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 length regulation protein TEL2 homolog

Gene

TELO2

Organism
Homo sapiens (Human)
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.2 Publications

GO - Molecular functioni

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

GO - Biological processi

  • positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  • positive regulation of TORC1 signaling Source: UniProtKB
  • positive regulation of TORC2 signaling Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • regulation of TOR signaling Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

SIGNORiQ9Y4R8.

Names & Taxonomyi

Protein namesi
Recommended name:
Telomere length regulation protein TEL2 homolog
Alternative name(s):
Protein clk-2 homolog
Short name:
hCLK2
Gene namesi
Name:TELO2
Synonyms:KIAA0683
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:29099. TELO2.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • intracellular Source: LIFEdb
  • membrane Source: UniProtKB-SubCell
  • nuclear periphery Source: UniProtKB
  • nucleus Source: UniProtKB
  • TORC1 complex Source: UniProtKB
  • TORC2 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Membrane, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi485 – 4851S → A: Abolishes phosphorylation by CK2 in response to growth factor deprivation and subsequent ubiquitination and degradation. 1 Publication

Organism-specific databases

PharmGKBiPA162405604.

Polymorphism and mutation databases

BioMutaiTELO2.
DMDMi166987394.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 837837Telomere length regulation protein TEL2 homologPRO_0000318515Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei374 – 3741Hydroxyproline1 Publication
Modified residuei419 – 4191Hydroxyproline1 Publication
Modified residuei422 – 4221Hydroxyproline1 Publication
Modified residuei456 – 4561PhosphoserineBy similarity
Modified residuei485 – 4851Phosphoserine; by CK21 Publication
Modified residuei487 – 4871Phosphoserine1 Publication
Modified residuei491 – 4911Phosphoserine1 Publication
Modified residuei688 – 6881PhosphoserineCombined sources
Modified residuei836 – 8361PhosphoserineCombined sources

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.1 Publication
Phosphorylated at Ser-485 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.1 Publication
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 mTORC1.1 Publication

Keywords - PTMi

Acetylation, Hydroxylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y4R8.
MaxQBiQ9Y4R8.
PaxDbiQ9Y4R8.
PRIDEiQ9Y4R8.

PTM databases

iPTMnetiQ9Y4R8.
PhosphoSiteiQ9Y4R8.

Expressioni

Gene expression databases

BgeeiQ9Y4R8.
CleanExiHS_TELO2.
ExpressionAtlasiQ9Y4R8. baseline and differential.
GenevisibleiQ9Y4R8. HS.

Organism-specific databases

HPAiHPA041348.
HPA041473.

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 which mediates interaction of TELO2 with the R2TP complex composed of RUVBL1, RUVBL2, PIH1D1, and RPAP3 (PubMed:20864032, PubMed:24656813).6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei490 – 4901Interaction with PIH1D1By similarity
Sitei491 – 4911Interaction with PIH1D1By similarity
Sitei492 – 4921Interaction with PIH1D1By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ATMQ133154EBI-1043674,EBI-495465
PIH1D1Q9NWS014EBI-1043674,EBI-357318
TTI1O431567EBI-1043674,EBI-1055680

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi115223. 42 interactions.
DIPiDIP-40568N.
IntActiQ9Y4R8. 26 interactions.
MINTiMINT-4713011.
STRINGi9606.ENSP00000262319.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PSIX-ray2.45D/E489-498[»]
ProteinModelPortaliQ9Y4R8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TEL2 family.Curated

Phylogenomic databases

eggNOGiKOG4346. Eukaryota.
ENOG410XR2X. LUCA.
GeneTreeiENSGT00390000006698.
HOGENOMiHOG000154542.
HOVERGENiHBG108557.
InParanoidiQ9Y4R8.
KOiK11137.
OMAiWDSFFLE.
OrthoDBiEOG7CZK5T.
PhylomeDBiQ9Y4R8.
TreeFamiTF313925.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR019337. Telomere_length_regulation_dom.
[Graphical view]
PfamiPF10193. Telomere_reg-2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 4 hits.

Sequencei

Sequence statusi: Complete.

Q9Y4R8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPAPSEVRL AVREAIHALS SSEDGGHIFC TLESLKRYLG EMEPPALPRE
60 70 80 90 100
KEEFASAHFS PVLRCLASRL SPAWLELLPH GRLEELWASF FLEGPADQAF
110 120 130 140 150
LVLMETIEGA AGPSFRLMKM ARLLARFLRE GRLAVLMEAQ CRQQTQPGFI
160 170 180 190 200
LLRETLLGKV VALPDHLGNR LQQENLAEFF PQNYFRLLGE EVVRVLQAVV
210 220 230 240 250
DSLQGGLDSS VSFVSQVLGK ACVHGRQQEI LGVLVPRLAA LTQGSYLHQR
260 270 280 290 300
VCWRLVEQVP DRAMEAVLTG LVEAALGPEV LSRLLGNLVV KNKKAQFVMT
310 320 330 340 350
QKLLFLQSRL TTPMLQSLLG HLAMDSQRRP LLLQVLKELL ETWGSSSAIR
360 370 380 390 400
HTPLPQQRHV SKAVLICLAQ LGEPELRDSR DELLASMMAG VKCRLDSSLP
410 420 430 440 450
PVRRLGMIVA EVVSARIHPE GPPLKFQYEE DELSLELLAL ASPQPAGDGA
460 470 480 490 500
SEAGTSLVPA TAEPPAETPA EIVDGGVPQA QLAGSDSDLD SDDEFVPYDM
510 520 530 540 550
SGDRELKSSK APAYVRDCVE ALTTSEDIER WEAALRALEG LVYRSPTATR
560 570 580 590 600
EVSVELAKVL LHLEEKTCVV GFAGLRQRAL VAVTVTDPAP VADYLTSQFY
610 620 630 640 650
ALNYSLRQRM DILDVLTLAA QELSRPGCLG RTPQPGSPSP NTPCLPEAAV
660 670 680 690 700
SQPGSAVASD WRVVVEERIR SKTQRLSKGG PRQGPAGSPS RFNSVAGHFF
710 720 730 740 750
FPLLQRFDRP LVTFDLLGED QLVLGRLAHT LGALMCLAVN TTVAVAMGKA
760 770 780 790 800
LLEFVWALRF HIDAYVRQGL LSAVSSVLLS LPAARLLEDL MDELLEARSW
810 820 830
LADVAEKDPD EDCRTLALRA LLLLQRLKNR LLPPASP
Length:837
Mass (Da):91,747
Last modified:February 5, 2008 - v2
Checksum:i76CB619C73C1F1A7
GO

Sequence cautioni

The sequence BAA31658.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71E → R in BAA31658 (PubMed:9734811).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71E → G.
Corresponds to variant rs2667661 [ dbSNP | Ensembl ].
VAR_038752
Natural varianti7 – 71E → Q.
Corresponds to variant rs2667660 [ dbSNP | Ensembl ].
VAR_061839
Natural varianti146 – 1461Q → R.4 Publications
Corresponds to variant rs2235624 [ dbSNP | Ensembl ].
VAR_038753
Natural varianti511 – 5111A → V.
Corresponds to variant rs58099766 [ dbSNP | Ensembl ].
VAR_061840
Natural varianti674 – 6741Q → R.
Corresponds to variant rs2248128 [ dbSNP | Ensembl ].
VAR_038754

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014583 mRNA. Translation: BAA31658.3. Different initiation.
AL080126 mRNA. Translation: CAB45724.1.
AL137394 mRNA. Translation: CAB70722.1.
AE006467 Genomic DNA. Translation: AAK61284.1.
AL031705 Genomic DNA. Translation: CAC37283.1.
CH471112 Genomic DNA. Translation: EAW85647.1.
CH471112 Genomic DNA. Translation: EAW85649.1.
CH471112 Genomic DNA. Translation: EAW85650.1.
BC017188 mRNA. Translation: AAH17188.1.
CCDSiCCDS32363.1.
PIRiT12514.
RefSeqiNP_057195.2. NM_016111.3.
UniGeneiHs.271044.

Genome annotation databases

EnsembliENST00000262319; ENSP00000262319; ENSG00000100726.
GeneIDi9894.
KEGGihsa:9894.
UCSCiuc002cly.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014583 mRNA. Translation: BAA31658.3. Different initiation.
AL080126 mRNA. Translation: CAB45724.1.
AL137394 mRNA. Translation: CAB70722.1.
AE006467 Genomic DNA. Translation: AAK61284.1.
AL031705 Genomic DNA. Translation: CAC37283.1.
CH471112 Genomic DNA. Translation: EAW85647.1.
CH471112 Genomic DNA. Translation: EAW85649.1.
CH471112 Genomic DNA. Translation: EAW85650.1.
BC017188 mRNA. Translation: AAH17188.1.
CCDSiCCDS32363.1.
PIRiT12514.
RefSeqiNP_057195.2. NM_016111.3.
UniGeneiHs.271044.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PSIX-ray2.45D/E489-498[»]
ProteinModelPortaliQ9Y4R8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115223. 42 interactions.
DIPiDIP-40568N.
IntActiQ9Y4R8. 26 interactions.
MINTiMINT-4713011.
STRINGi9606.ENSP00000262319.

PTM databases

iPTMnetiQ9Y4R8.
PhosphoSiteiQ9Y4R8.

Polymorphism and mutation databases

BioMutaiTELO2.
DMDMi166987394.

Proteomic databases

EPDiQ9Y4R8.
MaxQBiQ9Y4R8.
PaxDbiQ9Y4R8.
PRIDEiQ9Y4R8.

Protocols and materials databases

DNASUi9894.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262319; ENSP00000262319; ENSG00000100726.
GeneIDi9894.
KEGGihsa:9894.
UCSCiuc002cly.4. human.

Organism-specific databases

CTDi9894.
GeneCardsiTELO2.
H-InvDBHIX0012685.
HGNCiHGNC:29099. TELO2.
HPAiHPA041348.
HPA041473.
MIMi611140. gene.
neXtProtiNX_Q9Y4R8.
PharmGKBiPA162405604.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4346. Eukaryota.
ENOG410XR2X. LUCA.
GeneTreeiENSGT00390000006698.
HOGENOMiHOG000154542.
HOVERGENiHBG108557.
InParanoidiQ9Y4R8.
KOiK11137.
OMAiWDSFFLE.
OrthoDBiEOG7CZK5T.
PhylomeDBiQ9Y4R8.
TreeFamiTF313925.

Enzyme and pathway databases

SIGNORiQ9Y4R8.

Miscellaneous databases

ChiTaRSiTELO2. human.
GeneWikiiTELO2.
GenomeRNAii9894.
PROiQ9Y4R8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y4R8.
CleanExiHS_TELO2.
ExpressionAtlasiQ9Y4R8. baseline and differential.
GenevisibleiQ9Y4R8. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR019337. Telomere_length_regulation_dom.
[Graphical view]
PfamiPF10193. Telomere_reg-2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 4 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-146.
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-146.
    Tissue: Testis.
  4. "Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
    Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
    Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-146.
  7. "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], VARIANT ARG-146.
    Tissue: Placenta.
  8. "Human CLK2 links cell cycle progression, apoptosis, and telomere length regulation."
    Jiang N., Benard C.Y., Kebir H., Shoubridge E.A., Hekimi S.
    J. Biol. Chem. 278:21678-21684(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "A genetic screen identifies the Triple T complex required for DNA damage signaling and ATM and ATR stability."
    Hurov K.E., Cotta-Ramusino C., Elledge S.J.
    Genes Dev. 24:1939-1950(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TTI1 AND TTI2.
  12. "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: INTERACTION WITH ATM; ATR; MTOR; PRKDC; RUVBL2; TTI1 AND TTI2.
  13. "Tti1 and Tel2 are critical factors in mammalian target of rapamycin complex assembly."
    Kaizuka T., Hara T., Oshiro N., Kikkawa U., Yonezawa K., Takehana K., Iemura S., Natsume T., Mizushima N.
    J. Biol. Chem. 285:20109-20116(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TTI1; MTOR; ATM; ATR; PRKDC; SMG1 AND TRRAP.
  14. "CK2 phospho-dependent binding of R2TP complex to TEL2 is essential for mTOR and SMG1 stability."
    Horejsi Z., Takai H., Adelman C.A., Collis S.J., Flynn H., Maslen S., Skehel J.M., de Lange T., Boulton S.J.
    Mol. Cell 39:839-850(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIH1D1.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-836, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "PHD3-dependent hydroxylation of HCLK2 promotes the DNA damage response."
    Xie L., Pi X., Mishra A., Fong G., Peng J., Patterson C.
    J. Clin. Invest. 122:2827-2836(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: HYDROXYLATION AT PRO-374; PRO-419 AND PRO-422 BY PHD3.
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "SCF(Fbxo9) and CK2 direct the cellular response to growth factor withdrawal via Tel2/Tti1 degradation and promote survival in multiple myeloma."
    Fernandez-Saiz V., Targosz B.S., Lemeer S., Eichner R., Langer C., Bullinger L., Reiter C., Slotta-Huspenina J., Schroeder S., Knorn A.M., Kurutz J., Peschel C., Pagano M., Kuster B., Bassermann F.
    Nat. Cell Biol. 15:72-81(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MTORC1 COMPLEX, IDENTIFICATION IN THE MTORC2 COMPLEX, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-485; SER-487 AND SER-491, UBIQUITINATION, MUTAGENESIS OF SER-485.
  21. "Phosphorylation-dependent PIH1D1 interactions define substrate specificity of the R2TP cochaperone complex."
    Horejsi Z., Stach L., Flower T.G., Joshi D., Flynn H., Skehel J.M., O'Reilly N.J., Ogrodowicz R.W., Smerdon S.J., Boulton S.J.
    Cell Rep. 7:19-26(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 489-498 IN COMPLEX WITH PIH1D1, INTERACTION WITH PIH1D1.

Entry informationi

Entry nameiTELO2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4R8
Secondary accession number(s): D3DU73
, O75168, Q7LDV4, Q9BR21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: June 8, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Cells overexpressing TELO2 are hypersensitive to hydroxyurea (HU) and undergo apoptotic death in response to treatment with HU.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.