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 27-MAR-2024, entry version 211. 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). RN [31] {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: Required for 60S ribosomal subunit biogenesis. Core component CC of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. CC Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 CC snoRNAs. Part of the small subunit (SSU) processome, first precursor of CC the small eukaryotic ribosomal subunit. During the assembly of the SSU CC processome in the nucleolus, many ribosome biogenesis factors, an RNA CC chaperone and ribosomal proteins associate with the nascent pre-rRNA CC and work in concert to generate RNA folding, modifications, CC rearrangements and cleavage as well as targeted degradation of pre- CC ribosomal RNA by the RNA exosome (PubMed:34516797). CC {ECO:0000269|PubMed:15574333, ECO:0000269|PubMed:17636026, CC ECO:0000269|PubMed:19620283, ECO:0000269|PubMed:34516797}. 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). Part of the CC small subunit (SSU) processome, composed of more than 70 proteins and CC the RNA chaperone small nucleolar RNA (snoRNA) U3 (PubMed:34516797). CC {ECO:0000269|PubMed:10606270, ECO:0000269|PubMed:17636026, CC ECO:0000269|PubMed:19620283, ECO:0000269|PubMed:33367824, CC ECO:0000269|PubMed:34516797}. CC -!- INTERACTION: CC Q9Y2X3; Q96RS0: TGS1; NbExp=2; IntAct=EBI-395469, EBI-949244; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:33367824, CC ECO:0000269|PubMed:34516797}. Nucleus, nucleoplasm CC {ECO:0000269|PubMed:33367824}. Note=Localizes to the nucleolus with a CC minor part present in the nucleoplasm. {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-23936; -. DR EMDB; EMD-23937; -. DR EMDB; EMD-23938; -. DR SMR; Q9Y2X3; -. DR BioGRID; 119631; 301. DR ComplexPortal; CPX-2511; Small ribosomal subunit processome. DR CORUM; Q9Y2X3; -. DR DIP; DIP-32926N; -. DR IntAct; Q9Y2X3; 94. 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 EPD; Q9Y2X3; -. DR jPOST; Q9Y2X3; -. DR MassIVE; Q9Y2X3; -. DR MaxQB; Q9Y2X3; -. DR PaxDb; 9606-ENSP00000264279; -. DR PeptideAtlas; Q9Y2X3; -. DR ProteomicsDB; 85927; -. DR Pumba; Q9Y2X3; -. DR Antibodypedia; 19944; 194 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 AGR; HGNC:29926; -. 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; KGKMARI; -. DR OrthoDB; 5489581at2759; -. 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; 819 hits in 1132 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 189 other cell types or tissues. DR ExpressionAtlas; Q9Y2X3; baseline and differential. 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; IDA:UniProtKB. 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:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB. DR GO; GO:0006364; P:rRNA processing; TAS:UniProtKB. DR GO; GO:0048254; P:snoRNA localization; IMP:UniProtKB. DR Gene3D; 1.10.287.4070; -; 1. DR Gene3D; 1.10.246.90; Nop domain; 1. DR InterPro; IPR045056; Nop56/Nop58. DR InterPro; IPR012974; NOP58/56_N. DR InterPro; IPR042239; Nop_C. DR InterPro; IPR002687; Nop_dom. DR InterPro; IPR036070; Nop_dom_sf. DR InterPro; IPR012976; NOSIC. DR PANTHER; PTHR10894; NUCLEOLAR PROTEIN 5 NUCLEOLAR PROTEIN NOP5 NOP58; 1. DR PANTHER; PTHR10894:SF1; NUCLEOLAR PROTEIN 58; 1. DR Pfam; PF01798; Nop; 1. DR Pfam; PF08156; NOP5NT; 1. DR SMART; SM00931; NOSIC; 1. DR SUPFAM; SSF89124; Nop domain; 1. DR PROSITE; PS51358; NOP; 1. DR SWISS-2DPAGE; Q9Y2X3; -. DR Genevisible; Q9Y2X3; HS. 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 //