HPR1_YEAST
ID HPR1_YEAST Reviewed; 752 AA.
AC P17629; D6VSC1; Q03918;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=THO complex subunit HPR1;
DE AltName: Full=Hyperrecombination protein 1;
GN Name=HPR1; OrderedLocusNames=YDR138W; ORFNames=YD9302.14;
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].
RX PubMed=2181275; DOI=10.1128/mcb.10.4.1439-1451.1990;
RA Aguilera A., Klein H.L.;
RT "HPR1, a novel yeast gene that prevents intrachromosomal excision
RT recombination, shows carboxy-terminal homology to the Saccharomyces
RT cerevisiae TOP1 gene.";
RL Mol. Cell. Biol. 10:1439-1451(1990).
RN [2]
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 [3]
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 [4]
RP IDENTIFICATION IN THO COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11060033; DOI=10.1093/emboj/19.21.5824;
RA Chavez S., Beilharz T., Rondon A.G., Erdjument-Bromage H., Tempst P.,
RA Svejstrup J.Q., Lithgow T., Aguilera A.;
RT "A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2,
RT connects transcription elongation with mitotic recombination in
RT Saccharomyces cerevisiae.";
RL EMBO J. 19:5824-5834(2000).
RN [5]
RP FUNCTION.
RX PubMed=12093753; DOI=10.1093/emboj/cdf335;
RA Jimeno S., Rondon A.G., Luna R., Aguilera A.;
RT "The yeast THO complex and mRNA export factors link RNA metabolism with
RT transcription and genome instability.";
RL EMBO J. 21:3526-3535(2002).
RN [6]
RP IDENTIFICATION IN TREX COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11979277; DOI=10.1038/nature746;
RA Straesser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M.,
RA Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R.,
RA Hurt E.;
RT "TREX is a conserved complex coupling transcription with messenger RNA
RT export.";
RL Nature 417:304-308(2002).
RN [7]
RP FUNCTION.
RX PubMed=12871933; DOI=10.1074/jbc.m305718200;
RA Rondon A.G., Jimeno S., Garcia-Rubio M., Aguilera A.;
RT "Molecular evidence that the eukaryotic THO/TREX complex is required for
RT efficient transcription elongation.";
RL J. Biol. Chem. 278:39037-39043(2003).
RN [8]
RP FUNCTION.
RX PubMed=14527416; DOI=10.1016/j.molcel.2003.08.010;
RA Huertas P., Aguilera A.;
RT "Cotranscriptionally formed DNA:RNA hybrids mediate transcription
RT elongation impairment and transcription-associated recombination.";
RL Mol. Cell 12:711-721(2003).
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.
RX PubMed=15192704; DOI=10.1038/sj.emboj.7600261;
RA Abruzzi K.C., Lacadie S., Rosbash M.;
RT "Biochemical analysis of TREX complex recruitment to intronless and intron-
RT containing yeast genes.";
RL EMBO J. 23:2620-2631(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, 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: Component the THO subcomplex of the TREX complex, which
CC operates in coupling transcription elongation to mRNA export. The THO
CC complex is recruited to transcribed genes and moves along the gene with
CC the elongating polymerase during transcription. THO is important for
CC stabilizing nascent RNA in the RNA polymerase II elongation complex by
CC preventing formation of DNA:RNA hybrids behind the elongating
CC polymerase. It functions in cotranscriptional formation of an export-
CC competent messenger ribonucleoprotein particle (mRNP) by facilitating
CC the loading of ATP-dependent RNA helicase SUB2 and the mRNA export
CC factor YRA1 along the nascent mRNA. {ECO:0000269|PubMed:12093753,
CC ECO:0000269|PubMed:12871933, ECO:0000269|PubMed:14527416,
CC ECO:0000269|PubMed:15192704}.
CC -!- SUBUNIT: Component of the THO complex, which is composed of HPR1, MFT1,
CC THO2 and THP2. Together with SUB2, TEX1 and YRA1, THO forms the
CC transcription/export (TREX) complex. THO associates with DNA and RNA in
CC vitro. {ECO:0000269|PubMed:11060033, ECO:0000269|PubMed:11979277}.
CC -!- INTERACTION:
CC P17629; Q99257: MEX67; NbExp=4; IntAct=EBI-8526, EBI-11642;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11060033,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: HPR1 is not required for sporulation, and is not
CC essential for DNA repair. It is probably not a DNA topoisomerase.
CC -!- MISCELLANEOUS: Present with 1340 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M30484; AAA34685.1; -; Genomic_DNA.
DR EMBL; Z48179; CAA88220.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11981.1; -; Genomic_DNA.
DR PIR; S51866; S51866.
DR RefSeq; NP_010422.1; NM_001180445.1.
DR PDB; 7APX; EM; 3.40 A; B=1-720.
DR PDB; 7AQO; EM; 4.50 A; B/H=1-720.
DR PDB; 7LUV; EM; 3.70 A; A=1-603.
DR PDBsum; 7APX; -.
DR PDBsum; 7AQO; -.
DR PDBsum; 7LUV; -.
DR AlphaFoldDB; P17629; -.
DR SMR; P17629; -.
DR BioGRID; 32192; 168.
DR ComplexPortal; CPX-1792; THO complex.
DR ComplexPortal; CPX-1793; TREX complex.
DR DIP; DIP-6266N; -.
DR IntAct; P17629; 26.
DR MINT; P17629; -.
DR STRING; 4932.YDR138W; -.
DR TCDB; 3.A.22.1.1; the transcription-coupled trex/tap nuclear mrna export complex (trex) family.
DR iPTMnet; P17629; -.
DR MaxQB; P17629; -.
DR PaxDb; P17629; -.
DR PRIDE; P17629; -.
DR EnsemblFungi; YDR138W_mRNA; YDR138W; YDR138W.
DR GeneID; 851716; -.
DR KEGG; sce:YDR138W; -.
DR SGD; S000002545; HPR1.
DR VEuPathDB; FungiDB:YDR138W; -.
DR eggNOG; ENOG502QU83; Eukaryota.
DR HOGENOM; CLU_022496_0_0_1; -.
DR InParanoid; P17629; -.
DR OMA; ISYKQPL; -.
DR BioCyc; YEAST:G3O-29735-MON; -.
DR PRO; PR:P17629; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P17629; protein.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IPI:SGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:0000446; C:nucleoplasmic THO complex; IMP:SGD.
DR GO; GO:0000445; C:THO complex part of transcription export complex; IDA:SGD.
DR GO; GO:0000346; C:transcription export complex; IPI:ComplexPortal.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:SGD.
DR GO; GO:0003676; F:nucleic acid binding; IDA:SGD.
DR GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IMP:SGD.
DR GO; GO:2001209; P:positive regulation of transcription elongation from RNA polymerase I promoter; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:SGD.
DR InterPro; IPR021861; THO_THOC1.
DR Pfam; PF11957; efThoc1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..752
FT /note="THO complex subunit HPR1"
FT /id="PRO_0000084046"
FT REGION 648..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CONFLICT 404
FT /note="F -> L (in Ref. 1; AAA34685)"
FT /evidence="ECO:0000305"
FT HELIX 3..21
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 62..77
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 174..190
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 197..213
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 251..267
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 280..319
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 344..360
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 393..415
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 418..429
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 443..455
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 456..459
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 460..463
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 471..490
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 526..531
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 538..540
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 577..586
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 587..589
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 591..596
FT /evidence="ECO:0007829|PDB:7APX"
SQ SEQUENCE 752 AA; 87829 MW; CBD92432F099AD22 CRC64;
MSNTEELIQN SIGFLQKTFK ALPVSFDSIR HEPLPSSMLH ASVLNFEWEP LEKNISAIHD
RDSLIDIILK RFIIDSMTNA IEDEEENNLE KGLLNSCIGL DFVYNSRFNR SNPASWGNTF
FELFSTIIDL LNSPSTFLKF WPYAESRIEW FKMNTSVEPV SLGESNLISY KQPLYEKLRH
WNDILAKLEN NDILNTVKHY NMKYKLENFL SELLPINEES NFNRSASISA LQESDNEWNR
SARERESNRS SDVIFAADYN FVFYHLIICP IEFAFSDLEY KNDVDRSLSP LLDAILEIEE
NFYSKIKMNN RTRYSLEEAL NTEYYANYDV MTPKLPVYMK HSNAMKMDRN EFWANLQNIK
ESDDYTLRPT IMDISLSNTT CLYKQLTQED DDYYRKQFIL QLCFTTNLIR NLISSDETRN
FYKSCYLREN PLSDIDFENL DEVNKKRGLN LCSYICDNRV LKFYKIKDPD FYRVIRKLMS
SDEKFTTAKI DGFKEFQNFR ISKEKIPPPA FDETFKKFTF IKMGNKLINN VWKIPTGLDK
IEQEVKKPEG VYEAAQAKWE SKISSETSGG EAKDEIIRQW QTLRFLRSRY LFDFDKVNEK
TGVDGLFEEP RKVEALDDSF KEKLLYKINQ EHRKKLQDAR EYKIGKERKK RALEEEASFP
EREQKIKSQR INSASQTEGD ELKSEQTQPK GEISEENTKI KSSEVSSQDP DSGVAGEFAP
QNTTAQLENP KTEDNNAATS NISNGSSTQD MK
