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Entry version 131 (11 Dec 2019)
Sequence version 1 (29 Mar 2005)
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Protein

ATP-dependent protease ATPase subunit HslU

Gene

hslU

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

ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.7 Publications

<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

Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc.
  1. KM=0.31 mM for ATP (in the absence of HslV)2 Publications
  2. KM=0.28 mM for ATP (in the presence of HslV)2 Publications
  3. KM=5.2 µM for Arc-MYL-st11 (at 37 degrees Celsius)2 Publications
  1. Vmax=57 pmol/min/mg enzyme (in the absence of HslV)2 Publications
  2. Vmax=213 pmol/min/mg enzyme (in the presence of HslV)2 Publications

Temperature dependencei

Optimum temperature is 55 degrees Celsius.2 Publications

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 sitei18ATP; via amide nitrogen and carbonyl oxygen1
Binding sitei256ATP1
Binding sitei321ATP1
Binding sitei393ATP1

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 bindingi60 – 65ATP6

<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 functionChaperone
Biological processStress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11881-MONOMER
ECOL316407:JW3902-MONOMER
MetaCyc:EG11881-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_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:
ATP-dependent protease ATPase subunit HslU
Alternative name(s):
Heat shock protein HslU
Unfoldase HslU
<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:hslU
Synonyms:htpI
Ordered Locus Names:b3931, JW3902
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • 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

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi63K → T: Can neither bind nor hydrolyze ATP. Do not form multimers, but stays as monomer. 1 Publication1
Mutagenesisi80K → T: Some effect on protease activity. 1 Publication1
Mutagenesisi88E → Q: Severely reduced protease activity. 1 Publication1
Mutagenesisi91Y → G: Partial loss of protease activity. 1 Publication1
Mutagenesisi92V → G: Partial loss of protease activity. 1 Publication1
Mutagenesisi93G → A: Almost no protease or ATP hydrolysis activity. 1 Publication1
Mutagenesisi95E → W: Partial loss of protease activity. 1 Publication1
Mutagenesisi262C → V: No effect on ATP hydrolysis. Can support HslV-mediated proteolysis at wild-type levels. 1 Publication1
Mutagenesisi266E → Q: No effect. 1 Publication1
Mutagenesisi286E → Q: Reduced protease activity. 1 Publication1
Mutagenesisi288C → V: No ATP hydrolysis activity. Binds ATP with lower affinity than wild-type. Can support HslV-mediated proteolysis to some extent. 1 Publication1
Mutagenesisi312I → W: No effect. 1 Publication1
Mutagenesisi321E → Q: Complete loss of activity. 1 Publication1
Mutagenesisi325R → E: Complete loss of activity. Forms wild-type complexes with HslV and is able to bind ATP. 1 Publication1
Mutagenesisi385E → K: No effect. 1 Publication1
Mutagenesisi393R → A: Complete loss of activity. 1 Publication1
Mutagenesisi436E → K: Partial loss of protease activity; when associated with K-437. 1
Mutagenesisi437D → K: Partial loss of protease activity; when associated with K-436. 1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001605001 – 443ATP-dependent protease ATPase subunit HslUAdd BLAST443

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0A6H5

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A6H5

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

More...
PaxDbi
P0A6H5

PRoteomics IDEntifications database

More...
PRIDEi
P0A6H5

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P0A6H5

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By heat shock.1 Publication

<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

A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP.

2 Publications

<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

Show more details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261787, 251 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2104 HslUV protease complex

Database of interacting proteins

More...
DIPi
DIP-31855N

Protein interaction database and analysis system

More...
IntActi
P0A6H5, 47 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3931

<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

1443
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
P0A6H5

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
P0A6H5

<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

<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 ClpX chaperone family. HslU subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C4N Bacteria
COG1220 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000010036

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A6H5

KEGG Orthology (KO)

More...
KOi
K03667

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A6H5

Family and domain databases

Database of protein disorder

More...
DisProti
DP00100

HAMAP database of protein families

More...
HAMAPi
MF_00249 HslU, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR019489 Clp_ATPase_C
IPR004491 HslU
IPR027417 P-loop_NTPase

The PANTHER Classification System

More...
PANTHERi
PTHR43815 PTHR43815, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00004 AAA, 1 hit
PF07724 AAA_2, 1 hit
PF10431 ClpB_D2-small, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382 AAA, 1 hit
SM01086 ClpB_D2-small, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00390 hslU, 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.

P0A6H5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEMTPREIV SELDKHIIGQ DNAKRSVAIA LRNRWRRMQL NEELRHEVTP
60 70 80 90 100
KNILMIGPTG VGKTEIARRL AKLANAPFIK VEATKFTEVG YVGKEVDSII
110 120 130 140 150
RDLTDAAVKM VRVQAIEKNR YRAEELAEER ILDVLIPPAK NNWGQTEQQQ
160 170 180 190 200
EPSAARQAFR KKLREGQLDD KEIEIDLAAA PMGVEIMAPP GMEEMTSQLQ
210 220 230 240 250
SMFQNLGGQK QKARKLKIKD AMKLLIEEEA AKLVNPEELK QDAIDAVEQH
260 270 280 290 300
GIVFIDEIDK ICKRGESSGP DVSREGVQRD LLPLVEGCTV STKHGMVKTD
310 320 330 340 350
HILFIASGAF QIAKPSDLIP ELQGRLPIRV ELQALTTSDF ERILTEPNAS
360 370 380 390 400
ITVQYKALMA TEGVNIEFTD SGIKRIAEAA WQVNESTENI GARRLHTVLE
410 420 430 440
RLMEEISYDA SDLSGQNITI DADYVSKHLD ALVADEDLSR FIL
Length:443
Mass (Da):49,594
Last modified:March 29, 2005 - 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:iD2188639EA9AEF4C
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
L19201 Genomic DNA Translation: AAB03063.1
U00096 Genomic DNA Translation: AAC76913.1
AP009048 Genomic DNA Translation: BAE77379.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JT0761

NCBI Reference Sequences

More...
RefSeqi
NP_418366.1, NC_000913.3
WP_001293341.1, NZ_STEB01000017.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76913; AAC76913; b3931
BAE77379; BAE77379; BAE77379

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948430

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3902
eco:b3931

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2774

<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
L19201 Genomic DNA Translation: AAB03063.1
U00096 Genomic DNA Translation: AAC76913.1
AP009048 Genomic DNA Translation: BAE77379.1
PIRiJT0761
RefSeqiNP_418366.1, NC_000913.3
WP_001293341.1, NZ_STEB01000017.1

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
1DO0X-ray3.00A/B/C/D/E/F2-443[»]
1DO2X-ray4.00A/B/C/D2-443[»]
1E94X-ray2.80E/F2-443[»]
1G4AX-ray3.00E/F1-443[»]
1G4BX-ray7.00E/F/K/L1-443[»]
1HQYX-ray2.80E/F2-443[»]
1HT1X-ray2.80E/F/G/I2-443[»]
1HT2X-ray2.80E/F/G/H2-443[»]
1YYFX-ray4.16A/B1-443[»]
5JI3X-ray3.00E/F1-443[»]
5TXVX-ray7.09A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X2-443[»]
SMRiP0A6H5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4261787, 251 interactors
ComplexPortaliCPX-2104 HslUV protease complex
DIPiDIP-31855N
IntActiP0A6H5, 47 interactors
STRINGi511145.b3931

2D gel databases

SWISS-2DPAGEiP0A6H5

Proteomic databases

EPDiP0A6H5
jPOSTiP0A6H5
PaxDbiP0A6H5
PRIDEiP0A6H5

Genome annotation databases

EnsemblBacteriaiAAC76913; AAC76913; b3931
BAE77379; BAE77379; BAE77379
GeneIDi948430
KEGGiecj:JW3902
eco:b3931
PATRICifig|1411691.4.peg.2774

Organism-specific databases

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

More...
EchoBASEi
EB1827

Phylogenomic databases

eggNOGiENOG4105C4N Bacteria
COG1220 LUCA
HOGENOMiHOG000010036
InParanoidiP0A6H5
KOiK03667
PhylomeDBiP0A6H5

Enzyme and pathway databases

BioCyciEcoCyc:EG11881-MONOMER
ECOL316407:JW3902-MONOMER
MetaCyc:EG11881-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A6H5

Protein Ontology

More...
PROi
PR:P0A6H5

Family and domain databases

DisProtiDP00100
HAMAPiMF_00249 HslU, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR003959 ATPase_AAA_core
IPR019489 Clp_ATPase_C
IPR004491 HslU
IPR027417 P-loop_NTPase
PANTHERiPTHR43815 PTHR43815, 1 hit
PfamiView protein in Pfam
PF00004 AAA, 1 hit
PF07724 AAA_2, 1 hit
PF10431 ClpB_D2-small, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SM01086 ClpB_D2-small, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00390 hslU, 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 nameiHSLU_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: P0A6H5
Secondary accession number(s): P32168, Q2M8M7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: December 11, 2019
This is version 131 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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