVVSFNP -> TIP (in isoform 8)" FT /evidence="ECO:0000305" FT /id="VSP_047064" FT VAR_SEQ 84..144 FT /note="Missing (in isoform 4, isoform 5 and isoform 6)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_045226" FT VAR_SEQ 144 FT /note="E -> ENSCQHLWKVDWNEERQNEGSKTSEEALVTVQ (in isoform FT 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_047065" FT VAR_SEQ 145..195 FT /note="RLIDKSRVTCVKWVPGSESLFLVAHSSGNMYLYNVEHTCGTTAPHYQLLKQ FT -> NSCQHLWKVDWNEERQNEGSKTSEEALVTVQPAEHFCRQEDRMQGVLQDQN (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043412" FT VAR_SEQ 196..569 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043413" FT VAR_SEQ 565..569 FT /note="VSFNP -> GSLSSPSQASSPGGTVV (in isoform 2 and isoform FT 6)" FT /evidence="ECO:0000303|Ref.5" FT /id="VSP_024387" FT VARIANT 159 FT /note="P -> H (in dbSNP:rs17852545)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_031580" FT VARIANT 444 FT /note="G -> C (in dbSNP:rs12888595)" FT /id="VAR_053425" FT MUTAGEN 262 FT /note="F->A: Impaired binding to USP12. Does not induce FT plasma localization of USP12; when associated with A-306." FT /evidence="ECO:0000269|PubMed:27373336, FT ECO:0000269|PubMed:30466959" FT MUTAGEN 306 FT /note="W->A: Impaired binding to USP12. Does not induce FT plasma localization of USP12; when associated with A-262." FT /evidence="ECO:0000269|PubMed:27373336, FT ECO:0000269|PubMed:30466959" FT MUTAGEN 464 FT /note="L->A: Induces partial relocation of WDR20 from the FT cytoplasm to the nucleus; when associated with A-466." FT /evidence="ECO:0000269|PubMed:30466959" FT MUTAGEN 466 FT /note="L->A: Induces partial relocation of WDR20 from the FT cytoplasm to the nucleus; when associated with A-464." FT /evidence="ECO:0000269|PubMed:30466959" FT CONFLICT 195 FT /note="Q -> H (in Ref. 5; AAL56014)" FT /evidence="ECO:0000305" FT CONFLICT 299 FT /note="R -> K (in Ref. 5; AAL56014)" FT /evidence="ECO:0000305" FT CONFLICT 337 FT /note="L -> P (in Ref. 2; BAG60080)" FT /evidence="ECO:0000305" FT CONFLICT 353 FT /note="S -> P (in Ref. 2; BAG60080)" FT /evidence="ECO:0000305" FT CONFLICT 474 FT /note="H -> L (in Ref. 6; CAB63713)" FT /evidence="ECO:0000305" FT STRAND 15..19 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 22..26 FT /evidence="ECO:0007829|PDB:5K19" FT HELIX 28..30 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:5K1C" FT STRAND 63..68 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 70..77 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 91..95 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 101..106 FT /evidence="ECO:0007829|PDB:5K19" FT TURN 108..110 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 118..122 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 127..130 FT /evidence="ECO:0007829|PDB:5K19" FT TURN 132..134 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 138..142 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 152..157 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 162..169 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 172..178 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 190..196 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 199..204 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 210..221 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 223..228 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 232..239 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 242..248 FT /evidence="ECO:0007829|PDB:5K19" FT TURN 249..252 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 253..259 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 265..270 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 274..281 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 286..290 FT /evidence="ECO:0007829|PDB:5K19" FT TURN 291..293 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 295..300 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 307..312 FT /evidence="ECO:0007829|PDB:5K19" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:5K1C" FT STRAND 366..373 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 376..384 FT /evidence="ECO:0007829|PDB:5K19" FT HELIX 385..388 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 512..514 FT /evidence="ECO:0007829|PDB:5K1C" FT TURN 517..519 FT /evidence="ECO:0007829|PDB:5K1C" FT STRAND 526..530 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 536..541 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 543..550 FT /evidence="ECO:0007829|PDB:5K19" FT STRAND 555..559 FT /evidence="ECO:0007829|PDB:5K19" SQ SEQUENCE 569 AA; 62893 MW; 5779A68D94C34CAF CRC64; MATEGGGKEM NEIKTQFTTR EGLYKLLPHS EYSRPNRVPF NSQGSNPVRV SFVNLNDQSG NGDRLCFNVG RELYFYIYKG VRKAADLSKP IDKRIYKGTQ PTCHDFNHLT ATAESVSLLV GFSAGQVQLI DPIKKETSKL FNEERLIDKS RVTCVKWVPG SESLFLVAHS SGNMYLYNVE HTCGTTAPHY QLLKQGESFA VHTCKSKSTR NPLLKWTVGE GALNEFAFSP DGKFLACVSQ DGFLRVFNFD SVELHGTMKS YFGGLLCVCW SPDGKYIVTG GEDDLVTVWS FVDCRVIARG HGHKSWVSVV AFDPYTTSVE EGDPMEFSGS DEDFQDLLHF GRDRANSTQS RLSKRNSTDS RPVSVTYRFG SVGQDTQLCL WDLTEDILFP HQPLSRARTH TNVMNATSPP AGSNGNSVTT PGNSVPPPLP RSNSLPHSAV SNAGSKSSVM DGAIASGVSK FATLSLHDRK ERHHEKDHKR NHSMGHISSK SSDKLNLVTK TKTDPAKTLG TPLCPRMEDV PLLEPLICKK IAHERLTVLI FLEDCIVTAC QEGFICTWGR PGKVVSFNP //