ID YRB2_YEAST Reviewed; 327 AA.
AC P40517; D6VVM1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 184.
DE RecName: Full=Ran-specific GTPase-activating protein 2;
DE AltName: Full=Ran-binding protein 2;
DE Short=RANBP2;
GN Name=YRB2; OrderedLocusNames=YIL063C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SRM1.
RX PubMed=9395535; DOI=10.1074/jbc.272.50.31877;
RA Taura T., Schlenstedt G., Silver P.A.;
RT "Yrb2p is a nuclear protein that interacts with Prp20p, a yeast Rcc1
RT homologue.";
RL J. Biol. Chem. 272:31877-31884(1997).
RN [5]
RP CHARACTERIZATION.
RX PubMed=9636166; DOI=10.1073/pnas.95.13.7427;
RA Taura T., Krebber H., Silver P.A.;
RT "A member of the Ran-binding protein family, Yrb2p, is involved in nuclear
RT protein export.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:7427-7432(1998).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND SER-179, AND
RP IDENTIFICATION BY 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 [9]
RP IDENTIFICATION BY 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
CC GSP1. {ECO:0000269|PubMed:9395535}.
CC -!- SUBUNIT: Interacts with GSP1, XPO1 and SRM1.
CC {ECO:0000269|PubMed:9395535}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9395535}.
CC -!- DOMAIN: Contains X-F-X-F-G repeats.
CC -!- MISCELLANEOUS: Present with 3620 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z38060; CAA86160.1; -; Genomic_DNA.
DR EMBL; AY557879; AAS56205.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08487.1; -; Genomic_DNA.
DR PIR; S48416; S48416.
DR RefSeq; NP_012201.1; NM_001179413.1.
DR PDB; 3WYF; X-ray; 2.22 A; B/E=90-327.
DR PDBsum; 3WYF; -.
DR AlphaFoldDB; P40517; -.
DR SMR; P40517; -.
DR BioGRID; 34929; 50.
DR DIP; DIP-2243N; -.
DR IntAct; P40517; 6.
DR MINT; P40517; -.
DR STRING; 4932.YIL063C; -.
DR iPTMnet; P40517; -.
DR MaxQB; P40517; -.
DR PaxDb; 4932-YIL063C; -.
DR PeptideAtlas; P40517; -.
DR EnsemblFungi; YIL063C_mRNA; YIL063C; YIL063C.
DR GeneID; 854747; -.
DR KEGG; sce:YIL063C; -.
DR AGR; SGD:S000001325; -.
DR SGD; S000001325; YRB2.
DR VEuPathDB; FungiDB:YIL063C; -.
DR eggNOG; KOG0864; Eukaryota.
DR HOGENOM; CLU_052718_0_0_1; -.
DR InParanoid; P40517; -.
DR OMA; IRLVMRS; -.
DR OrthoDB; 2168911at2759; -.
DR BioCyc; YEAST:G3O-31331-MONOMER; -.
DR BioGRID-ORCS; 854747; 8 hits in 10 CRISPR screens.
DR PRO; PR:P40517; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40517; Protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; 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:0060090; F:molecular adaptor activity; IDA:DisProt.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IBA:GO_Central.
DR GO; GO:0006611; P:protein export from nucleus; IMP:SGD.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:SGD.
DR CDD; cd13180; RanBD_RanBP3; 1.
DR DisProt; DP01079; -.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR IDEAL; IID50276; -.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR PANTHER; PTHR23138; RAN BINDING PROTEIN; 1.
DR PANTHER; PTHR23138:SF87; RANBD1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00638; Ran_BP1; 1.
DR SMART; SM00160; RanBD; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50196; RANBD1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTPase activation; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..327
FT /note="Ran-specific GTPase-activating protein 2"
FT /id="PRO_0000213671"
FT DOMAIN 191..327
FT /note="RanBD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3WYF"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:3WYF"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:3WYF"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3WYF"
FT STRAND 212..225
FT /evidence="ECO:0007829|PDB:3WYF"
FT STRAND 232..244
FT /evidence="ECO:0007829|PDB:3WYF"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:3WYF"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:3WYF"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:3WYF"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:3WYF"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3WYF"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:3WYF"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:3WYF"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:3WYF"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:3WYF"
SQ SEQUENCE 327 AA; 36054 MW; 7A1A626B9171646D CRC64;
MSETNGGNAA RENSEVKQTA VENPIDKLDG TPKRPREKDQ DEQAEETSDK SEAPNKNDEE
KKEEGKKDQE PSHKKIKVDD GKTVESGIVE DDKKEDKFVF GAASKFGTGF GVAKKDTKDG
DATTSTESLP ASDSKTKKPF AFGSGLSFGS GFNILKNKTE NNSESEKKAT DVDKDKVHSG
SEQLANASED TKDKPKPLKL QKQEVKSGEE SEECIYQVNA KLYQLSNIKE GWKERGVGII
KINKSKDDVE KTRIVMRSRG ILKVILNIQL VKGFTVQKGF TGSLQSEKFI RLLAVDDNGD
PAQYAIKTGK KETTDELYNI IVKSVPK
//
