THP2_YEAST
ID THP2_YEAST Reviewed; 261 AA.
AC O13539; D3DLB6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=THO complex subunit THP2;
GN Name=THP2; OrderedLocusNames=YHR167W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [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 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 [11]
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).
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 O13539; P33441: MFT1; NbExp=4; IntAct=EBI-30898, EBI-10841;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11060033,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U00027; AAB68025.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06860.1; -; Genomic_DNA.
DR PIR; S52609; S52609.
DR RefSeq; NP_012037.1; NM_001179298.1.
DR PDB; 7APX; EM; 3.40 A; C=1-261.
DR PDB; 7AQO; EM; 4.50 A; C/J=1-261.
DR PDB; 7LUV; EM; 3.70 A; B=1-261.
DR PDBsum; 7APX; -.
DR PDBsum; 7AQO; -.
DR PDBsum; 7LUV; -.
DR AlphaFoldDB; O13539; -.
DR SMR; O13539; -.
DR BioGRID; 36601; 423.
DR ComplexPortal; CPX-1792; THO complex.
DR ComplexPortal; CPX-1793; TREX complex.
DR DIP; DIP-4246N; -.
DR IntAct; O13539; 31.
DR MINT; O13539; -.
DR STRING; 4932.YHR167W; -.
DR TCDB; 3.A.22.1.1; the transcription-coupled trex/tap nuclear mrna export complex (trex) family.
DR iPTMnet; O13539; -.
DR MaxQB; O13539; -.
DR PaxDb; O13539; -.
DR PRIDE; O13539; -.
DR EnsemblFungi; YHR167W_mRNA; YHR167W; YHR167W.
DR GeneID; 856572; -.
DR KEGG; sce:YHR167W; -.
DR SGD; S000001210; THP2.
DR VEuPathDB; FungiDB:YHR167W; -.
DR eggNOG; ENOG502RXUV; Eukaryota.
DR HOGENOM; CLU_091043_0_0_1; -.
DR InParanoid; O13539; -.
DR OMA; EWDDIEM; -.
DR BioCyc; YEAST:G3O-31201-MON; -.
DR PRO; PR:O13539; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; O13539; protein.
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:0003676; F:nucleic acid binding; IDA:SGD.
DR GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0034063; P:stress granule assembly; IMP:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR InterPro; IPR018557; THO_cplx_su_Thp2.
DR Pfam; PF09432; THP2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..261
FT /note="THO complex subunit THP2"
FT /id="PRO_0000267642"
FT HELIX 9..37
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 47..82
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 97..122
FT /evidence="ECO:0007829|PDB:7APX"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:7APX"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:7APX"
FT HELIX 167..234
FT /evidence="ECO:0007829|PDB:7APX"
SQ SEQUENCE 261 AA; 30299 MW; 16EFA6F464507C57 CRC64;
MTKEEGRTYF ESLCEEEQSL QESQTHLLNI LDILSVLADP RSSDDLLTES LKKLPDLHRE
LINSSIRLRY DKYQTREAQL LEDTKTGRDV AAGVQNPKSI SEYYSTFEHL NRDTLRYINL
LKRLSVDLAK QVEVSDPSVT VYEMDKWVPS EKLQGILEQY CAPDTDIRGV DAQIKNYLDQ
IKMARAKFGL ENKYSLKERL STLTKELNHW RKEWDDIEML MFGDDAHSMK KMIQKIDSLK
SEINAPSESY PVDKEGDIVL E
