WDR20_HUMAN
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 03-AUG-2022, entry version 168.
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 AlphaFoldDB; Q8TBZ3; -.
DR SMR; Q8TBZ3; -.
DR BioGRID; 124884; 81.
DR CORUM; Q8TBZ3; -.
DR IntAct; Q8TBZ3; 45.
DR MINT; Q8TBZ3; -.
DR STRING; 9606.ENSP00000406084; -.
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 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; 110 antibodies from 22 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 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; 34 hits in 1095 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 172 other tissues.
DR ExpressionAtlas; Q8TBZ3; baseline and differential.
DR Genevisible; Q8TBZ3; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
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
