GTP-binding nuclear protein GSP1/CNR1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32835 (GSP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 121. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
GTP-binding nuclear protein GSP1/CNR1

Alternative name(s):
Chromosome stability protein 17
GTPase Ran homolog
Genetic suppressor of PRP20-1

Gene names

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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	219 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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, CEX1, RRP12, SRM1, and DIS3/RRP44. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Subcellular location	Nucleus.
Sequence similarities	Belongs to the small GTPase superfamily. Ran family.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Nucleus
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
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 Inferred from genetic interaction Ref.2. Source: SGD regulation of chromatin silencing at telomere Inferred from mutant phenotype. Source: SGD small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Traceable author statement. Source: SGD nucleus Inferred from direct assay Ref.2. Source: SGD
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from genetic interaction Ref.2. Source: SGD protein binding Inferred from physical interaction Ref.9. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BUD5	P25300	2	EBI-7926,EBI-3853
MOG1	P47123	4	EBI-7926,EBI-11145

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.12

Secondary structure

219

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P32835 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: C9D027033F8C70E1
Show »

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

« Hide

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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"Functional analysis of the yeast Ran exchange factor Prp20p: in vivo evidence for the RanGTP gradient model." Akhtar N., Hagan H., Lopilato J.E., Corbett A.H. Mol. Genet. Genomics 265:851-864(2001) [PubMed: 11523802] [Abstract] Cited for: INTERACTION WITH SRM1.
[9]	"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.
[10]	"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.
[11]	"Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae nuclear tRNA export machinery." McGuire A.T., Mangroo D. EMBO J. 26:288-300(2007) [PubMed: 17203074] [Abstract] Cited for: INTERACTION WITH CEX1.
[12]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X71945 Genomic DNA. Translation: CAA50747.1.
L08690 Genomic DNA. Translation: AAA34653.1.
U17243 Genomic DNA. Translation: AAB67339.1.
AY558363 Genomic DNA. Translation: AAS56689.1.
BK006945 Genomic DNA. Translation: DAA09605.1.

PIR

S35504.

RefSeq

NP_013396.1. NM_001182181.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2X19	X-ray	2.80	A	8-179	[»]
3ICQ	X-ray	3.20	B/C	9-179	[»]
3M1I	X-ray	2.00	A	1-219	[»]

ProteinModelPortal

P32835.

SMR

P32835. Positions 8-217.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-747N.

IntAct

P32835. 18 interactions.

MINT

MINT-384649.

STRING

P32835.

Protein family/group databases

TCDB

9.A.50.1.1. nuclear t-RNA exporter (t-Exporter) family.

2D gel databases

SWISS-2DPAGE

P32835.

Proteomic databases

PeptideAtlas

P32835.

PRIDE

P32835.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLR293C; YLR293C; YLR293C.

GeneID

851000.

KEGG

sce:YLR293C.

NMPDR

fig|4932.3.peg.4413.

Organism-specific databases

CYGD

YLR293c.

SGD

S000004284. GSP1.

Phylogenomic databases

eggNOG

fuNOG04440.

GeneTree

EFGT00050000002458.

HOGENOM

HBG745225.

OMA

HIPRWES.

OrthoDB

EOG4JT3FH.

Gene expression databases

ArrayExpress

P32835.

Genevestigator

P32835.

GermOnline

YLR293C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002041. Ran_GTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]

K07936.

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

NextBio

967543.

Entry information

Entry name

GSP1_YEAST

Accession

Primary (citable) accession number: P32835
Secondary accession number(s): D6VYT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	December 14, 2011
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents