Reviewed, UniProtKB/Swiss-Prot O14746 (TERT_HUMAN)

Names and origin

Protein names

Recommended name:
    Telomerase reverse transcriptase
    EC=2.7.7.49
Alternative name(s):
    Telomerase catalytic subunit
    HEST2
    Telomerase-associated protein 2
      Short name=TP2

Gene names

Name:	TERT
Synonyms:	EST2, TCS1, TRT

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1132 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Ref.8
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Subunit structure	Catalytic subunit of the telomerase holoenzyme complex at least composed of TERT, DKC1, WDR79/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC). Interacts with PINX1 and MCRS1. Ref.10
Subcellular location	Nucleus. Telomere.
Involvement in disease	Activation of telomerase has been implicated in cell immortalization and cancer cell pathogenesis. Defects in TERT are associated with susceptibilty to aplastic anemia (AA) [MIM:609135]. AA is a rare disease in which the reduction of the circulating blood cells results from damage to the stem cell pool in bone marrow. In most patients, the stem cell lesion is caused by an autoimmune attack. T-lymphocytes, activated by an endogenous or exogenous, and most often unknown antigenic stimulus, secrete cytokines, including IFN-gamma, which would in turn be able to suppress hematopoiesis. Ref.14 Genetic variations in TERT are associated with coronary artery disease (CAD). Ref.16 Defects in TERT are a cause of dyskeratosis congenita autosomal dominant (ADDKC) [MIM:127550]; also known as dyskeratosis congenita Scoggins type. ADDKC is a rare, progressive bone marrow failure syndrome characterized by the triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy. Ref.15 Defects in TERT increases susceptibility to idiopathic pulmonary fibrosis [MIM:178500]. Idiopathic pulmonary fibrosis is an adult-onset, lethal, scarring lung disease of unknown etiology. Its clinical features are shortness of breath, radiographically evident diffuse pulmonary infiltrates, and varying degrees in inflammation, fibrosis, or both on biopsy. It is rapidly progressive and characterized by sequential acute lung injury with subsequent scarring and endstage lung disease.
Sequence similarities	Belongs to the reverse transcriptase family. Telomerase subfamily. Contains 1 reverse transcriptase domain.

Ontologies

Keywords
Cellular component	Chromosomal protein Nucleus Telomere
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Dyskeratosis congenita
Ligand	DNA-binding
Molecular function	Nucleotidyltransferase RNA-directed DNA polymerase Ribonucleoprotein Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA strand elongation Inferred from direct assay. Source: UniProtKB anti-apoptosis Inferred from mutant phenotype. Source: UniProtKB senescence Inferred from mutant phenotype. Source: UniProtKB telomere formation via telomerase Inferred from direct assay. Source: UniProtKB telomere maintenance via telomerase Inferred from mutant phenotype. Source: UniProtKB
Cellular component	nuclear telomere cap complex Inferred by curator. Source: UniProtKB nucleoplasm Inferred from Experiment. Source: Reactome telomerase holoenzyme complex Inferred from direct assay. Source: UniProtKB
Molecular function	protein homodimerization activity Inferred from direct assay. Source: UniProtKB telomeric DNA binding Ref.2 Inferred by curator. Source: UniProtKB telomeric RNA binding Inferred from direct assay. Source: UniProtKB telomeric template RNA reverse transcriptase activity Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RUVBL1	Q9Y265	2	EBI-1772203,EBI-353675

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O14746-1)

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.

Isoform 2 (identifier: O14746-2)

The sequence of this isoform differs from the canonical sequence as follows:
     764-807: STLTDLQPYM...LNEASSGLFD → LRPVPGDPAG...AGRAAPAFGG
     808-1132: Missing.

Note: Phosphorylated on Ser-797.

Isoform 3 (identifier: O14746-3)

The sequence of this isoform differs from the canonical sequence as follows:
     885-947: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1132	1132	Telomerase reverse transcriptase		PRO_0000054925
Regions
	Domain	605 – 935	331	Reverse transcriptase
Amino acid modifications
	Modified residue	1113	1	Phosphothreonine Ref.11
	Modified residue	1125	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	764 – 807	44	STLTD…SGLFD → LRPVPGDPAGLHPLHAALQP VLRRHGEQAVCGDSAGRAAP AFGG in isoform 2.		VSP_019587
	Alternative sequence	808 – 1132	325	Missing in isoform 2.		VSP_019588
	Alternative sequence	885 – 947	63	Missing in isoform 3.		VSP_021727
	Natural variant	202	1	A → T in AA susceptibility; severe and moderate.		VAR_036863
	Natural variant	279	1	A → T Ref.14		VAR_036864
	Natural variant	412	1	H → Y in AA susceptibility; severe and moderate. dbSNP rs34094720.		VAR_025149
	Natural variant	441	1	Missing Ref.14		VAR_036865
	Natural variant	694	1	V → M in AA susceptibility; moderate.		VAR_036866
	Natural variant	772	1	Y → C in AA susceptibility; moderate.		VAR_036867
	Natural variant	865	1	R → H in idiopathic pulmonary fibrosis susceptibility. Ref.17		VAR_036868
	Natural variant	902	1	K → N in ADDKC. Ref.15		VAR_036869
	Natural variant	948	1	S → R: dbSNP rs34062885.		VAR_053726
	Natural variant	1062	1	A → T Ref.14 Ref.7		VAR_025150
	Natural variant	1090	1	V → M in AA susceptibility; severe.		VAR_036870
Experimental info
	Mutagenesis	712	1	D → A: Loss of telomerase activity. Ref.8
	Mutagenesis	868 – 869	2	DD → AA: Loss of telomerase activity. Ref.8
	Mutagenesis	868	1	D → A: Loss of telomerase activity. Ref.8
	Mutagenesis	869	1	D → A: Loss of telomerase activity. Ref.8
	Sequence conflict	516	1	D → G in AAC51724. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 94E35469C4CA33A0	FASTA	1,132	126,997
	10 20 30 40 50 60 MPRAPRCRAV RSLLRSHYRE VLPLATFVRR LGPQGWRLVQ RGDPAAFRAL VAQCLVCVPW 70 80 90 100 110 120 DARPPPAAPS FRQVSCLKEL VARVLQRLCE RGAKNVLAFG FALLDGARGG PPEAFTTSVR 130 140 150 160 170 180 SYLPNTVTDA LRGSGAWGLL LRRVGDDVLV HLLARCALFV LVAPSCAYQV CGPPLYQLGA 190 200 210 220 230 240 ATQARPPPHA SGPRRRLGCE RAWNHSVREA GVPLGLPAPG ARRRGGSASR SLPLPKRPRR 250 260 270 280 290 300 GAAPEPERTP VGQGSWAHPG RTRGPSDRGF CVVSPARPAE EATSLEGALS GTRHSHPSVG 310 320 330 340 350 360 RQHHAGPPST SRPPRPWDTP CPPVYAETKH FLYSSGDKEQ LRPSFLLSSL RPSLTGARRL 370 380 390 400 410 420 VETIFLGSRP WMPGTPRRLP RLPQRYWQMR PLFLELLGNH AQCPYGVLLK THCPLRAAVT 430 440 450 460 470 480 PAAGVCAREK PQGSVAAPEE EDTDPRRLVQ LLRQHSSPWQ VYGFVRACLR RLVPPGLWGS 490 500 510 520 530 540 RHNERRFLRN TKKFISLGKH AKLSLQELTW KMSVRDCAWL RRSPGVGCVP AAEHRLREEI 550 560 570 580 590 600 LAKFLHWLMS VYVVELLRSF FYVTETTFQK NRLFFYRKSV WSKLQSIGIR QHLKRVQLRE 610 620 630 640 650 660 LSEAEVRQHR EARPALLTSR LRFIPKPDGL RPIVNMDYVV GARTFRREKR AERLTSRVKA 670 680 690 700 710 720 LFSVLNYERA RRPGLLGASV LGLDDIHRAW RTFVLRVRAQ DPPPELYFVK VDVTGAYDTI 730 740 750 760 770 780 PQDRLTEVIA SIIKPQNTYC VRRYAVVQKA AHGHVRKAFK SHVSTLTDLQ PYMRQFVAHL 790 800 810 820 830 840 QETSPLRDAV VIEQSSSLNE ASSGLFDVFL RFMCHHAVRI RGKSYVQCQG IPQGSILSTL 850 860 870 880 890 900 LCSLCYGDME NKLFAGIRRD GLLLRLVDDF LLVTPHLTHA KTFLRTLVRG VPEYGCVVNL 910 920 930 940 950 960 RKTVVNFPVE DEALGGTAFV QMPAHGLFPW CGLLLDTRTL EVQSDYSSYA RTSIRASLTF 970 980 990 1000 1010 1020 NRGFKAGRNM RRKLFGVLRL KCHSLFLDLQ VNSLQTVCTN IYKILLLQAY RFHACVLQLP 1030 1040 1050 1060 1070 1080 FHQQVWKNPT FFLRVISDTA SLCYSILKAK NAGMSLGAKG AAGPLPSEAV QWLCHQAFLL 1090 1100 1110 1120 1130 KLTRHRVTYV PLLGSLRTAQ TQLSRKLPGT TLTALEAAAN PALPSDFKTI LD
	Isoform 2. Checksum: 199664460CE6D763	FASTA	807	90,226
	10 20 30 40 50 60 MPRAPRCRAV RSLLRSHYRE VLPLATFVRR LGPQGWRLVQ RGDPAAFRAL VAQCLVCVPW 70 80 90 100 110 120 DARPPPAAPS FRQVSCLKEL VARVLQRLCE RGAKNVLAFG FALLDGARGG PPEAFTTSVR 130 140 150 160 170 180 SYLPNTVTDA LRGSGAWGLL LRRVGDDVLV HLLARCALFV LVAPSCAYQV CGPPLYQLGA 190 200 210 220 230 240 ATQARPPPHA SGPRRRLGCE RAWNHSVREA GVPLGLPAPG ARRRGGSASR SLPLPKRPRR 250 260 270 280 290 300 GAAPEPERTP VGQGSWAHPG RTRGPSDRGF CVVSPARPAE EATSLEGALS GTRHSHPSVG 310 320 330 340 350 360 RQHHAGPPST SRPPRPWDTP CPPVYAETKH FLYSSGDKEQ LRPSFLLSSL RPSLTGARRL 370 380 390 400 410 420 VETIFLGSRP WMPGTPRRLP RLPQRYWQMR PLFLELLGNH AQCPYGVLLK THCPLRAAVT 430 440 450 460 470 480 PAAGVCAREK PQGSVAAPEE EDTDPRRLVQ LLRQHSSPWQ VYGFVRACLR RLVPPGLWGS 490 500 510 520 530 540 RHNERRFLRN TKKFISLGKH AKLSLQELTW KMSVRDCAWL RRSPGVGCVP AAEHRLREEI 550 560 570 580 590 600 LAKFLHWLMS VYVVELLRSF FYVTETTFQK NRLFFYRKSV WSKLQSIGIR QHLKRVQLRE 610 620 630 640 650 660 LSEAEVRQHR EARPALLTSR LRFIPKPDGL RPIVNMDYVV GARTFRREKR AERLTSRVKA 670 680 690 700 710 720 LFSVLNYERA RRPGLLGASV LGLDDIHRAW RTFVLRVRAQ DPPPELYFVK VDVTGAYDTI 730 740 750 760 770 780 PQDRLTEVIA SIIKPQNTYC VRRYAVVQKA AHGHVRKAFK SHVLRPVPGD PAGLHPLHAA 790 800 LQPVLRRHGE QAVCGDSAGR AAPAFGG
	Isoform 3. Checksum: BE1E77A653B1C666	FASTA	1,069	120,048
	10 20 30 40 50 60 MPRAPRCRAV RSLLRSHYRE VLPLATFVRR LGPQGWRLVQ RGDPAAFRAL VAQCLVCVPW 70 80 90 100 110 120 DARPPPAAPS FRQVSCLKEL VARVLQRLCE RGAKNVLAFG FALLDGARGG PPEAFTTSVR 130 140 150 160 170 180 SYLPNTVTDA LRGSGAWGLL LRRVGDDVLV HLLARCALFV LVAPSCAYQV CGPPLYQLGA 190 200 210 220 230 240 ATQARPPPHA SGPRRRLGCE RAWNHSVREA GVPLGLPAPG ARRRGGSASR SLPLPKRPRR 250 260 270 280 290 300 GAAPEPERTP VGQGSWAHPG RTRGPSDRGF CVVSPARPAE EATSLEGALS GTRHSHPSVG 310 320 330 340 350 360 RQHHAGPPST SRPPRPWDTP CPPVYAETKH FLYSSGDKEQ LRPSFLLSSL RPSLTGARRL 370 380 390 400 410 420 VETIFLGSRP WMPGTPRRLP RLPQRYWQMR PLFLELLGNH AQCPYGVLLK THCPLRAAVT 430 440 450 460 470 480 PAAGVCAREK PQGSVAAPEE EDTDPRRLVQ LLRQHSSPWQ VYGFVRACLR RLVPPGLWGS 490 500 510 520 530 540 RHNERRFLRN TKKFISLGKH AKLSLQELTW KMSVRDCAWL RRSPGVGCVP AAEHRLREEI 550 560 570 580 590 600 LAKFLHWLMS VYVVELLRSF FYVTETTFQK NRLFFYRKSV WSKLQSIGIR QHLKRVQLRE 610 620 630 640 650 660 LSEAEVRQHR EARPALLTSR LRFIPKPDGL RPIVNMDYVV GARTFRREKR AERLTSRVKA 670 680 690 700 710 720 LFSVLNYERA RRPGLLGASV LGLDDIHRAW RTFVLRVRAQ DPPPELYFVK VDVTGAYDTI 730 740 750 760 770 780 PQDRLTEVIA SIIKPQNTYC VRRYAVVQKA AHGHVRKAFK SHVSTLTDLQ PYMRQFVAHL 790 800 810 820 830 840 QETSPLRDAV VIEQSSSLNE ASSGLFDVFL RFMCHHAVRI RGKSYVQCQG IPQGSILSTL 850 860 870 880 890 900 LCSLCYGDME NKLFAGIRRD GLLLRLVDDF LLVTPHLTHA KTFLSYARTS IRASLTFNRG 910 920 930 940 950 960 FKAGRNMRRK LFGVLRLKCH SLFLDLQVNS LQTVCTNIYK ILLLQAYRFH ACVLQLPFHQ 970 980 990 1000 1010 1020 QVWKNPTFFL RVISDTASLC YSILKAKNAG MSLGAKGAAG PLPSEAVQWL CHQAFLLKLT 1030 1040 1050 1060 RHRVTYVPLL GSLRTAQTQL SRKLPGTTLT ALEAAANPAL PSDFKTILD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Telomerase catalytic subunit homologs from fission yeast and human." Nakamura T.M., Morin G.B., Chapman K.B., Weinrich S.L., Andrews W.H., Lingner J., Harley C.B., Cech T.R. Science 277:955-959(1997) [PubMed: 9252327] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Kidney.
[2]	"hEST2, the putative human telomerase catalytic subunit gene, is up-regulated in tumor cells and during immortalization." Meyerson M., Counter C.M., Eaton E.N., Ellisen L.W., Steiner P., Caddle S.D., Ziaugra L., Beijersbergen R.L., Davidoff M.J., Liu Q., Bacchetti S., Haber D.A., Weinberg R.A. Cell 90:785-795(1997) [PubMed: 9288757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Genomic organization and promoter characterization of the gene encoding the human telomerase reverse transcriptase (hTERT)." Wick M., Zubov D., Hagen G. Gene 232:97-106(1999) [PubMed: 10333526] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Expression profile of a gamma-deletion variant of the human telomerase reverse transcriptase gene." Hisatomi H., Ohyashiki K., Ohyashiki J.H., Nagao K., Kanamaru T., Hirata H., Hibi N., Tsukada Y. Neoplasia 5:193-197(2003) [PubMed: 12869302] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Stomach cancer.
[5]	"Differential alternative splicing expressions of telomerase reverse transcriptase in gastrointestinal cell lines." Nagao K., Katsumata K., Aizawa Y., Saito N., Hirata H., Sasaki H., Yamamoto S., Hikiji K., Koiwa T., Hisatomi H. Oncol. Rep. 11:127-131(2004) [PubMed: 14654914] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[6]	"Sequence of a BAC carrying the entire hTERT gene." Londono-Vallejo J.A. Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	NIEHS SNPs program Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TYR-412 AND THR-1062.
[8]	"Human telomerase contains evolutionarily conserved catalytic and structural subunits." Harrington L., Zhou W., McPhail T., Oulton R., Yeung D.S., Mar V., Bass M.B., Robinson M.O. Genes Dev. 11:3109-3115(1997) [PubMed: 9389643] [Abstract] Cited for: FUNCTION IN TELOMERASE ACTIVITY, TISSUE SPECIFICITY, ASSOCIATION WITH TEP1, MUTAGENESIS OF ASP-712; ASP-868 AND ASP-869.
[9]	"Polymerization defects within human telomerase are distinct from telomerase RNA and TEP1 binding." Beattie T.L., Zhou W., Robinson M.O., Harrington L. Mol. Biol. Cell 11:3329-3340(2000) [PubMed: 11029039] [Abstract] Cited for: ASSOCIATION WITH TEP1.
[10]	"Human MCRS2, a cell-cycle-dependent protein, associates with LPTS/PinX1 and reduces the telomere length." Song H., Li Y., Chen G., Xing Z., Zhao J., Yokoyama K.K., Li T., Zhao M. Biochem. Biophys. Res. Commun. 316:1116-1123(2004) [PubMed: 15044100] [Abstract] Cited for: INTERACTION WITH MCRS1.
[11]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry 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) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1113 AND SER-1125, MASS SPECTROMETRY. Tissue: T-cell.
[12]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis." Venteicher A.S., Abreu E.B., Meng Z., McCann K.E., Terns R.M., Veenstra T.D., Terns M.P., Artandi S.E. Science 323:644-648(2009) [PubMed: 19179534] [Abstract] Cited for: IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
[14]	"Mutations in TERT, the gene for telomerase reverse transcriptase, in aplastic anemia." Yamaguchi H., Calado R.T., Ly H., Kajigaya S., Baerlocher G.M., Chanock S.J., Lansdorp P.M., Young N.S. N. Engl. J. Med. 352:1413-1424(2005) [PubMed: 15814878] [Abstract] Cited for: VARIANTS AA SUSCEPTIBILITY THR-202; TYR-412; MET-694; CYS-772 AND MET-1090, VARIANTS THR-279; GLU-441 DEL AND THR-1062.
[15]	"Haploinsufficiency of telomerase reverse transcriptase leads to anticipation in autosomal dominant dyskeratosis congenita." Armanios M., Chen J.-L., Chang Y.-P.C., Brodsky R.A., Hawkins A., Griffin C.A., Eshleman J.R., Cohen A.R., Chakravarti A., Hamosh A., Greider C.W. Proc. Natl. Acad. Sci. U.S.A. 102:15960-15964(2005) [PubMed: 16247010] [Abstract] Cited for: VARIANT ADDKC ASN-902.
[16]	"Coronary artery disease and a functional polymorphism of hTERT." Matsubara Y., Murata M., Watanabe K., Saito I., Miyaki K., Omae K., Ishikawa M., Matsushita K., Iwanaga S., Ogawa S., Ikeda Y. Biochem. Biophys. Res. Commun. 348:669-672(2006) [PubMed: 16890917] [Abstract] Cited for: INVOLVEMENT IN CAD SUSCEPTIBILITY.
[17]	"Adult-onset pulmonary fibrosis caused by mutations in telomerase." Tsakiri K.D., Cronkhite J.T., Kuan P.J., Xing C., Raghu G., Weissler J.C., Rosenblatt R.L., Shay J.W., Garcia C.K. Proc. Natl. Acad. Sci. U.S.A. 104:7552-7557(2007) [PubMed: 17460043] [Abstract] Cited for: VARIANT IDIOPATHIC PULMONARY FIBROSIS SUSCEPTIBILITY HIS-865.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF015950 mRNA. Translation: AAC51672.1.
AF018167 mRNA. Translation: AAC51724.1.
AF128894, AF128893 Genomic DNA. Translation: AAD30037.1.
AB085628 mRNA. Translation: BAC11010.1.
AB086379 mRNA. Translation: BAC11014.1.
AY007685 Genomic DNA. Translation: AAG23289.1.
DQ264729 Genomic DNA. Translation: ABB72674.1.

IPI

IPI00168908.
IPI00298218.
IPI00384469.

PIR

T03844.

RefSeq

NP_937983.2.
NP_937986.1.

UniGene

Hs.492203

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BCK	X-ray	2.80	C/F	461-469	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O14746. 5 interactions.

PTM databases

PhosphoSite

O14746.

Proteomic databases

PRIDE

O14746.

Genome annotation databases

Ensembl

ENSG00000164362. Homo sapiens. [Contig view]

GeneID

7015.

KEGG

hsa:7015.

Organism-specific databases

GeneCards

GC05M001306.

H-InvDB

HIX0031945.

HGNC

HGNC:11730. TERT.

MIM

127550. phenotype.
178500. phenotype.
187270. gene+phenotype.
609135. phenotype.

Orphanet

88. Aplastic anemia.
1775. Dyskeratosis congenita.
2032. Pulmonary fibrosis, idiopathic.
3088. Retinopathy - anemia- central nervous system anomalies.

PharmGKB

PA36447.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O14746.

OMA

O14746. NHARCPY.

Enzyme and pathway databases

BRENDA

2.7.7.49. 247.

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
telomerasepathway. Regulation of Telomerase.

Reactome

REACT_7970. Telomere Maintenance.

Gene expression databases

ArrayExpress

O14746.

Bgee

O14746.

CleanEx

HS_TERT.

GermOnline

ENSG00000164362. Homo sapiens.

Family and domain databases

InterPro

IPR000477. DNA_pol_RVTase.
IPR003545. Telomerase_RT.
[Graphical view]

PRINTS

PR01365. TELOMERASERT.

PROSITE

PS50878. RT_POL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

27405.

SOURCE

Search...

Entry information

Entry name

TERT_HUMAN

Accession

Primary (citable) accession number: O14746
Secondary accession number(s): O14783 , Q2XS35, Q8N6C3, Q8NG46

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)