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LSG1_YEAST
ID   LSG1_YEAST              Reviewed;         640 AA.
AC   P53145; D6VU46;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 184.
DE   RecName: Full=Large subunit GTPase 1;
DE            EC=3.6.1.-;
GN   Name=LSG1; OrderedLocusNames=YGL099W;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9290212;
RX   DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA   Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT   "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT   chromosome VII.";
RL   Yeast 13:1077-1090(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [3]
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   [4]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH 60S RIBOSOMAL SUBUNIT.
RX   PubMed=12773575; DOI=10.1128/mcb.23.12.4344-4355.2003;
RA   Kallstrom G., Hedges J., Johnson A.;
RT   "The putative GTPases Nog1p and Lsg1p are required for 60S ribosomal
RT   subunit biogenesis and are localized to the nucleus and cytoplasm,
RT   respectively.";
RL   Mol. Cell. Biol. 23:4344-4355(2003).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
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   [7]
RP   FUNCTION, AND MUTAGENESIS OF ILE-204 AND LYS-349.
RX   PubMed=15660131; DOI=10.1038/sj.emboj.7600547;
RA   Hedges J., West M., Johnson A.W.;
RT   "Release of the export adapter, Nmd3p, from the 60S ribosomal subunit
RT   requires Rpl10p and the cytoplasmic GTPase Lsg1p.";
RL   EMBO J. 24:567-579(2005).
RN   [8]
RP   FUNCTION.
RX   PubMed=15831484; DOI=10.1128/mcb.25.9.3802-3813.2005;
RA   West M., Hedges J.B., Chen A., Johnson A.W.;
RT   "Defining the order in which Nmd3p and Rpl10p load onto nascent 60S
RT   ribosomal subunits.";
RL   Mol. Cell. Biol. 25:3802-3813(2005).
RN   [9]
RP   INTERACTION WITH ARB1.
RX   PubMed=16260602; DOI=10.1128/mcb.25.22.9859-9873.2005;
RA   Dong J., Lai R., Jennings J.L., Link A.J., Hinnebusch A.G.;
RT   "The novel ATP-binding cassette protein ARB1 is a shuttling factor that
RT   stimulates 40S and 60S ribosome biogenesis.";
RL   Mol. Cell. Biol. 25:9859-9873(2005).
RN   [10]
RP   FUNCTION.
RX   PubMed=17015443; DOI=10.1074/jbc.m606798200;
RA   Hedges J., Chen Y.I., West M., Bussiere C., Johnson A.W.;
RT   "Mapping the functional domains of yeast NMD3, the nuclear export adapter
RT   for the 60 S ribosomal subunit.";
RL   J. Biol. Chem. 281:36579-36587(2006).
RN   [11]
RP   FUNCTION.
RX   PubMed=17761675; DOI=10.1074/jbc.m705057200;
RA   Hofer A., Bussiere C., Johnson A.W.;
RT   "Mutational analysis of the ribosomal protein Rpl10 from yeast.";
RL   J. Biol. Chem. 282:32630-32639(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103, 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: GTPase required for the nuclear export of the 60S ribosomal
CC       subunit. Acts by mediating the release of NMD3 from the 60S ribosomal
CC       subunit after export into the cytoplasm. {ECO:0000269|PubMed:15660131,
CC       ECO:0000269|PubMed:15831484, ECO:0000269|PubMed:17015443,
CC       ECO:0000269|PubMed:17761675}.
CC   -!- SUBUNIT: Associates with the 60S ribosomal subunit. Interacts with
CC       ARB1. {ECO:0000269|PubMed:12773575, ECO:0000269|PubMed:16260602}.
CC   -!- INTERACTION:
CC       P53145; P38344: REI1; NbExp=5; IntAct=EBI-23885, EBI-21136;
CC       P53145; Q12522: TIF6; NbExp=5; IntAct=EBI-23885, EBI-9046;
CC       P53145; Q02256: YVH1; NbExp=3; IntAct=EBI-23885, EBI-14322;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12773575,
CC       ECO:0000269|PubMed:14562095}.
CC   -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC       characterized by a circular permutation of the GTPase motifs described
CC       by a G4-G1-G3 pattern.
CC   -!- MISCELLANEOUS: Present with 19400 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. LSG1
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR   EMBL; Z72621; CAA96805.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08007.1; -; Genomic_DNA.
DR   PIR; S64106; S64106.
DR   RefSeq; NP_011416.3; NM_001180964.3.
DR   PDB; 5T62; EM; 3.30 A; W=1-640.
DR   PDB; 6N8N; EM; 3.80 A; W=1-640.
DR   PDB; 6N8O; EM; 3.50 A; W=1-640.
DR   PDB; 6QIK; EM; 3.10 A; o=1-640.
DR   PDB; 6QTZ; EM; 3.50 A; o=1-640.
DR   PDB; 6RI5; EM; 3.30 A; o=1-640.
DR   PDB; 6RZZ; EM; 3.20 A; o=1-640.
DR   PDB; 6S05; EM; 3.90 A; o=1-640.
DR   PDBsum; 5T62; -.
DR   PDBsum; 6N8N; -.
DR   PDBsum; 6N8O; -.
DR   PDBsum; 6QIK; -.
DR   PDBsum; 6QTZ; -.
DR   PDBsum; 6RI5; -.
DR   PDBsum; 6RZZ; -.
DR   PDBsum; 6S05; -.
DR   AlphaFoldDB; P53145; -.
DR   SMR; P53145; -.
DR   BioGRID; 33150; 146.
DR   DIP; DIP-6659N; -.
DR   IntAct; P53145; 37.
DR   MINT; P53145; -.
DR   STRING; 4932.YGL099W; -.
DR   iPTMnet; P53145; -.
DR   MaxQB; P53145; -.
DR   PaxDb; P53145; -.
DR   PRIDE; P53145; -.
DR   EnsemblFungi; YGL099W_mRNA; YGL099W; YGL099W.
DR   GeneID; 852779; -.
DR   KEGG; sce:YGL099W; -.
DR   SGD; S000003067; LSG1.
DR   VEuPathDB; FungiDB:YGL099W; -.
DR   eggNOG; KOG1424; Eukaryota.
DR   GeneTree; ENSGT00940000156442; -.
DR   HOGENOM; CLU_011072_2_0_1; -.
DR   InParanoid; P53145; -.
DR   OMA; VNKADMM; -.
DR   BioCyc; YEAST:G3O-30599-MON; -.
DR   PRO; PR:P53145; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53145; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR   GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISS:SGD.
DR   GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR   GO; GO:0000054; P:ribosomal subunit export from nucleus; IMP:SGD.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR043358; GNL1-like.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45709; PTHR45709; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..640
FT                   /note="Large subunit GTPase 1"
FT                   /id="PRO_0000122454"
FT   DOMAIN          188..394
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..630
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         236..239
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         343..350
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000305"
FT   BINDING         387..390
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         103
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MUTAGEN         204
FT                   /note="I->T: Impairs the nuclear export of 60S ribosomal
FT                   subunit in cytoplasm."
FT                   /evidence="ECO:0000269|PubMed:15660131"
FT   MUTAGEN         349
FT                   /note="K->T: Dominant negative mutant; prevents the nuclear
FT                   export of 60S ribosomal subunit in cytoplasm."
FT                   /evidence="ECO:0000269|PubMed:15660131"
SQ   SEQUENCE   640 AA;  72728 MW;  15FD76541A2E8410 CRC64;
     MPPKEAPKKW KAPKGPKPTH RKNKNKLELG RAIKYARQKE NAIEYLPDGE MRFTTDKHEA
     NWVKLRSVTQ ESALDEFLST AALADKDFTA DRHSNVKIIR MDSGNDSATS QGFSMTNEQR
     GNLNAKQRAL AKDLIVPRRP EWNEGMSKFQ LDRQEKEAFL EWRRKLAHLQ ESNEDLLLTP
     FERNIEVWKQ LWRVVERSDL VVQIVDARNP LLFRSVDLER YVKESDDRKA NLLLVNKADL
     LTKKQRIAWA KYFISKNISF TFYSALRANQ LLEKQKEMGE DYREQDFEEA DKEGFDADEK
     VMEKVKILSI DQLEELFLSK APNEPLLPPL PGQPPLINIG LVGYPNVGKS STINSLVGAK
     KVSVSSTPGK TKHFQTIKLS DSVMLCDCPG LVFPNFAYNK GELVCNGVLP IDQLRDYIGP
     AGLVAERIPK YYIEAIYGIH IQTKSRDEGG NGDIPTAQEL LVAYARARGY MTQGYGSADE
     PRASRYILKD YVNGKLLYVN PPPHLEDDTP YTREECEEFN KDLYVFDRLP DTRKEQVQNA
     AKAKGIDIVD LARDLNQLTF SAHTGGDTQK EAKSVTHGGK QAALYNAAED LDRDFFKMNN
     VEGRLSTPFH KVQNSSAGKR HNKKNKSKNA KSKVFSIENN
 
 
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