GSP1_YEAST
ID GSP1_YEAST Reviewed; 219 AA.
AC P32835; D6VYT9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=GTP-binding nuclear protein GSP1/CNR1;
DE AltName: Full=Chromosome stability protein 17;
DE AltName: Full=GTPase Ran homolog;
DE AltName: Full=Genetic suppressor of PRP20-1;
GN Name=GSP1; Synonyms=CNR1, CST17; OrderedLocusNames=YLR293C;
GN ORFNames=L8003.19;
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].
RX PubMed=7687541; DOI=10.1002/j.1460-2075.1993.tb05955.x;
RA Kadowaki T., Goldfarb D., Spitz L.M., Tartakoff A.M., Ohno M.;
RT "Regulation of RNA processing and transport by a nuclear guanine nucleotide
RT release protein and members of the Ras superfamily.";
RL EMBO J. 12:2929-2937(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8455603; DOI=10.1128/mcb.13.4.2152-2161.1993;
RA Belhumeur P., Lee A., Tam R., Dipaolo T., Fortin N., Clark M.W.;
RT "GSP1 and GSP2, genetic suppressors of the prp20-1 mutant in Saccharomyces
RT cerevisiae: GTP-binding proteins involved in the maintenance of nuclear
RT organization.";
RL Mol. Cell. Biol. 13:2152-2161(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP PROTEIN SEQUENCE OF 64-73.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [7]
RP INTERACTION WITH DIS3.
RX PubMed=8896453; DOI=10.1002/j.1460-2075.1996.tb00944.x;
RA Noguchi E., Hayashi N., Azuma Y., Seki T., Nakamura M., Nakashima N.,
RA Yanagida M., He X., Mueller U., Sazer S., Nishimoto T.;
RT "Dis3, implicated in mitotic control, binds directly to Ran and enhances
RT the GEF activity of RCC1.";
RL EMBO J. 15:5595-5605(1996).
RN [8]
RP INTERACTION WITH SRM1.
RX PubMed=11523802; DOI=10.1007/s004380100480;
RA Akhtar N., Hagan H., Lopilato J.E., Corbett A.H.;
RT "Functional analysis of the yeast Ran exchange factor Prp20p: in vivo
RT evidence for the RanGTP gradient model.";
RL Mol. Genet. Genomics 265:851-864(2001).
RN [9]
RP INTERACTION WITH BUD5.
RX PubMed=11589573; DOI=10.1007/s004380100511;
RA Clement M., Lavallee F., Barbes-Morin G., de Repentigny L., Belhumeur P.;
RT "Overexpression of Bud5p can suppress mutations in the Gsp1p guanine
RT nucleotide exchange factor Prp20p in Saccharomyces cerevisiae.";
RL Mol. Genet. Genomics 266:20-27(2001).
RN [10]
RP INTERACTION WITH RRP12.
RX PubMed=14729571; DOI=10.1101/gad.285604;
RA Oeffinger M., Dlakic M., Tollervey D.;
RT "A pre-ribosome-associated HEAT-repeat protein is required for export of
RT both ribosomal subunits.";
RL Genes Dev. 18:196-209(2004).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [12]
RP INTERACTION WITH CEX1.
RX PubMed=17203074; DOI=10.1038/sj.emboj.7601493;
RA McGuire A.T., Mangroo D.;
RT "Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae
RT nuclear tRNA export machinery.";
RL EMBO J. 26:288-300(2007).
CC -!- FUNCTION: GTP-binding protein involved in nucleocytoplasmic transport.
CC Required for the import of protein into the nucleus and also for RNA
CC export. Essential for cell viability. By analogy with Ras, Ran may be
CC activated when GTP is exchanged for bound GDP by RCC1 and inactivated
CC when GTP is hydrolyzed by Ran upon activation by RanGAP1.
CC -!- SUBUNIT: Found in a nuclear export complex with RanGTP, exportin and
CC pre-miRNA (By similarity). Forms a complex with YRB1. Interacts with
CC BUD5, CEX1, RRP12, SRM1, and DIS3/RRP44. {ECO:0000250|UniProtKB:P62825,
CC ECO:0000269|PubMed:11523802, ECO:0000269|PubMed:11589573,
CC ECO:0000269|PubMed:14729571, ECO:0000269|PubMed:17203074,
CC ECO:0000269|PubMed:8896453}.
CC -!- INTERACTION:
CC P32835; P43583: BLM10; NbExp=2; IntAct=EBI-7926, EBI-22761;
CC P32835; P25300: BUD5; NbExp=2; IntAct=EBI-7926, EBI-3853;
CC P32835; P53067: KAP114; NbExp=3; IntAct=EBI-7926, EBI-9174;
CC P32835; O94258: los1; Xeno; NbExp=2; IntAct=EBI-7926, EBI-15799183;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family.
CC {ECO:0000305}.
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DR EMBL; X71945; CAA50747.1; -; Genomic_DNA.
DR EMBL; L08690; AAA34653.1; -; Genomic_DNA.
DR EMBL; U17243; AAB67339.1; -; Genomic_DNA.
DR EMBL; AY558363; AAS56689.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09605.1; -; Genomic_DNA.
DR PIR; S35504; S35504.
DR RefSeq; NP_013396.1; NM_001182181.1.
DR PDB; 2X19; X-ray; 2.80 A; A=8-179.
DR PDB; 3ICQ; X-ray; 3.20 A; B/C=9-179.
DR PDB; 3M1I; X-ray; 2.00 A; A=1-219.
DR PDB; 3WYG; X-ray; 2.15 A; A=1-182.
DR PDBsum; 2X19; -.
DR PDBsum; 3ICQ; -.
DR PDBsum; 3M1I; -.
DR PDBsum; 3WYG; -.
DR AlphaFoldDB; P32835; -.
DR SMR; P32835; -.
DR BioGRID; 31559; 363.
DR DIP; DIP-747N; -.
DR IntAct; P32835; 32.
DR MINT; P32835; -.
DR STRING; 4932.YLR293C; -.
DR BindingDB; P32835; -.
DR MoonDB; P32835; Predicted.
DR TCDB; 9.A.50.1.1; the nuclear t-rna exporter (trna-e) family.
DR iPTMnet; P32835; -.
DR SWISS-2DPAGE; P32835; -.
DR MaxQB; P32835; -.
DR PaxDb; P32835; -.
DR PRIDE; P32835; -.
DR EnsemblFungi; YLR293C_mRNA; YLR293C; YLR293C.
DR GeneID; 851000; -.
DR KEGG; sce:YLR293C; -.
DR SGD; S000004284; GSP1.
DR VEuPathDB; FungiDB:YLR293C; -.
DR eggNOG; KOG0096; Eukaryota.
DR GeneTree; ENSGT00940000153786; -.
DR HOGENOM; CLU_041217_13_0_1; -.
DR InParanoid; P32835; -.
DR OMA; IRFNIWD; -.
DR BioCyc; YEAST:G3O-32388-MON; -.
DR Reactome; R-SCE-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR EvolutionaryTrace; P32835; -.
DR PRO; PR:P32835; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32835; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0006997; P:nucleus organization; IGI:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:1901987; P:regulation of cell cycle phase transition; IDA:SGD.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IDA:SGD.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002041; Ran_GTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR24071; PTHR24071; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00627; GTPRANTC4.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51418; RAN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; GTP-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377"
FT CHAIN 2..219
FT /note="GTP-binding nuclear protein GSP1/CNR1"
FT /id="PRO_0000208733"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT BINDING 70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT BINDING 152..154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P62825"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:3M1I"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:3M1I"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:3M1I"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:3M1I"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3M1I"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:3M1I"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:3M1I"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:3M1I"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:3M1I"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3ICQ"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:3M1I"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3M1I"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:3M1I"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:3M1I"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:3M1I"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:3M1I"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:3M1I"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:3M1I"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:3M1I"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:3M1I"
SQ SEQUENCE 219 AA; 24810 MW; C9D027033F8C70E1 CRC64;
MSAPAANGEV PTFKLVLVGD GGTGKTTFVK RHLTGEFEKK YIATIGVEVH PLSFYTNFGE
IKFDVWDTAG QEKFGGLRDG YYINAQCAII MFDVTSRITY KNVPNWHRDL VRVCENIPIV
LCGNKVDVKE RKVKAKTITF HRKKNLQYYD ISAKSNYNFE KPFLWLARKL AGNPQLEFVA
SPALAPPEVQ VDEQLMQQYQ QEMEQATALP LPDEDDADL
