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Entry version 162 (07 Apr 2021)
Sequence version 2 (11 Oct 2004)
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Protein

NAD-capped RNA hydrolase NudC

Gene

nudC

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

mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA (PubMed:25533955, PubMed:27561816, PubMed:27428510). The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing (PubMed:25533955). Has preference for mRNAs with a 5'-end purine (PubMed:27428510). Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates, but uniquely prefers the reduced form of NADH (PubMed:7829480, PubMed:25533955).4 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 '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

Protein has several cofactor binding sites:

<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

  1. KM=0.11 mM for NADH1 Publication
  2. KM=5.1 mM for NAD+1 Publication
  3. KM=0.29 mM for deamino-NADH1 Publication
  4. KM=2.6 mM for deamino-NAD+1 Publication
  5. KM=0.67 mM for AppA1 Publication
  6. KM=1.8 mM for ADP-ribose1 Publication
  1. Vmax=7.6 µmol/min/mg enzyme with NADH as substrate1 Publication
  2. Vmax=2.9 µmol/min/mg enzyme with NAD+ as substrate1 Publication
  3. Vmax=8.9 µmol/min/mg enzyme with deamino-NADH as substrate1 Publication
  4. Vmax=3.2 µmol/min/mg enzyme with deamino-NAD+ as substrate1 Publication
  5. Vmax=4.7 µmol/min/mg enzyme with AppA as substrate1 Publication
  6. Vmax=4.8 µmol/min/mg enzyme with ADP-ribose as substrate1 Publication

pH dependencei

Optimum pH is 8.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei25SubstrateCombined sources1 Publication1
Binding sitei69SubstrateCombined sources1 Publication1
<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 bindingi98ZincCombined sources3 Publications1
Metal bindingi101ZincCombined sources3 Publications1
Binding sitei111SubstrateCombined sources1 Publication1
Metal bindingi116ZincCombined sources3 Publications1
Metal bindingi119ZincCombined sources3 Publications1
Binding sitei124SubstrateCombined sources2 Publications1
Metal bindingi158Divalent metal cation 1; via carbonyl oxygenBy similarity1
Metal bindingi174Divalent metal cation 2By similarity1
Metal bindingi174Divalent metal cation 3By similarity1
Metal bindingi178Divalent metal cation 1By similarity1
Metal bindingi178Divalent metal cation 3By similarity1
Metal bindingi219Divalent metal cation 1By similarity1
Metal bindingi219Divalent metal cation 3By similarity1
Binding sitei241Substrate; via amide nitrogenCombined sources2 Publications1

<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
LigandMagnesium, Manganese, Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11702-MONOMER
MetaCyc:EG11702-MONOMER

<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:
NAD-capped RNA hydrolase NudCCurated (EC:3.6.1.-3 Publications)
Short name:
DeNADding enzyme NudCCurated
Alternative name(s):
NADH pyrophosphatase1 Publication (EC:3.6.1.221 Publication)
<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:nudC
Synonyms:yjaD
Ordered Locus Names:b3996, JW5548
<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

<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%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>Mutagenesisi69R → A: Does not affect deNADding activity. 1 Publication1
Mutagenesisi160F → A: Abolished deNADding activity. 1 Publication1
Mutagenesisi174E → Q: Abolished deNADding activity. 1 Publication1
Mutagenesisi178E → Q: Abolished deNADding activity. 3 Publications1
Mutagenesisi188Y → A or Q: Abolished deNADding activity without disrupting homodimerization. 1 Publication1
Mutagenesisi194W → A: Abolished deNADding activity. 1 Publication1
Mutagenesisi214V → A: Abolished deNADding activity. 1 Publication1
Mutagenesisi219E → Q: Abolished deNADding activity. 1 Publication1
Mutagenesisi236P → A: Strongly reduced but not abolished deNADding activity. 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_00000569631 – 257NAD-capped RNA hydrolase NudCAdd BLAST257

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P32664

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

More...
PaxDbi
P32664

PRoteomics IDEntifications database

More...
PRIDEi
P32664

<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.

2 Publications2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4263215, 137 interactors

Protein interaction database and analysis system

More...
IntActi
P32664, 1 interactor

STRING: functional protein association networks

More...
STRINGi
511145.b3996

<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

1257
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
P32664

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
P32664

<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>Domaini125 – 248Nudix hydrolasePROSITE-ProRule annotationAdd BLAST124

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>Regioni192 – 199Substrate bindingCombined sources2 Publications8

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>Motifi159 – 180Nudix boxPROSITE-ProRule annotationAdd 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 Nudix hydrolase family. NudC subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG2816, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_037162_0_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32664

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P32664

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_00297, Nudix_NudC, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR022925, NADH_pyroPase_NudC
IPR015797, NUDIX_hydrolase-like_dom_sf
IPR020084, NUDIX_hydrolase_CS
IPR000086, NUDIX_hydrolase_dom
IPR015376, Znr_NADH_PPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00293, NUDIX, 1 hit
PF09297, zf-NADH-PPase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55811, SSF55811, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51462, NUDIX, 1 hit
PS00893, NUDIX_BOX, 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.

P32664-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDRIIEKLDH GWWVVSHEQK LWLPKGELPY GEAANFDLVG QRALQIGEWQ
60 70 80 90 100
GEPVWLVQQQ RRHDMGSVRQ VIDLDVGLFQ LAGRGVQLAE FYRSHKYCGY
110 120 130 140 150
CGHEMYPSKT EWAMLCSHCR ERYYPQIAPC IIVAIRRDDS ILLAQHTRHR
160 170 180 190 200
NGVHTVLAGF VEVGETLEQA VAREVMEESG IKVKNLRYVT SQPWPFPQSL
210 220 230 240 250
MTAFMAEYDS GDIVIDPKEL LEANWYRYDD LPLLPPPGTV ARRLIEDTVA

MCRAEYE
Length:257
Mass (Da):29,689
Last modified:October 11, 2004 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i368FAE0480AF4CB3
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence D12624 differs from that shown. Reason: Frameshift.Curated

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 conflicti33A → R in AAC43094 (PubMed:8265357).Curated1

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
D12624 Genomic DNA No translation available.
U00006 Genomic DNA Translation: AAC43094.1
U00096 Genomic DNA Translation: AAT48238.1
AP009048 Genomic DNA Translation: BAE77323.1

Protein sequence database of the Protein Information Resource

More...
PIRi
G65206

NCBI Reference Sequences

More...
RefSeqi
WP_000373940.1, NZ_STEB01000045.1
YP_026280.1, NC_000913.3

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAT48238; AAT48238; b3996
BAE77323; BAE77323; BAE77323

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
57730787
948498

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW5548
eco:b3996

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2715

<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
D12624 Genomic DNA No translation available.
U00006 Genomic DNA Translation: AAC43094.1
U00096 Genomic DNA Translation: AAT48238.1
AP009048 Genomic DNA Translation: BAE77323.1
PIRiG65206
RefSeqiWP_000373940.1, NZ_STEB01000045.1
YP_026280.1, NC_000913.3

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
1VK6X-ray2.20A1-257[»]
2GB5X-ray2.30A/B1-257[»]
5ISYX-ray2.35A/C1-257[»]
5IW4X-ray2.60A/B1-257[»]
5IW5X-ray2.70A/B1-257[»]
SMRiP32664
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4263215, 137 interactors
IntActiP32664, 1 interactor
STRINGi511145.b3996

Proteomic databases

jPOSTiP32664
PaxDbiP32664
PRIDEiP32664

Genome annotation databases

EnsemblBacteriaiAAT48238; AAT48238; b3996
BAE77323; BAE77323; BAE77323
GeneIDi57730787
948498
KEGGiecj:JW5548
eco:b3996
PATRICifig|1411691.4.peg.2715

Organism-specific databases

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

More...
EchoBASEi
EB1653

Phylogenomic databases

eggNOGiCOG2816, Bacteria
HOGENOMiCLU_037162_0_1_6
InParanoidiP32664
PhylomeDBiP32664

Enzyme and pathway databases

BioCyciEcoCyc:EG11702-MONOMER
MetaCyc:EG11702-MONOMER

Miscellaneous databases

EvolutionaryTraceiP32664

Protein Ontology

More...
PROi
PR:P32664

Family and domain databases

HAMAPiMF_00297, Nudix_NudC, 1 hit
InterProiView protein in InterPro
IPR022925, NADH_pyroPase_NudC
IPR015797, NUDIX_hydrolase-like_dom_sf
IPR020084, NUDIX_hydrolase_CS
IPR000086, NUDIX_hydrolase_dom
IPR015376, Znr_NADH_PPase
PfamiView protein in Pfam
PF00293, NUDIX, 1 hit
PF09297, zf-NADH-PPase, 1 hit
SUPFAMiSSF55811, SSF55811, 2 hits
PROSITEiView protein in PROSITE
PS51462, NUDIX, 1 hit
PS00893, NUDIX_BOX, 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 nameiNUDC_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: P32664
Secondary accession number(s): Q2M8T3, Q6BEX6
<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: October 1, 1993
Last sequence update: October 11, 2004
Last modified: April 7, 2021
This is version 162 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation 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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