TAH1_YEAST
ID TAH1_YEAST Reviewed; 111 AA.
AC P25638; D6VR65;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=TPR repeat-containing protein associated with Hsp90;
GN Name=TAH1; OrderedLocusNames=YCR060W; ORFNames=YCR60W;
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 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 INTERACTION WITH HSP90, IDENTIFICATION IN THE R2PT COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15766533; DOI=10.1016/j.cell.2004.12.024;
RA Zhao R., Davey M.G., Hsu Y.-C., Kaplanek P., Tong A., Parsons A.B.,
RA Krogan N.J., Cagney G., Mai D., Greenblatt J.F., Boone C., Emili A.,
RA Houry W.A.;
RT "Navigating the chaperone network: an integrative map of physical and
RT genetic interactions mediated by the hsp90 chaperone.";
RL Cell 120:715-727(2005).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 -!- SUBUNIT: Component of the R2TP complex composed at least of RVB1, RVB2,
CC TAH1 and PIH1. Interacts also with HSP90.
CC {ECO:0000269|PubMed:15766533}.
CC -!- INTERACTION:
CC P25638; P02829: HSP82; NbExp=10; IntAct=EBI-21956, EBI-8659;
CC P25638; P38768: PIH1; NbExp=17; IntAct=EBI-21956, EBI-24499;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1660 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X59720; CAA42288.1; -; Genomic_DNA.
DR EMBL; AY558151; AAS56477.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07534.1; -; Genomic_DNA.
DR PIR; S19475; S19475.
DR RefSeq; NP_009986.1; NM_001178771.1.
DR PDB; 2L6J; NMR; -; A=1-111.
DR PDB; 2LSU; NMR; -; A=2-111.
DR PDB; 2LSV; NMR; -; A=2-111.
DR PDB; 2MNJ; NMR; -; A=93-111.
DR PDB; 4CGQ; X-ray; 2.00 A; A=1-111.
DR PDB; 4CGU; X-ray; 2.11 A; A=1-111.
DR PDBsum; 2L6J; -.
DR PDBsum; 2LSU; -.
DR PDBsum; 2LSV; -.
DR PDBsum; 2MNJ; -.
DR PDBsum; 4CGQ; -.
DR PDBsum; 4CGU; -.
DR AlphaFoldDB; P25638; -.
DR BMRB; P25638; -.
DR SMR; P25638; -.
DR BioGRID; 31037; 113.
DR ComplexPortal; CPX-1814; R2TP co-chaperone complex.
DR DIP; DIP-5000N; -.
DR IntAct; P25638; 8.
DR MINT; P25638; -.
DR STRING; 4932.YCR060W; -.
DR iPTMnet; P25638; -.
DR PaxDb; P25638; -.
DR PRIDE; P25638; -.
DR EnsemblFungi; YCR060W_mRNA; YCR060W; YCR060W.
DR GeneID; 850424; -.
DR KEGG; sce:YCR060W; -.
DR SGD; S000000656; TAH1.
DR VEuPathDB; FungiDB:YCR060W; -.
DR eggNOG; KOG1124; Eukaryota.
DR HOGENOM; CLU_132745_0_0_1; -.
DR InParanoid; P25638; -.
DR OMA; PIGYSNK; -.
DR BioCyc; YEAST:G3O-29365-MON; -.
DR ChiTaRS; TAH1; yeast.
DR PRO; PR:P25638; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25638; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0097255; C:R2TP complex; IDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IDA:SGD.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:InterPro.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IMP:SGD.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR DisProt; DP01243; -.
DR Gene3D; 1.25.40.10; -; 1.
DR IDEAL; IID50204; -.
DR InterPro; IPR045248; Sti1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR22904; PTHR22904; 2.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW TPR repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..111
FT /note="TPR repeat-containing protein associated with Hsp90"
FT /id="PRO_0000106352"
FT REPEAT 4..37
FT /note="TPR 1"
FT REPEAT 39..71
FT /note="TPR 2"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:4CGQ"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:4CGQ"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:4CGQ"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:4CGQ"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:4CGU"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:4CGQ"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:4CGU"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:4CGU"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:2L6J"
SQ SEQUENCE 111 AA; 12511 MW; 3738DE6F227F803A CRC64;
MSQFEKQKEQ GNSLFKQGLY REAVHCYDQL ITAQPQNPVG YSNKAMALIK LGEYTQAIQM
CQQGLRYTST AEHVAIRSKL QYRLELAQGA VGSVQIPVVE VDELPEGYDR S
