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 27-MAR-2024, entry version 188.
DE RecName: Full=WD repeat-containing protein 75;
DE AltName: Full=U3 small nucleolar RNA-associated protein 17 homolog;
GN Name=WDR75 {ECO:0000312|HGNC:HGNC:25725}; 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).
RN [20] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=34516797; DOI=10.1126/science.abj5338;
RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.;
RT "Nucleolar maturation of the human small subunit processome.";
RL Science 373:eabj5338-eabj5338(2021).
CC -!- FUNCTION: Ribosome biogenesis factor. Part of the small subunit (SSU)
CC processome, first precursor of the small eukaryotic ribosomal subunit.
CC During the assembly of the SSU processome in the nucleolus, many
CC ribosome biogenesis factors, an RNA chaperone and ribosomal proteins
CC associate with the nascent pre-rRNA and work in concert to generate RNA
CC folding, modifications, rearrangements and cleavage as well as targeted
CC degradation of pre-ribosomal RNA by the RNA exosome. Involved in
CC nucleolar processing of pre-18S ribosomal RNA. Required for optimal
CC pre-ribosomal RNA transcription by RNA polymerase I.
CC {ECO:0000269|PubMed:17699751, ECO:0000269|PubMed:34516797}.
CC -!- SUBUNIT: Component of the proposed t-UTP subcomplex of the ribosomal
CC small subunit (SSU) processome. SSU processome is composed of more than
CC 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3
CC (PubMed:17699751, PubMed:22916032). {ECO:0000269|PubMed:34516797,
CC ECO:0000305|PubMed:17699751, ECO:0000305|PubMed:22916032}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:22916032, ECO:0000269|PubMed:34516797}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14503.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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 EMDB; EMD-23936; -.
DR EMDB; EMD-23937; -.
DR EMDB; EMD-23938; -.
DR SMR; Q8IWA0; -.
DR BioGRID; 123901; 99.
DR ComplexPortal; CPX-2450; UTP-A complex.
DR IntAct; Q8IWA0; 29.
DR MINT; Q8IWA0; -.
DR STRING; 9606.ENSP00000314193; -.
DR GlyCosmos; Q8IWA0; 1 site, 1 glycan.
DR GlyGen; Q8IWA0; 2 sites, 1 O-linked glycan (2 sites).
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; 9606-ENSP00000314193; -.
DR PeptideAtlas; Q8IWA0; -.
DR ProteomicsDB; 70825; -.
DR Pumba; Q8IWA0; -.
DR Antibodypedia; 52112; 26 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 AGR; HGNC:25725; -.
DR CTD; 84128; -.
DR DisGeNET; 84128; -.
DR GeneCards; WDR75; -.
DR HGNC; HGNC:25725; WDR75.
DR HPA; ENSG00000115368; Low tissue specificity.
DR MIM; 620341; gene.
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; 927410at2759; -.
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; 820 hits in 1165 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 190 other cell types or 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:0032040; C:small-subunit processome; IDA:UniProtKB.
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:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR44215; WD REPEAT-CONTAINING PROTEIN 75; 1.
DR PANTHER; PTHR44215:SF1; WD REPEAT-CONTAINING PROTEIN 75; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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
//
