NOG2_YEAST
ID NOG2_YEAST Reviewed; 486 AA.
AC P53742; D6W1M8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Nucleolar GTP-binding protein 2;
GN Name=NOG2; OrderedLocusNames=YNR053C; ORFNames=N3484;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11707418; DOI=10.1093/emboj/20.22.6475;
RA Saveanu C., Bienvenu D., Namane A., Gleizes P.-E., Gas N., Jacquier A.,
RA Fromont-Racine M.;
RT "Nog2p, a putative GTPase associated with pre-60S subunits and required for
RT late 60S maturation steps.";
RL EMBO J. 20:6475-6484(2001).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-155, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-155, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: GTPase that associates with pre-60S ribosomal subunits in the
CC nucleolus and is required for their nuclear export and maturation.
CC {ECO:0000269|PubMed:11707418}.
CC -!- INTERACTION:
CC P53742; Q12176: MAK21; NbExp=3; IntAct=EBI-28532, EBI-10944;
CC P53742; Q12522: TIF6; NbExp=4; IntAct=EBI-28532, EBI-9046;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11707418}.
CC -!- MISCELLANEOUS: Present with 67700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. NOG2
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; Z71668; CAA96334.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10594.1; -; Genomic_DNA.
DR PIR; S63384; S63384.
DR RefSeq; NP_014451.1; NM_001183230.1.
DR PDB; 3JCT; EM; 3.08 A; m=1-486.
DR PDB; 6FT6; EM; 3.90 A; m=1-486.
DR PDB; 6M62; EM; 3.20 A; m=1-486.
DR PDB; 6N8J; EM; 3.50 A; m=1-486.
DR PDB; 6YLG; EM; 3.00 A; m=1-486.
DR PDB; 6YLH; EM; 3.10 A; m=1-486.
DR PDB; 7BT6; EM; 3.12 A; m=1-486.
DR PDB; 7BTB; EM; 3.22 A; m=1-486.
DR PDB; 7OF1; EM; 3.10 A; m=1-486.
DR PDB; 7OH3; EM; 3.40 A; m=1-486.
DR PDB; 7OHQ; EM; 3.10 A; m=1-486.
DR PDB; 7OHT; EM; 4.70 A; m=1-486.
DR PDBsum; 3JCT; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6N8J; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHT; -.
DR AlphaFoldDB; P53742; -.
DR SMR; P53742; -.
DR BioGRID; 35878; 442.
DR DIP; DIP-976N; -.
DR IntAct; P53742; 58.
DR MINT; P53742; -.
DR STRING; 4932.YNR053C; -.
DR iPTMnet; P53742; -.
DR MaxQB; P53742; -.
DR PaxDb; P53742; -.
DR PRIDE; P53742; -.
DR EnsemblFungi; YNR053C_mRNA; YNR053C; YNR053C.
DR GeneID; 855789; -.
DR KEGG; sce:YNR053C; -.
DR SGD; S000005336; NOG2.
DR VEuPathDB; FungiDB:YNR053C; -.
DR eggNOG; KOG2423; Eukaryota.
DR GeneTree; ENSGT00810000125524; -.
DR HOGENOM; CLU_011106_4_0_1; -.
DR InParanoid; P53742; -.
DR OMA; PAPFQGR; -.
DR BioCyc; YEAST:G3O-33359-MON; -.
DR PRO; PR:P53742; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53742; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:SGD.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IDA:SGD.
DR GO; GO:2000200; P:regulation of ribosomal subunit export from nucleus; IMP:SGD.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR024929; NOG2.
DR InterPro; IPR012971; NOG2_N_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11089:SF9; PTHR11089:SF9; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF08153; NGP1NT; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis.
FT CHAIN 1..486
FT /note="Nucleolar GTP-binding protein 2"
FT /id="PRO_0000215817"
FT DOMAIN 212..373
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 322..329
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 366..370
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 486 AA; 55489 MW; D7F670973B85CCEB CRC64;
MGTGKKEKSR RIREGDTKDG NLRVKGENFY RDSKRVKFLN MYTSGKEIRN KKGNLIRAAS
FQDSTIPDAR VQPDRRWFGN TRVISQDALQ HFRSALGETQ KDTYQVLLRR NKLPMSLLEE
KDADESPKAR ILDTESYADA FGPKAQRKRP RLAASNLEDL VKATNEDITK YEEKQVLDAT
LGLMGNQEDK ENGWTSAAKE AIFSKGQSKR IWNELYKVID SSDVVIHVLD ARDPLGTRCK
SVEEYMKKET PHKHLIYVLN KCDLVPTWVA AAWVKHLSKE RPTLAFHASI TNSFGKGSLI
QLLRQFSQLH TDRKQISVGF IGYPNTGKSS IINTLRKKKV CQVAPIPGET KVWQYITLMK
RIFLIDCPGI VPPSSKDSEE DILFRGVVRV EHVTHPEQYI PGVLKRCQVK HLERTYEISG
WKDATEFIEI LARKQGRLLK GGEPDESGVS KQILNDFNRG KIPWFVLPPE KEGEEKPKKK
EVEKTA
