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Entry version 170 (07 Apr 2021)
Sequence version 3 (01 Nov 1997)
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Protein

Protein-glutamate methylesterase/protein-glutamine glutaminase

Gene

cheB

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

Involved in chemotaxis (PubMed:324984, PubMed:358191, PubMed:392505, PubMed:2188960). Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli (PubMed:392505, PubMed:2188960). Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR (PubMed:358191, PubMed:392505, PubMed:2188960). Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid (PubMed:6300110, PubMed:6304723). Catalyzes its own deactivation by removing the activating phosphoryl group (PubMed:2188960).6 Publications

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Methylesterase activity is activated via phosphorylation in response to negative chemotactic stimuli and is inhibited in the presence of attractants (PubMed:392505, PubMed:2188960). Activation requires both CheA and CheW (PubMed:2188960).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei164UniRule annotationBy similarity1
Active sitei190UniRule annotationBy similarity1
Active sitei286UniRule annotationBy similarity1

<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 functionHydrolase
Biological processChemotaxis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.1.61, 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:
Protein-glutamate methylesterase/protein-glutamine glutaminaseUniRule annotationCurated (EC:3.1.1.61UniRule annotation3 Publications, EC:3.5.1.44UniRule annotation2 Publications)
Alternative name(s):
Chemotaxis response regulator protein-glutamate methylesterase/glutamine deamidaseCurated
Methyl-accepting chemotaxis proteins-specific methylesterase/deamidaseCurated
Short name:
MCP-specific methylesterase/deamidaseCurated
<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:cheB1 PublicationUniRule annotation
Ordered Locus Names:b1883, JW1872
<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

Keywords - Cellular componenti

Cytoplasm

<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

Mutants are defective in chemotaxis. They exhibit very high tumbling rates.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>Mutagenesisi10D → N: Eliminates activation in response to negative stimuli, but does not affect response to positive stimuli. 1 Publication1
Mutagenesisi11D → E or N: Eliminates activation in response to negative stimuli, but does not affect response to positive stimuli. 1 Publication1
Mutagenesisi56D → E or N: Eliminates activation in response to negative stimuli, but does not affect response to positive stimuli. 1 Publication1
Mutagenesisi99L → P: Eliminates activation in response to negative stimuli, but does not affect response to positive stimuli. 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 polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001579921 – 349Protein-glutamate methylesterase/protein-glutamine glutaminaseAdd BLAST349

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 residuei564-aspartylphosphateUniRule annotationBy 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

Phosphorylated by CheA (PubMed:3280143, PubMed:2188960). Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity (PubMed:2188960).2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P07330

PRoteomics IDEntifications database

More...
PRIDEi
P07330

<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

Interacts with CheA (PubMed:7578071). Binds to a C-terminal pentapeptide sequence carried by certain receptors (PubMed:16573695).

2 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4260716, 222 interactors

Database of interacting proteins

More...
DIPi
DIP-9272N

Protein interaction database and analysis system

More...
IntActi
P07330, 10 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b1883

<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
P07330

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>Domaini5 – 122Response regulatoryUniRule annotationAdd BLAST118
Domaini152 – 344CheB-type methylesteraseUniRule annotationAdd BLAST193

<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

Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity.UniRule annotation1 Publication

<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 CheB family.UniRule annotationCurated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG2201, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000445_51_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07330

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P07330

Family and domain databases

Conserved Domains Database

More...
CDDi
cd16432, CheB_Rec, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.180, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00099, CheB_chemtxs, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008248, CheB-like
IPR035909, CheB_C
IPR011006, CheY-like_superfamily
IPR000673, Sig_transdc_resp-reg_Me-estase
IPR001789, Sig_transdc_resp-reg_receiver

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01339, CheB_methylest, 1 hit
PF00072, Response_reg, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000876, RR_chemtxs_CheB, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00448, REC, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52172, SSF52172, 1 hit
SSF52738, SSF52738, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50122, CHEB, 1 hit
PS50110, RESPONSE_REGULATORY, 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.

P07330-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKIRVLSVD DSALMRQIMT EIINSHSDME MVATAPDPLV ARDLIKKFNP
60 70 80 90 100
DVLTLDVEMP RMDGLDFLEK LMRLRPMPVV MVSSLTGKGS EVTLRALELG
110 120 130 140 150
AIDFVTKPQL GIREGMLAYN EMIAEKVRTA AKASLAAHKP LSAPTTLKAG
160 170 180 190 200
PLLSSEKLIA IGASTGGTEA IRHVLQPLPL SSPALLITQH MPPGFTRSFA
210 220 230 240 250
DRLNKLCQIG VKEAEDGERV LPGHAYIAPG DRHMELSRSG ANYQIKIHDG
260 270 280 290 300
PAVNRHRPSV DVLFHSVAKQ AGRNAVGVIL TGMGNDGAAG MLAMRQAGAW
310 320 330 340
TLAQNEASCV VFGMPREAIN MGGVCEVVDL SQVSQQMLAK ISAGQAIRI
Length:349
Mass (Da):37,468
Last modified:November 1, 1997 - v3
<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:i6F3D1AFB8D23D3F5
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 conflicti96A → P in AAA23569 (PubMed:3510184).Curated1
Sequence conflicti125E → Q in AAA23569 (PubMed:3510184).Curated1

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
M13463 Genomic DNA Translation: AAA23569.1
U00096 Genomic DNA Translation: AAC74953.1
AP009048 Genomic DNA Translation: BAA15699.1

Protein sequence database of the Protein Information Resource

More...
PIRi
D25195, XYECEB

NCBI Reference Sequences

More...
RefSeqi
NP_416397.1, NC_000913.3
WP_000036361.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74953; AAC74953; b1883
BAA15699; BAA15699; BAA15699

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946394

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1872
eco:b1883

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.364

<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
M13463 Genomic DNA Translation: AAA23569.1
U00096 Genomic DNA Translation: AAC74953.1
AP009048 Genomic DNA Translation: BAA15699.1
PIRiD25195, XYECEB
RefSeqiNP_416397.1, NC_000913.3
WP_000036361.1, NZ_LN832404.1

3D structure databases

SMRiP07330
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi4260716, 222 interactors
DIPiDIP-9272N
IntActiP07330, 10 interactors
STRINGi511145.b1883

Proteomic databases

PaxDbiP07330
PRIDEiP07330

Genome annotation databases

EnsemblBacteriaiAAC74953; AAC74953; b1883
BAA15699; BAA15699; BAA15699
GeneIDi946394
KEGGiecj:JW1872
eco:b1883
PATRICifig|1411691.4.peg.364

Organism-specific databases

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

More...
EchoBASEi
EB0145

Phylogenomic databases

eggNOGiCOG2201, Bacteria
HOGENOMiCLU_000445_51_0_6
InParanoidiP07330
PhylomeDBiP07330

Enzyme and pathway databases

BioCyciEcoCyc:CHEB-MONOMER
MetaCyc:CHEB-MONOMER
BRENDAi3.1.1.61, 2026

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P07330

Family and domain databases

CDDicd16432, CheB_Rec, 1 hit
Gene3Di3.40.50.180, 1 hit
HAMAPiMF_00099, CheB_chemtxs, 1 hit
InterProiView protein in InterPro
IPR008248, CheB-like
IPR035909, CheB_C
IPR011006, CheY-like_superfamily
IPR000673, Sig_transdc_resp-reg_Me-estase
IPR001789, Sig_transdc_resp-reg_receiver
PfamiView protein in Pfam
PF01339, CheB_methylest, 1 hit
PF00072, Response_reg, 1 hit
PIRSFiPIRSF000876, RR_chemtxs_CheB, 1 hit
SMARTiView protein in SMART
SM00448, REC, 1 hit
SUPFAMiSSF52172, SSF52172, 1 hit
SSF52738, SSF52738, 1 hit
PROSITEiView protein in PROSITE
PS50122, CHEB, 1 hit
PS50110, RESPONSE_REGULATORY, 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 nameiCHEB_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: P07330
Secondary accession number(s): P78070
<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, 1988
Last sequence update: November 1, 1997
Last modified: April 7, 2021
This is version 170 of the entry and version 3 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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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