GenomeNet

Database: UniProt
Entry: Q8TBZ3
LinkDB: Q8TBZ3
Original site: Q8TBZ3 
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   29-SEP-2021, entry version 165.
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] {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). {ECO:0000269|PubMed:20147737,
CC       ECO:0000269|PubMed:27373336}.
CC   -!- SUBUNIT: Interacts with USP12 (PubMed:20147737, PubMed:27373336).
CC       Component of the USP12/WDR20/WDR48 deubiquitinating complex
CC       (PubMed:20147737, PubMed:27373336). Interacts with USP46
CC       (PubMed:20147737). {ECO:0000269|PubMed:20147737,
CC       ECO:0000269|PubMed:27373336}.
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   -!- 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};
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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   SMR; Q8TBZ3; -.
DR   BioGRID; 124884; 65.
DR   CORUM; Q8TBZ3; -.
DR   IntAct; Q8TBZ3; 40.
DR   MINT; Q8TBZ3; -.
DR   STRING; 9606.ENSP00000406084; -.
DR   iPTMnet; Q8TBZ3; -.
DR   PhosphoSitePlus; Q8TBZ3; -.
DR   BioMuta; WDR20; -.
DR   DMDM; 143811476; -.
DR   jPOST; Q8TBZ3; -.
DR   MassIVE; Q8TBZ3; -.
DR   MaxQB; Q8TBZ3; -.
DR   PeptideAtlas; Q8TBZ3; -.
DR   PRIDE; 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   Antibodypedia; 134; 103 antibodies.
DR   DNASU; 91833; -.
DR   Ensembl; ENST00000299135; ENSP00000299135; ENSG00000140153. [Q8TBZ3-8]
DR   Ensembl; ENST00000322340; ENSP00000314209; ENSG00000140153. [Q8TBZ3-3]
DR   Ensembl; ENST00000335263; ENSP00000335434; ENSG00000140153. [Q8TBZ3-2]
DR   Ensembl; ENST00000342702; ENSP00000341037; ENSG00000140153. [Q8TBZ3-1]
DR   Ensembl; ENST00000454394; ENSP00000406084; ENSG00000140153. [Q8TBZ3-7]
DR   Ensembl; ENST00000555879; ENSP00000452470; ENSG00000140153. [Q8TBZ3-8]
DR   Ensembl; ENST00000556511; ENSP00000451633; ENSG00000140153. [Q8TBZ3-5]
DR   Ensembl; ENST00000556807; ENSP00000450636; ENSG00000140153. [Q8TBZ3-6]
DR   GeneID; 91833; -.
DR   KEGG; hsa:91833; -.
DR   UCSC; uc001ykz.4; human. [Q8TBZ3-1]
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; 907634at2759; -.
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; 28 hits in 1031 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 205 other tissues.
DR   ExpressionAtlas; Q8TBZ3; baseline and differential.
DR   Genevisible; Q8TBZ3; HS.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Phosphoprotein;
KW   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   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."
FT                   /evidence="ECO:0000269|PubMed:27373336"
FT   MUTAGEN         306
FT                   /note="W->A: Impaired binding to USP12."
FT                   /evidence="ECO:0000269|PubMed:27373336"
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
//
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