WDR75_HUMAN
ID WDR75_HUMAN Reviewed; 830 AA.
AC Q8IWA0; Q96J10; Q9H8U8; Q9H9U5; Q9H9V8; Q9UIX2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=WD repeat-containing protein 75;
DE AltName: Full=U3 small nucleolar RNA-associated protein 17 homolog;
GN Name=WDR75; Synonyms=UTP17;
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].
RC TISSUE=Retina, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-782.
RC TISSUE=Teratocarcinoma;
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 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-779 AND SER-782, AND
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17699751; DOI=10.1101/gad.436707;
RA Prieto J.L., McStay B.;
RT "Recruitment of factors linking transcription and processing of pre-rRNA to
RT NOR chromatin is UBF-dependent and occurs independent of transcription in
RT human cells.";
RL Genes Dev. 21:2041-2054(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-779; SER-782; SER-796 AND
RP SER-811, AND 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 [10]
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 [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-466, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-796, AND IDENTIFICATION BY
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782 AND SER-796, AND
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 [15]
RP POSSIBLE ASSOCIATION IN THE SSU PROCESSOME T-UTP SUBCOMPLEX.
RX PubMed=22916032; DOI=10.1371/journal.pgen.1002892;
RA Freed E.F., Prieto J.L., McCann K.L., McStay B., Baserga S.J.;
RT "NOL11, implicated in the pathogenesis of North American Indian childhood
RT cirrhosis, is required for pre-rRNA transcription and processing.";
RL PLoS Genet. 8:E1002892-E1002892(2012).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; SER-672; SER-796 AND
RP SER-811, 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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-427, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-427 AND LYS-676, 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 -!- FUNCTION: Ribosome biogenesis factor. Involved in nucleolar processing
CC of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA
CC transcription by RNA polymerase I. {ECO:0000269|PubMed:17699751}.
CC -!- SUBUNIT: May be a component of the proposed t-UTP subcomplex of the
CC ribosomal small subunit (SSU) processome containing at least UTP4,
CC WDR43, HEATR1, UTP15, WDR75 (PubMed:17699751, PubMed:22916032).
CC {ECO:0000305|PubMed:17699751, ECO:0000305|PubMed:22916032}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:22916032}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14503.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL122097; CAB59265.1; -; mRNA.
DR EMBL; CR749440; CAH18278.1; -; mRNA.
DR EMBL; AC013439; AAX93081.1; -; Genomic_DNA.
DR EMBL; BC040567; AAH40567.1; -; mRNA.
DR EMBL; BC006816; AAH06816.1; -; mRNA.
DR EMBL; AK022581; BAB14111.1; -; mRNA.
DR EMBL; AK022607; BAB14126.1; -; mRNA.
DR EMBL; AK023276; BAB14503.1; ALT_INIT; mRNA.
DR CCDS; CCDS2298.1; -.
DR PIR; T34531; T34531.
DR RefSeq; NP_001290025.1; NM_001303096.1.
DR RefSeq; NP_115544.1; NM_032168.2.
DR PDB; 7MQ8; EM; 3.60 A; LH=1-830.
DR PDB; 7MQ9; EM; 3.87 A; LH=1-830.
DR PDB; 7MQA; EM; 2.70 A; LH=1-830.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; Q8IWA0; -.
DR SMR; Q8IWA0; -.
DR BioGRID; 123901; 84.
DR IntAct; Q8IWA0; 26.
DR MINT; Q8IWA0; -.
DR STRING; 9606.ENSP00000314193; -.
DR GlyGen; Q8IWA0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IWA0; -.
DR PhosphoSitePlus; Q8IWA0; -.
DR SwissPalm; Q8IWA0; -.
DR BioMuta; WDR75; -.
DR DMDM; 73622083; -.
DR SWISS-2DPAGE; Q8IWA0; -.
DR EPD; Q8IWA0; -.
DR jPOST; Q8IWA0; -.
DR MassIVE; Q8IWA0; -.
DR MaxQB; Q8IWA0; -.
DR PaxDb; Q8IWA0; -.
DR PeptideAtlas; Q8IWA0; -.
DR PRIDE; Q8IWA0; -.
DR ProteomicsDB; 70825; -.
DR Antibodypedia; 52112; 24 antibodies from 12 providers.
DR DNASU; 84128; -.
DR Ensembl; ENST00000314761.9; ENSP00000314193.4; ENSG00000115368.10.
DR GeneID; 84128; -.
DR KEGG; hsa:84128; -.
DR MANE-Select; ENST00000314761.9; ENSP00000314193.4; NM_032168.3; NP_115544.1.
DR UCSC; uc002uql.2; human.
DR CTD; 84128; -.
DR DisGeNET; 84128; -.
DR GeneCards; WDR75; -.
DR HGNC; HGNC:25725; WDR75.
DR HPA; ENSG00000115368; Low tissue specificity.
DR neXtProt; NX_Q8IWA0; -.
DR OpenTargets; ENSG00000115368; -.
DR PharmGKB; PA142670579; -.
DR VEuPathDB; HostDB:ENSG00000115368; -.
DR eggNOG; KOG1963; Eukaryota.
DR GeneTree; ENSGT00390000006303; -.
DR HOGENOM; CLU_005417_2_0_1; -.
DR InParanoid; Q8IWA0; -.
DR OMA; WILNTRI; -.
DR OrthoDB; 1437651at2759; -.
DR PhylomeDB; Q8IWA0; -.
DR TreeFam; TF323469; -.
DR PathwayCommons; Q8IWA0; -.
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; Q8IWA0; -.
DR BioGRID-ORCS; 84128; 783 hits in 1087 CRISPR screens.
DR ChiTaRS; WDR75; human.
DR GenomeRNAi; 84128; -.
DR Pharos; Q8IWA0; Tbio.
DR PRO; PR:Q8IWA0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8IWA0; protein.
DR Bgee; ENSG00000115368; Expressed in upper arm skin and 188 other tissues.
DR ExpressionAtlas; Q8IWA0; baseline and differential.
DR Genevisible; Q8IWA0; HS.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:2000234; P:positive regulation of rRNA processing; IMP:UniProtKB.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribosome biogenesis; rRNA processing;
KW Transcription; Transcription regulation; Ubl conjugation; WD repeat.
FT CHAIN 1..830
FT /note="WD repeat-containing protein 75"
FT /id="PRO_0000051430"
FT REPEAT 4..43
FT /note="WD 1"
FT REPEAT 47..86
FT /note="WD 2"
FT REPEAT 90..131
FT /note="WD 3"
FT REPEAT 145..184
FT /note="WD 4"
FT REPEAT 193..231
FT /note="WD 5"
FT REPEAT 237..276
FT /note="WD 6"
FT REPEAT 279..318
FT /note="WD 7"
FT REPEAT 324..362
FT /note="WD 8"
FT REPEAT 376..423
FT /note="WD 9"
FT REPEAT 430..474
FT /note="WD 10"
FT REPEAT 487..525
FT /note="WD 11"
FT REPEAT 529..569
FT /note="WD 12"
FT REPEAT 574..611
FT /note="WD 13"
FT REGION 763..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..788
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 466
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692"
FT MOD_RES 796
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 811
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 427
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 676
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 116
FT /note="F -> L (in Ref. 4; BAB14503)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="D -> N (in Ref. 4; BAB14111)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="M -> T (in Ref. 4; BAB14111)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="T -> I (in Ref. 4; BAB14503)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="A -> T (in Ref. 4; BAB14111)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="S -> T (in Ref. 4; BAB14126)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="L -> H (in Ref. 4; BAB14126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 830 AA; 94499 MW; AE2A3C2C156C0939 CRC64;
MVEEENIRVV RCGGSELNFR RAVFSADSKY IFCVSGDFVK VYSTVTEECV HILHGHRNLV
TGIQLNPNNH LQLYSCSLDG TIKLWDYIDG ILIKTFIVGC KLHALFTLAQ AEDSVFVIVN
KEKPDIFQLV SVKLPKSSSQ EVEAKELSFV LDYINQSPKC IAFGNEGVYV AAVREFYLSV
YFFKKKTTSR FTLSSSRNKK HAKNNFTCVA CHPTEDCIAS GHMDGKIRLW RNFYDDKKYT
YTCLHWHHDM VMDLAFSVTG TSLLSGGRES VLVEWRDATE KNKEFLPRLG ATIEHISVSP
AGDLFCTSHS DNKIIIIHRN LEASAVIQGL VKDRSIFTGL MIDPRTKALV LNGKPGHLQF
YSLQSDKQLY NLDIIQQEYI NDYGLIQIEL TKAAFGCFGN WLATVEQRQE KETELELQMK
LWMYNKKTQG FILNTKINMP HEDCITALCF CNAEKSEQPT LVTASKDGYF KVWILTDDSD
IYKKAVGWTC DFVGSYHKYQ ATNCCFSEDG SLLAVSFEEI VTIWDSVTWE LKCTFCQRAG
KIRHLCFGRL TCSKYLLGAT ENGILCCWNL LSCALEWNAK LNVRVMEPDP NSENIAAISQ
SSVGSDLFVF KPSEPRPLYI QKGISREKVQ WGVFVPRDVP ESFTSEAYQW LNRSQFYFLT
KSQSLLTFST KSPEEKLTPT SKQLLAEESL PTTPFYFILG KHRQQQDEKL NETLENELVQ
LPLTENIPAI SELLHTPAHV LPSAAFLCSM FVNSLLLSKE TKSAKEIPED VDMEEEKESE
DSDEENDFTE KVQDTSNTGL GEDIIHQLSK SEEKELRKFR KIDYSWIAAL
