O14746 (TERT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Telomerase reverse transcriptase
EC=2.7.7.49

Alternative name(s):
HEST2
Telomerase catalytic subunit
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.
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. 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. Ref.9 Ref.15 Ref.18 Ref.20 Ref.22 Ref.24 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Subunit structure	Homodimer; dimerization is required to produce a functional complex. Oligomer; can form oligomers in the absence of the telomerase RNA template component (TERC). Catalytic subunit of the telomerase holoenzyme complex composed minimally of TERT and TERC. The telomerase complex is composed of TERT, DKC1, WDR79/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC). The molecular chaperone HSP90/P23 complex is required for correct assembly and stabilization of the active telomerase. Interacts directly with HSP90A and PTGES3. Interacts with HSPA1A; the interaction occurs in the absence of TERC and dissociates once the complex has formed. Interacts with RAN; the interaction promotes nuclear export of TERT. Interacts with XPO1. Interacts with PTPN11; the interaction retains TERT in the nucleus. Interacts with NCL (via RRM1 and C-terminal RRM4/Arg/Gly-rich domains); the interaction is important for nucleolar localization of TERT. Interacts with SMARCA4 (via the bromodomain); the interaction regulates Wnt-mediated signaling. Interacts with MCRS1 (isoform MCRS2); the interaction inhibits in vitro telomerase activity. Interacts with PIF1; the interaction has no effect on the elongation activity of TERT. Interacts with PML; the interaction recruits TERT to PML bodies and inhibits telomerase activity. Ref.12 Ref.13 Ref.14 Ref.17 Ref.19 Ref.25 Ref.28 Ref.30 Ref.31
Subcellular location	Nucleus › nucleolus. Nucleus › nucleoplasm. Nucleus. Chromosome › telomere. Cytoplasm. Nucleus › PML body. Note: Shuttling between nuclear and cytoplasm depends on cell cycle, phosphorylation states, transformation and DNA damage. Diffuse localization in the nucleoplasm. Enriched in nucleoli of certain cell types. Translocated to the cytoplasm via nuclear pores in a CRM1/RAN-dependent manner involving oxidative stress-mediated phosphorylation at Tyr-707. Dephosphorylation at this site by SHP2 retains TERT in the nucleus. Translocated to the nucleus by phosphorylation by AKT. Ref.13 Ref.15 Ref.16 Ref.17 Ref.28 Ref.29 Ref.30
Tissue specificity	Expressed at a high level in thymocyte subpopulations, at an intermediate level in tonsil T lymphocytes, and at a low to undetectable level in peripheral blood T lymphocytes. Ref.8 Ref.9
Induction	Activated by cytotoxic events and down-regulated during aging. In peripheral T lymphocytes, induced By CD3 and by PMA/ionomycin. Inhibited by herbimycin B. Ref.8
Domain	The primer grip sequence in the RT domain is required for telomerase activity and for stable association with short telomeric primers. Ref.18 The RNA-interacting domain 1 (RD1)/N-terminal extension (NTE) is required for interaction with the pseudoknot-template domain of each of TERC dimers. It contains anchor sites that bind primer nucleotides upstream of the RNA-DNA hybrid and is thus an essential determinant of repeat addition processivity. Ref.18 The RNA-interacting domain 2 (RD2) is essential for both interaction with the CR4-CR5 domain of TERC and for DNA sythesis. Ref.18
Post-translational modification	Ubiquitinated, leading to proteasomal degradation. Ref.19 Phosphorylation at Tyr-707 under oxidative stress leads to translocation of TERT to the cytoplasm and reduces its antiapoptotic activity. Dephosphorylated by SHP2/PTPN11 leading to nuclear retention. Phosphorylation by the AKT pathway promotes nuclear location. Ref.13 Ref.21 Ref.23 Ref.24 Ref.28 Ref.29
Involvement in disease	Note=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.35 Ref.36 Ref.40 Ref.41 Ref.45 Note=Genetic variations in TERT are associated with coronary artery disease (CAD). Ref.38 Defects in TERT are the cause of dyskeratosis congenita autosomal dominant type 2 (DKCA2) [MIM:613989]. A rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy. Ref.35 Ref.37 Defects in TERT are the cause of dyskeratosis congenita autosomal recessive type 4 (DKCB4) [MIM:613989]. A rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy. Defects in TERT are a cause of susceptibility to pulmonary fibrosis idiopathic (IPF) [MIM:178500]. Pulmonary fibrosis is a lung disease characterized by shortness of breath, radiographically evident diffuse pulmonary infiltrates, and varying degrees of inflammation and fibrosis on biopsy. It results in 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	Chromosome Cytoplasm Nucleus Telomere
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Dyskeratosis congenita
Ligand	DNA-binding Magnesium Metal-binding
Molecular function	Nucleotidyltransferase RNA-directed DNA polymerase Ribonucleoprotein Transferase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA strand elongation Inferred from direct assay. Source: BHF-UCL anti-apoptosis Inferred from mutant phenotype. Source: BHF-UCL replicative senescence Inferred from mutant phenotype. Source: BHF-UCL telomere formation via telomerase Inferred from direct assay. Source: BHF-UCL telomere maintenance via telomerase Inferred from mutant phenotype. Source: BHF-UCL
Cellular component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear telomere cap complex Inferred by curator. Source: BHF-UCL nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell telomerase holoenzyme complex Inferred from direct assay. Source: UniProtKB
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Inferred from direct assay. Source: BHF-UCL telomeric DNA binding Traceable author statement. Source: ProtInc telomeric RNA binding Inferred from direct assay. Source: BHF-UCL telomeric template RNA reverse transcriptase activity Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RUVBL1	Q9Y265	11	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.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

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
	Region	1 – 230	230	RNA-interacting domain 1
	Region	58 – 197	140	GQ motif
	Region	137 – 141	5	Required for regulating specificity for telomeric DNA and for processivity for primer elongation
	Region	231 – 324	94	Linker
	Region	301 – 538	238	Required for oligomerization
	Region	325 – 550	226	RNA-interacting domain 2
	Region	376 – 521	146	QFP motif
	Region	397 – 417	21	CP motif
	Region	914 – 928	15	Required for oligomerization
	Region	930 – 934	5	Primer grip sequence
	Region	936 – 1132	197	CTE
Sites
	Metal binding	712	1	Magnesium; catalytic By similarity
	Metal binding	868	1	Magnesium; catalytic By similarity
	Metal binding	869	1	Magnesium; catalytic By similarity
	Site	169	1	Required for optimal binding of telomeric ssDNA and incorporation of nucleotides at the second position of the template
	Site	867	1	Required for nucleotide incorporation and primer extension rate
Amino acid modifications
	Modified residue	707	1	Phosphotyrosine; by SRC-type Tyr-kinases Ref.13 Ref.28
	Modified residue	1113	1	Phosphothreonine Ref.21
	Modified residue	1125	1	Phosphoserine Ref.21
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	55	1	L → Q in idiopathic pulmonary fibrosis susceptibility; impaired telomerase acivity. Ref.43		VAR_062535
	Natural variant	65	1	P → A Associated with acute myeloid leukemia. Ref.45 Ref.46		VAR_062780
	Natural variant	202	1	A → T in AA; severe and moderate; shorter telomeres. Ref.35 Ref.36 Ref.45		VAR_036863
	Natural variant	279	1	A → T. Ref.36		VAR_036864
	Natural variant	299	1	V → M Associated with acute myeloid leukemia. Ref.45 Ref.46		VAR_062781
	Natural variant	412	1	H → Y in AA susceptibility; severe and moderate; associated with susceptibility to acute myelogenous leukemia. Ref.7 Ref.36 Ref.45 Ref.46 Corresponds to variant rs34094720 [ dbSNP | Ensembl ].		VAR_025149
	Natural variant	441	1	Missing in AA susceptibility; associated with susceptibility to acute myeloid leukemia.		VAR_036865
	Natural variant	522	1	R → K Associated with acute myeloid leukemia. Ref.45 Ref.46		VAR_062782
	Natural variant	570	1	K → N in AA susceptibility; abolishes telomerase catalytic activity but no effect on binding to TERC. Ref.41 Ref.45		VAR_062536
	Natural variant	631	1	R → Q in AA susceptibility. Ref.45		VAR_062783
	Natural variant	682	1	G → D in AA susceptibility; non-severe; abolishes telomerase catalytic activity but little effect on binding to TERC. Ref.40 Ref.41		VAR_062537
	Natural variant	694	1	V → M in AA susceptibility; moderate. Ref.36 Ref.45		VAR_036866
	Natural variant	721	1	P → R in DKCB4; no effect on telomerase catalytic activity and little effect on binding to TERC. Ref.39 Ref.41		VAR_062538
	Natural variant	726	1	T → M in AA susceptibility; very severe; no effect on telomerase catalytic activity but shortened telomeres. Ref.40 Ref.41		VAR_062539
	Natural variant	772	1	Y → C in AA susceptibility; moderate. Ref.36		VAR_036867
	Natural variant	785	1	P → L in AA susceptibility. Ref.45		VAR_062784
	Natural variant	811	1	R → C in DKCB4; 50% reduction in telomerase activity. Ref.42		VAR_062540
	Natural variant	865	1	R → H in idiopathic pulmonary fibrosis susceptibility. Ref.44		VAR_036868
	Natural variant	901	1	R → W in DKCB4; severe phenotype overlapping with Hoyeraal-Hreidarsson syndrome; very short telomeres and greatly reduced telomerase activity. Ref.42		VAR_062541
	Natural variant	902	1	K → N in DKCA2; abolishes telomerase catalytic activity but no effect on binding to TERC. Ref.37 Ref.41		VAR_036869
	Natural variant	948	1	S → R. Corresponds to variant rs34062885 [ dbSNP | Ensembl ].		VAR_053726
	Natural variant	979	1	R → W in DKCA2; shortened telomeres but no effect on telomerase catalytic activity nor on binding to TERC. Ref.35 Ref.41		VAR_062542
	Natural variant	1062	1	A → T Increased incidence in sporadic acute myeloid leukemia. Ref.7 Ref.36 Ref.45 Ref.46 Corresponds to variant rs35719940 [ dbSNP | Ensembl ].		VAR_025150
	Natural variant	1090	1	V → M in AA susceptibility; severe. Ref.36		VAR_036870
	Natural variant	1110	1	T → M in idiopathic pulmonary fibrosis susceptibility; impaired telomerase acivity. Ref.43		VAR_062543
	Natural variant	1127	1	F → L in DKCA2; severe; shortened telomeres but no effect on telomerase catalytic activity nor on binding to TERC. Ref.35 Ref.41		VAR_062544
Experimental info
	Mutagenesis	137 – 141	5	WGLLL → AAAAA: Reduced catalytic activity and repeat addition processivity. Complete loss of catalytic activity but no loss of binding to telomeric primers; when associated with 930-A--A-934. Ref.26
	Mutagenesis	169	1	Q → A: About 80% loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. Little effect on repeat addition processivity, nor on TR interaction nor on protein levels. Ref.32
	Mutagenesis	169	1	Q → N: About 85% loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. No effect on protein levels nor on TR interaction. Ref.32
	Mutagenesis	169	1	Q → T: About 90% loss of enzymatic activity. Greatly reduced incorporation of second nucleotide. Altered strength of binding to ssDNA. No effect on protein levels nor on TR interaction. Ref.32
	Mutagenesis	547	1	W → A: Defective in high-affinity TERC interactions. Ref.18
	Mutagenesis	631	1	R → A: Abolishes telomerase catalytic activity. Ref.22
	Mutagenesis	707	1	Y → F: Abolishes oxidative stress-induced phosphorylation and RAN binding. Impaired nuclear export and enhanced antiapoptotic activity against ROS-dependent apoptosis induction. Impaired interaction with PTPN11. No dephosphorylation by PTPN11. Ref.13 Ref.28
	Mutagenesis	712	1	D → A: Loss of telomerase activity. In the absence of TR, no loss of binding to telomeric primers. Ref.9 Ref.10 Ref.22 Ref.26
	Mutagenesis	866	1	L → Y: Moderate reduction in telomerase activity, no change in repeat extension rate nor on nucleotide incorporation fidelity. Little further reduction in activity but 13.5-fold increase in nucleotide incorporation fidelity; when associated with M-867. Ref.27
	Mutagenesis	867	1	V → A: About 75% reduction in telomerase activity, about 80% reduction in repeat reduction rate and 3.9-fold increase in nucleotide incorporation fidelity. Ref.27
	Mutagenesis	867	1	V → M: About 75% reduction in telomerase activity, about 50% reduction in repeat extension rate and 5.2-fold increase in nucleotide incorporation fidelity. Little further reduction in activity and 13.5-fold increase in nucleotide incorporation fidelity; when associated with Y-866. Ref.27
	Mutagenesis	867	1	V → T: Severe reduction in telomerase activity, about 50% reduction in repeat extension rate and 2.2-fold increase in nucleotide incorporation fidelity. No further reduction in activity but 2.8-fold increase in nucleotide incorporation fidelity; when associated with Y-866. Ref.27
	Mutagenesis	868 – 869	2	DD → AA: Loss of telomerase activity. Ref.9 Ref.10 Ref.18 Ref.20 Ref.22
	Mutagenesis	868	1	D → A: Loss of telomerase activity. Ref.9 Ref.10 Ref.18 Ref.20 Ref.22
	Mutagenesis	869	1	D → A: Loss of telomerase activity. Ref.9 Ref.10
	Mutagenesis	930 – 934	5	WCGLL → AAAAA: Completely abolishes telomerase-mediated primer extension and reduced binding to short telomeric primers. Complete loss of catalytic activity but no further loss of binding to telomeric primers; when associated with 137-A--A-141. Ref.26
	Sequence conflict	516	1	D → G in AAC51724. Ref.1

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 [UniParc]. 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 [UniParc]. 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]	"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).
[2]	"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: Embryonic kidney.
[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).
[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). Tissue: Stomach cancer.
[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]	"Regulated expression of telomerase activity in human T lymphocyte development and activation." Weng N.P., Levine B.L., June C.H., Hodes R.J. J. Exp. Med. 183:2471-2479(1996) [PubMed: 8676067] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[9]	"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.
[10]	"Reconstitution of human telomerase activity in vitro." Beattie T.L., Zhou W., Robinson M.O., Harrington L. Curr. Biol. 8:177-180(1998) [PubMed: 9443919] [Abstract] Cited for: RECONSTITUTION OF THE TELOMERASE COMPLEX, MUTAGENESIS OF ASP-712; ASP-868 AND ASP-869.
[11]	"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.
[12]	"Stable association of hsp90 and p23, but Not hsp70, with active human telomerase." Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E. J. Biol. Chem. 276:15571-15574(2001) [PubMed: 11274138] [Abstract] Cited for: INTERACTION WITH HSPA1A; HSP90A AND PTGES3.
[13]	"Hydrogen peroxide triggers nuclear export of telomerase reverse transcriptase via Src kinase family-dependent phosphorylation of tyrosine 707." Haendeler J., Hoffmann J., Brandes R.P., Zeiher A.M., Dimmeler S. Mol. Cell. Biol. 23:4598-4610(2003) [PubMed: 12808100] [Abstract] Cited for: PHOSPHORYLATION AT TYR-707, SUBCELLULAR LOCATION, INTERACTION WITH RAN AND XP01, MUTAGENESIS OF TYR-707.
[14]	"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.
[15]	"Antioxidants inhibit nuclear export of telomerase reverse transcriptase and delay replicative senescence of endothelial cells." Haendeler J., Hoffmann J., Diehl J.F., Vasa M., Spyridopoulos I., Zeiher A.M., Dimmeler S. Circ. Res. 94:768-775(2004) [PubMed: 14963003] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION.
[16]	"Immunohistochemical localization of hTERT protein in human tissues." Yan P., Benhattar J., Seelentag W., Stehle J.C., Bosman F.T. Histochem. Cell Biol. 121:391-397(2004) [PubMed: 15138842] [Abstract] Cited for: SUBCELLULAR LOCATION.
[17]	"Nucleolin interacts with telomerase." Khurts S., Masutomi K., Delgermaa L., Arai K., Oishi N., Mizuno H., Hayashi N., Hahn W.C., Murakami S. J. Biol. Chem. 279:51508-51515(2004) [PubMed: 15371412] [Abstract] Cited for: INTERACTION WITH NCL, SUBCELLULAR LOCATION.
[18]	"Functional organization of repeat addition processivity and DNA synthesis determinants in the human telomerase multimer." Moriarty T.J., Marie-Egyptienne D.T., Autexier C. Mol. Cell. Biol. 24:3720-3733(2004) [PubMed: 15082768] [Abstract] Cited for: FUNCTIONAL DOMAINS, MUTAGENESIS OF TRP-547 AND ASP-868.
[19]	"Ubiquitin ligase MKRN1 modulates telomere length homeostasis through a proteolysis of hTERT." Kim J.H., Park S.-M., Kang M.R., Oh S.-Y., Lee T.H., Muller M.T., Chung I.K. Genes Dev. 19:776-781(2005) [PubMed: 15805468] [Abstract] Cited for: INTERACTION WITH MKRN1, UBIQUITINATION.
[20]	"An anchor site-type defect in human telomerase that disrupts telomere length maintenance and cellular immortalization." Moriarty T.J., Ward R.J., Taboski M.A., Autexier C. Mol. Biol. Cell 16:3152-3161(2005) [PubMed: 15857955] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-868.
[21]	"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: Leukemic T-cell.
[22]	"Telomerase with mutated catalytic motifs has dominant negative effects on telomerase activity and inhibits cell growth." Rahman R., Mo L., Cui W. Biochem. Biophys. Res. Commun. 350:796-802(2006) [PubMed: 17026956] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ARG-631; ASP-712 AND ASP-868.
[23]	"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: Cervix adenocarcinoma.
[24]	"The loss of telomerase activity in highly differentiated CD8+CD28-CD27- T cells is associated with decreased Akt (Ser473) phosphorylation." Plunkett F.J., Franzese O., Finney H.M., Fletcher J.M., Belaramani L.L., Salmon M., Dokal I., Webster D., Lawson A.D., Akbar A.N. J. Immunol. 178:7710-7719(2007) [PubMed: 17548608] [Abstract] Cited for: PHOSPHORYLATION, FUNCTION.
[25]	"Purification of human telomerase complexes identifies factors involved in telomerase biogenesis and telomere length regulation." Fu D., Collins K. Mol. Cell 28:773-785(2007) [PubMed: 18082603] [Abstract] Cited for: INTERACTION WITH NAT10.
[26]	"Characterization of physical and functional anchor site interactions in human telomerase." Wyatt H.D., Lobb D.A., Beattie T.L. Mol. Cell. Biol. 27:3226-3240(2007) [PubMed: 17296728] [Abstract] Cited for: FUNCTION, DNA-BINDING, MUTAGENESIS OF 137-TRP--LEU-141; ASP-712 AND 930-TRP--LEU-934.
[27]	"The active site residue Valine 867 in human telomerase reverse transcriptase influences nucleotide incorporation and fidelity." Drosopoulos W.C., Prasad V.R. Nucleic Acids Res. 35:1155-1168(2007) [PubMed: 17264120] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LEU-866 AND VAL-867.
[28]	"Nuclear protein tyrosine phosphatase Shp-2 is one important negative regulator 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) [PubMed: 18829466] [Abstract] Cited for: INTERACTION WITH PTPN11, PHOSPHORYLATION AT TYR-707, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-707.
[29]	"Ionizing radiation up-regulates telomerase activity in cancer cell lines by post-translational mechanism via ras/phosphatidylinositol 3-kinase/Akt pathway." Ram R., Uziel O., Eldan O., Fenig E., Beery E., Lichtenberg S., Nordenberg Y., Lahav M. Clin. Cancer Res. 15:914-923(2009) [PubMed: 19188162] [Abstract] Cited for: PHOSPHORYLATION, FUNCTION, SUBCELLULAR LOCATION.
[30]	"PML-IV functions as a negative regulator of telomerase by interacting with TERT." Oh W., Ghim J., Lee E.W., Yang M.R., Kim E.T., Ahn J.H., Song J. J. Cell Sci. 122:2613-2622(2009) [PubMed: 19567472] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PML.
[31]	"Telomerase modulates Wnt signalling by association with target gene chromatin." Park J.I., Venteicher A.S., Hong J.Y., Choi J., Jun S., Shkreli M., Chang W., Meng Z., Cheung P., Ji H., McLaughlin M., Veenstra T.D., Nusse R., McCrea P.D., Artandi S.E. Nature 460:66-72(2009) [PubMed: 19571879] [Abstract] Cited for: INTERACTION WITH SMARCA4, FUNCTION.
[32]	"Human telomerase reverse transcriptase (hTERT) Q169 is essential for telomerase function in vitro and in vivo." Wyatt H.D., Tsang A.R., Lobb D.A., Beattie T.L. PLoS ONE 4:E7176-E7176(2009) [PubMed: 19777057] [Abstract] Cited for: FUNCTION, DNA-BINDING, MUTAGENESIS OF GLN-169.
[33]	"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.
[34]	"Crystal structure of HLA-A*2402 complexed with a telomerase peptide." Cole D.K., Rizkallah P.J., Gao F., Watson N.I., Boulter J.M., Bell J.I., Sami M., Gao G.F., Jakobsen B.K. Eur. J. Immunol. 36:170-179(2006) [PubMed: 16323248] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 461-469 IN COMPLEX WITH CLASS I MAJOR HISTOCOMPATIBILITY COMPLEX (MHC).
[35]	"Mutations in the reverse transcriptase component of telomerase (TERT) in patients with bone marrow failure." Vulliamy T.J., Walne A., Baskaradas A., Mason P.J., Marrone A., Dokal I. Blood Cells Mol. Dis. 34:257-263(2005) [PubMed: 15885610] [Abstract] Cited for: VARIANT AA THR-202, VARIANTS DKCA2 TRP-979 AND LEU-1127, CHARACTERIZATION OF VARIANT AA THR-202, CHARACTERIZATION OF VARIANTS DKCA2 TRP-979 AND LEU-1127.
[36]	"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.
[37]	"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 DKCA2 ASN-902, CHARACTERIZATION OF VARIANT DKCA2 ASN-902.
[38]	"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.
[39]	"Mutations in dyskeratosis congenita: their impact on telomere length and the diversity of clinical presentation." Vulliamy T.J., Marrone A., Knight S.W., Walne A., Mason P.J., Dokal I. Blood 107:2680-2685(2006) [PubMed: 16332973] [Abstract] Cited for: VARIANT DKCB4 ARG-721.
[40]	"Mutations in telomerase catalytic protein in Japanese children with aplastic anemia." Liang J., Yagasaki H., Kamachi Y., Hama A., Matsumoto K., Kato K., Kudo K., Kojima S. Haematologica 91:656-658(2006) [PubMed: 16627250] [Abstract] Cited for: VARIANTS AA SUSCEPTIBILITY ASP-682 AND MET-726, CHARACTERIZATION OF MET-726.
[41]	"Functional characterization of natural telomerase mutations found in patients with hematologic disorders." Xin Z.T., Beauchamp A.D., Calado R.T., Bradford J.W., Regal J.A., Shenoy A., Liang Y., Lansdorp P.M., Young N.S., Ly H. Blood 109:524-532(2007) [PubMed: 16990594] [Abstract] Cited for: VARIANT AA SUSCEPTIBILITY ASN-570, CHARACTERIZATION OF VARIANTS ASN-570; ASP-682; ARG-721; MET-726; ASN-902; TRP-979 AND LEU-1127.
[42]	"Telomerase reverse-transcriptase homozygous mutations in autosomal recessive dyskeratosis congenita and Hoyeraal-Hreidarsson syndrome." Marrone A., Walne A., Tamary H., Masunari Y., Kirwan M., Beswick R., Vulliamy T., Dokal I. Blood 110:4198-4205(2007) [PubMed: 17785587] [Abstract] Cited for: VARIANTS DKCB4 CYS-811 AND TRP-901, CHARACTERIZATION OF VARIANTS DKCB4 CYS-811 AND TRP-901.
[43]	"Telomerase mutations in families with idiopathic pulmonary fibrosis." Armanios M.Y., Chen J.J., Cogan J.D., Alder J.K., Ingersoll R.G., Markin C., Lawson W.E., Xie M., Vulto I., Phillips J.A., Lansdorp P.M., Greider C.W., Loyd J.E. N. Engl. J. Med. 356:1317-1326(2007) [PubMed: 17392301] [Abstract] Cited for: VARIANTS IDIOPATHIC PULMONARY FIBROSIS SUSCEPTIBILITY GLN-55 AND MET-1110, CHARACTERIZATION OF VARIANTS GLN-55 AND MET-1110.
[44]	"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.
[45]	"Defining the pathogenic role of telomerase mutations in myelodysplastic syndrome and acute myeloid leukemia." Kirwan M., Vulliamy T., Marrone A., Walne A.J., Beswick R., Hillmen P., Kelly R., Stewart A., Bowen D., Schonland S.O., Whittle A.M., McVerry A., Gilleece M., Dokal I. Hum. Mutat. 30:1567-1573(2009) [PubMed: 19760749] [Abstract] Cited for: VARIANTS ALA-65; MET-299; LYS-522 AND THR-1062, VARIANTS AA SUSCEPTIBILITY THR-202; TYR-412; GLU-441 DEL; ASN-570; GLN-631; MET-694 AND LEU-785.
[46]	"Constitutional hypomorphic telomerase mutations in patients with acute myeloid leukemia." Calado R.T., Regal J.A., Hills M., Yewdell W.T., Dalmazzo L.F., Zago M.A., Lansdorp P.M., Hogge D., Chanock S.J., Estey E.H., Falcao R.P., Young N.S. Proc. Natl. Acad. Sci. U.S.A. 106:1187-1192(2009) [PubMed: 19147845] [Abstract] Cited for: VARIANTS ALA-65; MET-299; TYR-412; GLU-441 DEL; LYS-522 AND THR-1062.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF018167 mRNA. Translation: AAC51724.1.
AF015950 mRNA. Translation: AAC51672.1.
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_001180305.1. NM_001193376.1.
NP_937983.2. NM_198253.2.

UniGene

Hs.492203.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

O14746.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40646N.

IntAct

O14746. 3 interactions.

MINT

MINT-133963.

STRING

O14746.

PTM databases

PhosphoSite

O14746.

Proteomic databases

PRIDE

O14746.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310581; ENSP00000309572; ENSG00000164362.

GeneID

7015.

KEGG

hsa:7015.

UCSC

uc003jca.1. human.
uc003jcc.1. human.

Organism-specific databases

CTD

7015.

GeneCards

GC05M001306.

H-InvDB

HIX0031945.

HGNC

HGNC:11730. TERT.

MIM

178500. phenotype.
187270. gene+phenotype.
609135. phenotype.
613989. phenotype.

neXtProt

NX_O14746.

Orphanet

1775. Dyskeratosis congenita.
88. Idiopathic aplastic anemia.
2032. Idiopathic pulmonary fibrosis.

PharmGKB

PA36447.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG04020.

HOGENOM

HBG282044.

HOVERGEN

HBG000460.

InParanoid

O14746.

OMA

VETIFLG.

PhylomeDB

O14746.

Enzyme and pathway databases

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_22172. Chromosome Maintenance.

Gene expression databases

Bgee

O14746.

CleanEx

HS_TERT.

Genevestigator

O14746.

GermOnline

ENSG00000164362. Homo sapiens.

Family and domain databases

InterPro

IPR000477. RVT.
IPR021891. Telomerase_RBD.
IPR003545. Telomerase_RT.
[Graphical view]

KO

K11126.

Pfam

PF00078. RVT_1. 1 hit.
PF12009. Telomerase_RBD. 1 hit.
[Graphical view]

PRINTS

PR01365. TELOMERASERT.

SMART

SM00975. Telomerase_RBD. 1 hit.
[Graphical view]

PROSITE

PS50878. RT_POL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

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:	January 25, 2012
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.