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Entry version 85 (29 Sep 2021)
Sequence version 1 (24 May 2004)
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Protein

Aspartokinase

Gene

ask

Organism
Thermus thermophilus
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

Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine.

2 Publications

<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 <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

Inhibited by threonine.3 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

Kcat is 1500 (min-1).
  1. KM=0.27 mM for aspartate1 Publication
  2. KM=0.5 mM for ATP1 Publication

Temperature dependencei

Thermostable.1 Publication

<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: L-lysine biosynthesis via DAP pathway

This protein is involved in step 1 of the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate. This subpathway is part of the pathway L-lysine biosynthesis via DAP pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate, the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

Pathwayi: L-methionine biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes L-homoserine from L-aspartate. This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homoserine from L-aspartate, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Pathwayi: L-threonine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-threonine from L-aspartate. This subpathway is part of the pathway L-threonine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-threonine from L-aspartate, the pathway L-threonine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei7Contribution to the catalysis1
<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 sitei41ATPBy similarity1
Binding sitei74SubstrateBy similarity1
Sitei74Contribution to the catalysis1
Binding sitei153SubstrateBy similarity1
Binding sitei209ATPBy similarity1
Binding sitei270Substrate1
Binding sitei294Substrate1

<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 functionKinase, Transferase
Biological processAmino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.2.4, 2305

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P61489

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

More...
UniPathwayi
UPA00034;UER00015
UPA00050;UER00461
UPA00051;UER00462

<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:
Aspartokinase (EC:2.7.2.4)
Alternative name(s):
Aspartate kinase
Short name:
AK
Short name:
ASK
Threonine-sensitive AK
Short name:
ThrA
<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:ask
Synonyms:askAB
<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>OrganismiThermus thermophilus
<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 identifieri274 [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 lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

<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>Mutagenesisi7K → A: Loss of aspartokinase activity. 1 Publication1
Mutagenesisi7K → M: Loss of aspartokinase activity. 1 Publication1
Mutagenesisi9G → M: Loss of aspartokinase activity. 1 Publication1
Mutagenesisi10G → A: Significant decrease in the catalytic efficiency. 1 Publication1
Mutagenesisi41S → A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type. 1 Publication1
Mutagenesisi42A → S: Loss of aspartokinase activity. 1 Publication1
Mutagenesisi47T → A: Significant decrease in the affinity for aspartic acid. Requires higher concentration of magnesium ion than wild-type. 1 Publication1
Mutagenesisi74E → A: Loss of aspartokinase activity. 1 Publication1
Mutagenesisi74E → Q: Loss of aspartokinase activity. 1 Publication1
Mutagenesisi135G → A: Very low catalytic efficiency. 1 Publication1
Mutagenesisi135G → S: Loss of aspartokinase activity. 1 Publication1
Mutagenesisi150R → A: Significant decrease in the catalytic efficiency. 1 Publication1
Mutagenesisi154D → A: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type. 1 Publication1
Mutagenesisi154D → N: Significant decrease in the catalytic efficiency. Requires higher concentration of magnesium ion than wild-type. 1 Publication1
Mutagenesisi174D → A: Significant decrease in the catalytic efficiency. 1 Publication1
Mutagenesisi182D → A: Significant decrease in the catalytic efficiency.Requires higher concentration of magnesium ion than wild-type. 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_00000023891 – 405AspartokinaseAdd BLAST405

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P61489

<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

Heterotetramer consisting of 2 isoforms Alpha (catalytic and regulation) and of a homodimer of 2 isoforms Beta (regulation and thermostability).

2 Publications

<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

1405
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
P61489

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
P61489

<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>Domaini263 – 342ACT 1PROSITE-ProRule annotationAdd BLAST80
Domaini344 – 405ACT 2PROSITE-ProRule annotationAdd BLAST62

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>Regioni7 – 10ATP bindingBy similarity4
Regioni25 – 30Substrate bindingBy similarity6
Regioni47 – 49Substrate bindingBy similarity3
Regioni125 – 126Substrate bindingBy similarity2
Regioni150 – 153Substrate acid bindingBy similarity4
Regioni173 – 174ATP bindingBy similarity2
Regioni179 – 184ATP bindingBy similarity6
Regioni274 – 275Substrate binding2
Regioni288 – 290Substrate bindingBy similarity3
Regioni355 – 356Substrate bindingBy similarity2
Regioni369 – 370Substrate binding2
Regioni376 – 377Substrate bindingBy similarity2

<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 aspartokinase family.Curated

Keywords - Domaini

Repeat

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04261, AAK_AKii-LysC-BS, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1160.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036393, AceGlu_kinase-like_sf
IPR002912, ACT_dom
IPR041740, AKii-LysC-BS
IPR001048, Asp/Glu/Uridylate_kinase
IPR005260, Asp_kin_monofn
IPR001341, Asp_kinase
IPR018042, Aspartate_kinase_CS
IPR027795, CASTOR_ACT_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00696, AA_kinase, 1 hit
PF01842, ACT, 1 hit
PF13840, ACT_7, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000726, Asp_kin, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53633, SSF53633, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00656, asp_kin_monofn, 1 hit
TIGR00657, asp_kinases, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51671, ACT, 1 hit
PS00324, ASPARTOKINASE, 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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
Isoform Alpha (identifier: P61489-1) [UniParc]FASTAAdd to basket
Also known as: Aspartokinase subunit alpha

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MALVVQKYGG TSVGDLERIH KVAQRIAHYR EKGHRLAVVV SAMGHTTDEL
60 70 80 90 100
IALAKRVNPR PPFRELDLLT TTGEQVSVAL LSMQLWAMGI PAKGFVQHQI
110 120 130 140 150
GITTDGRYGD ARILEVNPAR IREALDQGFV AVIAGFMGTT PEGEITTLGR
160 170 180 190 200
GGSDTTAVAI AAALGAKECE IYTDTEGVYT TDPHLIPEAR KLSVIGYDQM
210 220 230 240 250
LEMAALGARV LHPRAVYYAK RYGVVLHVRS SFSYNPGTLV KEVAMEMDKA
260 270 280 290 300
VTGVALDLDH AQIGLIGIPD QPGIAAKVFQ ALAERGIAVD MIIQGVPGHD
310 320 330 340 350
PSRQQMAFTV KKDFAQEALE ALEPVLAEIG GEAILRPDIA KVSIVGVGLA
360 370 380 390 400
STPEVPAKMF QAVASTGANI EMIATSEVRI SVIIPAEYAE AALRAVHQAF

ELDKA
Length:405
Mass (Da):43,319
Last modified:May 24, 2004 - 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:i47A3A29E2B82D0EA
GO
Isoform Beta (identifier: P61489-2) [UniParc]FASTAAdd to basket
Also known as: Aspartokinase subunit beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-244: Missing.

Show »
Length:161
Mass (Da):16,895
Checksum:i94BDE8A671CC54EA
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0186651 – 244Missing in isoform Beta. CuratedAdd BLAST244

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
D37928 Genomic DNA Translation: BAA07146.1
D37928 Genomic DNA Translation: BAA07147.1

NCBI Reference Sequences

More...
RefSeqi
WP_024118988.1, NZ_AP024270.1 [P61489-1]

Keywords - Coding sequence diversityi

Alternative initiation

<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
D37928 Genomic DNA Translation: BAA07146.1
D37928 Genomic DNA Translation: BAA07147.1
RefSeqiWP_024118988.1, NZ_AP024270.1 [P61489-1]

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
2DT9X-ray2.15A/B245-405[»]
2ZHOX-ray2.98A/B/C/D/E/F245-405[»]
SMRiP61489
ModBaseiSearch...
PDBe-KBiSearch...

Proteomic databases

PRIDEiP61489

Enzyme and pathway databases

UniPathwayiUPA00034;UER00015
UPA00050;UER00461
UPA00051;UER00462
BRENDAi2.7.2.4, 2305
SABIO-RKiP61489

Miscellaneous databases

EvolutionaryTraceiP61489

Family and domain databases

CDDicd04261, AAK_AKii-LysC-BS, 1 hit
Gene3Di3.40.1160.10, 1 hit
InterProiView protein in InterPro
IPR036393, AceGlu_kinase-like_sf
IPR002912, ACT_dom
IPR041740, AKii-LysC-BS
IPR001048, Asp/Glu/Uridylate_kinase
IPR005260, Asp_kin_monofn
IPR001341, Asp_kinase
IPR018042, Aspartate_kinase_CS
IPR027795, CASTOR_ACT_dom
PfamiView protein in Pfam
PF00696, AA_kinase, 1 hit
PF01842, ACT, 1 hit
PF13840, ACT_7, 1 hit
PIRSFiPIRSF000726, Asp_kin, 1 hit
SUPFAMiSSF53633, SSF53633, 1 hit
TIGRFAMsiTIGR00656, asp_kin_monofn, 1 hit
TIGR00657, asp_kinases, 1 hit
PROSITEiView protein in PROSITE
PS51671, ACT, 1 hit
PS00324, ASPARTOKINASE, 1 hit

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 nameiAK_THETH
<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: P61489
Secondary accession number(s): P77991, P97151
<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: May 24, 2004
Last sequence update: May 24, 2004
Last modified: September 29, 2021
This is version 85 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

Documents

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