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Protein Page:
TERT (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
TERT telomerase reverse transcriptase is a ribonucleoprotein polymerase that maintains telomere ends by addition of the telomere repeat TTAGGG. The holoenzyme consists of TERT and an RNA component which serves as a template for the telomere repeat. Telomerase expression plays a role in cellular senescence, as it is normally repressed in postnatal somatic cells resulting in progressive shortening of telomeres. Deregulation of telomerase expression in somatic cells may be involved in oncogenesis. Studies in mouse suggest that telomerase also participates in chromosomal repair, since de novo synthesis of telomere repeats may occur at double-stranded breaks. Alternatively spliced isoforms have been identified, although the full-length sequence of some variants has not been determined. Note: This description may include information from UniProtKB.
Protein type: DNA binding protein; Transferase; EC 2.7.7.49
Cellular Component: nucleoplasm; PML body; chromosome, telomeric region; nuclear telomere cap complex; cytoplasm; telomerase holoenzyme complex; nucleolus
Molecular Function: telomerase activity; protein binding; protein homodimerization activity; metal ion binding; telomeric DNA binding; telomeric template RNA reverse transcriptase activity
Biological Process: DNA strand elongation; telomere formation via telomerase; telomere maintenance via telomerase; telomere maintenance
Reference #:  O14746 (UniProtKB)
Alt. Names/Synonyms: EST2; HEST2; TCS1; Telomerase catalytic subunit; Telomerase reverse transcriptase; Telomerase-associated protein 2; TERT; TP2; TRT
Gene Symbols: TERT
Molecular weight: 126,997 Da
Basal Isoelectric point: 10.54  Predict pI for various phosphorylation states
Select Structure to View Below

TERT

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: Y707‑p
enzymatic activity, induced: S227‑p, S824‑p
intracellular localization: Y707‑p
molecular association, regulation: Y707‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
1 0 K78 FRQVSCLKELVARVL
1 0 K94 RLCERGAKNVLAFGF
2 0 S227-p GARRRGGsASRSLPL
1 0 K236 SRSLPLPKRPRRGAA
1 0 K329 PPVYAETKHFLYSSG
1 0 K338 FLYSSGDKEQLRPSF
4 0 Y707-p QDPPPELyFVKVDVT
2 0 S824-p AVRIRGKsYVQCQGI
0 1 G976 NMRRKLFGVLRLKCH
0 1 T1113-p KLPGTTLtALEAAAN
0 1 S1125-p AANPALPsDFKTILD
0 1 - gap
  TERT iso2  
K78 FRQVSCLKELVARVL
K94 RLCERGAKNVLAFGF
S227 GARRRGGSASRSLPL
K236 SRSLPLPKRPRRGAA
K329 PPVYAETKHFLYSSG
K338 FLYSSGDKEQLRPSF
Y707 QDPPPELYFVKVDVT
- gap
- gap
- gap
- gap
S797-p EQAVCGDsAGRAAPA
  TERT iso3  
K78-u FRQVSCLkELVARVL
K94-u RLCERGAkNVLAFGF
S227 GARRRGGSASRSLPL
K236-u SRSLPLPkRPRRGAA
K329-u PPVYAETkHFLYSSG
K338-u FLYSSGDkEQLRPSF
Y707 QDPPPELYFVKVDVT
S824 AVRIRGKSYVQCQGI
G913 NMRRKLFGVLRLKCH
T1050 KLPGTTLTALEAAAN
S1062 AANPALPSDFKTILD
- gap
  mouse

 
K78 FHQVSSLKELVARVV
R94 RLCERNERNVLAFGF
L236 GTKRHLSLTSTSVPS
K245 STSVPSAKKARCYPV
R333 LRPFIETRHFLYSRG
Q343 LYSRGDGQERLNPSF
Y697 LDQTPRMYFVKADVT
C817 VVKIGDRCYTQCQGI
S969-p TMRNKLLsVLRLKCH
T1103 KLPEATMTILKAAAD
T1115 AADPALSTDFQTILD
- gap
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