NOP2_HUMAN
ID NOP2_HUMAN Reviewed; 812 AA.
AC P46087; A1A4Z3; B3KPD6; Q05BA7; Q0P5S5; Q3KQS4; Q58F30;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Probable 28S rRNA (cytosine(4447)-C(5))-methyltransferase;
DE EC=2.1.1.- {ECO:0000305|PubMed:23913415};
DE AltName: Full=Nucleolar protein 1;
DE AltName: Full=Nucleolar protein 2 homolog;
DE AltName: Full=Proliferating-cell nucleolar antigen p120;
DE AltName: Full=Proliferation-associated nucleolar protein p120;
GN Name=NOP2; Synonyms=NOL1, NSUN1;
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] (ISOFORM 1), DEVELOPMENTAL STAGE, AND VARIANT
RP SER-73.
RX PubMed=2576976;
RA Fonagy A., Henning D., Jhiang S., Haidar M.A., Busch R.K., Larson R.G.,
RA Valdez B., Busch H.;
RT "Cloning of the cDNA and sequence of the human proliferating-cell nucleolar
RT protein P120.";
RL Cancer Commun. 1:243-251(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2372471; DOI=10.3727/095535490820874704;
RA Larson R.G., Henning D., Haidar M.A., Jhiang S., Lin W.L., Zhang W.W.,
RA Busch H.;
RT "Genomic structure of the human proliferating cell nucleolar protein
RT p120.";
RL Cancer Commun. 2:63-71(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-73.
RX PubMed=1394192;
RA Valdez B.C., Perlaky L., Saijo Y., Henning D., Zhu C., Busch R.K.,
RA Zhang W.W., Busch H.;
RT "A region of antisense RNA from human p120 cDNA with high homology to mouse
RT p120 cDNA inhibits NIH 3T3 proliferation.";
RL Cancer Res. 52:5681-5686(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Colon, Eye, and Ovary;
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 [7]
RP INTERACTION WITH MCRS1.
RX PubMed=9654073; DOI=10.1046/j.1432-1327.1998.2530734.x;
RA Ren Y., Busch R.K., Perlaky L., Busch H.;
RT "The 58-kDa microspherule protein (MSP58), a nucleolar protein, interacts
RT with nucleolar protein p120.";
RL Eur. J. Biochem. 253:734-742(1998).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND THR-185, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [12]
RP IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-181 AND THR-185, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-67; SER-181; THR-185;
RP SER-666; SER-675; SER-732; SER-734; THR-739; THR-776; SER-786 AND SER-812,
RP 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; THR-185 AND SER-732, 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-649, 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 [18]
RP INTERACTION WITH RRP1B.
RX PubMed=20926688; DOI=10.1091/mbc.e10-04-0287;
RA Chamousset D., De Wever V., Moorhead G.B., Chen Y., Boisvert F.M.,
RA Lamond A.I., Trinkle-Mulcahy L.;
RT "RRP1B targets PP1 to mammalian cell nucleoli and is associated with pre-
RT 60S ribosomal subunits.";
RL Mol. Biol. Cell 21:4212-4226(2010).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; THR-185; SER-732;
RP SER-786 AND SER-812, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-181; THR-185;
RP THR-195; SER-732; SER-786 AND SER-801, AND IDENTIFICATION BY MASS
RP 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 [22]
RP FUNCTION.
RX PubMed=24120868; DOI=10.1016/j.celrep.2013.08.049;
RA Sloan K.E., Bohnsack M.T., Watkins N.J.;
RT "The 5S RNP couples p53 homeostasis to ribosome biogenesis and nucleolar
RT stress.";
RL Cell Rep. 5:237-247(2013).
RN [23]
RP INTERACTION WITH WDR46.
RX PubMed=23848194; DOI=10.1111/gtc.12077;
RA Hirai Y., Louvet E., Oda T., Kumeta M., Watanabe Y., Horigome T.,
RA Takeyasu K.;
RT "Nucleolar scaffold protein, WDR46, determines the granular compartmental
RT localization of nucleolin and DDX21.";
RL Genes Cells 18:780-797(2013).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-67; SER-732 AND
RP SER-786, 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 [25]
RP PROBABLE FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23913415; DOI=10.1093/nar/gkt679;
RA Sharma S., Yang J., Watzinger P., Kotter P., Entian K.D.;
RT "Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA,
RT respectively.";
RL Nucleic Acids Res. 41:9062-9076(2013).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-615, AND IDENTIFICATION BY MASS
RP 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-71; LYS-272 AND LYS-615, 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: Involved in ribosomal large subunit assembly
CC (PubMed:24120868). S-adenosyl-L-methionine-dependent methyltransferase
CC that specifically methylates the C(5) position of cytosine 4447 in 28S
CC rRNA (Probable). May play a role in the regulation of the cell cycle
CC and the increased nucleolar activity that is associated with the cell
CC proliferation (Probable). {ECO:0000269|PubMed:24120868, ECO:0000305,
CC ECO:0000305|PubMed:23913415}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(4447) in 28S rRNA + S-adenosyl-L-methionine = 5-
CC methylcytidine(4447) in 28S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:47792, Rhea:RHEA-COMP:11917, Rhea:RHEA-COMP:11918,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000305|PubMed:23913415};
CC -!- SUBUNIT: Interacts with MCRS1 (PubMed:9654073). Interacts with WDR46
CC (PubMed:23848194). Interacts with RRP1B (PubMed:20926688).
CC {ECO:0000269|PubMed:20926688, ECO:0000269|PubMed:23848194,
CC ECO:0000269|PubMed:9654073}.
CC -!- INTERACTION:
CC P46087; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-356811, EBI-5278764;
CC P46087; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-356811, EBI-739624;
CC P46087; O60684: KPNA6; NbExp=3; IntAct=EBI-356811, EBI-359923;
CC P46087; P04733: MT1F; NbExp=3; IntAct=EBI-356811, EBI-10209483;
CC P46087; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-356811, EBI-2799833;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P46087-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P46087-2; Sequence=VSP_023494;
CC Name=3;
CC IsoId=P46087-3; Sequence=VSP_023494, VSP_045309;
CC Name=4;
CC IsoId=P46087-4; Sequence=VSP_045308;
CC -!- DEVELOPMENTAL STAGE: Expressed in G1 and peaks during the early S phase
CC of the cell cycle. {ECO:0000269|PubMed:2576976}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36398.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA39119.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M32110; AAA36398.1; ALT_SEQ; mRNA.
DR EMBL; M33132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X55504; CAA39119.1; ALT_FRAME; mRNA.
DR EMBL; AK056208; BAG51648.1; -; mRNA.
DR EMBL; AC006064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082985; AAH82985.1; -; mRNA.
DR EMBL; BC000656; AAH00656.1; -; mRNA.
DR EMBL; BC065257; AAH65257.1; -; mRNA.
DR EMBL; BC106072; AAI06073.1; -; mRNA.
DR EMBL; BC128183; AAI28184.1; -; mRNA.
DR EMBL; BC128184; AAI28185.1; -; mRNA.
DR CCDS; CCDS44811.1; -. [P46087-2]
DR CCDS; CCDS58202.1; -. [P46087-3]
DR CCDS; CCDS58203.1; -. [P46087-1]
DR CCDS; CCDS58204.1; -. [P46087-4]
DR PIR; A48168; A48168.
DR RefSeq; NP_001028886.1; NM_001033714.2. [P46087-2]
DR RefSeq; NP_001245237.1; NM_001258308.1. [P46087-1]
DR RefSeq; NP_001245238.1; NM_001258309.1. [P46087-4]
DR RefSeq; NP_001245239.1; NM_001258310.1. [P46087-3]
DR RefSeq; NP_006161.2; NM_006170.3. [P46087-2]
DR RefSeq; XP_005253748.1; XM_005253691.1. [P46087-1]
DR AlphaFoldDB; P46087; -.
DR SMR; P46087; -.
DR BioGRID; 110902; 372.
DR IntAct; P46087; 122.
DR MINT; P46087; -.
DR STRING; 9606.ENSP00000371858; -.
DR GlyGen; P46087; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; P46087; -.
DR PhosphoSitePlus; P46087; -.
DR SwissPalm; P46087; -.
DR BioMuta; NOP2; -.
DR DMDM; 146289861; -.
DR SWISS-2DPAGE; P46087; -.
DR EPD; P46087; -.
DR jPOST; P46087; -.
DR MassIVE; P46087; -.
DR MaxQB; P46087; -.
DR PaxDb; P46087; -.
DR PeptideAtlas; P46087; -.
DR PRIDE; P46087; -.
DR ProteomicsDB; 55714; -. [P46087-1]
DR ProteomicsDB; 55715; -. [P46087-2]
DR ProteomicsDB; 58366; -.
DR ProteomicsDB; 61721; -.
DR TopDownProteomics; P46087-2; -. [P46087-2]
DR Antibodypedia; 22530; 108 antibodies from 26 providers.
DR DNASU; 4839; -.
DR Ensembl; ENST00000322166.10; ENSP00000313272.6; ENSG00000111641.12. [P46087-1]
DR Ensembl; ENST00000382421.7; ENSP00000371858.3; ENSG00000111641.12. [P46087-4]
DR Ensembl; ENST00000399466.6; ENSP00000382392.2; ENSG00000111641.12. [P46087-2]
DR Ensembl; ENST00000537442.5; ENSP00000444437.1; ENSG00000111641.12. [P46087-1]
DR Ensembl; ENST00000541778.5; ENSP00000443150.1; ENSG00000111641.12. [P46087-2]
DR Ensembl; ENST00000545200.5; ENSP00000439422.1; ENSG00000111641.12. [P46087-3]
DR Ensembl; ENST00000617555.4; ENSP00000484384.1; ENSG00000111641.12. [P46087-3]
DR Ensembl; ENST00000620535.4; ENSP00000479320.1; ENSG00000111641.12. [P46087-4]
DR GeneID; 4839; -.
DR KEGG; hsa:4839; -.
DR MANE-Select; ENST00000322166.10; ENSP00000313272.6; NM_001258308.2; NP_001245237.1.
DR UCSC; uc031yro.1; human. [P46087-1]
DR CTD; 4839; -.
DR DisGeNET; 4839; -.
DR GeneCards; NOP2; -.
DR HGNC; HGNC:7867; NOP2.
DR HPA; ENSG00000111641; Low tissue specificity.
DR MIM; 164031; gene.
DR neXtProt; NX_P46087; -.
DR OpenTargets; ENSG00000111641; -.
DR PharmGKB; PA164724026; -.
DR VEuPathDB; HostDB:ENSG00000111641; -.
DR eggNOG; KOG1122; Eukaryota.
DR GeneTree; ENSGT00940000161554; -.
DR HOGENOM; CLU_005316_2_0_1; -.
DR InParanoid; P46087; -.
DR OMA; XLLPIER; -.
DR OrthoDB; 1528896at2759; -.
DR PhylomeDB; P46087; -.
DR TreeFam; TF105660; -.
DR PathwayCommons; P46087; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-8869496; TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation.
DR SignaLink; P46087; -.
DR BioGRID-ORCS; 4839; 574 hits in 1095 CRISPR screens.
DR ChiTaRS; NOP2; human.
DR GeneWiki; NOL1; -.
DR GenomeRNAi; 4839; -.
DR Pharos; P46087; Tbio.
DR PRO; PR:P46087; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P46087; protein.
DR Bgee; ENSG00000111641; Expressed in granulocyte and 92 other tissues.
DR ExpressionAtlas; P46087; baseline and differential.
DR Genevisible; P46087; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:GO_Central.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:UniProtKB.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR012586; P120R_rpt.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023273; RCMT_NOP2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807; PTHR22807; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR Pfam; PF08062; P120R; 3.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02012; RCMTNOP2.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00446; nop2p; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Citrullination; Isopeptide bond;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA processing; S-adenosyl-L-methionine;
KW Transferase; Ubl conjugation.
FT CHAIN 1..812
FT /note="Probable 28S rRNA (cytosine(4447)-C(5))-
FT methyltransferase"
FT /id="PRO_0000211818"
FT REGION 1..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..158
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 517
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 392..398
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 416
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 443
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 460
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 102
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 164
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 181
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"
FT MOD_RES 185
FT /note="Phosphothreonine"
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"
FT MOD_RES 195
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 649
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 739
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 776
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 786
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 801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 812
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT CROSSLNK 71
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 272
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 615
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 VAR_SEQ 81..84
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_023494"
FT VAR_SEQ 158
FT /note="A -> AAGVQWLGLGSLQPPPPGFKQFSCLSFPSSWDLQ (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045308"
FT VAR_SEQ 597..812
FT /note="GNSETATPTNVDLPQVIPKSENSSQPAKKAKGAAKTKQQLQKQQHPKKASFQ
FT KLNGISKGADSELSTVPSVTKTQASSSFQDSSQPAGKAEGIREPKVTGKLKQRSPKLQS
FT SKKVAFLRQNAPPKGTDTQTPAVLSPSKTQATLKPKDHHQPLGRAKGVEKQQLPEQPFE
FT KAAFQKQNDTPKGPQPPTVSPIRSSRPPPAKRKKSQSRGNSQLLLS -> DGVLLCRSG
FT WTAVVQSQLIATSTFQVQAILVPQTPK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045309"
FT VARIANT 73
FT /note="L -> S (in dbSNP:rs1128164)"
FT /evidence="ECO:0000269|PubMed:1394192,
FT ECO:0000269|PubMed:2576976"
FT /id="VAR_030938"
FT CONFLICT 559
FT /note="F -> L (in Ref. 6; AAI28185)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="A -> G (in Ref. 1; AAA36398)"
FT /evidence="ECO:0000305"
FT CONFLICT 760..761
FT /note="LP -> FA (in Ref. 1; AAA36398 and 3; CAA39119)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 812 AA; 89302 MW; 4C7A1BE79388F1C5 CRC64;
MGRKLDPTKE KRGPGRKARK QKGAETELVR FLPAVSDENS KRLSSRARKR AAKRRLGSVE
APKTNKSPEA KPLPGKLPKG ISAGAVQTAG KKGPQSLFNA PRGKKRPAPG SDEEEEEEDS
EEDGMVNHGD LWGSEDDADT VDDYGADSNS EDEEEGEALL PIERAARKQK AREAAAGIQW
SEEETEDEEE EKEVTPESGP PKVEEADGGL QINVDEEPFV LPPAGEMEQD AQAPDLQRVH
KRIQDIVGIL RDFGAQREEG RSRSEYLNRL KKDLAIYYSY GDFLLGKLMD LFPLSELVEF
LEANEVPRPV TLRTNTLKTR RRDLAQALIN RGVNLDPLGK WSKTGLVVYD SSVPIGATPE
YLAGHYMLQG ASSMLPVMAL APQEHERILD MCCAPGGKTS YMAQLMKNTG VILANDANAE
RLKSVVGNLH RLGVTNTIIS HYDGRQFPKV VGGFDRVLLD APCSGTGVIS KDPAVKTNKD
EKDILRCAHL QKELLLSAID SVNATSKTGG YLVYCTCSIT VEENEWVVDY ALKKRNVRLV
PTGLDFGQEG FTRFRERRFH PSLRSTRRFY PHTHNMDGFF IAKFKKFSNS IPQSQTGNSE
TATPTNVDLP QVIPKSENSS QPAKKAKGAA KTKQQLQKQQ HPKKASFQKL NGISKGADSE
LSTVPSVTKT QASSSFQDSS QPAGKAEGIR EPKVTGKLKQ RSPKLQSSKK VAFLRQNAPP
KGTDTQTPAV LSPSKTQATL KPKDHHQPLG RAKGVEKQQL PEQPFEKAAF QKQNDTPKGP
QPPTVSPIRS SRPPPAKRKK SQSRGNSQLL LS
