ID   TTI1_YEAST              Reviewed;        1038 AA.
AC   P36097; D6VXQ3;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=TEL2-interacting protein 1;
GN   Name=TTI1; Synonyms=FMP47; OrderedLocusNames=YKL033W; ORFNames=YKL246;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8203146; DOI=10.1002/yea.320100112;
RA   Purnelle B., Skala J., van Dyck L., Goffeau A.;
RT   "Analysis of an 11.7 kb DNA fragment of chromosome XI reveals a new tRNA
RT   gene and four new open reading frames including a leucine zipper protein
RT   and a homologue to the yeast mitochondrial regulator ABF2.";
RL   Yeast 10:125-130(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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   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   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, 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).
RN   [9]
RP   INTERACTION WITH TEL2 AND TTI2.
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).
CC   -!- FUNCTION: Component of the ASTRA complex involved 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 TTI2. {ECO:0000269|PubMed:19040720, ECO:0000269|PubMed:20801936}.
CC   -!- INTERACTION:
CC       P36097; P47168: TTI2; NbExp=3; IntAct=EBI-26630, EBI-25698;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000305|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 721 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the tti1 family. {ECO:0000305}.
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DR   EMBL; X71622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z28033; CAA81868.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09123.1; -; Genomic_DNA.
DR   PIR; S37854; S37854.
DR   RefSeq; NP_012892.1; NM_001179599.1.
DR   AlphaFoldDB; P36097; -.
DR   BioGRID; 34099; 617.
DR   ComplexPortal; CPX-1422; TEL2-TTI1-TTI2 complex.
DR   DIP; DIP-1914N; -.
DR   IntAct; P36097; 5.
DR   MINT; P36097; -.
DR   STRING; 4932.YKL033W; -.
DR   iPTMnet; P36097; -.
DR   MaxQB; P36097; -.
DR   PaxDb; P36097; -.
DR   PRIDE; P36097; -.
DR   EnsemblFungi; YKL033W_mRNA; YKL033W; YKL033W.
DR   GeneID; 853834; -.
DR   KEGG; sce:YKL033W; -.
DR   SGD; S000001516; TTI1.
DR   VEuPathDB; FungiDB:YKL033W; -.
DR   eggNOG; KOG4524; Eukaryota.
DR   GeneTree; ENSGT00390000009748; -.
DR   HOGENOM; CLU_005544_0_0_1; -.
DR   InParanoid; P36097; -.
DR   OMA; GAHTCQV; -.
DR   BioCyc; YEAST:G3O-31836-MON; -.
DR   PRO; PR:P36097; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36097; protein.
DR   GO; GO:0070209; C:ASTRA complex; HDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR   GO; GO:0110078; C:TTT complex; IPI:ComplexPortal.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:2000003; P:positive regulation of DNA damage checkpoint; IC:ComplexPortal.
DR   GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR016441; Tti1.
DR   PIRSF; PIRSF005250; UCP005250; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1038
FT                   /note="TEL2-interacting protein 1"
FT                   /id="PRO_0000203185"
FT   REGION          810..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         817
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   1038 AA;  118889 MW;  D068AEC2F4556A72 CRC64;
     MNSDTNAFKD IRISCVELSR IAFLPTESFD PNSLTLLACL KKVEEKLSAY EDDSLSPKFA
     DYVFVPIASL LKQPALGESQ TEYVLLIIFH LLRTCWSSNG KFSEQLGQQL FPLITFLVSS
     DKDNQKLITR SDEFKYAGCL VLHQFFKSVR SQRYHKEFFS NSKPNLLPAL GHSVTILLKI
     LEQSPQNNEL QFKALASLEV LFQDIISDGE MLSFILPGNV SVFAKILTKP GRQIHYKVCV
     RTLEVLAKLL VLVYDDFSLD IKVNKLTDIR ELSDTKLKHE INQSFMFNGP IVLLRTDGKT
     HRDTSWLTAT SGQINIALEA FIPKLLKRNN ESIDEALATF VSILLTRCEN SLNNCEKVLV
     STLVHLERDP MSKLPSHLVK LKEVVNEDLH KLSDIIRFEN ADRLSSLSFA ITILEKNNER
     DTMINEVVRC LFESLNESIE PPSLINHKER IIEQSSQLTT TVNFENLEST NALIALPRLS
     EDMSLKLKKF TYHMGSLLLE RHILNDVVTE LISEQVDSPR TQKIVALWLS TNFIKAMEKQ
     PKEEEVYLQF ESDANYSSSM VEEVCLIVLE FCNELSQDIS MEIEGKGIKK SDEFAVCTVL
     FSIETICAVM REEFQPELID YIYTVVDALA SPSEAIRYVS QSCALRIADT LYHGSIPNMI
     LSNVDYLVES ISSRLNSGMT ERVSQILMVI CQLAGYETIE NFKDVIETIF KLLDYYHGYS
     DLCLQFFQLF KIIILEMKKK YINDDEMILK IANQHISQST FSPWGMTDFQ QVLNILDKET
     QVKDDITDEN DVDFLKDDNE PSNFQEYFDS KLREPDSDDD EEEREEEVEG SSKEYTDQWT
     SPIPSDSYKI LLQILGYGER LLTHPSKRLR VQILIVMRLI FPLLSTQHNL LIREVASTWD
     SIIQCVLCSD YSIVQPACSC VEQMIKYSGD FVAKRFIELW QKLCQDSFIL KELRIDPTVH
     NHEKKSISKH VKFPPVTENA LVSMVHMVLE GVKITEYLIS EAVLEQIIYC CIQVVPVEKI
     SSMSLIVGDI VWKIRNIN