Entry euk: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   10-MAY-2017, entry version 164.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND
RP   VARIANT SER-73.
RX   PubMed=2576976;
RA   Fonagy A., Henning D., Jhiang S., Haidar M.A., Busch R.K.,
RA   Larson R.G., Valdez B., Busch H.;
RT   "Cloning of the cDNA and sequence of the human proliferating-cell
RT   nucleolar protein P120.";
RL   Cancer Commun. 1:243-251(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2372471;
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
RT   mouse 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   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.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   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.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., 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
RT   project: 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,
RT   interacts 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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, AND IDENTIFICATION
RP   BY 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
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND IDENTIFICATION
RP   BY 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
RT   cells and high confident phosphopeptide identification by cross-
RT   validation of 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.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient 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,
RP   AND 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
RT   the 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;
RP   THR-185; SER-666; SER-675; SER-732; SER-734; THR-739; THR-776; SER-786
RP   AND SER-812, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; THR-185 AND
RP   SER-732, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; THR-185; SER-732;
RP   SER-786 AND SER-812, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [19]
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.,
RA   Buerckstuemmer T., 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   [20]
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.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [21]
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
RT   compartmental localization of nucleolin and DDX21.";
RL   Genes Cells 18:780-797(2013).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-67; SER-732 AND
RP   SER-786, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [23]
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   [24]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-615, AND IDENTIFICATION BY
RP   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).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC       specifically methylates the C(5) position of cytosine 4447 in 28S
CC       rRNA (Probable). May play a role in the regulation of the cell
CC       cycle and the increased nucleolar activity that is associated with
CC       the cell proliferation (Probable). {ECO:0000305,
CC       ECO:0000305|PubMed:23913415}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(4447) in
CC       28S rRNA = S-adenosyl-L-homocysteine + C(5)-methylcytosine(4447)
CC       in 28S rRNA. {ECO:0000305|PubMed:23913415}.
CC   -!- SUBUNIT: Interaction with MCRS1 (PubMed:9654073). Interacts with
CC       WDR46 (PubMed:23848194). {ECO:0000269|PubMed:23848194,
CC       ECO:0000269|PubMed:9654073}.
CC   -!- INTERACTION:
CC       Q96GN5:CDCA7L; NbExp=3; IntAct=EBI-356811, EBI-5278764;
CC       Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-356811, EBI-739624;
CC       O60684:KPNA6; NbExp=3; IntAct=EBI-356811, EBI-359923;
CC       P04733:MT1F; NbExp=3; IntAct=EBI-356811, EBI-10209483;
CC       Q8N1B4:VPS52; NbExp=3; IntAct=EBI-356811, EBI-2799833;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {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
CC       phase 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
CC       methyltransferase superfamily. RsmB/NOP family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01023}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA36398.1; Type=Frameshift; Positions=780; Evidence={ECO:0000305};
CC       Sequence=CAA39119.1; Type=Frameshift; Positions=780; 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   UniGene; Hs.534334; -.
DR   ProteinModelPortal; P46087; -.
DR   SMR; P46087; -.
DR   BioGrid; 110902; 158.
DR   IntAct; P46087; 45.
DR   MINT; MINT-1137742; -.
DR   STRING; 9606.ENSP00000382392; -.
DR   iPTMnet; P46087; -.
DR   PhosphoSitePlus; P46087; -.
DR   SwissPalm; P46087; -.
DR   BioMuta; NOP2; -.
DR   DMDM; 146289861; -.
DR   SWISS-2DPAGE; P46087; -.
DR   EPD; P46087; -.
DR   MaxQB; P46087; -.
DR   PaxDb; P46087; -.
DR   PeptideAtlas; P46087; -.
DR   PRIDE; P46087; -.
DR   TopDownProteomics; P46087-2; -. [P46087-2]
DR   Ensembl; ENST00000322166; ENSP00000313272; ENSG00000111641. [P46087-1]
DR   Ensembl; ENST00000382421; ENSP00000371858; ENSG00000111641. [P46087-4]
DR   Ensembl; ENST00000399466; ENSP00000382392; ENSG00000111641. [P46087-2]
DR   Ensembl; ENST00000537442; ENSP00000444437; ENSG00000111641. [P46087-1]
DR   Ensembl; ENST00000541778; ENSP00000443150; ENSG00000111641. [P46087-2]
DR   Ensembl; ENST00000545200; ENSP00000439422; ENSG00000111641. [P46087-3]
DR   Ensembl; ENST00000617555; ENSP00000484384; ENSG00000111641. [P46087-3]
DR   Ensembl; ENST00000620535; ENSP00000479320; ENSG00000111641. [P46087-4]
DR   GeneID; 4839; -.
DR   KEGG; hsa:4839; -.
DR   UCSC; uc031yro.1; human. [P46087-1]
DR   CTD; 4839; -.
DR   DisGeNET; 4839; -.
DR   GeneCards; NOP2; -.
DR   HGNC; HGNC:7867; NOP2.
DR   HPA; HPA040119; -.
DR   MIM; 164031; gene.
DR   neXtProt; NX_P46087; -.
DR   OpenTargets; ENSG00000111641; -.
DR   PharmGKB; PA164724026; -.
DR   eggNOG; KOG1122; Eukaryota.
DR   eggNOG; COG0144; LUCA.
DR   GeneTree; ENSGT00660000095341; -.
DR   HOGENOM; HOG000224258; -.
DR   HOVERGEN; HBG082043; -.
DR   InParanoid; P46087; -.
DR   KO; K14835; -.
DR   PhylomeDB; P46087; -.
DR   TreeFam; TF105660; -.
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   ChiTaRS; NOP2; human.
DR   GeneWiki; NOL1; -.
DR   GenomeRNAi; 4839; -.
DR   PRO; PR:P46087; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000111641; -.
DR   CleanEx; HS_NOP2; -.
DR   ExpressionAtlas; P46087; baseline and differential.
DR   Genevisible; P46087; HS.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0003723; F:RNA binding; IDA: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 proliferation; IDA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
DR   GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
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.
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; Complete proteome;
KW   Isopeptide bond; Methyltransferase; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; RNA-binding; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase; Ubl conjugation.
FT   CHAIN         1    812       Probable 28S rRNA (cytosine(4447)-C(5))-
FT                                methyltransferase.
FT                                /FTId=PRO_0000211818.
FT   REGION      392    398       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01023}.
FT   ACT_SITE    517    517       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     416    416       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01023}.
FT   BINDING     443    443       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01023}.
FT   BINDING     460    460       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01023}.
FT   MOD_RES      36     36       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES      58     58       Phosphoserine.
FT                                {ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES      67     67       Phosphoserine.
FT                                {ECO:0000244|PubMed:17924679,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     102    102       Citrulline. {ECO:0000250}.
FT   MOD_RES     164    164       Citrulline. {ECO:0000250}.
FT   MOD_RES     181    181       Phosphoserine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     185    185       Phosphothreonine.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES     195    195       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     649    649       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     666    666       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     675    675       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     732    732       Phosphoserine.
FT                                {ECO:0000244|PubMed:16964243,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     734    734       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     739    739       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     776    776       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     786    786       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     801    801       Phosphoserine.
FT                                {ECO:0000244|PubMed:21406692}.
FT   MOD_RES     812    812       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231}.
FT   CROSSLNK    615    615       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:25114211}.
FT   VAR_SEQ      81     84       Missing (in isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_023494.
FT   VAR_SEQ     158    158       A -> AAGVQWLGLGSLQPPPPGFKQFSCLSFPSSWDLQ
FT                                (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_045308.
FT   VAR_SEQ     597    812       GNSETATPTNVDLPQVIPKSENSSQPAKKAKGAAKTKQQLQ
FT                                KQQHPKKASFQKLNGISKGADSELSTVPSVTKTQASSSFQD
FT                                SSQPAGKAEGIREPKVTGKLKQRSPKLQSSKKVAFLRQNAP
FT                                PKGTDTQTPAVLSPSKTQATLKPKDHHQPLGRAKGVEKQQL
FT                                PEQPFEKAAFQKQNDTPKGPQPPTVSPIRSSRPPPAKRKKS
FT                                QSRGNSQLLLS -> DGVLLCRSGWTAVVQSQLIATSTFQV
FT                                QAILVPQTPK (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_045309.
FT   VARIANT      73     73       L -> S (in dbSNP:rs1128164).
FT                                {ECO:0000269|PubMed:1394192,
FT                                ECO:0000269|PubMed:2576976}.
FT                                /FTId=VAR_030938.
FT   CONFLICT    559    559       F -> L (in Ref. 6; AAI28185).
FT                                {ECO:0000305}.
FT   CONFLICT    630    630       A -> G (in Ref. 1; AAA36398).
FT                                {ECO:0000305}.
FT   CONFLICT    760    761       LP -> FA (in Ref. 1; AAA36398 and 3;
FT                                CAA39119). {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       454    465       ipat:NOL1_NOP2_SUN [T]
FT   MYHIT       623    644       ipfam:P120R [T]
FT   MYHIT       749    768       ipfam:P120R [T]
FT   MYHIT       377    585       ipfam:Methyltr_RsmB-F [T]
FT   MYHIT       295    374       ipfam:Methyltr_RsmF_N [T]
FT   MYHIT       300    587       iprf:SAM_MT_RSMB_NOP [T]
FT   MYHIT       683    705       ipfam:P120R [T]
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
//