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Protein

Ran-specific GTPase-activating protein 1

Gene

YRB1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Important for the export of protein containing nuclear export signal (NES) out of the nucleus. Stimulates the GTPase activity of GSP1 and GSP2.

GO - Molecular functioni

  1. GTPase activator activity Source: UniProtKB-KW
  2. Ran GTPase binding Source: SGD

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: SGD
  2. protein import into nucleus Source: SGD
  3. RNA export from nucleus Source: SGD
  4. ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29624-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ran-specific GTPase-activating protein 1
Alternative name(s):
Chromosome stability protein 20
Perinuclear array-localized protein
Ran-binding protein 1
Short name:
RANBP1
Gene namesi
Name:YRB1
Synonyms:CST20, HTN1, SFO1
Ordered Locus Names:YDR002W
ORF Names:YD8119.08
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR002w.
SGDiS000002409. YRB1.

Subcellular locationi

Cytoplasm. Nucleus
Note: Shuttles between the nucleus and cytoplasm.

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Ran-specific GTPase-activating protein 1PRO_0000213670Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41920.
PaxDbiP41920.
PeptideAtlasiP41920.
PRIDEiP41920.

Expressioni

Gene expression databases

GenevestigatoriP41920.

Interactioni

Subunit structurei

Interacts with GSP1 and PRP20.

Protein-protein interaction databases

BioGridi32055. 68 interactions.
DIPiDIP-838N.
IntActiP41920. 4 interactions.
MINTiMINT-398068.
STRINGi4932.YDR002W.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi83 – 9715Combined sources
Turni98 – 1014Combined sources
Beta strandi102 – 11615Combined sources
Turni117 – 1193Combined sources
Beta strandi122 – 1276Combined sources
Turni129 – 1313Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi153 – 16311Combined sources
Beta strandi165 – 1684Combined sources
Beta strandi170 – 18011Combined sources
Helixi181 – 19919Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M1IX-ray2.00B11-201[»]
4GMXX-ray2.10B62-201[»]
4GPTX-ray2.22B62-201[»]
4HATX-ray1.78B62-201[»]
4HAUX-ray2.00B62-201[»]
4HAVX-ray2.00B62-201[»]
4HAWX-ray1.90B62-201[»]
4HAXX-ray2.28B62-201[»]
4HAYX-ray2.30B62-201[»]
4HAZX-ray1.90B62-201[»]
4HB0X-ray2.20B62-201[»]
4HB2X-ray1.80B62-201[»]
4HB3X-ray2.80B62-201[»]
4HB4X-ray2.05B62-201[»]
ProteinModelPortaliP41920.
SMRiP41920. Positions 71-201.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41920.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 200137RanBD1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RANBP1 family.Curated
Contains 1 RanBD1 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5171.
GeneTreeiENSGT00720000108825.
HOGENOMiHOG000176323.
InParanoidiP41920.
KOiK15306.
OMAiLKHRENG.
OrthoDBiEOG7TF7N6.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
[Graphical view]
PfamiPF00638. Ran_BP1. 1 hit.
[Graphical view]
SMARTiSM00160. RanBD. 1 hit.
[Graphical view]
PROSITEiPS50196. RANBD1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41920-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSEDKKPVV DKKEEAAPKP PSSAVFSMFG GKKAEKPETK KDEEDTKEET
60 70 80 90 100
KKEGDDAPES PDIHFEPVVH LEKVDVKTME EDEEVLYKVR AKLFRFDADA
110 120 130 140 150
KEWKERGTGD CKFLKNKKTN KVRILMRRDK TLKICANHII APEYTLKPNV
160 170 180 190 200
GSDRSWVYAC TADIAEGEAE AFTFAIRFGS KENADKFKEE FEKAQEINKK

A
Length:201
Mass (Da):22,953
Last modified:October 31, 1995 - v1
Checksum:i46C3766B0906A75B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z33503 Genomic DNA. Translation: CAA83911.1.
X65925 Genomic DNA. No translation available.
L38489 Genomic DNA. Translation: AAA57276.1.
Z48008 Genomic DNA. Translation: CAA88062.1.
BK006938 Genomic DNA. Translation: DAA11849.1.
PIRiS50219.
RefSeqiNP_010285.1. NM_001180310.1.

Genome annotation databases

EnsemblFungiiYDR002W; YDR002W; YDR002W.
GeneIDi851565.
KEGGisce:YDR002W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z33503 Genomic DNA. Translation: CAA83911.1.
X65925 Genomic DNA. No translation available.
L38489 Genomic DNA. Translation: AAA57276.1.
Z48008 Genomic DNA. Translation: CAA88062.1.
BK006938 Genomic DNA. Translation: DAA11849.1.
PIRiS50219.
RefSeqiNP_010285.1. NM_001180310.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M1IX-ray2.00B11-201[»]
4GMXX-ray2.10B62-201[»]
4GPTX-ray2.22B62-201[»]
4HATX-ray1.78B62-201[»]
4HAUX-ray2.00B62-201[»]
4HAVX-ray2.00B62-201[»]
4HAWX-ray1.90B62-201[»]
4HAXX-ray2.28B62-201[»]
4HAYX-ray2.30B62-201[»]
4HAZX-ray1.90B62-201[»]
4HB0X-ray2.20B62-201[»]
4HB2X-ray1.80B62-201[»]
4HB3X-ray2.80B62-201[»]
4HB4X-ray2.05B62-201[»]
ProteinModelPortaliP41920.
SMRiP41920. Positions 71-201.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32055. 68 interactions.
DIPiDIP-838N.
IntActiP41920. 4 interactions.
MINTiMINT-398068.
STRINGi4932.YDR002W.

Proteomic databases

MaxQBiP41920.
PaxDbiP41920.
PeptideAtlasiP41920.
PRIDEiP41920.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR002W; YDR002W; YDR002W.
GeneIDi851565.
KEGGisce:YDR002W.

Organism-specific databases

CYGDiYDR002w.
SGDiS000002409. YRB1.

Phylogenomic databases

eggNOGiCOG5171.
GeneTreeiENSGT00720000108825.
HOGENOMiHOG000176323.
InParanoidiP41920.
KOiK15306.
OMAiLKHRENG.
OrthoDBiEOG7TF7N6.

Enzyme and pathway databases

BioCyciYEAST:G3O-29624-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP41920.
NextBioi969007.
PROiP41920.

Gene expression databases

GenevestigatoriP41920.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
[Graphical view]
PfamiPF00638. Ran_BP1. 1 hit.
[Graphical view]
SMARTiSM00160. RanBD. 1 hit.
[Graphical view]
PROSITEiPS50196. RANBD1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast homologue of mammalian Ran binding protein 1."
    Butler G., Wolfe K.H.
    Biochim. Biophys. Acta 1219:711-712(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: H9.
  2. "Molecular analysis of the neutral trehalase gene from Saccharomyces cerevisiae."
    Kopp M., Mueller H., Holzer H.
    J. Biol. Chem. 268:4766-4774(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Ran-binding protein-1 is an essential component of the Ran/RCC1 molecular switch system in budding yeast."
    Ouspenski I.I., Mueller U.W., Matynia A., Sazer S., Elledge S.J., Brinkley B.R.
    J. Biol. Chem. 270:1975-1978(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  4. Trueheart J., Richards S., Macara I.G., Thorner J.
    Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "Mutants in a yeast Ran binding protein are defective in nuclear transport."
    Schlenstedt G., Wong D.H., Koepp D.M., Silver P.A.
    EMBO J. 14:5367-5378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. "Yeast Ran-binding protein 1 (Yrb1) shuttles between the nucleus and cytoplasm and is exported from the nucleus via a CRM1 (XPO1)-dependent pathway."
    Kunzler M., Gerstberger T., Stutz F., Bischoff F.R., Hurt E.
    Mol. Cell. Biol. 20:4295-4308(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiYRB1_YEAST
AccessioniPrimary (citable) accession number: P41920
Secondary accession number(s): D6VRY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1995
Last sequence update: October 31, 1995
Last modified: January 6, 2015
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.