P53038 · TEL2_YEAST

Function

function

Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins (By similarity).
Required for telomere length regulation and telomere position effect. Regulates telomere length and participates in gene silencing at subtelomeric regions. Binds to telomeric DNA repeats

Miscellaneous

Present with 638 molecules/cell in log phase SD medium.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromosome, telomeric region
Cellular Componentcytosol
Cellular Componentnucleus
Cellular ComponentTTT Hsp90 cochaperone complex
Molecular FunctionHsp90 protein binding
Molecular Functiontelomeric DNA binding
Biological Process'de novo' cotranslational protein folding
Biological Processpositive regulation of DNA damage checkpoint
Biological Processprotein localization to chromosome
Biological Processprotein stabilization
Biological Processtelomere maintenance
Biological Processtelomere maintenance via telomerase

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Telomere length regulation protein TEL2

Gene names

    • Name
      TEL2
    • Ordered locus names
      YGR099W

Organism names

Accessions

  • Primary accession
    P53038
  • Secondary accessions
    • D6VUN1

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variant129in TEL2-1; short telomere length
Mutagenesis333Does not inhibit interaction with TTI1 or TTI2. Inhibits interaction with TTI1 or TTI2; when associated with E-345.
Mutagenesis345Does not inhibit weakly interaction with TTI1 or TTI2. Inhibits interaction with TTI1 or TTI2; when associated with Q-333.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 18 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002155611-688Telomere length regulation protein TEL2
Modified residue417Phosphoserine
Modified residue419Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Component of the TTT complex composed of TEL2, TTI1 and TTI2. Interacts with TTI1 and TTI2.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Sequence similarities

Belongs to the TEL2 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    688
  • Mass (Da)
    78,687
  • Last updated
    1996-10-01 v1
  • Checksum
    617B5DF89C6A9033
MVLETLKQGLDSSQIHEALIQLDSYPREPVDLDASMVLIKFVIPVYPSLPERSKVILRRLASKSFTFLCQIVTFSRTISGRDGLQEIRIYQEILEDIISFEPGCLTFYLKASTTSKADRDSIKALFFGSKLFNVLANRIDMAKYLGYLRLQWKFLLESNETDPPGFLGEWLVSSFLLNPVLAADMLLGELFLLKESYFFSFQKIISASSLIDQKRLIAKFLLPYIQVIVTLENLNDVRKILRRFDLDKIISLSVLFEIQSLPLKEVIVRLMSNHSSTKFVSALVSKFADFTDEEVDTKTCELLVLFAVHNLNHSQREEIAHDERFLNGVTKHLGSNEREARERAMFIAKLLSGGHLKYESDFKINIPNVKFESNSDDKIIDFQSLKNPSICNTQTDVGKDKITEVSGHVQSLTLDCSDSDDEDENDEREIVKRIVFLKDLMKEYEKTGESRKAPLIPLLKQTVKLIRQKADFQLEVGYYAQGILSSIVCLNNEFDEPLFEQWRINALTSILVVLPEKVNGAINILFNSELSLQQRMSLLSALGLSARELRGLDDPTIVKPKFDFPTNRLPWDDQSHHNSRLVEVQESTSMIKKTKTVWKSRKLGKDREKGTQNRFRKYAGLFFYPLAHGWLNGIDVGTYNQLFKSHYLTTLRIIYSCANPVHDFESMTELMNHIISSAIEEGISLNKG

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict226in Ref. 1; AAB60317

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U38538
EMBL· GenBank· DDBJ
AAB60317.1
EMBL· GenBank· DDBJ
Genomic DNA
Z72884
EMBL· GenBank· DDBJ
CAA97102.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006941
EMBL· GenBank· DDBJ
DAA08192.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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