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Protein

Threonine synthase 2, chloroplastic

Gene

TS2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-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 gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.1 Publication

Miscellaneous

Binds 4 S-adenosyl-L-methionine (SAM) molecules per dimer. Although SAM3 and SAM4 have equivalent positions, their interactions with the protein are not identical. SAM3 interacts with Lys-172 and Asn-178 of monomer B, whereas SAM4 interacts only with Lys-172 of monomer A (By similarity).By similarity
Much less active than TS1 at physiological concentrations of S-adenosyl-methionine (20 µM).

<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

<p>This subsection of the ‘Function’ 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

Allosterically activated by S-adenosyl-methionine (SAM).

<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-threonine biosynthesis

This protein is involved in step 5 of the subpathway that synthesizes L-threonine from L-aspartate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Aspartokinase (AXX17_At5g13510), Aspartokinase (AXX17_At3g01160), Aspartokinase (AXX17_At3g01160), Aspartokinase (CARAB-AK-LYS), Aspartokinase (AXX17_At3g01160), AK1 (AXX17_At5g12690), Aspartokinase 3, chloroplastic (AK3), Aspartokinase 2, chloroplastic (AK2), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1), Aspartokinase 1, chloroplastic (AK1), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2)
  2. no protein annotated in this organism
  3. Homoserine dehydrogenase (AXX17_At5g21030), Homoserine dehydrogenase (At5g21060), Homoserine dehydrogenase, Homoserine dehydrogenase (At5g21060), Homoserine dehydrogenase (AXX17_At5g21030), Homoserine dehydrogenase (At5g21060), Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic (AKHSDH1), Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic (AKHSDH2)
  4. Homoserine kinase (HSK)
  5. Threonine synthase 1, chloroplastic (TS1), Threonine synthase 2, chloroplastic (TS2)
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 of the ‘Function’ 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 sitei163S-adenosyl-L-methionine 2; shared with dimeric partnerBy similarity1
Binding sitei164S-adenosyl-L-methionine 2; via amide nitrogen and carbonyl oxygen; shared with dimeric partnerBy similarity1
Binding sitei172S-adenosyl-L-methionine 3; in monomer BBy similarity1
Binding sitei172S-adenosyl-L-methionine 4; in monomer ABy similarity1
Binding sitei178S-adenosyl-L-methionine 3; in monomer BBy similarity1
Binding sitei464Pyridoxal phosphateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • pyridoxal phosphate binding Source: GO_Central
  • threonine synthase activity Source: GO_Central

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 functionAllosteric enzyme, Lyase
Biological processAmino-acid biosynthesis, Threonine biosynthesis
LigandPyridoxal phosphate, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
ARA:AT1G72810-MONOMER

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

More...
UniPathwayi
UPA00050;UER00065

<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:
Threonine synthase 2, chloroplastic (EC:4.2.3.1)
<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:TS2
Ordered Locus Names:At1g72810
ORF Names:F3N23.1
<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>OrganismiArabidopsis thaliana (Mouse-ear cress)
<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 identifieri3702 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<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
  • UP000006548 <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 1

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT1G72810

The Arabidopsis Information Resource

More...
TAIRi
locus:2032632 AT1G72810

<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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 33ChloroplastCuratedAdd BLAST33
<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_000037951634 – 516Threonine synthase 2, chloroplasticAdd BLAST483

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei194N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

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

More...
PaxDbi
Q9SSP5

PRoteomics IDEntifications database

More...
PRIDEi
Q9SSP5

<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

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9SSP5 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9SSP5 AT

<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

Homodimer.By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
3702.AT1G72810.1

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q9SSP5

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9SSP5

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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

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>Regioni133 – 135S-adenosyl-L-methionine 1 binding; shared with dimeric partnerBy similarity3
Regioni156 – 158S-adenosyl-L-methionine 1 binding; shared with dimeric partnerBy similarity3
Regioni326 – 330Pyridoxal phosphate bindingBy similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi150 – 153Poly-Asp4

<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 threonine synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IITN Eukaryota
COG0498 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000076502

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9SSP5

KEGG Orthology (KO)

More...
KOi
K01733

Identification of Orthologs from Complete Genome Data

More...
OMAi
GTHLRAI

Database of Orthologous Groups

More...
OrthoDBi
EOG0936061W

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9SSP5

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001926 PLP-dep
IPR000634 Ser/Thr_deHydtase_PyrdxlP-BS
IPR004450 Thr_synthase-like
IPR036052 Trypto_synt_PLP_dependent

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00291 PALP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53686 SSF53686, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00260 thrC, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00165 DEHYDRATASE_SER_THR, 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>.<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q9SSP5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASFSLPHSA TYFPSHSETS LKPHSAASFT VRCTSASPAV PPQTPQKPRR
60 70 80 90 100
SPDENIRDEA RRRPHQLQNL SARYVPFNAP PSSTESYSLD EIVYRSQSGA
110 120 130 140 150
LLDVQHDFAA LKRYDGEFWR NLFDSRVGKT NWPYGSGVWS KKEWVLPEID
160 170 180 190 200
DDDIVSAFEG NSNLFWAERF GKQYLQMNDL WVKHCGISHT GSFKDLGMSV
210 220 230 240 250
LVSQVNRLRK MNKPVIGVGC ASTGDTSAAL SAYCASAGIP SIVFLPADKI
260 270 280 290 300
SMAQLVQPIA NGAFVLSIDT DFDGCMHLIR EVTAELPIYL ANSLNSLRLE
310 320 330 340 350
GQKTAAIEIL QQFNWQVPDW VIVPGGNLGN IYAFYKGFHM CKELGLVDRI
360 370 380 390 400
PRLVCAQAAN ANPLYLHYKS GFKEDFNPLK ANTTFASAIQ IGDPVSIDRA
410 420 430 440 450
VYALKKSNGI VEEATEEELM DATALADSTG MFICPHTGVA LTALMKLRKS
460 470 480 490 500
GVIGANDRTV VVSTAHGLKF TQSKIDYHSK NIKEMACRLA NPPVKVKAKF
510
GSVMDVLKEY LKSNDK
Length:516
Mass (Da):56,925
Last modified:May 1, 2000 - 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:i6BB95F6CD125B1C9
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AC008017 Genomic DNA Translation: AAD55628.1
CP002684 Genomic DNA Translation: AEE35375.1
AY099629 mRNA Translation: AAM20480.1
BT002151 mRNA Translation: AAN72162.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A96753

NCBI Reference Sequences

More...
RefSeqi
NP_565047.1, NM_105939.4

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
At.11666

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT1G72810.1; AT1G72810.1; AT1G72810

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
843612

Gramene; a comparative resource for plants

More...
Gramenei
AT1G72810.1; AT1G72810.1; AT1G72810

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT1G72810

<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
AC008017 Genomic DNA Translation: AAD55628.1
CP002684 Genomic DNA Translation: AEE35375.1
AY099629 mRNA Translation: AAM20480.1
BT002151 mRNA Translation: AAN72162.1
PIRiA96753
RefSeqiNP_565047.1, NM_105939.4
UniGeneiAt.11666

3D structure databases

ProteinModelPortaliQ9SSP5
SMRiQ9SSP5
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G72810.1

Proteomic databases

PaxDbiQ9SSP5
PRIDEiQ9SSP5

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G72810.1; AT1G72810.1; AT1G72810
GeneIDi843612
GrameneiAT1G72810.1; AT1G72810.1; AT1G72810
KEGGiath:AT1G72810

Organism-specific databases

AraportiAT1G72810
TAIRilocus:2032632 AT1G72810

Phylogenomic databases

eggNOGiENOG410IITN Eukaryota
COG0498 LUCA
HOGENOMiHOG000076502
InParanoidiQ9SSP5
KOiK01733
OMAiGTHLRAI
OrthoDBiEOG0936061W
PhylomeDBiQ9SSP5

Enzyme and pathway databases

UniPathwayi
UPA00050;UER00065

BioCyciARA:AT1G72810-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q9SSP5

Gene expression databases

ExpressionAtlasiQ9SSP5 baseline and differential
GenevisibleiQ9SSP5 AT

Family and domain databases

InterProiView protein in InterPro
IPR001926 PLP-dep
IPR000634 Ser/Thr_deHydtase_PyrdxlP-BS
IPR004450 Thr_synthase-like
IPR036052 Trypto_synt_PLP_dependent
PfamiView protein in Pfam
PF00291 PALP, 1 hit
SUPFAMiSSF53686 SSF53686, 1 hit
TIGRFAMsiTIGR00260 thrC, 1 hit
PROSITEiView protein in PROSITE
PS00165 DEHYDRATASE_SER_THR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiTHRC2_ARATH
<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: Q9SSP5
<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: July 7, 2009
Last sequence update: May 1, 2000
Last modified: December 5, 2018
This is version 111 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 programPlant 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
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