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Entry version 136 (05 Jun 2019)
Sequence version 1 (01 Mar 2001)
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Protein

Inosine-5'-monophosphate dehydrogenase

Gene

guaB

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Unreviewed-Annotation score:

Annotation score:4 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

Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.UniRule annotation

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.UniRule annotation

<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

K+UniRule annotation

<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

Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: XMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes XMP from IMP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Inosine-5'-monophosphate dehydrogenase (guaB)
This subpathway is part of the pathway XMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes XMP from IMP, the pathway XMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei98ATP; via amide nitrogen and carbonyl oxygenCombined sources1
Binding sitei153ATPCombined sources1
Binding sitei159ATP; via amide nitrogen and carbonyl oxygenCombined sources1
Binding sitei247NADUniRule annotation1
<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 bindingi299Potassium; via carbonyl oxygenUniRule annotation1
Metal bindingi301Potassium; via carbonyl oxygenUniRule annotation1
Binding sitei302IMPUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei304Thioimidate intermediateUniRule annotation1
Metal bindingi304Potassium; via carbonyl oxygenUniRule annotation1
Active sitei402Proton acceptorUniRule annotation1
Binding sitei417IMPUniRule annotation1
Metal bindingi471Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi472Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1
Metal bindingi473Potassium; via carbonyl oxygen; shared with tetrameric partnerUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi118 – 120ATPCombined sources3
Nucleotide bindingi134 – 137ATPCombined sources4
Nucleotide bindingi180 – 181ATPCombined sources2
Nucleotide bindingi198 – 199ATPCombined sources2
Nucleotide bindingi247 – 249NADUniRule annotation3
Nucleotide bindingi297 – 299NADUniRule annotation3

<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 functionOxidoreductaseUniRule annotation
Biological processGMP biosynthesisUniRule annotation, Purine biosynthesis
LigandATP-bindingCombined sources, Metal-bindingUniRule annotation, NADUniRule annotation, Nucleotide-binding, PotassiumUniRule annotation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
PAER208964:G1FZ6-3841-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.205 5087

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00601;UER00295

<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:
Inosine-5'-monophosphate dehydrogenaseUniRule annotation (EC:1.1.1.205UniRule annotation)
Short name:
IMP dehydrogenaseUniRule annotation
Short name:
IMPDUniRule annotation
Short name:
IMPDHUniRule annotation
<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:guaBUniRule annotationImported
Ordered Locus Names:PA3770Imported
<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>OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)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 identifieri208964 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002438 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

Organism-specific databases

Pseudomonas genome database

More...
PseudoCAPi
PA3770

<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

Proteomic databases

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

More...
PaxDbi
Q9HXM5

PRoteomics IDEntifications database

More...
PRIDEi
Q9HXM5

<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.

UniRule annotation

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-16056797,EBI-16056797

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-60162N

<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
Q9HXM5

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini93 – 148CBSInterPro annotationAdd BLAST56
Domaini152 – 210CBSInterPro annotationAdd BLAST59

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>Regioni337 – 339IMP bindingUniRule annotation3
Regioni360 – 361IMP bindingUniRule annotation2
Regioni384 – 388IMP bindingUniRule annotation5

<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 IMPDH/GMPR family.UniRule annotation

Keywords - Domaini

CBS domainPROSITE-ProRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CP4 Bacteria
COG0516 LUCA
COG0517 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000165755

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9HXM5

KEGG Orthology (KO)

More...
KOi
K00088

Identification of Orthologs from Complete Genome Data

More...
OMAi
SSMGYCG

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9HXM5

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00381 IMPDH, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01964 IMPDH, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013785 Aldolase_TIM
IPR000644 CBS_dom
IPR005990 IMP_DH
IPR015875 IMP_DH/GMP_Rdtase_CS
IPR001093 IMP_DH_GMPRt

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00571 CBS, 2 hits
PF00478 IMPDH, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000130 IMPDH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00116 CBS, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01302 IMP_dehydrog, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51371 CBS, 2 hits
PS00487 IMP_DH_GMP_RED, 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.

Q9HXM5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLRISQEALT FDDVLLIPGY SEVLPKDVSL KTRLTRGIEL NIPLVSAAMD
60 70 80 90 100
TVTEARLAIA MAQEGGIGII HKNMGIEQQA AEVRKVKKHE TAIVRDPVTV
110 120 130 140 150
TPSTKIIELL QMAREYGFSG FPVVEQGELV GIVTGRDLRV KPNAGDTVAA
160 170 180 190 200
IMTPKDKLVT AREGTPLEEM KAKLYENRIE KMLVVDENFY LRGLVTFRDI
210 220 230 240 250
EKAKTYPLAS KDEQGRLRVG AAVGTGADTG ERVAALVAAG VDVVVVDTAH
260 270 280 290 300
GHSKGVIERV RWVKQTFPDV QVIGGNIATA EAAKALAEAG ADAVKVGIGP
310 320 330 340 350
GSICTTRIVA GVGVPQISAI ANVAAALEGT GVPLIADGGI RFSGDLAKAM
360 370 380 390 400
VAGAYCVMMG SMFAGTEEAP GEIELFQGRS YKSYRGMGSL GAMSGSQGSS
410 420 430 440 450
DRYFQDASAG AEKLVPEGIE GRVPYKGALS AIVHQLMGGL RAAMGYTGSA
460 470 480
DIQQMRTQPQ FVRITGAGMA ESHVHDVQIT KEAPNYRVG
Length:489
Mass (Da):51,707
Last modified:March 1, 2001 - 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:i6D2320AFD52C888B
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
AE004091 Genomic DNA Translation: AAG07157.1

Protein sequence database of the Protein Information Resource

More...
PIRi
H83173

NCBI Reference Sequences

More...
RefSeqi
NP_252459.1, NC_002516.2
WP_003092702.1, NZ_QZGE01000001.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAG07157; AAG07157; PA3770

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
880535

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pae:PA3770

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|208964.12.peg.3947

<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
AE004091 Genomic DNA Translation: AAG07157.1
PIRiH83173
RefSeqiNP_252459.1, NC_002516.2
WP_003092702.1, NZ_QZGE01000001.1

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
3ZFHX-ray2.25A1-489[»]
4AVFX-ray2.23A/B/C/D1-489[»]
4DQWX-ray2.51A/B1-489[»]
5AHLX-ray1.95A1-489[»]
5AHMX-ray1.74A/B1-489[»]
5AHNX-ray1.65A1-489[»]
6GJVX-ray2.11A/B/C/D/E/F/G/H1-489[»]
6GK9X-ray2.54A/B/C/D/E/F/G/H1-489[»]
SMRiQ9HXM5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-60162N

Proteomic databases

PaxDbiQ9HXM5
PRIDEiQ9HXM5

Genome annotation databases

EnsemblBacteriaiAAG07157; AAG07157; PA3770
GeneIDi880535
KEGGipae:PA3770
PATRICifig|208964.12.peg.3947

Organism-specific databases

PseudoCAPiPA3770

Phylogenomic databases

eggNOGiENOG4105CP4 Bacteria
COG0516 LUCA
COG0517 LUCA
HOGENOMiHOG000165755
InParanoidiQ9HXM5
KOiK00088
OMAiSSMGYCG
PhylomeDBiQ9HXM5

Enzyme and pathway databases

UniPathwayiUPA00601;UER00295
BioCyciPAER208964:G1FZ6-3841-MONOMER
BRENDAi1.1.1.205 5087

Family and domain databases

CDDicd00381 IMPDH, 1 hit
Gene3Di3.20.20.70, 1 hit
HAMAPiMF_01964 IMPDH, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR000644 CBS_dom
IPR005990 IMP_DH
IPR015875 IMP_DH/GMP_Rdtase_CS
IPR001093 IMP_DH_GMPRt
PfamiView protein in Pfam
PF00571 CBS, 2 hits
PF00478 IMPDH, 1 hit
PIRSFiPIRSF000130 IMPDH, 1 hit
SMARTiView protein in SMART
SM00116 CBS, 2 hits
TIGRFAMsiTIGR01302 IMP_dehydrog, 1 hit
PROSITEiView protein in PROSITE
PS51371 CBS, 2 hits
PS00487 IMP_DH_GMP_RED, 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 nameiQ9HXM5_PSEAE
<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: Q9HXM5
<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/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: June 5, 2019
This is version 136 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 statusiUnreviewed (UniProtKB/TrEMBL)

<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-structureCombined sources, Complete proteome, Reference proteomeImported
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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