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NOG1_YEAST
ID   NOG1_YEAST              Reviewed;         647 AA.
AC   Q02892; D6W3S4;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=Nucleolar GTP-binding protein 1;
GN   Name=NOG1; OrderedLocusNames=YPL093W; ORFNames=LPG15W;
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=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(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   SUBCELLULAR LOCATION.
RX   PubMed=11112701; DOI=10.1242/jcs.114.1.173;
RA   Park J.-H., Jensen B.C., Kifer C.T., Parsons M.;
RT   "A novel nucleolar G-protein conserved in eukaryotes.";
RL   J. Cell Sci. 114:173-185(2001).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH RLP24.
RX   PubMed=12808088; DOI=10.1128/mcb.23.13.4449-4460.2003;
RA   Saveanu C., Namane A., Gleizes P.-E., Lebreton A., Rousselle J.-C.,
RA   Noaillac-Depeyre J., Gas N., Jacquier A., Fromont-Racine M.;
RT   "Sequential protein association with nascent 60S ribosomal particles.";
RL   Mol. Cell. Biol. 23:4449-4460(2003).
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, AND IDENTIFICATION BY
RP   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: Involved in the biogenesis of the 60S ribosomal subunit.
CC       {ECO:0000269|PubMed:12808088}.
CC   -!- SUBUNIT: Associated with nucleolar and cytoplasmic pre-60S particles.
CC       Directly interacts with RLP24. {ECO:0000269|PubMed:12808088}.
CC   -!- INTERACTION:
CC       Q02892; Q04660: ERB1; NbExp=4; IntAct=EBI-12105, EBI-28098;
CC       Q02892; Q03532: HAS1; NbExp=2; IntAct=EBI-12105, EBI-8170;
CC       Q02892; P43586: LOC1; NbExp=4; IntAct=EBI-12105, EBI-22906;
CC       Q02892; Q12176: MAK21; NbExp=3; IntAct=EBI-12105, EBI-10944;
CC       Q02892; P40991: NOP2; NbExp=2; IntAct=EBI-12105, EBI-12110;
CC       Q02892; P37838: NOP4; NbExp=3; IntAct=EBI-12105, EBI-12122;
CC       Q02892; P53261: NOP7; NbExp=4; IntAct=EBI-12105, EBI-13145;
CC       Q02892; P53136: NSA1; NbExp=4; IntAct=EBI-12105, EBI-23920;
CC       Q02892; P40078: NSA2; NbExp=4; IntAct=EBI-12105, EBI-22681;
CC       Q02892; P40693: RLP7; NbExp=3; IntAct=EBI-12105, EBI-15415;
CC       Q02892; P36160: RPF2; NbExp=6; IntAct=EBI-12105, EBI-15881;
CC       Q02892; P0C2I0: RPL20B; NbExp=2; IntAct=EBI-12105, EBI-15298;
CC       Q02892; P05736: RPL2B; NbExp=2; IntAct=EBI-12105, EBI-15328;
CC       Q02892; P26321: RPL5; NbExp=2; IntAct=EBI-12105, EBI-15398;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11112701}.
CC   -!- MISCELLANEOUS: Present with 28000 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. NOG subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU01047}.
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DR   EMBL; U43281; AAB68206.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11340.1; -; Genomic_DNA.
DR   PIR; S61973; S61973.
DR   RefSeq; NP_015232.1; NM_001183907.1.
DR   PDB; 3JCT; EM; 3.08 A; b=1-647.
DR   PDB; 4V7F; EM; 8.70 A; o=1-647.
DR   PDB; 5FL8; EM; 9.50 A; o=1-647.
DR   PDB; 5JCS; EM; 9.50 A; o=1-647.
DR   PDB; 6C0F; EM; 3.70 A; W=1-647.
DR   PDB; 6ELZ; EM; 3.30 A; b=1-647.
DR   PDB; 6EM1; EM; 3.60 A; b=1-647.
DR   PDB; 6EM5; EM; 4.30 A; b=1-647.
DR   PDB; 6FT6; EM; 3.90 A; b=1-647.
DR   PDB; 6M62; EM; 3.20 A; b=1-647.
DR   PDB; 6N8J; EM; 3.50 A; b=1-647.
DR   PDB; 6N8K; EM; 3.60 A; b=1-647.
DR   PDB; 6N8L; EM; 3.60 A; b=1-647.
DR   PDB; 6YLG; EM; 3.00 A; b=1-647.
DR   PDB; 6YLH; EM; 3.10 A; b=1-647.
DR   PDB; 6YLX; EM; 3.90 A; b=1-647.
DR   PDB; 6YLY; EM; 3.80 A; b=1-647.
DR   PDB; 7BT6; EM; 3.12 A; b=1-647.
DR   PDB; 7BTB; EM; 3.22 A; b=1-647.
DR   PDB; 7OF1; EM; 3.10 A; b=1-647.
DR   PDB; 7OH3; EM; 3.40 A; b=1-647.
DR   PDB; 7OHP; EM; 3.90 A; b=1-647.
DR   PDB; 7OHQ; EM; 3.10 A; b=1-647.
DR   PDB; 7OHR; EM; 4.72 A; b=1-647.
DR   PDB; 7OHS; EM; 4.38 A; b=1-647.
DR   PDB; 7OHT; EM; 4.70 A; b=1-647.
DR   PDB; 7OHU; EM; 3.70 A; b=1-647.
DR   PDB; 7OHV; EM; 3.90 A; b=1-647.
DR   PDB; 7OHW; EM; 3.50 A; b=1-647.
DR   PDB; 7OHX; EM; 3.30 A; b=1-647.
DR   PDB; 7OHY; EM; 3.90 A; b=1-647.
DR   PDBsum; 3JCT; -.
DR   PDBsum; 4V7F; -.
DR   PDBsum; 5FL8; -.
DR   PDBsum; 5JCS; -.
DR   PDBsum; 6C0F; -.
DR   PDBsum; 6ELZ; -.
DR   PDBsum; 6EM1; -.
DR   PDBsum; 6EM5; -.
DR   PDBsum; 6FT6; -.
DR   PDBsum; 6M62; -.
DR   PDBsum; 6N8J; -.
DR   PDBsum; 6N8K; -.
DR   PDBsum; 6N8L; -.
DR   PDBsum; 6YLG; -.
DR   PDBsum; 6YLH; -.
DR   PDBsum; 6YLX; -.
DR   PDBsum; 6YLY; -.
DR   PDBsum; 7BT6; -.
DR   PDBsum; 7BTB; -.
DR   PDBsum; 7OF1; -.
DR   PDBsum; 7OH3; -.
DR   PDBsum; 7OHP; -.
DR   PDBsum; 7OHQ; -.
DR   PDBsum; 7OHR; -.
DR   PDBsum; 7OHS; -.
DR   PDBsum; 7OHT; -.
DR   PDBsum; 7OHU; -.
DR   PDBsum; 7OHV; -.
DR   PDBsum; 7OHW; -.
DR   PDBsum; 7OHX; -.
DR   PDBsum; 7OHY; -.
DR   AlphaFoldDB; Q02892; -.
DR   SMR; Q02892; -.
DR   BioGRID; 36088; 390.
DR   DIP; DIP-2785N; -.
DR   IntAct; Q02892; 101.
DR   MINT; Q02892; -.
DR   STRING; 4932.YPL093W; -.
DR   iPTMnet; Q02892; -.
DR   MaxQB; Q02892; -.
DR   PaxDb; Q02892; -.
DR   PRIDE; Q02892; -.
DR   EnsemblFungi; YPL093W_mRNA; YPL093W; YPL093W.
DR   GeneID; 856012; -.
DR   KEGG; sce:YPL093W; -.
DR   SGD; S000006014; NOG1.
DR   VEuPathDB; FungiDB:YPL093W; -.
DR   eggNOG; KOG1490; Eukaryota.
DR   GeneTree; ENSGT00390000018475; -.
DR   HOGENOM; CLU_011784_4_1_1; -.
DR   InParanoid; Q02892; -.
DR   OMA; EWKNDVM; -.
DR   BioCyc; YEAST:G3O-33997-MON; -.
DR   PRO; PR:Q02892; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q02892; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR   GO; GO:0005525; F:GTP binding; ISS:SGD.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IMP:SGD.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:SGD.
DR   GO; GO:0000054; P:ribosomal subunit export from nucleus; IMP:SGD.
DR   GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR024926; NOG1.
DR   InterPro; IPR041623; NOG1_N.
DR   InterPro; IPR010674; NOG1_Rossman_fold_dom.
DR   InterPro; IPR012973; NOG_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF06858; NOG1; 1.
DR   Pfam; PF17835; NOG1_N; 1.
DR   Pfam; PF08155; NOGCT; 1.
DR   PIRSF; PIRSF038919; NOG1; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51710; G_OBG; 1.
PE   1: Evidence at protein level;
KW   3D-structure; GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Ribosome biogenesis.
FT   CHAIN           1..647
FT                   /note="Nucleolar GTP-binding protein 1"
FT                   /id="PRO_0000195035"
FT   DOMAIN          168..340
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   REGION          594..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         174..181
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         220..224
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         288..291
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   MOD_RES         563
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   647 AA;  74410 MW;  640324779AE4D716 CRC64;
     MQLSWKDIPT VAPANDLLDI VLNRTQRKTP TVIRPGFKIT RIRAFYMRKV KYTGEGFVEK
     FEDILKGFPN INDVHPFHRD LMDTLYEKNH YKISLAAISR AKSLVEQVAR DYVRLLKFGQ
     SLFQCKQLKR AALGRMATIV KKLRDPLAYL EQVRQHIGRL PSIDPNTRTL LICGYPNVGK
     SSFLRCITKS DVDVQPYAFT TKSLYVGHFD YKYLRFQAID TPGILDRPTE EMNNIEMQSI
     YAIAHLRSCV LYFMDLSEQC GFTIEAQVKL FHSIKPLFAN KSVMVVINKT DIIRPEDLDE
     ERAQLLESVK EVPGVEIMTS SCQLEENVME VRNKACEKLL ASRIENKLKS QSRINNVLNK
     IHVAQPQARD DVKRTPFIPE SVKNLKKYDP EDPNRRKLAR DIEAENGGAG VFNVNLKDKY
     LLEDDEWKND IMPEILDGKN VYDFLDPEIA AKLQALEEEE EKLENEGFYN SDDEEEIYDG
     FEASEVDDIK EKAAWIRNRQ KTMIAEARNR KSLKNKAIMP RSKLTKSFGK MEEHMSTLGH
     DMSALQDKQN RAARKNRYVE RGSDVVFGDQ DALTASTENG VKLRQTDRLL DGVADGSMRS
     KADRMAKMER RERNRHAKQG ESDRHNAVSL SKHLFSGKRG VGKTDFR
 
 
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