Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 116 (08 May 2019)
Sequence version 1 (11 Oct 2004)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Telomerase reverse transcriptase

Gene

Tert

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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 (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei169Required for optimal binding of telomeric ssDNA and incorporation of nucleotides at the second position of the templateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi702Magnesium; catalyticPROSITE-ProRule annotation1
Sitei860Required for nucleotide incorporation and primer extension rateBy similarity1
Metal bindingi861Magnesium; catalyticPROSITE-ProRule annotation1
Metal bindingi862Magnesium; catalyticPROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Nucleotidyltransferase, Ribonucleoprotein, RNA-directed DNA polymerase, Transferase
LigandMagnesium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-171319 Telomere Extension By Telomerase
R-RNO-201722 Formation of the beta-catenin:TCF transactivating complex

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Telomerase reverse transcriptase (EC:2.7.7.49)
Alternative name(s):
Telomerase catalytic subunit
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TertImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Rat genome database

More...
RGDi
70494 Tert

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus, Telomere

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3108654

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002451651 – 1125Telomerase reverse transcriptaseAdd BLAST1125

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei447Phosphoserine; by DYRK2By similarity1
Modified residuei697Phosphotyrosine; by SRC-type Tyr-kinasesBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Tyr-697 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 at the G2/M phase at Ser-447 by DYRK2 promotes ubiquitination by the EDVP complex and degradation (By similarity).By similarity
Ubiquitinated by the EDVP complex, a E3 ligase complex following phosphorylation at Ser-447 by DYRK2. Ubiquitinated leads to proteasomal degradation (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q673L6

PRoteomics IDEntifications database

More...
PRIDEi
Q673L6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Isoform 1 and isoform 2 expressed in thymus, liver, spleen, lung, kidney and testis. High level of inactive isoform 3 in adult hippocampus, low level in heart, cortex and cerebellum.2 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

High activity in cortex at embryonic stage 16 and postnatal day 2. Low activity in cortex from postnatal day 5.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Down-regulated by TGFbeta in fibroblasts. This inhibition is mediated by SMAD3.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000025327 Expressed in 9 organ(s), highest expression level in liver

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Catalytic component of the telomerase holoenzyme complex composed of one molecule of TERT, one molecule of WRAP53/TCAB1, two molecules of H/ACA ribonucleoprotein complex subunits DKC1, NOP10, NHP2 and GAR1, and a telomerase RNA template component (TERC). The telomerase holoenzyme complex is associated with TEP1, SMG6/EST1A and POT1. 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 (By similarity).

Interacts with SMARCA4 (via the bromodomain); the interaction regulates Wnt-mediated signaling (By similarity).

Interacts with MCRS1 (isoform MCRS2); the interaction inhibits in vitro telomerase activity (By similarity).

Interacts with PIF1; the interaction has no effect on the elongation activity of TERT (By similarity).

Interacts with PML; the interaction recruits TERT to PML bodies and inhibits telomerase activity (By similarity).

Interacts with GNL3L (By similarity).

Interacts with isoform 1 and isoform 2 of NVL (By similarity).

Interacts with DHX36 (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000022683

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q673L6

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q673L6

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini595 – 928Reverse transcriptasePROSITE-ProRule annotationAdd BLAST334

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 239RNA-interacting domain 1By similarityAdd BLAST239
Regioni58 – 205GQ motifBy similarityAdd BLAST148
Regioni137 – 141Required for regulating specificity for telomeric DNA and for processivity for primer elongationBy similarity5
Regioni240 – 328LinkerBy similarityAdd BLAST89
Regioni306 – 528Required for oligomerizationBy similarityAdd BLAST223
Regioni329 – 540RNA-interacting domain 2By similarityAdd BLAST212
Regioni381 – 511QFP motifBy similarityAdd BLAST131
Regioni402 – 422CP motifBy similarityAdd BLAST21
Regioni907 – 921Required for oligomerizationBy similarityAdd BLAST15
Regioni923 – 927Primer grip sequenceBy similarity5
Regioni929 – 1125CTEBy similarityAdd BLAST197

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi332 – 337TFLY; involved in RNA bindingBy similarity6

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The primer grip sequence in the RT domain is required for telomerase activity and for stable association with short telomeric primers.By similarity
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 (By similarity).By similarity
The RNA-interacting domain 2 (RD2) is essential for both interaction with the CR4-CR5 domain of TERC and for DNA synthesis.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the reverse transcriptase family. Telomerase subfamily.Sequence analysis

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1005 Eukaryota
ENOG410XQJH LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000018531

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000148780

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q673L6

KEGG Orthology (KO)

More...
KOi
K11126

Identification of Orthologs from Complete Genome Data

More...
OMAi
GNHARCP

Database of Orthologous Groups

More...
OrthoDBi
1297956at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q673L6

TreeFam database of animal gene trees

More...
TreeFami
TF329048

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000477 RT_dom
IPR021891 Telomerase_RBD
IPR003545 Telomerase_RT

The PANTHER Classification System

More...
PANTHERi
PTHR12066 PTHR12066, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00078 RVT_1, 1 hit
PF12009 Telomerase_RBD, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01365 TELOMERASERT

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00975 Telomerase_RBD, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50878 RT_POL, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 11 Publication (identifier: Q673L6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MPRAPRCPAV RSLLRSRYRE VWPLATFVRR LGLEGSRLVQ PGDPKVFRTL
60 70 80 90 100
VAQCLVCVPW GSQPPPADLS FHQVSSLKEL VSRVVQKLCE RGERNVLAFG
110 120 130 140 150
FALLNGARGG PPMAFTTSVH SYLPNSVTES LCVSGAWMLL LSRVGDDLLV
160 170 180 190 200
YLLSHCALYL LVPPSCAYQV CGSPLYQICA TTDTWSSVPA GYRPTRPVGG
210 220 230 240 250
NFTNLGSAHQ IKNSGHQEAP KPQALPSRGT KRLLSLTSTN VPSAKKARFE
260 270 280 290 300
PALRVDKGPH RQVVPTPSGK TWAPSPAASP KVPPAAKNLS LKGKASDPSL
310 320 330 340 350
SGSVCCKHKP SSSSLLSSPP QDAEKLRPFT ETRHFLYSRG GGQEELNPSF
360 370 380 390 400
LLNSLPPSLT GARRLVEIIF LGSRPRTSGP FCRTRRLPRR YWQMRPLFQQ
410 420 430 440 450
LLMNHAKCQY VRFLRSHCRF RTANQRVPDA MDTSPSHLTS LLRLHSSPWQ
460 470 480 490 500
VYGFLRACLR ELVPAGLWGT RHNERRFLKN VKKFISLGKY AKLSLQELMW
510 520 530 540 550
RVKVEDCHWL RSSPEKDTVP AAEHRLRERI LAMFLFWLMD TYVVQLLRSF
560 570 580 590 600
FYITETTFQK NRLFFYRKSV WSKLQSIGIR QQLERVQLRE LSQEEVKHHQ
610 620 630 640 650
DTWLAMPICR LRFIPKLNGL RPIVNMSYGM DTRAFGKKKQ TQCFTQSLKT
660 670 680 690 700
LFSVLNYERT KHPNLMGASV LGTSDSYRIW RTFVLRVRAL DQTPRMYFVK
710 720 730 740 750
ADVTGAYDAI PQDKLVEIVA NIIRRSESMY CIRQYAVVQK DSQGQVHKSF
760 770 780 790 800
RRQVSTLSDL QPYMGQFTKH LQDSDASALR NSVVIEQSIS MNETGSSLLH
810 820 830 840 850
FFLRFVRHSV VKIDGRFYVQ CQGIPQGSSL STLLCSLCFG DMENKLFAEV
860 870 880 890 900
QQDGLLLRFV DDFLLVTPHL AHAKAFLSTL VHGVPEYGCM INLQKTVVNF
910 920 930 940 950
PVETGALGGA APHQLPAHCL FPWCGLLLDT RTLEVFCDYS GYGRTSIKMS
960 970 980 990 1000
LTFQGVSRAG KTMRYKLLSV LRLKCHGLFL DLQVNSLQTV CINIYKIFLL
1010 1020 1030 1040 1050
QAYRFHACVI RLPFGQHVRK NHAFFLGIIS NLASCCYAIL KVKNPGVSLR
1060 1070 1080 1090 1100
AKGAPGSFPP EATRWLCYQA FLLKLAAHSV TYKCLLGPLR TAQKQLCRKL
1110 1120
PEATMTLLKT AADPALSTDF QTILD
Length:1,125
Mass (Da):126,934
Last modified:October 11, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB8B2A11C914372DF
GO
Isoform 21 Publication (identifier: Q673L6-2) [UniParc]FASTAAdd to basket
Also known as: a1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     641-646: Missing.

Show »
Length:1,119
Mass (Da):126,225
Checksum:i4CABB74D64E3F972
GO
Isoform 31 Publication (identifier: Q673L6-3) [UniParc]FASTAAdd to basket
Also known as: b1 Publication, c1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     515-615: EKDTVPAAEH...MPICRLRFIP → ACTSFWDSPS...VPEEPPFLLP
     616-1125: Missing.

Note: Inactive form.
Show »
Length:615
Mass (Da):68,614
Checksum:i2892840D86620B63
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti521A → V in DAA01427 (PubMed:15057822).Curated1
Sequence conflicti528E → V in DAA01427 (PubMed:15057822).Curated1
Sequence conflicti550 – 551FF → LL in DAA01427 (PubMed:15057822).Curated2
Sequence conflicti583L → P in DAA01427 (PubMed:15057822).Curated1
Sequence conflicti630M → L in DAA01427 (PubMed:15057822).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_052081515 – 615EKDTV…LRFIP → ACTSFWDSPSPSQVSFIFIT AGKPSFPWIRRPLRYLETHR VELTHPAWQEGHCPCRRAPS EGEDPCHVPVLANGHICGTA AEVILLHHRDHVPEEPPFLL P in isoform 3. 1 PublicationAdd BLAST101
Alternative sequenceiVSP_052082616 – 1125Missing in isoform 3. 1 PublicationAdd BLAST510
Alternative sequenceiVSP_052083641 – 646Missing in isoform 2. 1 Publication6

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY539717 mRNA Translation: AAT09124.1
AY539718 mRNA Translation: AAT09125.1
AY539719 mRNA Translation: AAT09126.1
AY539720 mRNA Translation: AAT09127.1
AC123569 Genomic DNA No translation available.
DQ021473 Genomic DNA Translation: AAY40300.1
AJ440965 mRNA Translation: CAD29524.1
AJ440966 Genomic DNA Translation: CAD29525.2
BK000660 mRNA Translation: DAA01427.1

NCBI Reference Sequences

More...
RefSeqi
NP_445875.1, NM_053423.1 [Q673L6-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000022683; ENSRNOP00000022683; ENSRNOG00000025327 [Q673L6-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
301965

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:301965

UCSC genome browser

More...
UCSCi
RGD:70494 rat [Q673L6-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY539717 mRNA Translation: AAT09124.1
AY539718 mRNA Translation: AAT09125.1
AY539719 mRNA Translation: AAT09126.1
AY539720 mRNA Translation: AAT09127.1
AC123569 Genomic DNA No translation available.
DQ021473 Genomic DNA Translation: AAY40300.1
AJ440965 mRNA Translation: CAD29524.1
AJ440966 Genomic DNA Translation: CAD29525.2
BK000660 mRNA Translation: DAA01427.1
RefSeqiNP_445875.1, NM_053423.1 [Q673L6-1]

3D structure databases

SMRiQ673L6
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022683

Chemistry databases

BindingDBiQ673L6
ChEMBLiCHEMBL3108654

Proteomic databases

PaxDbiQ673L6
PRIDEiQ673L6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022683; ENSRNOP00000022683; ENSRNOG00000025327 [Q673L6-1]
GeneIDi301965
KEGGirno:301965
UCSCiRGD:70494 rat [Q673L6-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7015
RGDi70494 Tert

Phylogenomic databases

eggNOGiKOG1005 Eukaryota
ENOG410XQJH LUCA
GeneTreeiENSGT00390000018531
HOGENOMiHOG000148780
InParanoidiQ673L6
KOiK11126
OMAiGNHARCP
OrthoDBi1297956at2759
PhylomeDBiQ673L6
TreeFamiTF329048

Enzyme and pathway databases

ReactomeiR-RNO-171319 Telomere Extension By Telomerase
R-RNO-201722 Formation of the beta-catenin:TCF transactivating complex

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q673L6

Gene expression databases

BgeeiENSRNOG00000025327 Expressed in 9 organ(s), highest expression level in liver

Family and domain databases

InterProiView protein in InterPro
IPR000477 RT_dom
IPR021891 Telomerase_RBD
IPR003545 Telomerase_RT
PANTHERiPTHR12066 PTHR12066, 1 hit
PfamiView protein in Pfam
PF00078 RVT_1, 1 hit
PF12009 Telomerase_RBD, 1 hit
PRINTSiPR01365 TELOMERASERT
SMARTiView protein in SMART
SM00975 Telomerase_RBD, 1 hit
PROSITEiView protein in PROSITE
PS50878 RT_POL, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTERT_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q673L6
Secondary accession number(s): Q1LZ57
, Q4U0V7, Q673L3, Q673L5, Q80SU5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 11, 2004
Last modified: May 8, 2019
This is version 116 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again