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Entry version 49 (29 Sep 2021)
Sequence version 1 (01 Mar 2002)
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Protein

Terminal uridylyltransferase 1

Gene

KRET1

Organism
Leishmania tarentolae (Sauroleishmania tarentolae)
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 protein 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

Terminal uridylyltransferase which is involved in the post-transcriptional editing of mitochondrial RNA, a process involving the addition and deletion of uridine (U) nucleotides in the pre-mRNA. Specifically, catalyzes the addition of Us to the 3'-hydroxyl group of guided RNA (gRNA), with a preference for RNAs terminating in 6 Us, but also can add Us to RNAs terminating in 6 adenines (A), 6 cytosines (C), or 6 guanines (G) (PubMed:11893335, PubMed:15060068).

Can mediate RNA-independent UTP polymerization in vitro (PubMed:15060068).

Can mediate pyrophosphate-dependent degradation of synthetic RNA ending with U residues in vitro (PubMed:15060068).

2 Publications

<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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 1 Mg2+ or Mn2+ per subunit (PubMed:11893335). The type of divalent cation used by the enzyme affects the nucleotide specificity; Mg2+ induces predominantly uridine (U) incorporation while Mn2+ induces also substantial incorporation of both adenine (A) and cytosine (C) (PubMed:11893335).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Zinc-binding is required for catalytic activity.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

KM is 45-65 µM for UTP (at 27 degrees Celsius) (PubMed:15060068). KM is 18-30 µM for RNA (at 27 degrees Celsius) (PubMed:15060068).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi227ZincBy similarity1
Metal bindingi230ZincBy similarity1
Metal bindingi244Zinc; via tele nitrogenBy similarity1
Metal bindingi249Zinc; via tele nitrogenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei330UTP; via amide nitrogenBy similarity1
Metal bindingi342Magnesium or manganese; catalyticBy similarity1
Metal bindingi344Magnesium or manganese; catalyticBy similarity1
Binding sitei390RNABy similarity1
Metal bindingi548Magnesium or manganese; catalytic1 Publication1
<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>Sitei548Important for catalytic activityBy similarity1
Binding sitei580UTPBy similarity1
Binding sitei584UTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri222 – 253C2H2-type; atypicalBy similarityAdd BLAST32
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi341 – 344UTPBy similarity4
Nucleotide bindingi555 – 559UTPBy similarity5
Nucleotide bindingi598 – 599UTPBy similarity2

<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 functionNucleotidyltransferase, RNA-binding, Transferase
Biological processmRNA processing
LigandMagnesium, Manganese, Metal-binding, Nucleotide-binding, Zinc

<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:
Terminal uridylyltransferase 1Curated (EC:2.7.7.522 Publications)
Short name:
TUTase 11 Publication
Alternative name(s):
3' terminal uridylyl transferase1 Publication
Short name:
3' TUTase1 Publication
RNA editing terminal uridylyltransferase 1Curated
Short name:
RET1Curated
Short name:
RNA editing TUTase 1Curated
<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:KRET1Curated
ORF Names:LtaPh_1409400Imported
<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>OrganismiLeishmania tarentolae (Sauroleishmania tarentolae)Imported
<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 identifieri5689 [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 lineageiEukaryotaDiscobaEuglenozoaKinetoplasteaMetakinetoplastinaTrypanosomatidaTrypanosomatidaeLeishmaniinaeLeishmanializard Leishmania

<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

Mitochondrion

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi328F → G: 3-fold reduction in affinity for RNA. Does not affect affinity for UTP. 1 Publication1
Mutagenesisi330S → A: 50-fold reduction in affinity for RNA and 7-fold increase in affinity for UTP. 1 Publication1
Mutagenesisi342D → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi344D → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi390R → F: Loss of catalytic activity. 1 Publication1
Mutagenesisi395K → D: Loss of catalytic activity. 1 Publication1
Mutagenesisi400 – 543Missing : Loss of catalytic activity. Does not affect tetramerization. 1 PublicationAdd BLAST144
Mutagenesisi548D → A: Loss of catalytic activity. Does not affect gRNA binding. 1 Publication1
Mutagenesisi580K → A: 6-fold reduction in affinity for UTP. Does not affect affinity for RNA. 1 Publication1
Mutagenesisi598S → A: Does not affect affinity for RNA and UTP. 1 Publication1
Mutagenesisi599Y → F: Does not affect affinity for RNA and UTP. 1 Publication1
Mutagenesisi775D → A: 25-fold reduction in affinity for RNA. 2-fold increase in affinity for UTP. 1 Publication1

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – ?MitochondrionCurated
<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_0000450679? – 1120Terminal uridylyltransferase 1

<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

Homotetramer (PubMed:11893335, PubMed:15060068).

Part of a 700kDa complex (PubMed:11893335).

Interacts with p45 and p50 RNA ligases (PubMed:11893335).

2 Publications

<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

<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>Domaini659 – 697PAP-associatedSequence analysisAdd BLAST39

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 – 156DisorderedSequence analysisAdd BLAST156
Regioni196 – 221DisorderedSequence analysisAdd BLAST26
Regioni750 – 1120Important for catalytic activity and RNA binding1 PublicationAdd BLAST371
Regioni800 – 900Involved in oligomerization1 PublicationAdd BLAST101
Regioni1047 – 1076DisorderedSequence analysisAdd BLAST30

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>Motifi773 – 782Nucleotide recognition motif (NRM)By similarity10

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1 – 56Polar residuesSequence analysisAdd BLAST56
Compositional biasi87 – 101Basic and acidic residuesSequence analysisAdd BLAST15
Compositional biasi102 – 128Polar residuesSequence analysisAdd BLAST27
Compositional biasi205 – 221Polar residuesSequence analysisAdd BLAST17
Compositional biasi1047 – 1068Polar residuesSequence analysisAdd BLAST22

<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 DNA polymerase type-B-like family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri222 – 253C2H2-type; atypicalBy similarityAdd BLAST32

Keywords - Domaini

Transit peptide, Zinc-finger

Phylogenomic databases

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8WQX6

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.460.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR043519, NT_sf
IPR002058, PAP_assoc

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03828, PAP_assoc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF81301, SSF81301, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50157, ZINC_FINGER_C2H2_2, 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>Sequencei

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q8WQX6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKYSLLFNQ GTKDGTNASS GSEANSANIT SSSAPASSTN TSSPTSSESA
60 70 80 90 100
VVSPPASTSP RRRLIHRRHG SAGAAEVAPL SLPKRPQQPN EEKHENFISD
110 120 130 140 150
SVHHCSNRGA SGSELKALTT SGSETVMSAS PDIAFEAPSP PTASASPPLE
160 170 180 190 200
STSAVESDGD VVIDDMMRYQ EGDSGGSRSA TSAAAAGRAV STNDAAALIN
210 220 230 240 250
GDPGPLSSAV SSSSSGSPHT PPRLFTCDMC LQYVSTSYEA LEQHALDQHG
260 270 280 290 300
DALADYTRLR SVAEKLVPVW DEVLKRKASV VQQWGKRIFA VAVQRDAGAE
310 320 330 340 350
KMAEAHRARA QLELVVQRWH PRAKVFIFGS SVAFGVWDGI SDIDFTVVDV
360 370 380 390 400
DELEAGTWPP SEKNAVRSIT ELLRRAGFSF INLEPISHAR VPIIKHHASL
410 420 430 440 450
PIRLTDEQRH RLYEEARQSA AAVDLVAAES LASSSPSSAQ ETTDEKGLTQ
460 470 480 490 500
LEAELIIARS VRYSLNLPAG PPDSAILEAS IRLAVGSAAV QQVWWNRTRD
510 520 530 540 550
MCCMTFDTTT NAVKASTCPL HFMSAGMRAR VQPLHEECRP ELYGMDFDLS
560 570 580 590 600
FRAFGIRNSH LLRRYLLSHP CARPGALVLK DWSKTSGVNN SVNGYLTSYA
610 620 630 640 650
INIMWIYYLV HRGVIRYVCP ARDIPASLRC NVDADPQYAA MVDPTWTPEE
660 670 680 690 700
RAAMEAQAGE LLLGFFYYYA FEFDWVNHVV SLNRPGITTK ASLGWDVEDV
710 720 730 740 750
AQTGSPAPHF GVAGSQHQYN LAGAEGQQGD LHSGTSLSAP QTRPLTGYDG
760 770 780 790 800
MMASSASAAA RRSRATTRYS FCIEDPYEEN LNLGRHMGVT KTLRVQTELY
810 820 830 840 850
RGLLSLLKDD PQHCCVFAGS TNSSGSTDSN GAMASGAAEP AMVAARTPSE
860 870 880 890 900
PTELPVRVLY KLMAISTREL AIARRRYSAT VTAGTEFPGA LLSDLEAAFL
910 920 930 940 950
AQAPTEWKLA RQVWNKHQLL HRLGLKLHAR EYVLPRREVG VRRLAAKAPP
960 970 980 990 1000
GVVPASAPEP TFTAEEVAAA AAESGQAPFS AEHAPTSSEE VTQMNRAFLG
1010 1020 1030 1040 1050
AFPARRLPED LMLAMTKGYS CLTPSWVAWS KPWAALSAWW TDRLHSPSTT
1060 1070 1080 1090 1100
TQGEDPLASG TCEQGGVSPS LPTGAPHHIS AVPEKSAGAM HQTRTQLRRH
1110 1120
VVAEIASTPA ARRVLRLLFR
Length:1,120
Mass (Da):120,930
Last modified:March 1, 2002 - 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:iEA45A807ECB0A328
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY029069 Genomic DNA Translation: AAK38333.1
BLBS01000018 Genomic DNA Translation: GET87125.1

<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
AY029069 Genomic DNA Translation: AAK38333.1
BLBS01000018 Genomic DNA Translation: GET87125.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Phylogenomic databases

PhylomeDBiQ8WQX6

Family and domain databases

Gene3Di3.30.460.10, 1 hit
InterProiView protein in InterPro
IPR043519, NT_sf
IPR002058, PAP_assoc
PfamiView protein in Pfam
PF03828, PAP_assoc, 1 hit
SUPFAMiSSF81301, SSF81301, 1 hit
PROSITEiView protein in PROSITE
PS50157, ZINC_FINGER_C2H2_2, 1 hit

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 nameiTUT1_LEITA
<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: Q8WQX6
<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: August 12, 2020
Last sequence update: March 1, 2002
Last modified: September 29, 2021
This is version 49 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)

<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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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