GTP-binding nuclear protein GSP1/CNR1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P32835 (GSP1_YEAST)

Last modified June 16, 2009. Version 92. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    GTP-binding nuclear protein GSP1/CNR1
Alternative name(s):
    GTPase Ran homolog
    Genetic suppressor of PRP20-1
    Chromosome stability protein 17

Gene names

Name:	GSP1
Synonyms:	CNR1, CST17
Ordered Locus Names:	YLR293C
ORF Names:	L8003.19

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	219 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Essential for cell viability. By analogy with Ras, Ran may be activated when GTP is exchanged for bound GDP by RCC1 and inactivated when GTP is hydrolyzed by Ran upon activation by RanGAP1.
Subunit structure	Forms a complex with YRB1. Interacts with BUD5, RRP12 and DIS3/RRP44. Ref.6 Ref.7 Ref.8
Subcellular location	Nucleus.
Sequence similarities	Belongs to the small GTPase superfamily. Ran family.

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Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Nucleus
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from mutant phenotype. Source: SGD intracellular protein transport Inferred from electronic annotation. Source: InterPro nucleocytoplasmic transport Traceable author statement. Source: SGD nucleus organization Ref.2 Inferred from genetic interaction. Source: SGD regulation of chromatin silencing at telomere Inferred from mutant phenotype. Source: SGD signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Traceable author statement. Source: SGD nucleus Ref.2 Inferred from direct assay. Source: SGD
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Ref.2 Inferred from genetic interaction. Source: SGD protein binding Ref.7 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
BUD5	P25300	2	EBI-7926,EBI-3853
SSM4	P40318	1	EBI-7926,EBI-18208

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 219

219

GTP-binding nuclear protein GSP1/CNR1

PRO_0000208733

Regions

Nucleotide binding

19 – 26

GTP By similarity

Nucleotide binding

67 – 71

GTP By similarity

Nucleotide binding

124 – 127

GTP By similarity

Amino acid modifications

Modified residue

181

Phosphoserine Ref.9

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Sequences

Sequence

Length

Mass (Da)

Tools

P32835-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: C9D027033F8C70E1
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FASTA

219

24,810

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation of RNA processing and transport by a nuclear guanine nucleotide release protein and members of the Ras superfamily." Kadowaki T., Goldfarb D., Spitz L.M., Tartakoff A.M., Ohno M. EMBO J. 12:2929-2937(1993) [PubMed: 7687541] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"GSP1 and GSP2, genetic suppressors of the prp20-1 mutant in Saccharomyces cerevisiae: GTP-binding proteins involved in the maintenance of nuclear organization." Belhumeur P., Lee A., Tam R., Dipaolo T., Fortin N., Clark M.W. Mol. Cell. Biol. 13:2152-2161(1993) [PubMed: 8455603] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." 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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." 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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Protein identifications for a Saccharomyces cerevisiae protein database." Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S. Electrophoresis 15:1466-1486(1994) [PubMed: 7895733] [Abstract] Cited for: PROTEIN SEQUENCE OF 64-73. Strain: ATCC 204508 / S288c.
[6]	"Dis3, implicated in mitotic control, binds directly to Ran and enhances the GEF activity of RCC1." Noguchi E., Hayashi N., Azuma Y., Seki T., Nakamura M., Nakashima N., Yanagida M., He X., Mueller U., Sazer S., Nishimoto T. EMBO J. 15:5595-5605(1996) [PubMed: 8896453] [Abstract] Cited for: INTERACTION WITH DIS3.
[7]	"Overexpression of Bud5p can suppress mutations in the Gsp1p guanine nucleotide exchange factor Prp20p in Saccharomyces cerevisiae." Clement M., Lavallee F., Barbes-Morin G., de Repentigny L., Belhumeur P. Mol. Genet. Genomics 266:20-27(2001) [PubMed: 11589573] [Abstract] Cited for: INTERACTION WITH BUD5.
[8]	"A pre-ribosome-associated HEAT-repeat protein is required for export of both ribosomal subunits." Oeffinger M., Dlakic M., Tollervey D. Genes Dev. 18:196-209(2004) [PubMed: 14729571] [Abstract] Cited for: INTERACTION WITH RRP12.
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	X71945 Genomic DNA. Translation: CAA50747.1. L08690 Genomic DNA. Translation: AAA34653.1. U17243 Genomic DNA. Translation: AAB67339.1. AY558363 Genomic DNA. Translation: AAS56689.1.
PIR	S35504.
RefSeq	NP_013396.1.
3D structure databases
HSSP	HSSP built from PDB template 1I2M based on UniProtKB P17080.
SMR	P32835. Positions 5-216.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:747N.
IntAct	P32835. 13 interactions.
Protein family/group databases
TCDB	9.A.50.1.1. nuclear t-RNA exporter (t-Exporter) family.
2-D gel databases
SWISS-2DPAGE	P32835.
Proteomic databases
PeptideAtlas	P32835.
PRIDE	P32835.
Genome annotation databases
Ensembl	YLR293C. Saccharomyces cerevisiae. [Contig view]
GeneID	851000.
GenomeReviews	Gene locus YLR293C in contig Y13138_GR.
KEGG	sce:YLR293C.
NMPDR	fig\|4932.3.peg.4413.
Organism-specific databases
CYGD	YLR293c.
SGD	S000004284. GSP1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P32835.
OMA	P32835. MERRELT.
Gene expression databases
GermOnline	YLR293C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR018210. GTP-bd_nuclear_protein_CS. IPR002041. Ran_GTPase. IPR013753. Ras. IPR005225. Small_GTP_bd. [Graphical view]
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00627. GTPRANTC4.
SMART	SM00176. RAN. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51418. RAN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	967543.

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Entry information

Entry name

GSP1_YEAST

Accession

Primary (citable) accession number: P32835

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents