NOP58_HUMAN
ID NOP58_HUMAN Reviewed; 529 AA.
AC Q9Y2X3; Q53SA4; Q6PK08; Q9P036; Q9UFN3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Nucleolar protein 58 {ECO:0000305};
DE AltName: Full=Nucleolar protein 5;
GN Name=NOP58 {ECO:0000312|HGNC:HGNC:29926}; Synonyms=NOL5, NOP5;
GN ORFNames=HSPC120;
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 [MRNA], SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10606270; DOI=10.1017/s1355838299991288;
RA Lyman S.K., Gerace L., Baserga S.J.;
RT "Human Nop5/Nop58 is a component common to the box C/D small nucleolar
RT ribonucleoproteins.";
RL RNA 5:1597-1604(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10925205; DOI=10.1016/s0378-1119(00)00232-8;
RA Nelson S.A., Santora K.E., LaRochelle W.J.;
RT "Isolation and characterization of a novel PDGF-induced human gene.";
RL Gene 253:87-93(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and Uterus;
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 [LARGE SCALE MRNA] OF 1-442.
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-529.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [7]
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 [8]
RP ASSOCIATION WITH U14 BOX C/D SNORNA.
RX PubMed=12417735; DOI=10.1128/mcb.22.23.8342-8352.2002;
RA Watkins N.J., Dickmanns A., Luhrmann R.;
RT "Conserved stem II of the box C/D motif is essential for nucleolar
RT localization and is required, along with the 15.5K protein, for the
RT hierarchical assembly of the box C/D snoRNP.";
RL Mol. Cell. Biol. 22:8342-8352(2002).
RN [9]
RP FUNCTION IN BOX C/D SNORNA BIOGENESIS, AND ASSOCIATION WITH U3 BOX C/D
RP SNORNA.
RX PubMed=15574333; DOI=10.1016/j.molcel.2004.11.012;
RA Watkins N.J., Lemm I., Ingelfinger D., Schneider C., Hossbach M.,
RA Urlaub H., Luehrmann R.;
RT "Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large
RT dynamic multiprotein complex.";
RL Mol. Cell 16:789-798(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-514, 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 [11]
RP FUNCTION IN U3 BOX C/D SNORNA BIOGENESIS, ASSOCIATION WITH U8 BOX C/D
RP SNORNA, AND INTERACTION WITH NUFIP1 AND PIH1D1.
RX PubMed=17636026; DOI=10.1128/mcb.01097-07;
RA McKeegan K.S., Debieux C.M., Boulon S., Bertrand E., Watkins N.J.;
RT "A dynamic scaffold of pre-snoRNP factors facilitates human box C/D snoRNP
RT assembly.";
RL Mol. Cell. Biol. 27:6782-6793(2007).
RN [12]
RP ASSOCIATION WITH U8 BOX C/D SNORNP COMPLEX.
RX PubMed=17709390; DOI=10.1128/mcb.00516-07;
RA Watkins N.J., Lemm I., Luhrmann R.;
RT "Involvement of nuclear import and export factors in U8 box C/D snoRNP
RT biogenesis.";
RL Mol. Cell. Biol. 27:7018-7027(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-514, AND
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; SER-502 AND SER-514, 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 [16]
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 [17]
RP FUNCTION IN U3 AND U8 BOX C/D SNORNA BIOGENESIS, AND INTERACTION WITH
RP RUVBL1 AND RUVBL2.
RX PubMed=19620283; DOI=10.1128/mcb.00752-09;
RA McKeegan K.S., Debieux C.M., Watkins N.J.;
RT "Evidence that the AAA+ proteins TIP48 and TIP49 bridge interactions
RT between 15.5K and the related NOP56 and NOP58 proteins during box C/D
RT snoRNP biogenesis.";
RL Mol. Cell. Biol. 29:4971-4981(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-514, AND
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 [19]
RP SUMOYLATION AT LYS-467 AND LYS-497.
RX PubMed=20797632; DOI=10.1016/j.molcel.2010.07.025;
RA Westman B.J., Verheggen C., Hutten S., Lam Y.W., Bertrand E., Lamond A.I.;
RT "A proteomic screen for nucleolar SUMO targets shows SUMOylation modulates
RT the function of Nop5/Nop58.";
RL Mol. Cell 39:618-631(2010).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; SER-483; SER-502 AND
RP SER-514, AND 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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-514, 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34; SER-109; SER-304;
RP SER-351; SER-502 AND SER-514, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND IDENTIFICATION BY
RP 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 [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-415; LYS-467 AND LYS-497, AND
RP IDENTIFICATION BY MASS 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 [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-465 AND LYS-467, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-467, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-467 AND LYS-497, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-157; LYS-353; LYS-411; LYS-422;
RP LYS-426; LYS-441; LYS-444; LYS-465; LYS-467; LYS-485 AND LYS-497, 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 [30]
RP INTERACTION WITH NOPCHAP1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ALA-283
RP AND 310-LYS--ALA-313.
RX PubMed=33367824; DOI=10.1093/nar/gkaa1226;
RA Abel Y., Paiva A.C.F., Bizarro J., Chagot M.E., Santo P.E., Robert M.C.,
RA Quinternet M., Vandermoere F., Sousa P.M.F., Fort P., Charpentier B.,
RA Manival X., Bandeiras T.M., Bertrand E., Verheggen C.;
RT "NOPCHAP1 is a PAQosome cofactor that helps loading NOP58 on RUVBL1/2
RT during box C/D snoRNP biogenesis.";
RL Nucleic Acids Res. 49:1094-1113(2021).
CC -!- FUNCTION: Required for 60S ribosomal subunit biogenesis (By
CC similarity). Core component of box C/D small nucleolar
CC ribonucleoprotein (snoRNP) particles. Required for the biogenesis of
CC box C/D snoRNAs such as U3, U8 and U14 snoRNAs. {ECO:0000250,
CC ECO:0000269|PubMed:15574333, ECO:0000269|PubMed:17636026,
CC ECO:0000269|PubMed:19620283}.
CC -!- SUBUNIT: Core component of box C/D small nucleolar ribonucleoprotein
CC (snoRNP) particles; the core proteins SNU13, NOP56, NOP58 and FBL
CC assemble stepwise onto the snoRNA. Interacts with NOLC1/Nopp140.
CC Interacts with NOPCHAP1, NUFIP1, RUVBL1 and RUVBL2; NOPCHAP1 bridges
CC the association of NOP58 with RUVBL1:RUVBL2 and NUFIP1
CC (PubMed:33367824). Interacts with PIH1D1 (PubMed:17636026).
CC {ECO:0000269|PubMed:10606270, ECO:0000269|PubMed:17636026,
CC ECO:0000269|PubMed:19620283, ECO:0000269|PubMed:33367824}.
CC -!- INTERACTION:
CC Q9Y2X3; Q96RS0: TGS1; NbExp=2; IntAct=EBI-395469, EBI-949244;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:33367824}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:33367824}. Note=Localizes to
CC the nucleolus with a minor part present in the nucleoplasm.
CC {ECO:0000269|PubMed:33367824}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Sumoylation is essential for high-affinity binding to snoRNAs.
CC {ECO:0000269|PubMed:20797632}.
CC -!- SIMILARITY: Belongs to the NOP5/NOP56 family. {ECO:0000305}.
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DR EMBL; AF123534; AAD27610.1; -; mRNA.
DR EMBL; AF263608; AAF91394.1; -; mRNA.
DR EMBL; AC064836; AAY24145.1; -; Genomic_DNA.
DR EMBL; BC032592; AAH32592.1; -; mRNA.
DR EMBL; BC009306; AAH09306.1; -; mRNA.
DR EMBL; AL117554; CAB55989.2; -; mRNA.
DR EMBL; AF161469; AAF29084.1; -; mRNA.
DR CCDS; CCDS2353.1; -.
DR PIR; T17299; T17299.
DR RefSeq; NP_057018.1; NM_015934.4.
DR PDB; 7MQ8; EM; 3.60 A; SB=1-529.
DR PDB; 7MQ9; EM; 3.87 A; SB=1-529.
DR PDB; 7MQA; EM; 2.70 A; SB=1-529.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; Q9Y2X3; -.
DR SMR; Q9Y2X3; -.
DR BioGRID; 119631; 257.
DR CORUM; Q9Y2X3; -.
DR DIP; DIP-32926N; -.
DR IntAct; Q9Y2X3; 88.
DR MINT; Q9Y2X3; -.
DR STRING; 9606.ENSP00000264279; -.
DR GlyGen; Q9Y2X3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2X3; -.
DR MetOSite; Q9Y2X3; -.
DR PhosphoSitePlus; Q9Y2X3; -.
DR SwissPalm; Q9Y2X3; -.
DR BioMuta; NOP58; -.
DR DMDM; 17380155; -.
DR SWISS-2DPAGE; Q9Y2X3; -.
DR EPD; Q9Y2X3; -.
DR jPOST; Q9Y2X3; -.
DR MassIVE; Q9Y2X3; -.
DR MaxQB; Q9Y2X3; -.
DR PaxDb; Q9Y2X3; -.
DR PeptideAtlas; Q9Y2X3; -.
DR PRIDE; Q9Y2X3; -.
DR ProteomicsDB; 85927; -.
DR Antibodypedia; 19944; 162 antibodies from 26 providers.
DR DNASU; 51602; -.
DR Ensembl; ENST00000264279.10; ENSP00000264279.5; ENSG00000055044.11.
DR GeneID; 51602; -.
DR KEGG; hsa:51602; -.
DR MANE-Select; ENST00000264279.10; ENSP00000264279.5; NM_015934.5; NP_057018.1.
DR UCSC; uc002uzb.4; human.
DR CTD; 51602; -.
DR DisGeNET; 51602; -.
DR GeneCards; NOP58; -.
DR HGNC; HGNC:29926; NOP58.
DR HPA; ENSG00000055044; Low tissue specificity.
DR MIM; 616742; gene.
DR neXtProt; NX_Q9Y2X3; -.
DR OpenTargets; ENSG00000055044; -.
DR PharmGKB; PA164724092; -.
DR VEuPathDB; HostDB:ENSG00000055044; -.
DR eggNOG; KOG2572; Eukaryota.
DR GeneTree; ENSGT00940000153534; -.
DR HOGENOM; CLU_015495_5_2_1; -.
DR InParanoid; Q9Y2X3; -.
DR OMA; MGMRSNW; -.
DR OrthoDB; 632707at2759; -.
DR PhylomeDB; Q9Y2X3; -.
DR TreeFam; TF105688; -.
DR PathwayCommons; Q9Y2X3; -.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
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; Q9Y2X3; -.
DR BioGRID-ORCS; 51602; 786 hits in 1056 CRISPR screens.
DR ChiTaRS; NOP58; human.
DR GeneWiki; NOP5/NOP58; -.
DR GenomeRNAi; 51602; -.
DR Pharos; Q9Y2X3; Tbio.
DR PRO; PR:Q9Y2X3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y2X3; protein.
DR Bgee; ENSG00000055044; Expressed in epithelial cell of pancreas and 187 other tissues.
DR ExpressionAtlas; Q9Y2X3; baseline and differential.
DR Genevisible; Q9Y2X3; HS.
DR GO; GO:0031428; C:box C/D RNP complex; IDA:UniProtKB.
DR GO; GO:0015030; C:Cajal body; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0070761; C:pre-snoRNP complex; IDA:BHF-UCL.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IDA:BHF-UCL.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030515; F:snoRNA binding; IDA:BHF-UCL.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IPI:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; TAS:UniProtKB.
DR GO; GO:0048254; P:snoRNA localization; IMP:UniProtKB.
DR Gene3D; 1.10.246.90; -; 1.
DR InterPro; IPR045056; Nop56/Nop58.
DR InterPro; IPR012974; NOP5_N.
DR InterPro; IPR042239; Nop_C.
DR InterPro; IPR002687; Nop_dom.
DR InterPro; IPR036070; Nop_dom_sf.
DR InterPro; IPR012976; NOSIC.
DR PANTHER; PTHR10894; PTHR10894; 1.
DR Pfam; PF01798; Nop; 1.
DR Pfam; PF08156; NOP5NT; 1.
DR SMART; SM00931; NOSIC; 1.
DR SUPFAM; SSF89124; SSF89124; 1.
DR PROSITE; PS51358; NOP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosome biogenesis; Ubl conjugation.
FT CHAIN 1..529
FT /note="Nucleolar protein 58"
FT /id="PRO_0000219023"
FT DOMAIN 282..400
FT /note="Nop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00690"
FT REGION 155..400
FT /note="Sufficient for interaction with NOPCHAP1"
FT /evidence="ECO:0000269|PubMed:33367824"
FT REGION 409..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 411
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 415
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 426
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 441
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 467
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 485
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 497
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 497
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT VARIANT 387
FT /note="N -> T (in dbSNP:rs34748654)"
FT /id="VAR_059461"
FT VARIANT 389
FT /note="A -> P (in dbSNP:rs34458926)"
FT /id="VAR_059462"
FT VARIANT 400
FT /note="D -> A (in dbSNP:rs35900977)"
FT /id="VAR_059463"
FT VARIANT 508
FT /note="T -> P (in dbSNP:rs34523815)"
FT /id="VAR_059464"
FT MUTAGEN 283
FT /note="A->P: Restricted to nucleoplasm. Abolishes
FT interaction with NOPCHAP1."
FT /evidence="ECO:0000269|PubMed:33367824"
FT MUTAGEN 310..313
FT /note="KHAA->AHAR: Restricted to nucleoplasm. Decreases
FT interaction with NOPCHAP1."
FT /evidence="ECO:0000269|PubMed:33367824"
FT CONFLICT 2
FT /note="L -> M (in Ref. 5; CAB55989)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="G -> V (in Ref. 5; CAB55989)"
FT /evidence="ECO:0000305"
FT CONFLICT 202..221
FT /note="LTYCKCLQKVGDRKNYASAK -> YHTASVYRKLAIGRLCLCQ (in Ref.
FT 6; AAF29084)"
FT /evidence="ECO:0000305"
FT CONFLICT 235..260
FT /note="KAAAEISMGTEVSEEDICNILHLCTQ -> EGSCRDIHGNRGFRRRYLQYSA
FT SLHP (in Ref. 6; AAF29084)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="M -> V (in Ref. 5; CAB55989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 529 AA; 59578 MW; 27CD73CFF5B9A556 CRC64;
MLVLFETSVG YAIFKVLNEK KLQEVDSLWK EFETPEKANK IVKLKHFEKF QDTAEALAAF
TALMEGKINK QLKKVLKKIV KEAHEPLAVA DAKLGGVIKE KLNLSCIHSP VVNELMRGIR
SQMDGLIPGV EPREMAAMCL GLAHSLSRYR LKFSADKVDT MIVQAISLLD DLDKELNNYI
MRCREWYGWH FPELGKIISD NLTYCKCLQK VGDRKNYASA KLSELLPEEV EAEVKAAAEI
SMGTEVSEED ICNILHLCTQ VIEISEYRTQ LYEYLQNRMM AIAPNVTVMV GELVGARLIA
HAGSLLNLAK HAASTVQILG AEKALFRALK SRRDTPKYGL IYHASLVGQT SPKHKGKISR
MLAAKTVLAI RYDAFGEDSS SAMGVENRAK LEARLRTLED RGIRKISGTG KALAKTEKYE
HKSEVKTYDP SGDSTLPTCS KKRKIEQVDK EDEITEKKAK KAKIKVKVEE EEEEKVAEEE
ETSVKKKKKR GKKKHIKEEP LSEEEPCTST AIASPEKKKK KKKKRENED
