Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Telomere elongation protein EST1

Gene

EST1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Directly involved in telomere replication. Associates with telomerase and during its interaction with CDC13, telomerase activity is promoted.2 Publications

GO - Molecular functioni

  • RNA binding Source: SGD
  • single-stranded DNA binding Source: SGD
  • telomeric DNA binding Source: SGD

GO - Biological processi

  • G-quadruplex DNA formation Source: SGD
  • telomere maintenance Source: SGD
  • telomere maintenance via telomerase Source: SGD
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32344-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Telomere elongation protein EST1
Alternative name(s):
Ever shorter telomeres protein 1
Gene namesi
Name:EST1
Ordered Locus Names:YLR233C
ORF Names:L8083.15
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR233C.
SGDiS000004223. EST1.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: UniProtKB-SubCell
  • nucleolus Source: SGD
  • nucleus Source: SGD
  • telomerase holoenzyme complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 699699Telomere elongation protein EST1PRO_0000087072Add
BLAST

Proteomic databases

MaxQBiP17214.
PeptideAtlasiP17214.

PTM databases

iPTMnetiP17214.

Interactioni

Subunit structurei

Interacts with CDC13 and MPS3.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC13P327973EBI-6684,EBI-4187
EST2Q061632EBI-6684,EBI-3764464
MPS3P470693EBI-6684,EBI-25811

Protein-protein interaction databases

BioGridi31502. 507 interactions.
DIPiDIP-1306N.
IntActiP17214. 11 interactions.
MINTiMINT-387253.

Structurei

3D structure databases

ProteinModelPortaliP17214.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the EST1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000068698.
InParanoidiP17214.
KOiK11132.
OMAiNYERIND.
OrthoDBiEOG7V76G2.

Family and domain databases

InterProiIPR018834. DNA/RNA-bd_Est1-type.
IPR019458. EST1.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF10374. EST1. 1 hit.
PF10373. EST1_DNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.

Sequencei

Sequence statusi: Complete.

P17214-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNEEVNEEC MRLFFKNARA HLDKHLTSRL TCDENAYITF RCFLDGIHRK
60 70 80 90 100
STRFLEELLL KQENMYHNNN YERINDSVIP LVLKLLWLQI HEPTLQWFEH
110 120 130 140 150
WFHDIMRLSN RRKFRVFRIF QKKMIQFFKI THRYYYDIIE HLCAKYDMNS
160 170 180 190 200
VISNALFAKL NLMQYTDGLS THEKIILNTS NPLTFSIVIS LQRCVINLGS
210 220 230 240 250
THFYKTLLNK PSNKPKSVEG FEKSIRYLNI ASLYLPAVGD TYFQRAKIYL
260 270 280 290 300
ITGKFSLYFF ELVRGALVRI PSKCALNNLK DFILTPDFPE RRRLMKKLAI
310 320 330 340 350
LVSKDLKGEK SFFEGQIVLQ FLSIVEHTLV PQSWNASRAS NCWLLKEHLQ
360 370 380 390 400
MAALKYHSGN INVILENLAA TMGSFDLMFT TRKSKEQKNK LKYADLSERQ
410 420 430 440 450
VFFLDLSFDF IANIIDVVIK PSWQKNMEDF RYLAIIRLLM CWIKSYRSIL
460 470 480 490 500
QYTHRHRKFC TSFALLLNDL INSPLNCSGN IYSHRPKRSY LFREDIIFRE
510 520 530 540 550
FSCINFALTD FNDDYVYDSP DMINNIIGCP TLTKVLSPKE ECVLRIRSII
560 570 580 590 600
FSGMKFLEKN DTGVIWNASK YKFDLISPNI KIKRQIALSE ISSKINVKTQ
610 620 630 640 650
QERVVSSRKV EAKRDEQQRK RAGKIAVTEL EKQFANVRRT KKLSPLPEKD
660 670 680 690
GVSSELVKHA ASRGRKTITG PLSSDFLSYP DEAIDADEDI TVQVPDTPT
Length:699
Mass (Da):81,800
Last modified:November 1, 1997 - v2
Checksum:i9CF552AFDA6BDEDE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491R → C in AAA66908 (PubMed:2655926).Curated
Sequence conflicti85 – 851L → V in AAA66908 (PubMed:2655926).Curated
Sequence conflicti287 – 2871D → N in AAA66908 (PubMed:2655926).Curated
Sequence conflicti351 – 3511M → I in AAA66908 (PubMed:2655926).Curated
Sequence conflicti535 – 5351V → M in AAA66908 (PubMed:2655926).Curated
Sequence conflicti571 – 5711Y → H in AAA66908 (PubMed:2655926).Curated
Sequence conflicti579 – 5791N → D in AAA66908 (PubMed:2655926).Curated
Sequence conflicti582 – 5821I → M in AAA66908 (PubMed:2655926).Curated
Sequence conflicti665 – 6651R → K in AAA66908 (PubMed:2655926).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04849 Genomic DNA. Translation: AAA66908.1.
U19027 Genomic DNA. Translation: AAB67418.1.
BK006945 Genomic DNA. Translation: DAA09549.1.
PIRiS51454.
RefSeqiNP_013334.1. NM_001182120.1.

Genome annotation databases

EnsemblFungiiYLR233C; YLR233C; YLR233C.
GeneIDi850934.
KEGGisce:YLR233C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04849 Genomic DNA. Translation: AAA66908.1.
U19027 Genomic DNA. Translation: AAB67418.1.
BK006945 Genomic DNA. Translation: DAA09549.1.
PIRiS51454.
RefSeqiNP_013334.1. NM_001182120.1.

3D structure databases

ProteinModelPortaliP17214.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31502. 507 interactions.
DIPiDIP-1306N.
IntActiP17214. 11 interactions.
MINTiMINT-387253.

PTM databases

iPTMnetiP17214.

Proteomic databases

MaxQBiP17214.
PeptideAtlasiP17214.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR233C; YLR233C; YLR233C.
GeneIDi850934.
KEGGisce:YLR233C.

Organism-specific databases

EuPathDBiFungiDB:YLR233C.
SGDiS000004223. EST1.

Phylogenomic databases

GeneTreeiENSGT00530000068698.
InParanoidiP17214.
KOiK11132.
OMAiNYERIND.
OrthoDBiEOG7V76G2.

Enzyme and pathway databases

BioCyciYEAST:G3O-32344-MONOMER.

Miscellaneous databases

PROiP17214.

Family and domain databases

InterProiIPR018834. DNA/RNA-bd_Est1-type.
IPR019458. EST1.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF10374. EST1. 1 hit.
PF10373. EST1_DNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A mutant with a defect in telomere elongation leads to senescence in yeast."
    Lundblad V., Szostak J.W.
    Cell 57:633-643(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "RNA-dependent polymerase motifs in EST1: tentative identification of a protein component of an essential yeast telomerase."
    Lundblad V., Blackburn E.H.
    Cell 60:529-530(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PUTATIVE SIMILARITY TO REVERSE TRANSCRIPTASES.
  5. "Playing with blocks: some pitfalls of forcing multiple alignments."
    Henikoff S.
    New Biol. 3:1148-1154(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SHOWS THAT THIS SIMILARITY IS DOUBTFUL.
  6. "New function of CDC13 in positive telomere length regulation."
    Meier B., Driller L., Jaklin S., Feldmann H.M.
    Mol. Cell. Biol. 21:4233-4245(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDC13.
  7. "The nuclear envelope and spindle pole body-associated Mps3 protein bind telomere regulators and function in telomere clustering."
    Antoniacci L.M., Kenna M.A., Skibbens R.V.
    Cell Cycle 6:75-79(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MPS3.

Entry informationi

Entry nameiEST1_YEAST
AccessioniPrimary (citable) accession number: P17214
Secondary accession number(s): D6VYN3, Q05997
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: November 1, 1997
Last modified: June 8, 2016
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.