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Entry version 151 (02 Dec 2020)
Sequence version 1 (01 Apr 1993)
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Protein

Ribonuclease T

Gene

rnt

Organism
Escherichia coli (strain K12)
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

Trims short 3' overhangs of a variety of RNA species, leaving a one or two nucleotide 3' overhang. Responsible for the end-turnover of tRNA: specifically removes the terminal AMP residue from uncharged tRNA (tRNA-C-C-A). Also appears to be involved in tRNA biosynthesis, especially in strains lacking other exoribonucleases.UniRule annotation3 Publications

Miscellaneous

Member of the DEDD group of RNAses that are characterized by the presence of four acidic residues in the active site. These residues are conserved even when the proteins have highly divergent sequences.

<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+UniRule annotation4 PublicationsNote: Binds two Mg2+ per subunit. The active form of the enzyme binds two Mg2+ ions in its active site. The first Mg2+ forms only one salt bridge with the protein.UniRule annotation4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi23Magnesium 1; catalytic1
Metal bindingi23Magnesium 2; catalytic1
Metal bindingi25Magnesium 2; catalytic1
<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>Sitei29Important for substrate binding and specificity1
Sitei73Important for substrate binding and specificity1
Sitei77Important for substrate binding and specificity1
Sitei124Important for substrate binding and specificity1
Sitei146Important for substrate binding and specificity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei181Proton donor/acceptorUniRule annotation2 Publications1
Metal bindingi181Magnesium 2; catalytic1
Metal bindingi186Magnesium 2; catalytic1

<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 functionExonuclease, Hydrolase, Nuclease
Biological processtRNA processing
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11547-MONOMER
MetaCyc:EG11547-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.13.3, 2026

<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:
Ribonuclease TUniRule annotation (EC:3.1.13.-UniRule annotation)
Alternative name(s):
Exoribonuclease TUniRule annotation
Short name:
RNase TUniRule annotation
<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:rntUniRule annotation
Ordered Locus Names:b1652, JW1644
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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: Chromosome
  • UP000000625 Componenti: Chromosome

<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

GO - Cellular componenti

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Required for optimal growth.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi13R → A: Strongly reduces affinity for RNA. Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi15R → A: Strongly reduces affinity for RNA. 1 Publication1
Mutagenesisi23D → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi25E → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi29F → A: Abolishes enzyme activity; when associated with A-73 and A-77. 1 Publication1
Mutagenesisi73E → A: Reduces enzyme activity. Abolishes enzyme activity; when associated with A-29 and A-77. 1 Publication1
Mutagenesisi77F → A: Abolishes enzyme activity; when associated with A-29 and A-73. 1 Publication1
Mutagenesisi108K → A: Strongly reduces affinity for RNA. 1 Publication1
Mutagenesisi114R → A: Strongly reduces affinity for RNA. 1 Publication1
Mutagenesisi124F → A: Abolishes enzyme activity; when associated with A-146. 1 Publication1
Mutagenesisi139K → A: Reduces affinity for RNA. 1 Publication1
Mutagenesisi146F → A: Abolishes enzyme activity; when associated with A-124. 1 Publication1
Mutagenesisi150D → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi181H → A: Nearly abolishes enzyme activity. 1 Publication1
Mutagenesisi186D → A: Nearly abolishes enzyme activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3879866

<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_00002089601 – 215Ribonuclease TAdd BLAST215

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P30014

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

More...
PaxDbi
P30014

PRoteomics IDEntifications database

More...
PRIDEi
P30014

<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

Homodimer.

UniRule annotation2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4260267, 149 interactors
850519, 1 interactor

Database of interacting proteins

More...
DIPi
DIP-10734N

Protein interaction database and analysis system

More...
IntActi
P30014, 2 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b1652

<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

Secondary structure

1215
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P30014

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P30014

<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>Domaini20 – 194ExonucleaseUniRule annotationAdd BLAST175

<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 RNase T family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0847, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_082724_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P30014

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P30014

Family and domain databases

Conserved Domains Database

More...
CDDi
cd06134, RNaseT, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.420.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00157, RNase_T, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013520, Exonuclease_RNaseT/DNA_pol3
IPR005987, RNase_T
IPR012337, RNaseH-like_sf
IPR036397, RNaseH_sf

The PANTHER Classification System

More...
PANTHERi
PTHR30231:SF2, PTHR30231:SF2, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00929, RNase_T, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00479, EXOIII, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53098, SSF53098, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01298, RNaseT, 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.

P30014-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDNAQLTGL CDRFRGFYPV VIDVETAGFN AKTDALLEIA AITLKMDEQG
60 70 80 90 100
WLMPDTTLHF HVEPFVGANL QPEALAFNGI DPNDPDRGAV SEYEALHEIF
110 120 130 140 150
KVVRKGIKAS GCNRAIMVAH NANFDHSFMM AAAERASLKR NPFHPFATFD
160 170 180 190 200
TAALAGLALG QTVLSKACQT AGMDFDSTQA HSALYDTERT AVLFCEIVNR
210
WKRLGGWPLS AAEEV
Length:215
Mass (Da):23,523
Last modified:April 1, 1993 - 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:i502C1CCEFABF4B05
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
L01622 Genomic DNA Translation: AAC37008.1
U00096 Genomic DNA Translation: AAC74724.1
AP009048 Genomic DNA Translation: BAA15418.2

Protein sequence database of the Protein Information Resource

More...
PIRi
A45065

NCBI Reference Sequences

More...
RefSeqi
NP_416169.1, NC_000913.3
WP_001282283.1, NZ_SSZK01000001.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74724; AAC74724; b1652
BAA15418; BAA15418; BAA15418

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946159

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1644
eco:b1652

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.607

<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
L01622 Genomic DNA Translation: AAC37008.1
U00096 Genomic DNA Translation: AAC74724.1
AP009048 Genomic DNA Translation: BAA15418.2
PIRiA45065
RefSeqiNP_416169.1, NC_000913.3
WP_001282283.1, NZ_SSZK01000001.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IS3X-ray3.10A/B/C/D1-215[»]
3NGYX-ray2.20A/B/C/D1-215[»]
3NGZX-ray2.10A/B1-215[»]
3NH0X-ray2.30A/B1-215[»]
3NH1X-ray2.11A/B/C/D1-215[»]
3NH2X-ray2.30A/B/E/F1-215[»]
3V9SX-ray2.10A/B1-215[»]
3V9UX-ray2.30A/B/C/D1-215[»]
3V9WX-ray1.70A/B/C/D1-215[»]
3V9XX-ray1.90A/B/C/D1-215[»]
3V9ZX-ray1.80A/B1-215[»]
3VA0X-ray2.20A/B1-215[»]
3VA3X-ray2.71A/B1-215[»]
4KAZX-ray1.90A1-215[»]
4KB0X-ray2.00A/B1-215[»]
4KB1X-ray1.80A/B1-215[»]
SMRiP30014
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260267, 149 interactors
850519, 1 interactor
DIPiDIP-10734N
IntActiP30014, 2 interactors
STRINGi511145.b1652

Chemistry databases

ChEMBLiCHEMBL3879866

Proteomic databases

jPOSTiP30014
PaxDbiP30014
PRIDEiP30014

Genome annotation databases

EnsemblBacteriaiAAC74724; AAC74724; b1652
BAA15418; BAA15418; BAA15418
GeneIDi946159
KEGGiecj:JW1644
eco:b1652
PATRICifig|1411691.4.peg.607

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB1509

Phylogenomic databases

eggNOGiCOG0847, Bacteria
HOGENOMiCLU_082724_0_0_6
InParanoidiP30014
PhylomeDBiP30014

Enzyme and pathway databases

BioCyciEcoCyc:EG11547-MONOMER
MetaCyc:EG11547-MONOMER
BRENDAi3.1.13.3, 2026

Miscellaneous databases

EvolutionaryTraceiP30014

Protein Ontology

More...
PROi
PR:P30014

Family and domain databases

CDDicd06134, RNaseT, 1 hit
Gene3Di3.30.420.10, 1 hit
HAMAPiMF_00157, RNase_T, 1 hit
InterProiView protein in InterPro
IPR013520, Exonuclease_RNaseT/DNA_pol3
IPR005987, RNase_T
IPR012337, RNaseH-like_sf
IPR036397, RNaseH_sf
PANTHERiPTHR30231:SF2, PTHR30231:SF2, 1 hit
PfamiView protein in Pfam
PF00929, RNase_T, 1 hit
SMARTiView protein in SMART
SM00479, EXOIII, 1 hit
SUPFAMiSSF53098, SSF53098, 1 hit
TIGRFAMsiTIGR01298, RNaseT, 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 nameiRNT_ECOLI
<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: P30014
Secondary accession number(s): P76896
<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: April 1, 1993
Last sequence update: April 1, 1993
Last modified: December 2, 2020
This is version 151 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 programProkaryotic 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

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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