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EST1_YEAST
ID   EST1_YEAST              Reviewed;         699 AA.
AC   P17214; D6VYN3; Q05997;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Telomere elongation protein EST1;
DE   AltName: Full=Ever shorter telomeres protein 1;
GN   Name=EST1; OrderedLocusNames=YLR233C; ORFNames=L8083.15;
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=2655926; DOI=10.1016/0092-8674(89)90132-3;
RA   Lundblad V., Szostak J.W.;
RT   "A mutant with a defect in telomere elongation leads to senescence in
RT   yeast.";
RL   Cell 57:633-643(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   PUTATIVE SIMILARITY TO REVERSE TRANSCRIPTASES.
RX   PubMed=2406024; DOI=10.1016/0092-8674(90)90653-v;
RA   Lundblad V., Blackburn E.H.;
RT   "RNA-dependent polymerase motifs in EST1: tentative identification of a
RT   protein component of an essential yeast telomerase.";
RL   Cell 60:529-530(1990).
RN   [5]
RP   SHOWS THAT THIS SIMILARITY IS DOUBTFUL.
RX   PubMed=1669287;
RA   Henikoff S.;
RT   "Playing with blocks: some pitfalls of forcing multiple alignments.";
RL   New Biol. 3:1148-1154(1991).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH CDC13.
RX   PubMed=11390652; DOI=10.1128/mcb.21.13.4233-4245.2001;
RA   Meier B., Driller L., Jaklin S., Feldmann H.M.;
RT   "New function of CDC13 in positive telomere length regulation.";
RL   Mol. Cell. Biol. 21:4233-4245(2001).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH MPS3.
RX   PubMed=17245108; DOI=10.4161/cc.6.1.3647;
RA   Antoniacci L.M., Kenna M.A., Skibbens R.V.;
RT   "The nuclear envelope and spindle pole body-associated Mps3 protein bind
RT   telomere regulators and function in telomere clustering.";
RL   Cell Cycle 6:75-79(2007).
CC   -!- FUNCTION: Directly involved in telomere replication. Associates with
CC       telomerase and during its interaction with CDC13, telomerase activity
CC       is promoted. {ECO:0000269|PubMed:11390652,
CC       ECO:0000269|PubMed:17245108}.
CC   -!- SUBUNIT: Interacts with CDC13 and MPS3. {ECO:0000269|PubMed:11390652,
CC       ECO:0000269|PubMed:17245108}.
CC   -!- INTERACTION:
CC       P17214; P32797: CDC13; NbExp=3; IntAct=EBI-6684, EBI-4187;
CC       P17214; Q06163: EST2; NbExp=4; IntAct=EBI-6684, EBI-3764464;
CC       P17214; P47069: MPS3; NbExp=3; IntAct=EBI-6684, EBI-25811;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the EST1 family. {ECO:0000305}.
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DR   EMBL; J04849; AAA66908.1; -; Genomic_DNA.
DR   EMBL; U19027; AAB67418.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09549.1; -; Genomic_DNA.
DR   PIR; S51454; S51454.
DR   RefSeq; NP_013334.1; NM_001182120.1.
DR   AlphaFoldDB; P17214; -.
DR   SMR; P17214; -.
DR   BioGRID; 31502; 715.
DR   ComplexPortal; CPX-3298; Telomerase holoenzyme complex.
DR   DIP; DIP-1306N; -.
DR   IntAct; P17214; 36.
DR   MINT; P17214; -.
DR   STRING; 4932.YLR233C; -.
DR   iPTMnet; P17214; -.
DR   MaxQB; P17214; -.
DR   PaxDb; P17214; -.
DR   PRIDE; P17214; -.
DR   EnsemblFungi; YLR233C_mRNA; YLR233C; YLR233C.
DR   GeneID; 850934; -.
DR   KEGG; sce:YLR233C; -.
DR   SGD; S000004223; EST1.
DR   VEuPathDB; FungiDB:YLR233C; -.
DR   eggNOG; KOG2162; Eukaryota.
DR   GeneTree; ENSGT00940000176623; -.
DR   HOGENOM; CLU_394378_0_0_1; -.
DR   InParanoid; P17214; -.
DR   OMA; EFSCVNF; -.
DR   BioCyc; YEAST:G3O-32344-MON; -.
DR   Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:P17214; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P17214; protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005697; C:telomerase holoenzyme complex; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IPI:SGD.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR   GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
DR   GO; GO:0071919; P:G-quadruplex DNA formation; IDA:SGD.
DR   GO; GO:0032210; P:regulation of telomere maintenance via telomerase; IDA:SGD.
DR   GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; IDA:SGD.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR018834; DNA/RNA-bd_Est1-type.
DR   InterPro; IPR045153; Est1/Ebs1-like.
DR   InterPro; IPR019458; Est1_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR15696; PTHR15696; 1.
DR   Pfam; PF10374; EST1; 1.
DR   Pfam; PF10373; EST1_DNA_bind; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
PE   1: Evidence at protein level;
KW   Chromosome; DNA-binding; Nucleus; Reference proteome; Telomere.
FT   CHAIN           1..699
FT                   /note="Telomere elongation protein EST1"
FT                   /id="PRO_0000087072"
FT   REGION          641..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..662
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        49
FT                   /note="R -> C (in Ref. 1; AAA66908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="L -> V (in Ref. 1; AAA66908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="D -> N (in Ref. 1; AAA66908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        351
FT                   /note="M -> I (in Ref. 1; AAA66908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        535
FT                   /note="V -> M (in Ref. 1; AAA66908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        571
FT                   /note="Y -> H (in Ref. 1; AAA66908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        579
FT                   /note="N -> D (in Ref. 1; AAA66908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        582
FT                   /note="I -> M (in Ref. 1; AAA66908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        665
FT                   /note="R -> K (in Ref. 1; AAA66908)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   699 AA;  81800 MW;  9CF552AFDA6BDEDE CRC64;
     MDNEEVNEEC MRLFFKNARA HLDKHLTSRL TCDENAYITF RCFLDGIHRK STRFLEELLL
     KQENMYHNNN YERINDSVIP LVLKLLWLQI HEPTLQWFEH WFHDIMRLSN RRKFRVFRIF
     QKKMIQFFKI THRYYYDIIE HLCAKYDMNS VISNALFAKL NLMQYTDGLS THEKIILNTS
     NPLTFSIVIS LQRCVINLGS THFYKTLLNK PSNKPKSVEG FEKSIRYLNI ASLYLPAVGD
     TYFQRAKIYL ITGKFSLYFF ELVRGALVRI PSKCALNNLK DFILTPDFPE RRRLMKKLAI
     LVSKDLKGEK SFFEGQIVLQ FLSIVEHTLV PQSWNASRAS NCWLLKEHLQ MAALKYHSGN
     INVILENLAA TMGSFDLMFT TRKSKEQKNK LKYADLSERQ VFFLDLSFDF IANIIDVVIK
     PSWQKNMEDF RYLAIIRLLM CWIKSYRSIL QYTHRHRKFC TSFALLLNDL INSPLNCSGN
     IYSHRPKRSY LFREDIIFRE FSCINFALTD FNDDYVYDSP DMINNIIGCP TLTKVLSPKE
     ECVLRIRSII FSGMKFLEKN DTGVIWNASK YKFDLISPNI KIKRQIALSE ISSKINVKTQ
     QERVVSSRKV EAKRDEQQRK RAGKIAVTEL EKQFANVRRT KKLSPLPEKD GVSSELVKHA
     ASRGRKTITG PLSSDFLSYP DEAIDADEDI TVQVPDTPT
 
 
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