THP3_YEAST
ID THP3_YEAST Reviewed; 470 AA.
AC Q12049; D6W453; Q07109;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein THP3;
DE AltName: Full=THO-related protein 3;
GN Name=THP3; OrderedLocusNames=YPR045C; ORFNames=YP9499.03c;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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] OF 299-470.
RC STRAIN=ATCC 46191 / IL125-2B;
RA Waskiewicz-Staniorowska B.;
RL Thesis (1996), University of Wroclaw, Poland.
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND INTERACTION WITH CSN12 AND SEM1.
RX PubMed=19061648; DOI=10.1016/j.molcel.2008.11.012;
RA Wilmes G.M., Bergkessel M., Bandyopadhyay S., Shales M., Braberg H.,
RA Cagney G., Collins S.R., Whitworth G.B., Kress T.L., Weissman J.S.,
RA Ideker T., Guthrie C., Krogan N.J.;
RT "A genetic interaction map of RNA-processing factors reveals links between
RT Sem1/Dss1-containing complexes and mRNA export and splicing.";
RL Mol. Cell 32:735-746(2008).
RN [7]
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).
RN [8]
RP FUNCTION, AND INTERACTION WITH CSN12 AND SEM1.
RX PubMed=19289793; DOI=10.1083/jcb.200810059;
RA Faza M.B., Kemmler S., Jimeno S., Gonzalez-Aguilera C., Aguilera A.,
RA Hurt E., Panse V.G.;
RT "Sem1 is a functional component of the nuclear pore complex-associated
RT messenger RNA export machinery.";
RL J. Cell Biol. 184:833-846(2009).
RN [9]
RP FUNCTION, AND INTERACTION WITH CSN12.
RX PubMed=21149575; DOI=10.1128/mcb.01188-10;
RA Jimeno S., Tous C., Garcia-Rubio M.L., Ranes M., Gonzalez-Aguilera C.,
RA Marin A., Aguilera A.;
RT "New suppressors of THO mutations identify Thp3 (Ypr045c)-Csn12 as a
RT protein complex involved in transcription elongation.";
RL Mol. Cell. Biol. 31:674-685(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Forms a complex with CSN12 that is recruited to transcribed
CC genes and required for transcription elongation. May also be involved
CC in pre-mRNA splicing. {ECO:0000269|PubMed:19061648,
CC ECO:0000269|PubMed:19289793, ECO:0000269|PubMed:21149575}.
CC -!- SUBUNIT: Interacts with CSN12 and SEM1. {ECO:0000269|PubMed:19061648,
CC ECO:0000269|PubMed:19289793, ECO:0000269|PubMed:21149575}.
CC -!- INTERACTION:
CC Q12049; P47130: CSN12; NbExp=2; IntAct=EBI-34263, EBI-763;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the THP3 family. {ECO:0000305}.
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; Z49219; CAA89165.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94992.1; -; Genomic_DNA.
DR EMBL; Z73616; CAA97994.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11469.1; -; Genomic_DNA.
DR PIR; S54069; S54069.
DR RefSeq; NP_015370.1; NM_001184142.1.
DR AlphaFoldDB; Q12049; -.
DR SMR; Q12049; -.
DR BioGRID; 36221; 331.
DR DIP; DIP-3903N; -.
DR IntAct; Q12049; 10.
DR MINT; Q12049; -.
DR STRING; 4932.YPR045C; -.
DR TCDB; 3.A.22.1.1; the transcription-coupled trex/tap nuclear mrna export complex (trex) family.
DR iPTMnet; Q12049; -.
DR MaxQB; Q12049; -.
DR PaxDb; Q12049; -.
DR PRIDE; Q12049; -.
DR EnsemblFungi; YPR045C_mRNA; YPR045C; YPR045C.
DR GeneID; 856158; -.
DR KEGG; sce:YPR045C; -.
DR SGD; S000006249; THP3.
DR VEuPathDB; FungiDB:YPR045C; -.
DR eggNOG; KOG1861; Eukaryota.
DR GeneTree; ENSGT00390000008006; -.
DR HOGENOM; CLU_015513_4_2_1; -.
DR InParanoid; Q12049; -.
DR OMA; ENQFTVK; -.
DR BioCyc; YEAST:G3O-34200-MON; -.
DR PRO; PR:Q12049; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12049; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR045107; SAC3/GANP/THP3.
DR InterPro; IPR005062; SAC3/GANP/THP3_conserved.
DR PANTHER; PTHR12436; PTHR12436; 1.
DR Pfam; PF03399; SAC3_GANP; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..470
FT /note="Protein THP3"
FT /id="PRO_0000257823"
FT DOMAIN 276..450
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 470 AA; 53719 MW; EA682621C469CDE4 CRC64;
MQNPYGHFTN NTTEDREASS QGGPFGQSLN RPLDYAGSFP SLTYNNNNFI ANQQPSLPLP
EPRLSWNNVN QVSNPLMVTP LPGLQKRMNK NIKKKLPRVS KKASALSNGV SGNVMSNSNI
VGHGAVGSAS GWKVEMGGSD ELERRKRRAE RFSQGPSATT NSNDNLNEDF ANLNAISSKS
HQYDKKIHVV GRCQTLEKSY LRLTSEPNPD LIRPPNILQK MYCLLMDKYQ SKTATYTYLC
DQFKSMRQDL RVQMIENSFT IKVYQTHARI ALENGDLGEF NQCQNRIMAL FENPTIPKKS
YSEFICYSVL YSMLTEDYPS ISHLKLKLID DGSSEILEDE HVKMIFELSD MKLVGNYHYF
MKNYLKLHKF EKCLINSFLN LEKLIFLTII CKSYNQVNLD FVKSEFNFNS IEETTNFLNE
QNLTEFILNK QITDSNGKSS NIKILNTKGC RVQLIQNYMK SKKIDIKGQK
