TEL2_YEAST
ID TEL2_YEAST Reviewed; 688 AA.
AC P53038; D6VUN1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Telomere length regulation protein TEL2;
GN Name=TEL2; OrderedLocusNames=YGR099W;
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].
RX PubMed=8649421; DOI=10.1128/mcb.16.6.3094;
RA Runge K.W., Zakian V.A.;
RT "TEL2, an essential gene required for telomere length regulation and
RT telomere position effect in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:3094-3105(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-419, AND
RP IDENTIFICATION BY 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 [6]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), INTERACTION WITH TTI1 AND TTI2, AND
RP MUTAGENESIS OF LEU-333; 333-LEU--MET-345 AND MET-345.
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: Part of the TTT complex that is required to stabilize protein
CC levels of the phosphatidylinositol 3-kinase-related protein kinase
CC (PIKK) family proteins (By similarity). Required for telomere length
CC regulation and telomere position effect. Regulates telomere length and
CC participates in gene silencing at subtelomeric regions. Binds to
CC telomeric DNA repeats. {ECO:0000250}.
CC -!- SUBUNIT: Component of the TTT complex composed of TEL2, TTI1 and TTI2.
CC Interacts with TTI1 and TTI2. {ECO:0000269|PubMed:20801936}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 638 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TEL2 family. {ECO:0000305}.
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DR EMBL; U38538; AAB60317.1; -; Genomic_DNA.
DR EMBL; Z72884; CAA97102.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08192.1; -; Genomic_DNA.
DR PIR; S64404; S64404.
DR RefSeq; NP_011613.3; NM_001181228.3.
DR PDB; 3O4Z; X-ray; 3.10 A; A/B/C/D=1-386, A/B/C/D=428-688.
DR PDBsum; 3O4Z; -.
DR AlphaFoldDB; P53038; -.
DR SMR; P53038; -.
DR BioGRID; 33342; 556.
DR ComplexPortal; CPX-1422; TEL2-TTI1-TTI2 complex.
DR DIP; DIP-1245N; -.
DR IntAct; P53038; 10.
DR MINT; P53038; -.
DR STRING; 4932.YGR099W; -.
DR iPTMnet; P53038; -.
DR MaxQB; P53038; -.
DR PaxDb; P53038; -.
DR PRIDE; P53038; -.
DR EnsemblFungi; YGR099W_mRNA; YGR099W; YGR099W.
DR GeneID; 852991; -.
DR KEGG; sce:YGR099W; -.
DR SGD; S000003331; TEL2.
DR VEuPathDB; FungiDB:YGR099W; -.
DR eggNOG; KOG4346; Eukaryota.
DR GeneTree; ENSGT00390000006698; -.
DR HOGENOM; CLU_444244_0_0_1; -.
DR InParanoid; P53038; -.
DR OMA; ERTMFIA; -.
DR BioCyc; YEAST:G3O-30809-MON; -.
DR EvolutionaryTrace; P53038; -.
DR PRO; PR:P53038; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53038; protein.
DR GO; GO:0070209; C:ASTRA complex; HDA:SGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0110078; C:TTT complex; IPI:ComplexPortal.
DR GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
DR GO; GO:2000003; P:positive regulation of DNA damage checkpoint; IC:ComplexPortal.
DR GO; GO:0034502; P:protein localization to chromosome; IMP:SGD.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:SGD.
DR Gene3D; 1.25.40.720; -; 2.
DR InterPro; IPR038528; TEL2_C_sf.
DR InterPro; IPR019337; Telomere_length_regulation_dom.
DR Pfam; PF10193; Telomere_reg-2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Telomere.
FT CHAIN 1..688
FT /note="Telomere length regulation protein TEL2"
FT /id="PRO_0000215561"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT VARIANT 129
FT /note="S -> R (in TEL2-1; short telomere length)"
FT MUTAGEN 333
FT /note="L->Q: Does not inhibit interaction with TTI1 or
FT TTI2. Inhibits interaction with TTI1 or TTI2; when
FT associated with E-345."
FT /evidence="ECO:0000269|PubMed:20801936"
FT MUTAGEN 345
FT /note="M->E: Does not inhibit weakly interaction with TTI1
FT or TTI2. Inhibits interaction with TTI1 or TTI2; when
FT associated with Q-333."
FT /evidence="ECO:0000269|PubMed:20801936"
FT CONFLICT 226
FT /note="Q -> P (in Ref. 1; AAB60317)"
FT /evidence="ECO:0000305"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:3O4Z"
FT TURN 6..8
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:3O4Z"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 85..100
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 130..135
FT /evidence="ECO:0007829|PDB:3O4Z"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 141..157
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 252..257
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 273..288
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 293..309
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 338..351
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 437..444
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 456..467
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 476..489
FT /evidence="ECO:0007829|PDB:3O4Z"
FT TURN 497..500
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 501..513
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 518..525
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 532..550
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 616..618
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 619..632
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 642..657
FT /evidence="ECO:0007829|PDB:3O4Z"
FT STRAND 659..663
FT /evidence="ECO:0007829|PDB:3O4Z"
FT HELIX 664..681
FT /evidence="ECO:0007829|PDB:3O4Z"
SQ SEQUENCE 688 AA; 78687 MW; 617B5DF89C6A9033 CRC64;
MVLETLKQGL DSSQIHEALI QLDSYPREPV DLDASMVLIK FVIPVYPSLP ERSKVILRRL
ASKSFTFLCQ IVTFSRTISG RDGLQEIRIY QEILEDIISF EPGCLTFYLK ASTTSKADRD
SIKALFFGSK LFNVLANRID MAKYLGYLRL QWKFLLESNE TDPPGFLGEW LVSSFLLNPV
LAADMLLGEL FLLKESYFFS FQKIISASSL IDQKRLIAKF LLPYIQVIVT LENLNDVRKI
LRRFDLDKII SLSVLFEIQS LPLKEVIVRL MSNHSSTKFV SALVSKFADF TDEEVDTKTC
ELLVLFAVHN LNHSQREEIA HDERFLNGVT KHLGSNEREA RERAMFIAKL LSGGHLKYES
DFKINIPNVK FESNSDDKII DFQSLKNPSI CNTQTDVGKD KITEVSGHVQ SLTLDCSDSD
DEDENDEREI VKRIVFLKDL MKEYEKTGES RKAPLIPLLK QTVKLIRQKA DFQLEVGYYA
QGILSSIVCL NNEFDEPLFE QWRINALTSI LVVLPEKVNG AINILFNSEL SLQQRMSLLS
ALGLSARELR GLDDPTIVKP KFDFPTNRLP WDDQSHHNSR LVEVQESTSM IKKTKTVWKS
RKLGKDREKG TQNRFRKYAG LFFYPLAHGW LNGIDVGTYN QLFKSHYLTT LRIIYSCANP
VHDFESMTEL MNHIISSAIE EGISLNKG
