GBP2_YEAST
ID GBP2_YEAST Reviewed; 427 AA.
AC P25555; D6VR01;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Serine/arginine (SR)-type shuttling mRNA binding protein GBP2 {ECO:0000305};
DE AltName: Full=Polyadenylate-binding protein GBP2 {ECO:0000303|PubMed:12634846};
DE AltName: Full=RAP1 localization factor 6 {ECO:0000303|PubMed:7777547};
DE AltName: Full=Single-strand telomeric DNA-binding protein GBP2 {ECO:0000305};
DE Short=G-strand-binding protein 2 {ECO:0000303|PubMed:7800479};
GN Name=GBP2 {ECO:0000303|PubMed:7800479};
GN Synonyms=RLF6 {ECO:0000303|PubMed:7777547}; OrderedLocusNames=YCL011C;
GN ORFNames=YCL11C;
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=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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.
RX PubMed=7800479; DOI=10.1093/nar/22.23.4906;
RA Lin J.-J., Zakian V.A.;
RT "Isolation and characterization of two Saccharomyces cerevisiae genes that
RT encode proteins that bind to (TG1-3)n single strand telomeric DNA in
RT vitro.";
RL Nucleic Acids Res. 22:4906-4913(1994).
RN [5]
RP FUNCTION.
RX PubMed=7777547; DOI=10.1073/pnas.92.12.5558;
RA Konkel L.C., Enomoto S., Chamberlain E., McCune-Zierath P.,
RA Iyadurai S.J.P., Berman J.;
RT "A class of single-stranded telomeric DNA-binding proteins required for
RT Rap1p localization in yeast nuclei.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5558-5562(1995).
RN [6]
RP METHYLATION BY HMT1.
RX PubMed=9499403; DOI=10.1101/gad.12.5.679;
RA Shen E.C., Henry M.F., Weiss V.H., Valentini S.R., Silver P.A., Lee M.S.;
RT "Arginine methylation facilitates the nuclear export of hnRNP proteins.";
RL Genes Dev. 12:679-691(1998).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12634846; DOI=10.1038/sj.embor.embor763;
RA Windgassen M., Krebber H.;
RT "Identification of Gbp2 as a novel poly(A)+ RNA-binding protein involved in
RT the cytoplasmic delivery of messenger RNAs in yeast.";
RL EMBO Rep. 4:278-283(2003).
RN [8]
RP FUNCTION.
RX PubMed=12519786; DOI=10.1074/jbc.m208347200;
RA Pang T.-L., Wang C.-Y., Hsu C.-L., Chen M.-Y., Lin J.-J.;
RT "Exposure of single-stranded telomeric DNA causes G2/M cell cycle arrest in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:9318-9321(2003).
RN [9]
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 [10]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-15.
RX PubMed=14676199; DOI=10.1074/jbc.c300522200;
RA Haecker S., Krebber H.;
RT "Differential export requirements for shuttling serine/arginine-type mRNA-
RT binding proteins.";
RL J. Biol. Chem. 279:5049-5052(2004).
RN [11]
RP FUNCTION.
RX PubMed=14769921; DOI=10.1073/pnas.0308663100;
RA Hurt E., Luo M.J., Roether S., Reed R., Straesser K.;
RT "Cotranscriptional recruitment of the serine-arginine-rich (SR)-like
RT proteins Gbp2 and Hrb1 to nascent mRNA via the TREX complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1858-1862(2004).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=18981231; DOI=10.1083/jcb.200807043;
RA Buchan J.R., Muhlrad D., Parker R.;
RT "P bodies promote stress granule assembly in Saccharomyces cerevisiae.";
RL J. Cell Biol. 183:441-455(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, 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 [14]
RP SUBCELLULAR LOCATION.
RX PubMed=22932476; DOI=10.1186/2045-3701-2-30;
RA Dastidar R.G., Hooda J., Shah A., Cao T.M., Henke R.M., Zhang L.;
RT "The nuclear localization of SWI/SNF proteins is subjected to oxygen
RT regulation.";
RL Cell Biosci. 2:30-30(2012).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24452287; DOI=10.1038/ncomms4123;
RA Hackmann A., Wu H., Schneider U.M., Meyer K., Jung K., Krebber H.;
RT "Quality control of spliced mRNAs requires the shuttling SR proteins Gbp2
RT and Hrb1.";
RL Nat. Commun. 5:3123-3123(2014).
RN [16] {ECO:0007744|PDB:2MZQ}
RP STRUCTURE BY NMR OF 329-427, AND DOMAIN.
RX PubMed=26602689; DOI=10.1093/nar/gkv1303;
RA Martinez-Lumbreras S., Taverniti V., Zorrilla S., Seraphin B.,
RA Perez-Canadillas J.M.;
RT "Gbp2 interacts with THO/TREX through a novel type of RRM domain.";
RL Nucleic Acids Res. 44:437-448(2016).
RN [17]
RP PHOSPHORYLATION AT SER-24.
RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927;
RA Hamey J.J., Nguyen A., Wilkins M.R.;
RT "Discovery of arginine methylation, phosphorylation, and their co-
RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae.";
RL J. Proteome Res. 20:2420-2434(2021).
CC -!- FUNCTION: Binds to intron-containing transcripts and is involved in
CC quality control for the export of spliced mRNAs from the nucleus
CC (PubMed:14769921, PubMed:24452287). Binds to pre-mRNAs until splicing
CC is completed or until faulty mRNAs are degraded. On correctly spliced
CC mRNAs, GBP2 and HRB1 recruit MEX67 to allow nuclear export. On faulty
CC mRNAs, GBP2 and HRB1 associate with the TRAMP complex that guides those
CC pre-mRNAs to the exosome for degradation (PubMed:24452287). Binds
CC single-stranded telomeric sequences of the type (TG[1-3])n in vitro
CC (PubMed:7800479). Influences the localization of RAP1 in the nuclei
CC (PubMed:7777547). Involved in modulating telomere length
CC (PubMed:12519786). {ECO:0000269|PubMed:12519786,
CC ECO:0000269|PubMed:14769921, ECO:0000269|PubMed:24452287,
CC ECO:0000269|PubMed:7777547, ECO:0000269|PubMed:7800479}.
CC -!- INTERACTION:
CC P25555; Q01560: NPL3; NbExp=3; IntAct=EBI-7410, EBI-12114;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14676199,
CC ECO:0000269|PubMed:22932476, ECO:0000269|PubMed:24452287}. Nucleus
CC {ECO:0000269|PubMed:12634846, ECO:0000269|PubMed:14676199,
CC ECO:0000269|PubMed:22932476, ECO:0000269|PubMed:24452287}. Chromosome,
CC telomere {ECO:0000305|PubMed:7800479}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:18981231}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:18981231}. Note=Nuclear at steady state. Export is
CC dependent on active transcription and the export of mRNAs in general.
CC Depends on MFT1 and HPR1 for nuclear export (PubMed:14676199). Becomes
CC predominantly cytosolic after exposure to hypoxia (PubMed:22932476).
CC {ECO:0000269|PubMed:14676199, ECO:0000269|PubMed:22932476}.
CC -!- DOMAIN: RRM 1 and RRM 2 recognize preferentially RNAs containing the
CC core motif GGUG. The atypical C-terminal RRM domain (RRM 3) does not
CC interact with RNA/DNA, but is crucial for interaction with the THO/TREX
CC complex. {ECO:0000269|PubMed:26602689}.
CC -!- PTM: Methylated by HMT1. {ECO:0000269|PubMed:9499403}.
CC -!- MISCELLANEOUS: Present with 2540 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X59720; CAA42348.1; -; Genomic_DNA.
DR EMBL; AY692807; AAT92826.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07470.1; -; Genomic_DNA.
DR PIR; S19338; S19338.
DR RefSeq; NP_009916.1; NM_001178660.1.
DR PDB; 2MZQ; NMR; -; A=329-427.
DR PDBsum; 2MZQ; -.
DR AlphaFoldDB; P25555; -.
DR SMR; P25555; -.
DR BioGRID; 30970; 217.
DR DIP; DIP-2735N; -.
DR IntAct; P25555; 54.
DR MINT; P25555; -.
DR STRING; 4932.YCL011C; -.
DR iPTMnet; P25555; -.
DR MaxQB; P25555; -.
DR PaxDb; P25555; -.
DR PRIDE; P25555; -.
DR EnsemblFungi; YCL011C_mRNA; YCL011C; YCL011C.
DR GeneID; 850346; -.
DR KEGG; sce:YCL011C; -.
DR SGD; S000000517; GBP2.
DR VEuPathDB; FungiDB:YCL011C; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000168568; -.
DR HOGENOM; CLU_026447_2_0_1; -.
DR InParanoid; P25555; -.
DR OMA; MSSEYEL; -.
DR BioCyc; YEAST:G3O-29280-MON; -.
DR PRO; PR:P25555; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25555; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:SGD.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR GO; GO:2000815; P:regulation of mRNA stability involved in response to oxidative stress; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IDA:SGD.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Telomere.
FT CHAIN 1..427
FT /note="Serine/arginine (SR)-type shuttling mRNA binding
FT protein GBP2"
FT /id="PRO_0000081596"
FT DOMAIN 122..198
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 219..296
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 349..426
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 15
FT /note="S->A: Shifts localization of the protein to the
FT cytoplasm at steady state."
FT /evidence="ECO:0000269|PubMed:14676199"
FT HELIX 332..336
FT /evidence="ECO:0007829|PDB:2MZQ"
FT TURN 337..340
FT /evidence="ECO:0007829|PDB:2MZQ"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:2MZQ"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:2MZQ"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:2MZQ"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:2MZQ"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:2MZQ"
FT STRAND 390..398
FT /evidence="ECO:0007829|PDB:2MZQ"
FT HELIX 399..408
FT /evidence="ECO:0007829|PDB:2MZQ"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:2MZQ"
SQ SEQUENCE 427 AA; 48729 MW; 5341D7A0E07F208C CRC64;
MERELGMYGN DRSRSRSPVR RRLSDDRDRY DDYNDSSSNN GNGSRRQRRD RGSRFNDRYD
QSYGGSRYHD DRNWPPRRGG RGRGGSRSFR GGRGGGRGRT LGPIVERDLE RQFDATKRNF
ENSIFVRNLT FDCTPEDLKE LFGTVGEVVE ADIITSKGHH RGMGTVEFTK NESVQDAISK
FDGALFMDRK LMVRQDNPPP EAAKEFSKKA TREEIDNGFE VFIINLPYSM NWQSLKDMFK
ECGHVLRADV ELDFNGFSRG FGSVIYPTED EMIRAIDTFN GMEVEGRVLE VREGRFNKRK
NNDRYNQRRE DLEDTRGTEP GLAQDAAVHI DETAAKFTEG VNPGGDRNCF IYCSNLPFST
ARSDLFDLFG PIGKINNAEL KPQENGQPTG VAVVEYENLV DADFCIQKLN NYNYGGCSLQ
ISYARRD
