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Entry version 81 (02 Dec 2020)
Sequence version 2 (02 May 2006)
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Protein

Telomerase reverse transcriptase

Gene

TERT

Organism
Bos taurus (Bovine)
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>
-Protein inferred from homologyi <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%5Fsection">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%5Fsection">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 bindingi705Magnesium; 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

<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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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:TERT
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unplaced

<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

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus, Telomere

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002451661 – 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 residuei231Phosphoserine; by PKB/AKT1By similarity1
Modified residuei450Phosphoserine; by DYRK2By similarity1
Modified residuei700Phosphotyrosine; by SRC-type Tyr-kinasesBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-700 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 Ser-231 by the AKT pathway promotes nuclear location. Phosphorylation at the G2/M phase at Ser-450 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-450 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
Q27ID4

PRoteomics IDEntifications database

More...
PRIDEi
Q27ID4

<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%5Fsection">'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%5Fsection">'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).

Interacts with ATF7 (By similarity).

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000016685

<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
Q27ID4

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%5Fand%5Fdomains%5Fsection">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>Domaini598 – 928Reverse transcriptasePROSITE-ProRule annotationAdd BLAST331

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 – 234RNA-interacting domain 1By similarityAdd BLAST234
Regioni58 – 199GQ motifBy similarityAdd BLAST142
Regioni137 – 141Required for regulating specificity for telomeric DNA and for processivity for primer elongationBy similarity5
Regioni235 – 312LinkerBy similarityAdd BLAST78
Regioni290 – 531Required for oligomerizationBy similarityAdd BLAST242
Regioni313 – 543RNA-interacting domain 2By similarityAdd BLAST231
Regioni364 – 514QFP motifBy similarityAdd BLAST151
Regioni385 – 405CP 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>Motifi226 – 244Bipartite nuclear localization signalBy similarityAdd BLAST19
Motifi316 – 321TFLY; involved in RNA bindingBy similarity6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi180 – 185Poly-Ala6

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1005, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q27ID4

Database of Orthologous Groups

More...
OrthoDBi
1297956at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR043502, DNA/RNA_pol_sf
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

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PRINTSi
PR01365, TELOMERASERT

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56672, SSF56672, 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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q27ID4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPRAPRCRAV RALLRASYRQ VLPLAAFVRR LRPQGHRLVR RGDPAAFRAL
60 70 80 90 100
VAQCLVCVPW DAQPPPAAPS FRQVSCLKEL VARVVQRLCE RGARNVLAFG
110 120 130 140 150
FTLLAGARGG PPVAFTTSVR SYLPNTVTDT LRGSGAWGLL LHRVGDDVLT
160 170 180 190 200
HLLSRCALYL LVPPTCAYQV CGPPLYDLRA AAAAARRPTR QVGGTRAGFG
210 220 230 240 250
LPRPASSNGG HGEAEGLLEA RAQGARRRRS SARGRLPPAK RPRRGLEPGR
260 270 280 290 300
DLEGQVARSP PRVVTPTRDA AEAKSRKGDV PGPCRLFPGG ERGVGSASWR
310 320 330 340 350
LSPSEGEPGA GACAETKRFL YCSGGGEQLR RSFLLCSLPP SLAGARTLVE
360 370 380 390 400
TIFLDSKPGP PGAPRRPRRL PARYWQMRPL FRKLLGNHAR SPYGALLRAH
410 420 430 440 450
CPLPASAPRA GPDHQKCPGV GGCPSERPAA APEGEANSGR LVQLLRQHSS
460 470 480 490 500
PWQVYGLLRA CLRRLVPAGL WGSRHNERRF LRNVKKLLSL GKHGRLSQQE
510 520 530 540 550
LTWKMKVQDC AWLRASPGAR CVPAAEHRQR EAVLGRFLHW LMGAYVVELL
560 570 580 590 600
RSFFYVTETT FQKNRLFFFR KRIWSQLQRL GVRQHLDRVR LRELSEAEVR
610 620 630 640 650
QHQEARPALL TSRLRFVPKP GGLRPIVNVG CVEGAPAPPR DKKVQHLSSR
660 670 680 690 700
VKTLFAVLNY ERARRPGLLG ASVLGMDDIH RAWRAFVLPL RARGPAPPLY
710 720 730 740 750
FVKVDVVGAY DALPQDKLAE VIANVLQPQE NTYCVRHCAM VRTARGRMRK
760 770 780 790 800
SFKRHVSTFS DFQPYLRQLV EHLQAMGSLR DAVVIEQSCS LNEPGSSLFN
810 820 830 840 850
LFLHLVRSHV IRIGGRSYIQ CQGIPQGSIL STLLCSFCYG DMENKLFPGV
860 870 880 890 900
QQDGVLLRLV DDFLLVTPHL TRARDFLRTL VRGVPEYGCQ VNLRKTVVNF
910 920 930 940 950
PVEPGALGGA APLQLPAHCL FPWCGLLLDT RTLEVHGDHS SYARTSIRAS
960 970 980 990 1000
LTFTQGFKPG RNMRRKLLAV LQLKCHGLFL DLQVNSLQTV FTNVYKIFLL
1010 1020 1030 1040 1050
QAYRFHACVL QLPFSQPVRS SPAFFLQVIA DTASRGYALL KARNAGASLG
1060 1070 1080 1090 1100
ARGAAGLFPS EAAQWLCLHA FLLKLARHRV TYSRLLGALR TARARLHRQL
1110 1120
PGPTRAALEA AADPALTADF KTILD
Length:1,125
Mass (Da):124,447
Last modified:May 2, 2006 - v2
<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:i717F437B50BB747B
GO

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
DQ399842 Genomic DNA Translation: ABD61652.2

NCBI Reference Sequences

More...
RefSeqi
NP_001039707.1, NM_001046242.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
518884

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:518884

<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
DQ399842 Genomic DNA Translation: ABD61652.2
RefSeqiNP_001039707.1, NM_001046242.1

3D structure databases

SMRiQ27ID4
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016685

Proteomic databases

PaxDbiQ27ID4
PRIDEiQ27ID4

Genome annotation databases

GeneIDi518884
KEGGibta:518884

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7015

Phylogenomic databases

eggNOGiKOG1005, Eukaryota
InParanoidiQ27ID4
OrthoDBi1297956at2759

Family and domain databases

InterProiView protein in InterPro
IPR043502, DNA/RNA_pol_sf
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
SUPFAMiSSF56672, SSF56672, 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_BOVIN
<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: Q27ID4
<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%5Fand%5Fisoforms">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: May 2, 2006
Last modified: December 2, 2020
This is version 81 of the entry and version 2 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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