YRB1_YEAST
ID YRB1_YEAST Reviewed; 201 AA.
AC P41920; D6VRY9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ran-specific GTPase-activating protein 1;
DE AltName: Full=Chromosome stability protein 20;
DE AltName: Full=Perinuclear array-localized protein;
DE AltName: Full=Ran-binding protein 1;
DE Short=RANBP1;
GN Name=YRB1; Synonyms=CST20, HTN1, SFO1; OrderedLocusNames=YDR002W;
GN ORFNames=YD8119.08;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H9;
RX PubMed=7948031; DOI=10.1016/0167-4781(94)90233-x;
RA Butler G., Wolfe K.H.;
RT "Yeast homologue of mammalian Ran binding protein 1.";
RL Biochim. Biophys. Acta 1219:711-712(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8444853; DOI=10.1016/s0021-9258(18)53463-3;
RA Kopp M., Mueller H., Holzer H.;
RT "Molecular analysis of the neutral trehalase gene from Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 268:4766-4774(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=7836422; DOI=10.1074/jbc.270.5.1975;
RA Ouspenski I.I., Mueller U.W., Matynia A., Sazer S., Elledge S.J.,
RA Brinkley B.R.;
RT "Ran-binding protein-1 is an essential component of the Ran/RCC1 molecular
RT switch system in budding yeast.";
RL J. Biol. Chem. 270:1975-1978(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Trueheart J., Richards S., Macara I.G., Thorner J.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP CHARACTERIZATION.
RX PubMed=7489726; DOI=10.1002/j.1460-2075.1995.tb00221.x;
RA Schlenstedt G., Wong D.H., Koepp D.M., Silver P.A.;
RT "Mutants in a yeast Ran binding protein are defective in nuclear
RT transport.";
RL EMBO J. 14:5367-5378(1995).
RN [8]
RP CHARACTERIZATION.
RX PubMed=10825193; DOI=10.1128/mcb.20.12.4295-4308.2000;
RA Kunzler M., Gerstberger T., Stutz F., Bischoff F.R., Hurt E.;
RT "Yeast Ran-binding protein 1 (Yrb1) shuttles between the nucleus and
RT cytoplasm and is exported from the nucleus via a CRM1 (XPO1)-dependent
RT pathway.";
RL Mol. Cell. Biol. 20:4295-4308(2000).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Important for the export of protein containing nuclear export
CC signal (NES) out of the nucleus. Stimulates the GTPase activity of GSP1
CC and GSP2.
CC -!- SUBUNIT: Interacts with GSP1 and PRP20.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between the
CC nucleus and cytoplasm.
CC -!- SIMILARITY: Belongs to the RANBP1 family. {ECO:0000305}.
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DR EMBL; Z33503; CAA83911.1; -; Genomic_DNA.
DR EMBL; X65925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L38489; AAA57276.1; -; Genomic_DNA.
DR EMBL; Z48008; CAA88062.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11849.1; -; Genomic_DNA.
DR PIR; S50219; S50219.
DR RefSeq; NP_010285.1; NM_001180310.1.
DR PDB; 3M1I; X-ray; 2.00 A; B=11-201.
DR PDB; 4GMX; X-ray; 2.10 A; B=62-201.
DR PDB; 4GPT; X-ray; 2.22 A; B=62-201.
DR PDB; 4HAT; X-ray; 1.78 A; B=62-201.
DR PDB; 4HAU; X-ray; 2.00 A; B=62-201.
DR PDB; 4HAV; X-ray; 2.00 A; B=62-201.
DR PDB; 4HAW; X-ray; 1.90 A; B=62-201.
DR PDB; 4HAX; X-ray; 2.28 A; B=62-201.
DR PDB; 4HAY; X-ray; 2.30 A; B=62-201.
DR PDB; 4HAZ; X-ray; 1.90 A; B=62-201.
DR PDB; 4HB0; X-ray; 2.20 A; B=62-201.
DR PDB; 4HB2; X-ray; 1.80 A; B=62-201.
DR PDB; 4HB3; X-ray; 2.80 A; B=62-201.
DR PDB; 4HB4; X-ray; 2.05 A; B=62-201.
DR PDB; 4WVF; X-ray; 1.80 A; B=62-201.
DR PDB; 5DH9; X-ray; 2.55 A; B=62-201.
DR PDB; 5DHA; X-ray; 2.95 A; B=62-201.
DR PDB; 5DHF; X-ray; 2.29 A; B=62-201.
DR PDB; 5DI9; X-ray; 2.28 A; B=62-201.
DR PDB; 5DIF; X-ray; 2.09 A; B=62-201.
DR PDB; 5JLJ; X-ray; 2.50 A; B=62-201.
DR PDB; 5UWH; X-ray; 2.26 A; B=62-201.
DR PDB; 5UWI; X-ray; 2.14 A; B=62-201.
DR PDB; 5UWJ; X-ray; 2.22 A; B=62-201.
DR PDB; 5UWO; X-ray; 2.35 A; B=62-201.
DR PDB; 5UWP; X-ray; 2.05 A; B=62-201.
DR PDB; 5UWQ; X-ray; 2.28 A; B=62-201.
DR PDB; 5UWR; X-ray; 2.24 A; B=62-201.
DR PDB; 5UWS; X-ray; 2.40 A; B=62-201.
DR PDB; 5UWT; X-ray; 2.34 A; B=62-201.
DR PDB; 5UWU; X-ray; 2.24 A; B=62-201.
DR PDB; 5UWW; X-ray; 2.15 A; B=62-201.
DR PDB; 5YRO; X-ray; 2.40 A; B=62-201.
DR PDB; 5YST; X-ray; 2.04 A; B=62-200.
DR PDB; 5YSU; X-ray; 2.30 A; B=62-200.
DR PDB; 5YTB; X-ray; 2.30 A; B=62-200.
DR PDB; 5ZPU; X-ray; 2.60 A; B=62-201.
DR PDB; 6A38; X-ray; 2.69 A; B=62-201.
DR PDB; 6A3A; X-ray; 2.30 A; B=62-201.
DR PDB; 6A3B; X-ray; 2.51 A; B=62-201.
DR PDB; 6A3C; X-ray; 2.35 A; B=62-201.
DR PDB; 6A3E; X-ray; 2.70 A; B=62-201.
DR PDB; 6CIT; X-ray; 2.03 A; B=62-201.
DR PDB; 6KFT; X-ray; 2.51 A; B=62-201.
DR PDB; 6LQ9; X-ray; 2.50 A; B=62-201.
DR PDB; 6M60; X-ray; 2.17 A; B=62-201.
DR PDB; 6M6X; X-ray; 2.88 A; B=62-201.
DR PDB; 6X2M; X-ray; 2.35 A; B=62-201.
DR PDB; 6X2O; X-ray; 2.55 A; B=62-201.
DR PDB; 6X2P; X-ray; 2.40 A; B=62-201.
DR PDB; 6X2R; X-ray; 2.30 A; B=62-201.
DR PDB; 6X2S; X-ray; 2.50 A; B=62-201.
DR PDB; 6X2U; X-ray; 2.20 A; B=62-201.
DR PDB; 6X2V; X-ray; 2.82 A; B=62-201.
DR PDB; 6X2W; X-ray; 3.00 A; B=62-201.
DR PDB; 6X2X; X-ray; 2.46 A; B=62-201.
DR PDB; 6X2Y; X-ray; 2.30 A; B=62-201.
DR PDB; 6XJP; X-ray; 2.80 A; B=62-201.
DR PDB; 6XJR; X-ray; 1.94 A; B=62-201.
DR PDB; 6XJS; X-ray; 1.94 A; B=62-201.
DR PDB; 6XJT; X-ray; 2.41 A; B=62-201.
DR PDB; 6XJU; X-ray; 2.19 A; B=62-201.
DR PDB; 7CND; X-ray; 1.80 A; B=62-201.
DR PDB; 7DBG; X-ray; 2.06 A; B=62-201.
DR PDB; 7L5E; X-ray; 1.94 A; B=62-201.
DR PDBsum; 3M1I; -.
DR PDBsum; 4GMX; -.
DR PDBsum; 4GPT; -.
DR PDBsum; 4HAT; -.
DR PDBsum; 4HAU; -.
DR PDBsum; 4HAV; -.
DR PDBsum; 4HAW; -.
DR PDBsum; 4HAX; -.
DR PDBsum; 4HAY; -.
DR PDBsum; 4HAZ; -.
DR PDBsum; 4HB0; -.
DR PDBsum; 4HB2; -.
DR PDBsum; 4HB3; -.
DR PDBsum; 4HB4; -.
DR PDBsum; 4WVF; -.
DR PDBsum; 5DH9; -.
DR PDBsum; 5DHA; -.
DR PDBsum; 5DHF; -.
DR PDBsum; 5DI9; -.
DR PDBsum; 5DIF; -.
DR PDBsum; 5JLJ; -.
DR PDBsum; 5UWH; -.
DR PDBsum; 5UWI; -.
DR PDBsum; 5UWJ; -.
DR PDBsum; 5UWO; -.
DR PDBsum; 5UWP; -.
DR PDBsum; 5UWQ; -.
DR PDBsum; 5UWR; -.
DR PDBsum; 5UWS; -.
DR PDBsum; 5UWT; -.
DR PDBsum; 5UWU; -.
DR PDBsum; 5UWW; -.
DR PDBsum; 5YRO; -.
DR PDBsum; 5YST; -.
DR PDBsum; 5YSU; -.
DR PDBsum; 5YTB; -.
DR PDBsum; 5ZPU; -.
DR PDBsum; 6A38; -.
DR PDBsum; 6A3A; -.
DR PDBsum; 6A3B; -.
DR PDBsum; 6A3C; -.
DR PDBsum; 6A3E; -.
DR PDBsum; 6CIT; -.
DR PDBsum; 6KFT; -.
DR PDBsum; 6LQ9; -.
DR PDBsum; 6M60; -.
DR PDBsum; 6M6X; -.
DR PDBsum; 6X2M; -.
DR PDBsum; 6X2O; -.
DR PDBsum; 6X2P; -.
DR PDBsum; 6X2R; -.
DR PDBsum; 6X2S; -.
DR PDBsum; 6X2U; -.
DR PDBsum; 6X2V; -.
DR PDBsum; 6X2W; -.
DR PDBsum; 6X2X; -.
DR PDBsum; 6X2Y; -.
DR PDBsum; 6XJP; -.
DR PDBsum; 6XJR; -.
DR PDBsum; 6XJS; -.
DR PDBsum; 6XJT; -.
DR PDBsum; 6XJU; -.
DR PDBsum; 7CND; -.
DR PDBsum; 7DBG; -.
DR PDBsum; 7L5E; -.
DR AlphaFoldDB; P41920; -.
DR SMR; P41920; -.
DR BioGRID; 32055; 265.
DR DIP; DIP-838N; -.
DR IntAct; P41920; 6.
DR MINT; P41920; -.
DR STRING; 4932.YDR002W; -.
DR iPTMnet; P41920; -.
DR MaxQB; P41920; -.
DR PaxDb; P41920; -.
DR PRIDE; P41920; -.
DR EnsemblFungi; YDR002W_mRNA; YDR002W; YDR002W.
DR GeneID; 851565; -.
DR KEGG; sce:YDR002W; -.
DR SGD; S000002409; YRB1.
DR VEuPathDB; FungiDB:YDR002W; -.
DR eggNOG; KOG0864; Eukaryota.
DR GeneTree; ENSGT00900000141073; -.
DR HOGENOM; CLU_067861_2_1_1; -.
DR InParanoid; P41920; -.
DR OMA; HLEQTGN; -.
DR BioCyc; YEAST:G3O-29624-MON; -.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-4570464; SUMOylation of RNA binding proteins.
DR EvolutionaryTrace; P41920; -.
DR PRO; PR:P41920; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P41920; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IDA:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:0006405; P:RNA export from nucleus; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR CDD; cd13179; RanBD_RanBP1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR IDEAL; IID50175; -.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR InterPro; IPR045256; RanBP1_RanBD.
DR PANTHER; PTHR23138; PTHR23138; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTPase activation; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..201
FT /note="Ran-specific GTPase-activating protein 1"
FT /id="PRO_0000213670"
FT DOMAIN 64..200
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT STRAND 83..97
FT /evidence="ECO:0007829|PDB:4HAT"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 102..116
FT /evidence="ECO:0007829|PDB:4HAT"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:4HAT"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:5YST"
FT STRAND 153..163
FT /evidence="ECO:0007829|PDB:4HAT"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:4WVF"
FT STRAND 170..180
FT /evidence="ECO:0007829|PDB:4HAT"
FT HELIX 181..199
FT /evidence="ECO:0007829|PDB:4HAT"
SQ SEQUENCE 201 AA; 22953 MW; 46C3766B0906A75B CRC64;
MSSEDKKPVV DKKEEAAPKP PSSAVFSMFG GKKAEKPETK KDEEDTKEET KKEGDDAPES
PDIHFEPVVH LEKVDVKTME EDEEVLYKVR AKLFRFDADA KEWKERGTGD CKFLKNKKTN
KVRILMRRDK TLKICANHII APEYTLKPNV GSDRSWVYAC TADIAEGEAE AFTFAIRFGS
KENADKFKEE FEKAQEINKK A
