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UniProtKB/Swiss-Prot entry P32835


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GSP1_YEAST
Primary accession number P32835
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on October 1, 1993 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 82)
Name and origin of the protein
Protein name GTP-binding nuclear protein GSP1/CNR1
Synonym Chromosome stability protein 17
Gene name
Name: GSP1
Synonyms: CNR1, CST17
OrderedLocusNames: YLR293C
ORFNames: L8003.19
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8455603 [NCBI, ExPASy, EBI, Israel, Japan]
Belhumeur P., Lee A., Tam R., Dipaolo T., Fortin N., Clark M.W.;
"GSP1 and GSP2, genetic suppressors of the prp20-1 mutant in Saccharomyces cerevisiae: GTP-binding proteins involved in the maintenance of nuclear organization.";
Mol. Cell. Biol. 13:2152-2161(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7687541 [NCBI, ExPASy, EBI, Israel, Japan]
Kadowaki T., Goldfarb D., Spitz L.M., Tartakoff A.M., Ohno M.;
"Regulation of RNA processing and transport by a nuclear guanine nucleotide release protein and members of the Ras superfamily.";
EMBO J. 12:2929-2937(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169871 [NCBI, ExPASy, EBI, Israel, Japan]
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
PROTEIN SEQUENCE OF 64-73.
STRAIN=ATCC 204508 / S288c;
PubMed=7895733 [NCBI, ExPASy, EBI, Israel, Japan]
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein database.";
Electrophoresis 15:1466-1486(1994).
[6]
INTERACTION WITH BUD5.
DOI=10.1007/s004380100511; PubMed=11589573 [NCBI, ExPASy, EBI, Israel, Japan]
Clement M., Lavallee F., Barbes-Morin G., de Repentigny L., Belhumeur P.;
"Overexpression of Bud5p can suppress mutations in the Gsp1p guanine nucleotide exchange factor Prp20p in Saccharomyces cerevisiae.";
Mol. Genet. Genomics 266:20-27(2001).
[7]
INTERACTION WITH RRP12.
DOI=10.1101/gad.285604; PubMed=14729571 [NCBI, ExPASy, EBI, Israel, Japan]
Oeffinger M., Dlakic M., Tollervey D.;
"A pre-ribosome-associated HEAT-repeat protein is required for export of both ribosomal subunits.";
Genes Dev. 18:196-209(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L08690; AAA34653.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X71945; CAA50747.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U17243; AAB67339.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY558363; AAS56689.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S35504; S35504.
RefSeq NP_013396.1; -.
3D structure databases
HSSP P17080; 1I2M. [HSSP ENTRY / PDB]
SMR P32835; 5-216.
ModBase P32835.
Protein-protein interaction databases
DIP DIP:747N; -.
IntAct P32835; -.
2D gel databases
SWISS-2DPAGE P32835; -.
Organism-specific databases
CYGD YLR293c; -.
SGD S000004284; GSP1.
Yeast-GFP YLR293C.
Gene expression databases
GermOnline YLR293C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0003924; Molecular function: GTPase activity (inferred from genetic interaction from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006997; Biological process: nuclear organization and biogenesis (inferred from genetic interaction from SGD).
GO:0006913; Biological process: nucleocytoplasmic transport (traceable author statement from SGD).
GO:0006364; Biological process: rRNA processing (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR002041; Ran_GTPase.
IPR013753; Ras.
IPR001806; Ras_trnsfrmng.
IPR005225; Small_GTP_bd.
Graphical view of domain structure.
Pfam PF00071; Ras; 1.
Pfam graphical view of domain structure.
PRINTS PR00627; GTPRANTC4.
PR00449; RASTRNSFRMNG.
SMART SM00176; RAN; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00231; small_GTP; 1.
PROSITE PS01115; RAN; 1.
BLOCKS P32835.
Proteomic databases
PeptideAtlas P32835; -.
Genome annotation databases
Ensembl YLR293C; Saccharomyces cerevisiae. [Contig view]
GeneID 851000; -.
GenomeReviews Y13138_GR; YLR293C.
KEGG sce:YLR293C; -.
NMPDR fig|4932.3.peg.4413; -.
Phylogenomic databases
HOGENOM P32835; -.
Other
LinkHub P32835; -.
ProtoNet P32835.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   219  219     GTP-binding nuclear protein GSP1/CNR1. PRO_0000208733
NP_BIND   19    26  8     GTP (By similarity). 
NP_BIND   67    71  5     GTP (By similarity). 
NP_BIND   124   127  4     GTP (By similarity). 
MOD_RES   181   181        Phosphoserine. 
Sequence information
Length: 219 AA [This is the length of the unprocessed precursor] Molecular weight: 24810 Da [This is the MW of the unprocessed precursor] CRC64: C9D027033F8C70E1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSAPAANGEV PTFKLVLVGD GGTGKTTFVK RHLTGEFEKK YIATIGVEVH PLSFYTNFGE 

        70         80         90        100        110        120 
IKFDVWDTAG QEKFGGLRDG YYINAQCAII MFDVTSRITY KNVPNWHRDL VRVCENIPIV 

       130        140        150        160        170        180 
LCGNKVDVKE RKVKAKTITF HRKKNLQYYD ISAKSNYNFE KPFLWLARKL AGNPQLEFVA 

       190        200        210 
SPALAPPEVQ VDEQLMQQYQ QEMEQATALP LPDEDDADL 

P32835 in FASTA format

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