Full text data of NOP2
NOP2
(NOL1)
[Confidence: low (only semi-automatic identification from reviews)]
Putative ribosomal RNA methyltransferase NOP2; 2.1.1.- (Nucleolar protein 1; Nucleolar protein 2 homolog; Proliferating-cell nucleolar antigen p120; Proliferation-associated nucleolar protein p120)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Putative ribosomal RNA methyltransferase NOP2; 2.1.1.- (Nucleolar protein 1; Nucleolar protein 2 homolog; Proliferating-cell nucleolar antigen p120; Proliferation-associated nucleolar protein p120)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P46087
ID NOP2_HUMAN Reviewed; 812 AA.
AC P46087; A1A4Z3; B3KPD6; Q05BA7; Q0P5S5; Q3KQS4; Q58F30;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 06-MAR-2007, sequence version 2.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Putative ribosomal RNA methyltransferase NOP2;
DE EC=2.1.1.-;
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;
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], AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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).
CC -!- FUNCTION: May play a role in the regulation of the cell cycle and
CC the increased nucleolar activity that is associated with the cell
CC proliferation. May act as ribosomal RNA methyltransferase.
CC -!- SUBUNIT: Interaction with MCRS1.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
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.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC methyltransferase superfamily. RsmB/NOP family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36398.1; Type=Frameshift; Positions=780;
CC Sequence=CAA39119.1; Type=Frameshift; Positions=780;
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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 PIR; A48168; A48168.
DR RefSeq; NP_001028886.1; NM_001033714.2.
DR RefSeq; NP_001245237.1; NM_001258308.1.
DR RefSeq; NP_001245238.1; NM_001258309.1.
DR RefSeq; NP_001245239.1; NM_001258310.1.
DR RefSeq; NP_006161.2; NM_006170.3.
DR RefSeq; XP_005253748.1; XM_005253691.1.
DR UniGene; Hs.534334; -.
DR ProteinModelPortal; P46087; -.
DR SMR; P46087; 280-592.
DR IntAct; P46087; 16.
DR MINT; MINT-1137742; -.
DR STRING; 9606.ENSP00000382392; -.
DR PhosphoSite; P46087; -.
DR DMDM; 146289861; -.
DR SWISS-2DPAGE; P46087; -.
DR PaxDb; P46087; -.
DR PRIDE; P46087; -.
DR Ensembl; ENST00000322166; ENSP00000313272; ENSG00000111641.
DR Ensembl; ENST00000382421; ENSP00000371858; ENSG00000111641.
DR Ensembl; ENST00000399466; ENSP00000382392; ENSG00000111641.
DR Ensembl; ENST00000537442; ENSP00000444437; ENSG00000111641.
DR Ensembl; ENST00000541778; ENSP00000443150; ENSG00000111641.
DR Ensembl; ENST00000545200; ENSP00000439422; ENSG00000111641.
DR GeneID; 4839; -.
DR KEGG; hsa:4839; -.
DR UCSC; uc021qtz.2; human.
DR CTD; 4839; -.
DR GeneCards; GC12M006666; -.
DR HGNC; HGNC:7867; NOP2.
DR HPA; HPA040119; -.
DR MIM; 164031; gene.
DR neXtProt; NX_P46087; -.
DR PharmGKB; PA164724026; -.
DR eggNOG; COG0144; -.
DR HOGENOM; HOG000224258; -.
DR HOVERGEN; HBG082043; -.
DR KO; K14835; -.
DR OMA; DLQRVHK; -.
DR OrthoDB; EOG7FBRHF; -.
DR ChiTaRS; NOP2; human.
DR GeneWiki; NOL1; -.
DR GenomeRNAi; 4839; -.
DR NextBio; 18646; -.
DR PRO; PR:P46087; -.
DR ArrayExpress; P46087; -.
DR Bgee; P46087; -.
DR CleanEx; HS_NOP2; -.
DR Genevestigator; P46087; -.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR InterPro; IPR001678; Fmu/NOL1/Nop2p.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR012586; P120R.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023273; RCMT_NOP2.
DR Pfam; PF01189; Nol1_Nop2_Fmu; 1.
DR Pfam; PF08062; P120R; 3.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02012; RCMTNOP2.
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; Complete proteome;
KW Methyltransferase; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1 812 Putative ribosomal RNA methyltransferase
FT NOP2.
FT /FTId=PRO_0000211818.
FT REGION 392 398 S-adenosyl-L-methionine binding (By
FT similarity).
FT ACT_SITE 517 517 Nucleophile (By similarity).
FT BINDING 416 416 S-adenosyl-L-methionine (Potential).
FT BINDING 443 443 S-adenosyl-L-methionine (Potential).
FT BINDING 460 460 S-adenosyl-L-methionine (Potential).
FT MOD_RES 36 36 Phosphoserine.
FT MOD_RES 58 58 Phosphoserine.
FT MOD_RES 67 67 Phosphoserine.
FT MOD_RES 181 181 Phosphoserine.
FT MOD_RES 185 185 Phosphothreonine.
FT MOD_RES 195 195 Phosphothreonine.
FT MOD_RES 649 649 N6-acetyllysine.
FT MOD_RES 666 666 Phosphoserine.
FT MOD_RES 675 675 Phosphoserine.
FT MOD_RES 732 732 Phosphoserine.
FT MOD_RES 734 734 Phosphoserine.
FT MOD_RES 739 739 Phosphothreonine.
FT MOD_RES 776 776 Phosphothreonine.
FT MOD_RES 786 786 Phosphoserine.
FT MOD_RES 801 801 Phosphoserine.
FT MOD_RES 812 812 Phosphoserine.
FT VAR_SEQ 81 84 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_023494.
FT VAR_SEQ 158 158 A -> AAGVQWLGLGSLQPPPPGFKQFSCLSFPSSWDLQ
FT (in isoform 4).
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 /FTId=VSP_045309.
FT VARIANT 73 73 L -> S (in dbSNP:rs1128164).
FT /FTId=VAR_030938.
FT CONFLICT 559 559 F -> L (in Ref. 6; AAI28185).
FT CONFLICT 630 630 A -> G (in Ref. 1; AAA36398).
FT CONFLICT 760 761 LP -> FA (in Ref. 1; AAA36398 and 3;
FT CAA39119).
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
//
ID NOP2_HUMAN Reviewed; 812 AA.
AC P46087; A1A4Z3; B3KPD6; Q05BA7; Q0P5S5; Q3KQS4; Q58F30;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 06-MAR-2007, sequence version 2.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=Putative ribosomal RNA methyltransferase NOP2;
DE EC=2.1.1.-;
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;
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], AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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).
CC -!- FUNCTION: May play a role in the regulation of the cell cycle and
CC the increased nucleolar activity that is associated with the cell
CC proliferation. May act as ribosomal RNA methyltransferase.
CC -!- SUBUNIT: Interaction with MCRS1.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
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.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC methyltransferase superfamily. RsmB/NOP family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36398.1; Type=Frameshift; Positions=780;
CC Sequence=CAA39119.1; Type=Frameshift; Positions=780;
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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 PIR; A48168; A48168.
DR RefSeq; NP_001028886.1; NM_001033714.2.
DR RefSeq; NP_001245237.1; NM_001258308.1.
DR RefSeq; NP_001245238.1; NM_001258309.1.
DR RefSeq; NP_001245239.1; NM_001258310.1.
DR RefSeq; NP_006161.2; NM_006170.3.
DR RefSeq; XP_005253748.1; XM_005253691.1.
DR UniGene; Hs.534334; -.
DR ProteinModelPortal; P46087; -.
DR SMR; P46087; 280-592.
DR IntAct; P46087; 16.
DR MINT; MINT-1137742; -.
DR STRING; 9606.ENSP00000382392; -.
DR PhosphoSite; P46087; -.
DR DMDM; 146289861; -.
DR SWISS-2DPAGE; P46087; -.
DR PaxDb; P46087; -.
DR PRIDE; P46087; -.
DR Ensembl; ENST00000322166; ENSP00000313272; ENSG00000111641.
DR Ensembl; ENST00000382421; ENSP00000371858; ENSG00000111641.
DR Ensembl; ENST00000399466; ENSP00000382392; ENSG00000111641.
DR Ensembl; ENST00000537442; ENSP00000444437; ENSG00000111641.
DR Ensembl; ENST00000541778; ENSP00000443150; ENSG00000111641.
DR Ensembl; ENST00000545200; ENSP00000439422; ENSG00000111641.
DR GeneID; 4839; -.
DR KEGG; hsa:4839; -.
DR UCSC; uc021qtz.2; human.
DR CTD; 4839; -.
DR GeneCards; GC12M006666; -.
DR HGNC; HGNC:7867; NOP2.
DR HPA; HPA040119; -.
DR MIM; 164031; gene.
DR neXtProt; NX_P46087; -.
DR PharmGKB; PA164724026; -.
DR eggNOG; COG0144; -.
DR HOGENOM; HOG000224258; -.
DR HOVERGEN; HBG082043; -.
DR KO; K14835; -.
DR OMA; DLQRVHK; -.
DR OrthoDB; EOG7FBRHF; -.
DR ChiTaRS; NOP2; human.
DR GeneWiki; NOL1; -.
DR GenomeRNAi; 4839; -.
DR NextBio; 18646; -.
DR PRO; PR:P46087; -.
DR ArrayExpress; P46087; -.
DR Bgee; P46087; -.
DR CleanEx; HS_NOP2; -.
DR Genevestigator; P46087; -.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR InterPro; IPR001678; Fmu/NOL1/Nop2p.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR012586; P120R.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023273; RCMT_NOP2.
DR Pfam; PF01189; Nol1_Nop2_Fmu; 1.
DR Pfam; PF08062; P120R; 3.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02012; RCMTNOP2.
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; Complete proteome;
KW Methyltransferase; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1 812 Putative ribosomal RNA methyltransferase
FT NOP2.
FT /FTId=PRO_0000211818.
FT REGION 392 398 S-adenosyl-L-methionine binding (By
FT similarity).
FT ACT_SITE 517 517 Nucleophile (By similarity).
FT BINDING 416 416 S-adenosyl-L-methionine (Potential).
FT BINDING 443 443 S-adenosyl-L-methionine (Potential).
FT BINDING 460 460 S-adenosyl-L-methionine (Potential).
FT MOD_RES 36 36 Phosphoserine.
FT MOD_RES 58 58 Phosphoserine.
FT MOD_RES 67 67 Phosphoserine.
FT MOD_RES 181 181 Phosphoserine.
FT MOD_RES 185 185 Phosphothreonine.
FT MOD_RES 195 195 Phosphothreonine.
FT MOD_RES 649 649 N6-acetyllysine.
FT MOD_RES 666 666 Phosphoserine.
FT MOD_RES 675 675 Phosphoserine.
FT MOD_RES 732 732 Phosphoserine.
FT MOD_RES 734 734 Phosphoserine.
FT MOD_RES 739 739 Phosphothreonine.
FT MOD_RES 776 776 Phosphothreonine.
FT MOD_RES 786 786 Phosphoserine.
FT MOD_RES 801 801 Phosphoserine.
FT MOD_RES 812 812 Phosphoserine.
FT VAR_SEQ 81 84 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_023494.
FT VAR_SEQ 158 158 A -> AAGVQWLGLGSLQPPPPGFKQFSCLSFPSSWDLQ
FT (in isoform 4).
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 /FTId=VSP_045309.
FT VARIANT 73 73 L -> S (in dbSNP:rs1128164).
FT /FTId=VAR_030938.
FT CONFLICT 559 559 F -> L (in Ref. 6; AAI28185).
FT CONFLICT 630 630 A -> G (in Ref. 1; AAA36398).
FT CONFLICT 760 761 LP -> FA (in Ref. 1; AAA36398 and 3;
FT CAA39119).
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
//
MIM
164031
*RECORD*
*FIELD* NO
164031
*FIELD* TI
*164031 NUCLEOLAR PROTEIN 1; NOL1
;;NUCLEOLAR ANTIGEN p120; p120;;
PROLIFERATING CELL NUCLEOLAR PROTEIN P120
read more*FIELD* TX
CLONING
Freeman et al. (1988) identified p120, a 120-kD nucleolar antigen
associated with proliferating cells. Antigen p120 was detectable in a
broad range of human tumors but not in corresponding normal tissues. The
antigen was not detectable in growth-arrested cells but was expressed
early in G1 of the cell cycle.
Valdez et al. (1992) cloned cDNAs encoding mouse p120. The predicted
mouse and human proteins are 63% identical. Northern blot analysis
indicated that p120 was expressed as an approximately 2.8-kb mRNA in
both mouse and human cells.
GENE FUNCTION
Overexpression of human p120 leads to the transformation of NIH 3T3
cells. Expression of antisense p120 constructs causes the
p120-transformed cells to revert to their original phenotype (Perlaky et
al., 1992). Valdez et al. (1992) reported that the middle region of the
antisense p120 RNA inhibited proliferation of NIH 3T3 cells
approximately to the same extent as the full-length antisense construct.
The human NOL1 protein is a proliferation-associated antigen that is
temporally regulated during the cell cycle with a dramatic increase in
expression at the G1-S boundary, suggesting that NOL1 may play a role in
the regulation of the cell cycle and the increased nucleolar activity
that is associated with the cell proliferation (Fonagy et al., 1993).
MAPPING
By fluorescence in situ hybridization and by the application of the
polymerase chain reaction (PCR) in the analysis of somatic cell hybrids,
Baens et al. (1994) mapped the NOL1 gene to chromosome 12p13.
*FIELD* RF
1. Baens, M.; Chaffanet, M.; Aerssens, J.; Cassiman, J.-J.; Marynen,
P.: Assignment of the gene for the human proliferating cell nucleolar
protein P120 (NOL1) to chromosome 12p13 by fluorescence in situ hybridization
and polymerase chain reaction with somatic cell hybrids. Genomics 21:
296-297, 1994.
2. Fonagy, A.; Swiderski, C.; Wilson, A.; Bolton, W.; Kenyon, N.;
Freeman, J. W.: Cell cycle regulated expression of nucleolar antigen
P120 in normal and transformed human fibroblasts. J. Cell. Physiol. 154:
16-27, 1993.
3. Freeman, J. W.; Busch, R. K.; Gyorkey, F.; Gyorkey, P.; Ross, B.
E.; Busch, H.: Identification and characterization of a human proliferation-associated
nucleolar antigen with a molecular weight of 120,000 expressed in
early G1 phase. Cancer Res. 48: 1244-1251, 1988.
4. Perlaky, L.; Valdez, B. C.; Busch, R. K.; Larson, R. G.; Jhiang,
S. M.; Zhang, W. W.; Brattain, M.; Busch, H.: Increased growth of
NIH/3T3 cells by transfection with human p120 complementary DNA and
inhibition by a p120 antisense construct. Cancer Res. 52: 428-436,
1992.
5. Valdez, B. C.; Perlaky, L.; Saijo, Y.; Henning, D.; Zhu, C.; Busch,
R. K.; Zhang, W.-W.; Busch, H.: A region of antisense RNA from human
p120 cDNA with high homology to mouse p120 cDNA inhibits NIH 3T3 proliferation. Cancer
Res. 52: 5681-5687, 1992.
*FIELD* CN
Rebekah S. Rasooly - updated: 2/24/1999
*FIELD* CD
Victor A. McKusick: 6/17/1994
*FIELD* ED
carol: 01/13/2014
alopez: 2/24/1999
jason: 6/17/1994
*RECORD*
*FIELD* NO
164031
*FIELD* TI
*164031 NUCLEOLAR PROTEIN 1; NOL1
;;NUCLEOLAR ANTIGEN p120; p120;;
PROLIFERATING CELL NUCLEOLAR PROTEIN P120
read more*FIELD* TX
CLONING
Freeman et al. (1988) identified p120, a 120-kD nucleolar antigen
associated with proliferating cells. Antigen p120 was detectable in a
broad range of human tumors but not in corresponding normal tissues. The
antigen was not detectable in growth-arrested cells but was expressed
early in G1 of the cell cycle.
Valdez et al. (1992) cloned cDNAs encoding mouse p120. The predicted
mouse and human proteins are 63% identical. Northern blot analysis
indicated that p120 was expressed as an approximately 2.8-kb mRNA in
both mouse and human cells.
GENE FUNCTION
Overexpression of human p120 leads to the transformation of NIH 3T3
cells. Expression of antisense p120 constructs causes the
p120-transformed cells to revert to their original phenotype (Perlaky et
al., 1992). Valdez et al. (1992) reported that the middle region of the
antisense p120 RNA inhibited proliferation of NIH 3T3 cells
approximately to the same extent as the full-length antisense construct.
The human NOL1 protein is a proliferation-associated antigen that is
temporally regulated during the cell cycle with a dramatic increase in
expression at the G1-S boundary, suggesting that NOL1 may play a role in
the regulation of the cell cycle and the increased nucleolar activity
that is associated with the cell proliferation (Fonagy et al., 1993).
MAPPING
By fluorescence in situ hybridization and by the application of the
polymerase chain reaction (PCR) in the analysis of somatic cell hybrids,
Baens et al. (1994) mapped the NOL1 gene to chromosome 12p13.
*FIELD* RF
1. Baens, M.; Chaffanet, M.; Aerssens, J.; Cassiman, J.-J.; Marynen,
P.: Assignment of the gene for the human proliferating cell nucleolar
protein P120 (NOL1) to chromosome 12p13 by fluorescence in situ hybridization
and polymerase chain reaction with somatic cell hybrids. Genomics 21:
296-297, 1994.
2. Fonagy, A.; Swiderski, C.; Wilson, A.; Bolton, W.; Kenyon, N.;
Freeman, J. W.: Cell cycle regulated expression of nucleolar antigen
P120 in normal and transformed human fibroblasts. J. Cell. Physiol. 154:
16-27, 1993.
3. Freeman, J. W.; Busch, R. K.; Gyorkey, F.; Gyorkey, P.; Ross, B.
E.; Busch, H.: Identification and characterization of a human proliferation-associated
nucleolar antigen with a molecular weight of 120,000 expressed in
early G1 phase. Cancer Res. 48: 1244-1251, 1988.
4. Perlaky, L.; Valdez, B. C.; Busch, R. K.; Larson, R. G.; Jhiang,
S. M.; Zhang, W. W.; Brattain, M.; Busch, H.: Increased growth of
NIH/3T3 cells by transfection with human p120 complementary DNA and
inhibition by a p120 antisense construct. Cancer Res. 52: 428-436,
1992.
5. Valdez, B. C.; Perlaky, L.; Saijo, Y.; Henning, D.; Zhu, C.; Busch,
R. K.; Zhang, W.-W.; Busch, H.: A region of antisense RNA from human
p120 cDNA with high homology to mouse p120 cDNA inhibits NIH 3T3 proliferation. Cancer
Res. 52: 5681-5687, 1992.
*FIELD* CN
Rebekah S. Rasooly - updated: 2/24/1999
*FIELD* CD
Victor A. McKusick: 6/17/1994
*FIELD* ED
carol: 01/13/2014
alopez: 2/24/1999
jason: 6/17/1994