TERT_HUMAN - dbPTM
TERT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TERT_HUMAN
UniProt AC O14746
Protein Name Telomerase reverse transcriptase
Gene Name TERT
Organism Homo sapiens (Human).
Sequence Length 1132
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm. Nucleus. Chromosome, telomere. Cytoplasm. Nucleus, PML body. Shuttling between nuclear and cytoplasm depends on cell cycle, phosphorylation states, transformation and DNA damage. Diffuse localization in the
Protein Description Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis..
Protein Sequence MPRAPRCRAVRSLLRSHYREVLPLATFVRRLGPQGWRLVQRGDPAAFRALVAQCLVCVPWDARPPPAAPSFRQVSCLKELVARVLQRLCERGAKNVLAFGFALLDGARGGPPEAFTTSVRSYLPNTVTDALRGSGAWGLLLRRVGDDVLVHLLARCALFVLVAPSCAYQVCGPPLYQLGAATQARPPPHASGPRRRLGCERAWNHSVREAGVPLGLPAPGARRRGGSASRSLPLPKRPRRGAAPEPERTPVGQGSWAHPGRTRGPSDRGFCVVSPARPAEEATSLEGALSGTRHSHPSVGRQHHAGPPSTSRPPRPWDTPCPPVYAETKHFLYSSGDKEQLRPSFLLSSLRPSLTGARRLVETIFLGSRPWMPGTPRRLPRLPQRYWQMRPLFLELLGNHAQCPYGVLLKTHCPLRAAVTPAAGVCAREKPQGSVAAPEEEDTDPRRLVQLLRQHSSPWQVYGFVRACLRRLVPPGLWGSRHNERRFLRNTKKFISLGKHAKLSLQELTWKMSVRDCAWLRRSPGVGCVPAAEHRLREEILAKFLHWLMSVYVVELLRSFFYVTETTFQKNRLFFYRKSVWSKLQSIGIRQHLKRVQLRELSEAEVRQHREARPALLTSRLRFIPKPDGLRPIVNMDYVVGARTFRREKRAERLTSRVKALFSVLNYERARRPGLLGASVLGLDDIHRAWRTFVLRVRAQDPPPELYFVKVDVTGAYDTIPQDRLTEVIASIIKPQNTYCVRRYAVVQKAAHGHVRKAFKSHVSTLTDLQPYMRQFVAHLQETSPLRDAVVIEQSSSLNEASSGLFDVFLRFMCHHAVRIRGKSYVQCQGIPQGSILSTLLCSLCYGDMENKLFAGIRRDGLLLRLVDDFLLVTPHLTHAKTFLRTLVRGVPEYGCVVNLRKTVVNFPVEDEALGGTAFVQMPAHGLFPWCGLLLDTRTLEVQSDYSSYARTSIRASLTFNRGFKAGRNMRRKLFGVLRLKCHSLFLDLQVNSLQTVCTNIYKILLLQAYRFHACVLQLPFHQQVWKNPTFFLRVISDTASLCYSILKAKNAGMSLGAKGAAGPLPSEAVQWLCHQAFLLKLTRHRVTYVPLLGSLRTAQTQLSRKLPGTTLTALEAAANPALPSDFKTILD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
26PhosphorylationREVLPLATFVRRLGP
HHHHHHHHHHHHHCH		30.28-
122PhosphorylationFTTSVRSYLPNTVTD
HHHHHHHHCCCHHHH		18.66-
134PhosphorylationVTDALRGSGAWGLLL
HHHHHHCCCHHHHHH		20.92-
227PhosphorylationGARRRGGSASRSLPL
CCCCCCCCCCCCCCC		26.3722366458
249PhosphorylationAAPEPERTPVGQGSW
CCCCCCCCCCCCCCC		22.21-
283PhosphorylationARPAEEATSLEGALS
CCCHHHHCCCCHHHC		36.8022210691
284PhosphorylationRPAEEATSLEGALSG
CCHHHHCCCCHHHCC		31.3222210691
344PhosphorylationDKEQLRPSFLLSSLR
CHHHHCHHHHHHHCC		23.3030622161
348PhosphorylationLRPSFLLSSLRPSLT
HCHHHHHHHCCHHHC		29.4917081983
349PhosphorylationRPSFLLSSLRPSLTG
CHHHHHHHCCHHHCH		28.5025954137
353PhosphorylationLLSSLRPSLTGARRL
HHHHCCHHHCHHHHH		31.9324719451
457PhosphorylationQLLRQHSSPWQVYGF
HHHHHCCCHHHHHHH		28.2123362280
480PhosphorylationVPPGLWGSRHNERRF
CCCCCCCCCHHHHHH		20.8424719451
618PhosphorylationEARPALLTSRLRFIP
HHHHHHHHHCEEECC		16.7924719451
679PhosphorylationRPGLLGASVLGLDDI
CCCCCCCHHCCHHHH		18.9727251275
692PhosphorylationDIHRAWRTFVLRVRA
HHHHHHHHEEEEEEE		13.8527251275
707PhosphorylationQDPPPELYFVKVDVT
CCCCCCEEEEEEECC		12.5016627250
707 (in isoform 4)Phosphorylation-12.5012808100
731PhosphorylationRLTEVIASIIKPQNT
HHHHHHHHHHCCCCC		17.4524719451
767PhosphorylationKSHVSTLTDLQPYMR
HHHCCHHHHCHHHHH		34.45-
785 (in isoform 4)Phosphorylation-38.54-
797 (in isoform 2)Phosphorylation-40.22-
797PhosphorylationVVIEQSSSLNEASSG
EEEECCCCCCHHHHC		40.2216565220
824PhosphorylationAVRIRGKSYVQCQGI
HHHHCCCCEEECCCC		33.1022817900
948PhosphorylationEVQSDYSSYARTSIR
EECCCCHHHCHHCHH		19.31-
949PhosphorylationVQSDYSSYARTSIRA
ECCCCHHHCHHCHHE		8.31-
984PhosphorylationVLRLKCHSLFLDLQV
HHHHHHHHHHHHCCC		30.22-
1045PhosphorylationDTASLCYSILKAKNA
CHHHHHHHHHHHHHC		22.0524719451
1059AcetylationAGMSLGAKGAAGPLP
CCCCCCCCCCCCCCC		47.4830592905
1095PhosphorylationTYVPLLGSLRTAQTQ
CHHHHHHHHHHHHHH		18.0424719451
1101PhosphorylationGSLRTAQTQLSRKLP
HHHHHHHHHHHHCCC		29.0716094384
1113PhosphorylationKLPGTTLTALEAAAN
CCCCCHHHHHHHHHC		27.4016094384
1125PhosphorylationAANPALPSDFKTILD
HHCCCCCCCCCHHCC		57.4316094384
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
227SPhosphorylationKinaseAKT1P31749
Uniprot
227SPhosphorylationKinaseAKT-FAMILY-GPS
227SPhosphorylationKinasePKB_GROUP-PhosphoELM
249TPhosphorylationKinaseCDK1P06493
PSP
457SPhosphorylationKinaseDYRK2Q92630
Uniprot
707YPhosphorylationKinaseSRCP12931
PSP
707YPhosphorylationKinaseSRC-FAMILY-GPS
707YPhosphorylationKinaseSRC-TYPE TYR-KINASES-Uniprot
707YPhosphorylationKinaseSRC64-PhosphoELM
824SPhosphorylationKinaseAKT1P31749
PSP
824SPhosphorylationKinaseAKT-FAMILY-GPS
824SPhosphorylationKinasePKB_GROUP-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:20453884
-KUbiquitinationE3 ubiquitin ligaseDYRK2Q92630
PMID:23362280
-KUbiquitinationE3 ubiquitin ligaseMKRN1Q9UHC7
PMID:15805468
-KUbiquitinationE3 ubiquitin ligaseDCAF1Q9Y4B6
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
227SPhosphorylation

22366458
457SPhosphorylation

23362280
457SPhosphorylation

23362280
457Subiquitylation

23362280
457Subiquitylation

23362280
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TERT_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUCL_HUMANNCLphysical
15371412
EST1A_HUMANSMG6physical
12699629
SMG5_HUMANSMG5physical
12699629
XRCC5_HUMANXRCC5physical
12377759
XRCC6_HUMANXRCC6physical
12377759
1433Z_HUMANYWHAZphysical
10835362
1433T_HUMANYWHAQphysical
10835362
PML_HUMANPMLphysical
19567472
NAT10_HUMANNAT10physical
18082603
MDM2_HUMANMDM2physical
20453884
EST1A_HUMANSMG6physical
22011238
TEBP_HUMANPTGES3physical
10197982
XRCC5_HUMANXRCC5physical
21855630
POTE1_HUMANPOT1physical
21855630
CHIP_HUMANSTUB1physical
20959453
HS90A_HUMANHSP90AA1physical
20959453
TEBP_HUMANPTGES3physical
20959453
HS90A_HUMANHSP90AA1physical
19751963
TEBP_HUMANPTGES3physical
19751963
DYRK2_HUMANDYRK2physical
23362280
UBR5_HUMANUBR5physical
23362280
RUVB1_HUMANRUVBL1physical
18358808
RUVB2_HUMANRUVBL2physical
18358808
CIB1_HUMANCIB1physical
15190070
XCT_HUMANSLC7A11physical
23741361
UB2D3_HUMANUBE2D3physical
23741361
SR140_HUMANU2SURPphysical
23741361
IREB2_HUMANIREB2physical
23741361
TGFR2_HUMANTGFBR2physical
23741361
AGAL_HUMANGLAphysical
23741361
PAIRB_HUMANSERBP1physical
23741361
DYL1_HUMANDYNLL1physical
23741361
P20L1_HUMANPHF20L1physical
23741361
ATPB_HUMANATP5Bphysical
23741361
FAP24_HUMANC19orf40physical
23741361
PFD1_HUMANPFDN1physical
23741361
TCPE_HUMANCCT5physical
23741361
IF2A_HUMANEIF2S1physical
23741361
TIM21_HUMANTIMM21physical
23741361
TBA1B_HUMANTUBA1Bphysical
23741361
PABP1_HUMANPABPC1physical
23741361
ANXA2_HUMANANXA2physical
23741361
DDX51_HUMANDDX51physical
23741361
TOPK_HUMANPBKphysical
23741361
STEA4_HUMANSTEAP4physical
23741361
THIM_HUMANACAA2physical
23741361
ENOA_HUMANENO1physical
23741361
PPIA_HUMANPPIAphysical
23741361
TEBP_HUMANPTGES3physical
11274138
HS90A_HUMANHSP90AA1physical
11274138
HSP74_HUMANHSPA4physical
11274138
AKT1_HUMANAKT1physical
18775701
FOXO3_HUMANFOXO3physical
26370108
MDM2_HUMANMDM2physical
26370108
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=Activation of telomerase has been implicated in cell immortalization and cancer cell pathogenesis.
609135
Note=Genetic variations in TERT are associated with coronary artery disease (CAD).
613989
614742Pulmonary fibrosis, and/or bone marrow failure, telomere-related, 1 (PFBMFT1)
613989Dyskeratosis congenita, autosomal recessive, 4 (DKCB4)
178500Pulmonary fibrosis, idiopathic (IPF)
615134Melanoma, cutaneous malignant 9 (CMM9)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00495Zidovudine
Regulatory Network of TERT_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1113 AND SER-1125, ANDMASS SPECTROMETRY.
"Nuclear protein tyrosine phosphatase Shp-2 is one important negativeregulator of nuclear export of telomerase reverse transcriptase.";
Jakob S., Schroeder P., Lukosz M., Buchner N., Spyridopoulos I.,Altschmied J., Haendeler J.;
J. Biol. Chem. 283:33155-33161(2008).
Cited for: INTERACTION WITH PTPN11, PHOSPHORYLATION AT TYR-707, SUBCELLULARLOCATION, AND MUTAGENESIS OF TYR-707.
"Hydrogen peroxide triggers nuclear export of telomerase reversetranscriptase via Src kinase family-dependent phosphorylation oftyrosine 707.";
Haendeler J., Hoffmann J., Brandes R.P., Zeiher A.M., Dimmeler S.;
Mol. Cell. Biol. 23:4598-4610(2003).
Cited for: PHOSPHORYLATION AT TYR-707, SUBCELLULAR LOCATION, INTERACTION WITH RANAND XP01, AND MUTAGENESIS OF TYR-707.

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