HRB1_YEAST
ID HRB1_YEAST Reviewed; 454 AA.
AC P38922; A2TBM5; D6W1H3; Q06HN4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Serine/arginine (SR)-type shuttling mRNA binding protein HRB1 {ECO:0000305};
DE AltName: Full=Hypothetical RNA-binding protein 1 {ECO:0000303|PubMed:9499403};
DE AltName: Full=Polyadenylate-binding protein HRB1 {ECO:0000305};
DE AltName: Full=Protein TOM34;
GN Name=HRB1 {ECO:0000303|PubMed:9499403}; Synonyms=TOM34;
GN OrderedLocusNames=YNL004W; ORFNames=N2009;
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=S288c / GRF88;
RX PubMed=8402262;
RA Lalo D., Stettler S., Mariotte S., Slonimski P.P., Thuriaux P.;
RT "Two yeast chromosomes are related by a fossil duplication of their
RT centromeric regions.";
RL C. R. Acad. Sci. III, Sci. Vie 316:367-373(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=7941739; DOI=10.1002/yea.320100412;
RA Lalo D., Stettler S., Mariotte S., Gendreau E., Thuriaux P.;
RT "Organization of the centromeric region of chromosome XIV in Saccharomyces
RT cerevisiae.";
RL Yeast 10:523-533(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7985421; DOI=10.1002/yea.320100709;
RA Verhasselt P., Aert R., Voet M., Volckaert G.;
RT "Nucleotide sequence analysis of an 8887 bp region of the left arm of yeast
RT chromosome XIV, encompassing the centromere sequence.";
RL Yeast 10:945-951(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-134.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17351133; DOI=10.1101/gr.6049107;
RA Zhang Z., Hesselberth J.R., Fields S.;
RT "Genome-wide identification of spliced introns using a tiling microarray.";
RL Genome Res. 17:503-509(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-119.
RC STRAIN=ATCC 201390 / BY4743;
RX PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA Juneau K., Palm C., Miranda M., Davis R.W.;
RT "High-density yeast-tiling array reveals previously undiscovered introns
RT and extensive regulation of meiotic splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN [8]
RP SUBCELLULAR LOCATION, AND 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 [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
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 [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-355, AND
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-355, AND
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).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=23222640; DOI=10.1038/nsmb.2468;
RA Mitchell S.F., Jain S., She M., Parker R.;
RT "Global analysis of yeast mRNPs.";
RL Nat. Struct. Mol. Biol. 20:127-133(2013).
RN [17]
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 [18]
RP METHYLATION AT ARG-127, AND PHOSPHORYLATION AT SER-338;SER-343 AND SER-355.
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).
RN [19] {ECO:0007744|PDB:2MZR, ECO:0007744|PDB:2MZS, ECO:0007744|PDB:2MZT}
RP STRUCTURE BY NMR OF 357-454.
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).
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:14676199, PubMed:14769921, PubMed:24452287). Binds to pre-mRNAs
CC until splicing is completed or until faulty mRNAs are degraded. On
CC correctly spliced mRNAs, GBP2 and HRB1 recruit MEX67 to allow nuclear
CC export. On faulty mRNAs, GBP2 and HRB1 associate with the TRAMP complex
CC that guides those pre-mRNAs to the exosome for degradation
CC (PubMed:24452287). {ECO:0000269|PubMed:14676199,
CC ECO:0000269|PubMed:14769921, ECO:0000269|PubMed:24452287}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14676199,
CC ECO:0000269|PubMed:24452287, ECO:0000269|PubMed:9499403}. Nucleus
CC {ECO:0000269|PubMed:14676199, ECO:0000269|PubMed:24452287,
CC ECO:0000269|PubMed:9499403}. Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:23222640}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:23222640}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:23222640}. Note=Shuttles between nucleus and
CC cytoplasm (PubMed:9499403). Nuclear at steady state and its import is
CC mediated by the karyopherin MTR10. Export is dependent on active
CC transcription and the export of mRNAs in general. Depends on MFT1 and
CC HPR1 for nuclear export (PubMed:14676199).
CC {ECO:0000269|PubMed:14676199, ECO:0000269|PubMed:9499403}.
CC -!- PTM: Methylated by HMT1. {ECO:0000269|PubMed:9499403}.
CC -!- MISCELLANEOUS: Present with 1990 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA64803.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA54378.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA95863.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U02536; AAA64803.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X77114; CAA54378.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z71280; CAA95863.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ881449; ABI95876.1; -; mRNA.
DR EMBL; EF123128; ABM97472.1; -; mRNA.
DR EMBL; BK006947; DAA10539.1; -; Genomic_DNA.
DR PIR; S45459; S45459.
DR RefSeq; NP_014394.2; NM_001182843.1.
DR PDB; 2MZR; NMR; -; A=144-236.
DR PDB; 2MZS; NMR; -; A=262-358.
DR PDB; 2MZT; NMR; -; A=357-454.
DR PDBsum; 2MZR; -.
DR PDBsum; 2MZS; -.
DR PDBsum; 2MZT; -.
DR AlphaFoldDB; P38922; -.
DR SMR; P38922; -.
DR BioGRID; 35821; 233.
DR DIP; DIP-4959N; -.
DR IntAct; P38922; 25.
DR MINT; P38922; -.
DR STRING; 4932.YNL004W; -.
DR iPTMnet; P38922; -.
DR MaxQB; P38922; -.
DR PaxDb; P38922; -.
DR PRIDE; P38922; -.
DR EnsemblFungi; YNL004W_mRNA; YNL004W; YNL004W.
DR GeneID; 855728; -.
DR KEGG; sce:YNL004W; -.
DR SGD; S000004949; HRB1.
DR VEuPathDB; FungiDB:YNL004W; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000168568; -.
DR HOGENOM; CLU_026447_2_0_1; -.
DR InParanoid; P38922; -.
DR OMA; VKFATNP; -.
DR BioCyc; YEAST:G3O-33046-MON; -.
DR PRO; PR:P38922; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P38922; protein.
DR GO; GO:0005737; C:cytoplasm; 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:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:2000815; P:regulation of mRNA stability involved in response to oxidative stress; IBA:GO_Central.
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; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..454
FT /note="Serine/arginine (SR)-type shuttling mRNA binding
FT protein HRB1"
FT /id="PRO_0000081612"
FT DOMAIN 161..237
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 261..338
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 376..453
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 127
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:2MZR"
FT HELIX 174..181
FT /evidence="ECO:0007829|PDB:2MZR"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2MZR"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:2MZR"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:2MZR"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:2MZR"
FT TURN 218..222
FT /evidence="ECO:0007829|PDB:2MZR"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2MZR"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:2MZS"
FT HELIX 274..282
FT /evidence="ECO:0007829|PDB:2MZS"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:2MZS"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:2MZS"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:2MZS"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:2MZS"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:2MZS"
FT HELIX 359..363
FT /evidence="ECO:0007829|PDB:2MZT"
FT TURN 364..367
FT /evidence="ECO:0007829|PDB:2MZT"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:2MZT"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:2MZT"
FT HELIX 389..396
FT /evidence="ECO:0007829|PDB:2MZT"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:2MZT"
FT STRAND 402..413
FT /evidence="ECO:0007829|PDB:2MZT"
FT STRAND 415..425
FT /evidence="ECO:0007829|PDB:2MZT"
FT HELIX 426..435
FT /evidence="ECO:0007829|PDB:2MZT"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:2MZT"
FT STRAND 447..453
FT /evidence="ECO:0007829|PDB:2MZT"
SQ SEQUENCE 454 AA; 52142 MW; C54D858C77076583 CRC64;
MSDQERGSEN NNRSRSRSRS PVRRRMSDDH GYERDNHLSR RSGNYNGRRK FADTYRGSRD
RGEYRGGRER SDYRERERFN NRDNPRSRDR YDDRRRGRDV TGRYGNRRDD YPRSFRSRHN
TRDDSRRGGF GSSGARGDYG PLLARELDST YEEKVNRNYS NSIFVGNLTY DSTPEDLTEF
FSQIGKVVRA DIITSRGHHR GMGTVEFTNS DDVDRAIRQY DGAFFMDRKI FVRQDNPPPS
NNIKERKALD RGELRHNRKT HEVIVKNLPA SVNWQALKDI FKECGNVAHA DVELDGDGVS
TGSGTVSFYD IKDLHRAIEK YNGYSIEGNV LDVKSKESVH NHSDGDDVDI PMDDSPVNEE
ARKFTENVVG GGERNRLIYC SNLPFSTAKS DLYDLFETIG KVNNAELRYD SKGAPTGIAV
VEYDNVDDAD VCIERLNNYN YGGCDLDISY AKRL
