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 27-MAR-2024, entry version 194. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 227. DR DIP; DIP-2735N; -. DR IntAct; P25555; 54. DR MINT; P25555; -. DR STRING; 4932.YCL011C; -. DR iPTMnet; P25555; -. DR MaxQB; P25555; -. DR PaxDb; 4932-YCL011C; -. DR PeptideAtlas; P25555; -. DR EnsemblFungi; YCL011C_mRNA; YCL011C; YCL011C. DR GeneID; 850346; -. DR KEGG; sce:YCL011C; -. DR AGR; SGD:S000000517; -. 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; AFIRYDQ; -. DR OrthoDB; 317787at2759; -. DR BioCyc; YEAST:G3O-29280-MONOMER; -. DR BioGRID-ORCS; 850346; 9 hits in 10 CRISPR screens. 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:0000932; C:P-body; IEA:UniProtKB-SubCell. 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:0000723; P:telomere maintenance; IDA:SGD. DR CDD; cd21605; RRM1_HRB1_GBP2; 1. DR CDD; cd21606; RRM2_HRB1_GBP2; 1. DR CDD; cd21607; RRM3_HRB1_GBP2; 1. 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 PANTHER; PTHR23003:SF3; FI21236P1; 1. DR PANTHER; PTHR23003; RNA RECOGNITION MOTIF RRM DOMAIN CONTAINING PROTEIN; 1. DR Pfam; PF00076; RRM_1; 3. DR SMART; SM00360; RRM; 3. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 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 //