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Protein

Telomere length regulation protein TEL2 homolog

Gene

Telo2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals. May be involved in telomere length regulation (By similarity).By similarity

GO - Molecular functioni

  • Hsp90 protein binding Source: MGI
  • protein complex binding Source: MGI
  • protein complex scaffold Source: MGI
  • protein kinase binding Source: MGI

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Telomere length regulation protein TEL2 homolog
Gene namesi
Name:Telo2
Synonyms:Kiaa0683
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1918968. Telo2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Membrane, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi395 – 3951L → Q: Does not inhibit interaction with TTI1 or TTI2. Inhibits weakly interaction with TTI1 or TTI2; when associated with E-407 or R-424. Inhibits interaction with TTI1 or TTI2; when associated with E-407 and R-424. 1 Publication
Mutagenesisi407 – 4071M → E: Does not inhibit interaction with TTI1 or TTI2. Inhibits weakly interaction with TTI1 or TTI2; when associated with Q-395 or R-424. Inhibits interaction with TTI1 or TTI2; when associated with Q-395 and R-424. 1 Publication
Mutagenesisi424 – 4241L → R: Does not inhibit interaction with TTI1 or TTI2. Inhibits weakly interaction with TTI1 or TTI2; when associated with Q-395 or E-407. Inhibits interaction with TTI1 or TTI2; when associated with Q-395 and E-407. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 840840Telomere length regulation protein TEL2 homologPRO_0000318516Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei374 – 3741HydroxyprolineBy similarity
Modified residuei419 – 4191HydroxyprolineBy similarity
Modified residuei422 – 4221HydroxyprolineBy similarity
Modified residuei457 – 4571PhosphoserineCombined sources
Modified residuei486 – 4861Phosphoserine; by CK2By similarity
Modified residuei488 – 4881PhosphoserineBy similarity
Modified residuei492 – 4921PhosphoserineBy similarity
Modified residuei837 – 8371PhosphoserineBy similarity

Post-translational modificationi

Hydroxylation by PHD3 is required for a proper interaction with ATR, and activation of the ATR/CHK1/p53 pathway following DNA damage.By similarity
Phosphorylated at Ser-486 by CK2 following growth factor deprivation, leading to its subsequent ubiquitination by the SCF(FBXO9) complex. Phosphorylation by CK2 only takes place when TELO2 is bound to mTORC1, not mTORC2; leading to selective ubiquitination of mTORC1-associated protein (By similarity).By similarity
Ubiquitinated by the SCF(FBXO9) complex following phosphorylation by CK2 in response to growth factor deprivation, leading to its degradation by the proteasome. Only mTORC1-associated protein is ubiquitinated and degraded, leading to selective inactivation of mTORC1 to restrain cell growth and protein translation, while mTORC2 is activated due to the relief of feedback inhibition by mTORC1 (By similarity).By similarity

Keywords - PTMi

Acetylation, Hydroxylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9DC40.
MaxQBiQ9DC40.
PaxDbiQ9DC40.
PRIDEiQ9DC40.

PTM databases

iPTMnetiQ9DC40.
PhosphoSiteiQ9DC40.

Expressioni

Gene expression databases

BgeeiQ9DC40.
GenevisibleiQ9DC40. MM.

Interactioni

Subunit structurei

Component of the TTT complex composed of TELO2, TTI1 and TTI2. Interacts with ATM, ATR, MTOR, PRKDC, RUVBL2, TTI1, TTI2, SMG1 and TRRAP. Component of the mTORC1 and mTORC2 complexes. Interacts (phosphorylated form) with PIH1D1 (PubMed:24794838). Interaction with PIH1D1 mediates interaction of TELO2 with the R2TP complex composed of RUVBL1, RUVBL2, PIH1D1, and RPAP3 (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei491 – 4911Interaction with PIH1D11 Publication
Sitei492 – 4921Interaction with PIH1D11 Publication
Sitei493 – 4931Interaction with PIH1D11 Publication

GO - Molecular functioni

  • Hsp90 protein binding Source: MGI
  • protein complex binding Source: MGI
  • protein complex scaffold Source: MGI
  • protein kinase binding Source: MGI

Protein-protein interaction databases

BioGridi214877. 3 interactions.
DIPiDIP-60997N.
IntActiQ9DC40. 2 interactions.
STRINGi10090.ENSMUSP00000024987.

Structurei

Secondary structure

1
840
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi492 – 4943Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CKTX-ray3.00C/D489-496[»]
4CSEX-ray3.30C/D488-496[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TEL2 family.Curated

Phylogenomic databases

eggNOGiKOG4346. Eukaryota.
ENOG410XR2X. LUCA.
GeneTreeiENSGT00390000006698.
HOVERGENiHBG108557.
InParanoidiQ9DC40.
KOiK11137.
OMAiWDSFFLE.
OrthoDBiEOG7CZK5T.
PhylomeDBiQ9DC40.
TreeFamiTF313925.

Family and domain databases

InterProiIPR019337. Telomere_length_regulation_dom.
[Graphical view]
PfamiPF10193. Telomere_reg-2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9DC40-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDPALSAVRL TVQEAIHILS SSEDAGHILS TLGTLKRYLG GTEDPVLPEE
60 70 80 90 100
KEEFATVHFS AVLRCLVSKL SPGWLELSPG GQLERLWESF FLDGPPDQAF
110 120 130 140 150
LVLMEAIEST AGPSFRLMKM AQLLDTFLST GRVAALMEEQ CRPQTKPSFP
160 170 180 190 200
LFQETLLSKV VGLPDLLGNC LQRDNLTQFF PQNYFPLLGQ EVVQALKAVV
210 220 230 240 250
NFLQDGLDCS VSFVSRVLGK VCIQGRKREI LSVLVPQLTV LTQDSCLWQR
260 270 280 290 300
VCWRLVEQVP DRAVEAVLTG LVEAAPRPEV LSRLLGNLVV KNKKARFVVT
310 320 330 340 350
RKLLLLQYQH TTPMVQSLLG YLALDSQRRP LLIQVLKELL ETWGCSSAVR
360 370 380 390 400
HTPLEQQCYI SKAILVCLAH LGEPELQDIR DELLASMMAG VKCRLDSSLP
410 420 430 440 450
PVRRLGMIVA EVISSRIHPE GPLLKFQYED DEMSRELLAL ATPEPAGDCS
460 470 480 490 500
SVSRGPSPAP VDTESPVEMP EKAVESDVPP TQPQGSDSEL DSDDEFIPYD
510 520 530 540 550
MSGDRELKSS KEPLYIRDCV EALTTSEDME RWEASLKGLE GLVYRSPTAT
560 570 580 590 600
REVSVELAKV LLHLEEKTCV AEFEQLRQSA LVAVTVTDPE QVAKYLTSQF
610 620 630 640 650
YGLNYSLRQR MDILDVLVLA AQALSRPKSL QRRSQHGPPV PGTMCSPALA
660 670 680 690 700
VSQTGNVAAP DWQVVVEERI RSKTRRFSKG CPQRELSGVP NEFSSVAGYF
710 720 730 740 750
FFPLLQHFDR PLVTFDLLGD DQLVLGRLTH TLASLMYLAV NTTVAVPMGK
760 770 780 790 800
ALLEFVWALR FHVDIYVRRG LLSAVSSVLL SVPTERLLGD LPDELLEARS
810 820 830 840
WLADVAEKDV DEDCRELAVR ALLLLERLKD KLLSSSSPQP
Length:840
Mass (Da):93,313
Last modified:February 5, 2008 - v2
Checksum:iC3ADB9DCE1724EAC
GO
Isoform 2 (identifier: Q9DC40-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-386: Missing.
     680-690: GCPQRELSGVP → VTGLCSDPMLS
     691-840: Missing.

Note: No experimental confirmation available.
Show »
Length:304
Mass (Da):33,494
Checksum:i1C17E24740BEC671
GO

Sequence cautioni

The sequence BAE25556.1 differs from that shown. Reason: Erroneous termination at position 771. Translated as Leu.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181I → T in AAS21644 (Ref. 2) Curated
Sequence conflicti18 – 181I → T in AAH11077 (PubMed:15489334).Curated
Sequence conflicti106 – 1061A → T in BAE32791 (PubMed:16141072).Curated
Sequence conflicti205 – 2051D → G in AAS21644 (Ref. 2) Curated
Sequence conflicti205 – 2051D → G in AAH11077 (PubMed:15489334).Curated
Sequence conflicti461 – 4611V → A in AAS21644 (Ref. 2) Curated
Sequence conflicti461 – 4611V → A in AAH11077 (PubMed:15489334).Curated
Sequence conflicti465 – 4651S → P in AAS21644 (Ref. 2) Curated
Sequence conflicti465 – 4651S → P in AAH11077 (PubMed:15489334).Curated
Sequence conflicti509 – 5091S → N in AAS21644 (Ref. 2) Curated
Sequence conflicti509 – 5091S → N in AAH11077 (PubMed:15489334).Curated
Sequence conflicti548 – 5481T → A in AAS21644 (Ref. 2) Curated
Sequence conflicti548 – 5481T → A in AAH11077 (PubMed:15489334).Curated
Sequence conflicti638 – 6392PP → SL in AAS21644 (Ref. 2) Curated
Sequence conflicti638 – 6392PP → SL in AAH11077 (PubMed:15489334).Curated
Sequence conflicti664 – 6641V → M in AAS21644 (Ref. 2) Curated
Sequence conflicti664 – 6641V → M in AAH11077 (PubMed:15489334).Curated
Sequence conflicti689 – 6891V → I in BAC26051 (PubMed:16141072).Curated
Sequence conflicti775 – 7751V → M in BAB23388 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 386386Missing in isoform 2. 1 PublicationVSP_031207Add
BLAST
Alternative sequencei680 – 69011GCPQRELSGVP → VTGLCSDPMLS in isoform 2. 1 PublicationVSP_031208Add
BLAST
Alternative sequencei691 – 840150Missing in isoform 2. 1 PublicationVSP_031209Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004582 mRNA. Translation: BAB23388.1.
AK045321 mRNA. Translation: BAC32309.1.
AK028658 mRNA. Translation: BAC26051.1.
AK143827 mRNA. Translation: BAE25556.1. Sequence problems.
AK146963 mRNA. Translation: BAE27569.1.
AK154727 mRNA. Translation: BAE32791.1.
AY491413 Genomic DNA. Translation: AAS21644.1.
BC011077 mRNA. Translation: AAH11077.1.
CCDSiCCDS28507.1. [Q9DC40-1]
RefSeqiNP_001157133.1. NM_001163661.1. [Q9DC40-1]
NP_082156.2. NM_027880.2. [Q9DC40-1]
UniGeneiMm.288702.

Genome annotation databases

EnsembliENSMUST00000024987; ENSMUSP00000024987; ENSMUSG00000024170. [Q9DC40-1]
ENSMUST00000115181; ENSMUSP00000110835; ENSMUSG00000024170. [Q9DC40-1]
GeneIDi71718.
KEGGimmu:71718.
UCSCiuc008azq.2. mouse. [Q9DC40-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004582 mRNA. Translation: BAB23388.1.
AK045321 mRNA. Translation: BAC32309.1.
AK028658 mRNA. Translation: BAC26051.1.
AK143827 mRNA. Translation: BAE25556.1. Sequence problems.
AK146963 mRNA. Translation: BAE27569.1.
AK154727 mRNA. Translation: BAE32791.1.
AY491413 Genomic DNA. Translation: AAS21644.1.
BC011077 mRNA. Translation: AAH11077.1.
CCDSiCCDS28507.1. [Q9DC40-1]
RefSeqiNP_001157133.1. NM_001163661.1. [Q9DC40-1]
NP_082156.2. NM_027880.2. [Q9DC40-1]
UniGeneiMm.288702.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CKTX-ray3.00C/D489-496[»]
4CSEX-ray3.30C/D488-496[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214877. 3 interactions.
DIPiDIP-60997N.
IntActiQ9DC40. 2 interactions.
STRINGi10090.ENSMUSP00000024987.

PTM databases

iPTMnetiQ9DC40.
PhosphoSiteiQ9DC40.

Proteomic databases

EPDiQ9DC40.
MaxQBiQ9DC40.
PaxDbiQ9DC40.
PRIDEiQ9DC40.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024987; ENSMUSP00000024987; ENSMUSG00000024170. [Q9DC40-1]
ENSMUST00000115181; ENSMUSP00000110835; ENSMUSG00000024170. [Q9DC40-1]
GeneIDi71718.
KEGGimmu:71718.
UCSCiuc008azq.2. mouse. [Q9DC40-1]

Organism-specific databases

CTDi9894.
MGIiMGI:1918968. Telo2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG4346. Eukaryota.
ENOG410XR2X. LUCA.
GeneTreeiENSGT00390000006698.
HOVERGENiHBG108557.
InParanoidiQ9DC40.
KOiK11137.
OMAiWDSFFLE.
OrthoDBiEOG7CZK5T.
PhylomeDBiQ9DC40.
TreeFamiTF313925.

Miscellaneous databases

PROiQ9DC40.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DC40.
GenevisibleiQ9DC40. MM.

Family and domain databases

InterProiIPR019337. Telomere_length_regulation_dom.
[Graphical view]
PfamiPF10193. Telomere_reg-2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Kidney, Lung, Skin and Spleen.
  2. "Genomic sequence analysis in the mouse T-complex region."
    Brathwaite M., Waeltz P., Dudekula D., Nagaraja R.
    Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Mammary tumor.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes."
    Takai H., Xie Y., de Lange T., Pavletich N.P.
    Genes Dev. 24:2019-2030(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-395; 395-LEU--MET-407; 395-LEU--LEU-424; MET-407; 407-MET--LEU-424 AND LEU-424.
  6. "Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1."
    Pal M., Morgan M., Phelps S.E., Roe S.M., Parry-Morris S., Downs J.A., Polier S., Pearl L.H., Prodromou C.
    Structure 22:805-818(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 488-496 IN COMPLEX WITH PIH1D1, INTERACTION WITH PIH1D1.

Entry informationi

Entry nameiTELO2_MOUSE
AccessioniPrimary (citable) accession number: Q9DC40
Secondary accession number(s): Q3U3J5
, Q3UID7, Q3UP41, Q8BN03, Q8C1T3, Q91VQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: June 8, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.