ID   TTI2_YEAST              Reviewed;         421 AA.
AC   P47168; D6VWV5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=TEL2-interacting protein 2;
GN   Name=TTI2; OrderedLocusNames=YJR136C; ORFNames=J2124;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA   Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA   Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA   Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT   "Assigning function to yeast proteins by integration of technologies.";
RL   Mol. Cell 12:1353-1365(2003).
RN   [5]
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   [6]
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   [7]
RP   IDENTIFICATION IN THE ASTRA COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=19040720; DOI=10.1186/gb-2008-9-11-r167;
RA   Shevchenko A., Roguev A., Schaft D., Buchanan L., Habermann B., Sakalar C.,
RA   Thomas H., Krogan N.J., Shevchenko A., Stewart A.F.;
RT   "Chromatin Central: towards the comparative proteome by accurate mapping of
RT   the yeast proteomic environment.";
RL   Genome Biol. 9:R167.1-R167.22(2008).
RN   [8]
RP   INTERACTION WITH TEL2 AND TTI1.
RX   PubMed=20801936; DOI=10.1101/gad.1956410;
RA   Takai H., Xie Y., de Lange T., Pavletich N.P.;
RT   "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and
RT   ATR complexes.";
RL   Genes Dev. 24:2019-2030(2010).
RN   [9]
RP   IDENTIFICATION BY MASS 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: Component of the ASTRA complex probably in chromatin
CC       remodeling.
CC   -!- SUBUNIT: Component of the ASTRA chromatin remodeling machinery complex
CC       composed of at least RVB1, RVB2, TRA1, TEL2, TT1 and TTI2. Component of
CC       the TTT complex composed of TEL2, TTI1 and TTI2. Interacts with TEL2
CC       and TTI1. {ECO:0000269|PubMed:19040720, ECO:0000269|PubMed:20801936}.
CC   -!- INTERACTION:
CC       P47168; P36097: TTI1; NbExp=3; IntAct=EBI-25698, EBI-26630;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000305|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1470 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TTI2 family. {ECO:0000305}.
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DR   EMBL; Z49636; CAA89668.1; -; Genomic_DNA.
DR   EMBL; AY692606; AAT92625.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08921.1; -; Genomic_DNA.
DR   PIR; S57159; S57159.
DR   RefSeq; NP_012670.3; NM_001181794.3.
DR   AlphaFoldDB; P47168; -.
DR   BioGRID; 33892; 214.
DR   ComplexPortal; CPX-1422; TEL2-TTI1-TTI2 complex.
DR   DIP; DIP-1913N; -.
DR   IntAct; P47168; 9.
DR   MINT; P47168; -.
DR   STRING; 4932.YJR136C; -.
DR   iPTMnet; P47168; -.
DR   MaxQB; P47168; -.
DR   PaxDb; 4932-YJR136C; -.
DR   PeptideAtlas; P47168; -.
DR   EnsemblFungi; YJR136C_mRNA; YJR136C; YJR136C.
DR   GeneID; 853601; -.
DR   KEGG; sce:YJR136C; -.
DR   AGR; SGD:S000003897; -.
DR   SGD; S000003897; TTI2.
DR   VEuPathDB; FungiDB:YJR136C; -.
DR   eggNOG; ENOG502QU79; Eukaryota.
DR   HOGENOM; CLU_054067_0_0_1; -.
DR   InParanoid; P47168; -.
DR   OMA; SSNLWWI; -.
DR   OrthoDB; 1977924at2759; -.
DR   BioCyc; YEAST:G3O-31753-MONOMER; -.
DR   BioGRID-ORCS; 853601; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P47168; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47168; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0110078; C:TTT Hsp90 cochaperone complex; IPI:ComplexPortal.
DR   GO; GO:0034605; P:cellular response to heat; IMP:SGD.
DR   GO; GO:0031669; P:cellular response to nutrient levels; IMP:SGD.
DR   GO; GO:0071472; P:cellular response to salt stress; IMP:SGD.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:DNA damage response; IMP:SGD.
DR   GO; GO:2000003; P:positive regulation of DNA damage checkpoint; NAS:ComplexPortal.
DR   GO; GO:0050821; P:protein stabilization; NAS:ComplexPortal.
DR   InterPro; IPR018870; Tti2.
DR   Pfam; PF10521; Tti2; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..421
FT                   /note="TEL2-interacting protein 2"
FT                   /id="PRO_0000203122"
SQ   SEQUENCE   421 AA;  48649 MW;  12042525F61D8D3F CRC64;
     MTAVTDIIDE LNDSSLSSTR LRELCLQLRK KTDTGCAITV SDEVNLIESL SYHSISPGVD
     IQINTDVLQT IDYYFQRNKS EHDEIMCVLI SKLQPLLLKR KSNFELKEQR NLGLKPTLGM
     SLKEDNLMQA WVSQGGLKGI PLFYVILLHL KRRDISTNLS WIIPGILNIL DDTTDIRRIK
     LRGVLLLQTL LNHTFMNETN DSKWIQFSST GLFPLFEKTL INMCYFLPPS YNADETIAIW
     RVVFPTIQSL YKVEFLDNYT KYQYHLEKFM SEIILQNIIP RASLAYENLT LYALECTMNI
     LRLQREGSVV HLQRLIFVLG EYIVRNPFYT TFPKLISKTL SVVSTLIKVC PNERIVAHRF
     DILSLILVTY DKCSQEDALN ESILQQCKET ISWLLNCDCA MGEQLSTLSK QPRFQLLFEF
     S
//