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YEAST:RNA1

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) RNA1
Protein Name(s) Ran GTPase-activating protein 1

Protein involved in RNA production/processing

External Links
UniProt P11745
EMBL M27143
M27142
X17376
Z49939
X57160
BK006946
PIR A32492
RefSeq NP_013962.1
ProteinModelPortal P11745
SMR P11745
BioGrid 35413
DIP DIP-2509N
IntAct P11745
MINT MINT-558123
iPTMnet P11745
MaxQB P11745
PeptideAtlas P11745
EnsemblFungi [example_ID YMR235C]
GeneID 855275
KEGG sce:YMR235C
EuPathDB FungiDB:YMR235C
SGD S000004848
GeneTree ENSGT00440000039203
HOGENOM HOG000195026
InParanoid P11745
KO K14319
OMA DLQDNAF
OrthoDB EOG71ZPB0
BioCyc YEAST:G3O-32916-MONOMER
NextBio 978897
PRO PR:P11745
Proteomes UP000002311
GO GO:0000781
GO:0005829
GO:0005634
GO:0005096
GO:0006348
GO:0043547
GO:0006606
GO:0000054
GO:0006404
GO:0006407
GO:0006409
Gene3D 3.80.10.10
InterPro IPR032675
IPR027038
PANTHER PTHR24113

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0005737

cytoplasm

PMID:2116418[1]

ECO:0000314

C

Fig. 7 A shows the fractionation of endogenous levels of RNA1 protein as detected by an anti-peptide serum. The cytoplasm-enriched fraction (lanes 3 and 11) contain antigen, but there is no antigen detected in the purified nuclear fraction (lanes 1 and 10).

complete
CACAO 11788

involved_in

GO:0006606

protein import into nucleus

PMID:7657689[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006409

tRNA export from nucleus

PMID:22008473[3]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:Q12453

P

Seeded From UniProt

complete

involved_in

GO:0006409

tRNA export from nucleus

PMID:22008473[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006407

rRNA export from nucleus

PMID:11739405[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006404

RNA import into nucleus

PMID:16040803[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006348

chromatin silencing at telomere

PMID:17904525[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:2116418[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:8755533[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:8755533[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005096

GTPase activator activity

PMID:7657689[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005096

GTPase activator activity

PMID:9305944[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0000054

ribosomal subunit export from nucleus

PMID:11739405[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0000781

chromosome, telomeric region

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0006348

C

Seeded From UniProt

complete

involved_in

GO:0043547

positive regulation of GTPase activity

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0005096

P

Seeded From UniProt

complete

involved_in

GO:0043547

positive regulation of GTPase activity

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0005096

P

Seeded From UniProt

complete

involved_in

GO:0043547

positive regulation of GTPase activity

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0005096

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0005096

GTPase activator activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0343

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Hopper, AK et al. (1990) The yeast RNA1 gene product necessary for RNA processing is located in the cytosol and apparently excluded from the nucleus. J. Cell Biol. 111 309-21 PubMed GONUTS page
  2. 2.0 2.1 Corbett, AH et al. (1995) Rna1p, a Ran/TC4 GTPase activating protein, is required for nuclear import. J. Cell Biol. 130 1017-26 PubMed GONUTS page
  3. 3.0 3.1 McGuire, AT & Mangroo, D (2012) Cex1p facilitates Rna1p-mediated dissociation of the Los1p-tRNA-Gsp1p-GTP export complex. Traffic 13 234-56 PubMed GONUTS page
  4. 4.0 4.1 Gleizes, PE et al. (2001) Ultrastructural localization of rRNA shows defective nuclear export of preribosomes in mutants of the Nup82p complex. J. Cell Biol. 155 923-36 PubMed GONUTS page
  5. Shaheen, HH & Hopper, AK (2005) Retrograde movement of tRNAs from the cytoplasm to the nucleus in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 102 11290-5 PubMed GONUTS page
  6. Hayashi, N et al. (2007) Mutations in Ran system affected telomere silencing in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 363 788-94 PubMed GONUTS page
  7. 7.0 7.1 Traglia, HM et al. (1996) Nucleus-associated pools of Rna1p, the Saccharomyces cerevisiae Ran/TC4 GTPse activating protein involved in nucleus/cytosol transit. Proc. Natl. Acad. Sci. U.S.A. 93 7667-72 PubMed GONUTS page
  8. Haberland, J et al. (1997) The acidic C-terminal domain of rna1p is required for the binding of Ran.GTP and for RanGAP activity. J. Biol. Chem. 272 24717-26 PubMed GONUTS page