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Entry version 115 (08 May 2019)
Sequence version 1 (01 May 2000)
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Protein

3-oxo-Delta(4,5)-steroid 5-beta-reductase

Gene

VEP1

Organism
Arabidopsis thaliana (Mouse-ear cress)
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

Involved in vascular strand development. Catalyzes the stereospecific conversion of progesterone to 5-beta-pregnane-3,20-dione. Can use progesterone, testosterone, 21-acetyl cortexone, 2-cyclohexenone, but-1-en-3-one, ethyl acrylate, ethylmethacrylate, cortisone and canarigenone as substrates, lower activity with 3-methyl-2-cyclohexenone and 3,5,5-trimethyl-2-cyclohexenone as substrate, and no activity with canarigenin, canarigenin digitoxoside and pregnenolone. May be involved in the formation of 5-beta phytoecdysteroids.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 ‘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 10.11 min(-1) with progesterone as substrate. kcat is 66.85 min(-1) with 2-cyclohexen-1-one as substrate.
  1. KM=268 µM for progesterone2 Publications
  2. KM=755 µM for cortisol2 Publications
  3. KM=1423 µM for 4-androstene-3,17-dione2 Publications
  4. KM=764 µM for cortexone2 Publications
  5. KM=5 µM for NADPH2 Publications
  6. KM=116 µM for 2-cyclohexen-1-one2 Publications

    pH dependencei

    Optimum pH is 8.0.2 Publications

    Temperature dependencei

    Optimum temperature is 45 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 sitei105NADPBy similarity1
    Binding sitei143NADPBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei147By similarity1
    Active sitei178By similarity1
    Binding sitei178NADPBy similarity1
    Binding sitei205NADP; via amide nitrogenBy similarity1

    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 bindingi35 – 37NADPBy similarity3
    Nucleotide bindingi63 – 64NADPBy similarity2
    Nucleotide bindingi81 – 82NADPBy similarity2
    Nucleotide bindingi212 – 214NADPBy similarity3

    <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

    • response to wounding Source: TAIR
    • steroid metabolic process Source: TAIR
    • xylem and phloem pattern formation Source: TAIR

    <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 functionOxidoreductase
    LigandNADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:AT4G24220-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.3.1.3 399

    <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:
    3-oxo-Delta(4,5)-steroid 5-beta-reductase (EC:1.3.1.33 Publications)
    Alternative name(s):
    Delta(4)-3-oxosteroid 5-beta-reductase
    Delta-4,5-steroid 5-beta-reductase
    Short name:
    At5beta-StR
    Progesterone 5-beta-reductase
    Short name:
    5beta-POR
    Protein VEIN PATTERNING 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:VEP1
    Synonyms:AWI31
    Ordered Locus Names:At4g24220
    ORF Names:T22A6.50
    <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 4

    Organism-specific databases

    Arabidopsis Information Portal

    More...
    Araporti
    AT4G24220

    The Arabidopsis Information Resource

    More...
    TAIRi
    locus:2135932 AT4G24220

    <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 & Seán O’Donoghue; Source: COMPARTMENTS

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
    <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_00004199042 – 3883-oxo-Delta(4,5)-steroid 5-beta-reductaseAdd BLAST387

    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 residuei2N-acetylserineCombined sources1

    Keywords - PTMi

    Acetylation

    Proteomic databases

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

    More...
    PaxDbi
    Q9STX2

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9STX2

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9STX2

    <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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Expressed in roots, stems, leaves, flowers, seeds and siliques. Expressed in the vascular bundles.2 Publications

    <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

    Up-regulated by wounding. Not induced by drought, high salt, low temperature or herbicide treatment.2 Publications

    Gene expression databases

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9STX2 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9STX2 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.

    1 Publication

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    13812, 1 interactor

    STRING: functional protein association networks

    More...
    STRINGi
    3702.AT4G24220.1

    <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

    Secondary structure

    1388
    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
    Q9STX2

    Database of comparative protein structure models

    More...
    ModBasei
    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

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410IH3A Eukaryota
    ENOG410XPIJ LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000216741

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9STX2

    KEGG Orthology (KO)

    More...
    KOi
    K22419

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    LGNAMNM

    Database of Orthologous Groups

    More...
    OrthoDBi
    588707at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9STX2

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR036291 NAD(P)-bd_dom_sf

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 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.

    <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.

    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 splicing. AlignAdd to basket
    Isoform 1 (identifier: Q9STX2-1) [UniParc]FASTAAdd to basket

    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
    MSWWWAGAIG AAKKKLDEDE PSQSFESVAL IIGVTGIVGN SLAEILPLSD
    60 70 80 90 100
    TPGGPWKVYG VARRPRPTWN ADHPIDYIQC DVSDAEDTRS KLSPLTDVTH
    110 120 130 140 150
    VFYVTWTNRE SESENCEANG SMLRNVLQAI IPYAPNLRHV CLQTGTKHYL
    160 170 180 190 200
    GPFTNVDGPR HDPPFTEDMP RLQIQNFYYT QEDILFEEIK KIETVTWSIH
    210 220 230 240 250
    RPNMIFGFSP YSLMNIVGTL CVYAAICKHE GSPLLFPGSK KAWEGFMTAS
    260 270 280 290 300
    DADLIAEQQI WAAVDPYAKN EAFNCNNADI FKWKHLWKIL AEQFGIEEYG
    310 320 330 340 350
    FEEGKNLGLV EMMKGKERVW EEMVKENQLQ EKKLEEVGVW WFADVILGVE
    360 370 380
    GMIDSMNKSK EYGFLGFRNS NNSFISWIDK YKAFKIVP
    Length:388
    Mass (Da):44,230
    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:i5ED9D6C12330A161
    GO
    Isoform 2 (identifier: Q9STX2-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         13-13: Missing.

    Note: Derived from EST data. No experimental confirmation available.
    Show »
    Length:387
    Mass (Da):44,102
    Checksum:iCAC31EE997A67A1A
    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 CAA68126 differs from that shown. Reason: Frameshift at positions 225, 273 and 301.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 conflicti2S → R in CAA68126 (PubMed:9085278).Curated1
    Sequence conflicti36G → A in CAA68126 (PubMed:9085278).Curated1
    Sequence conflicti192I → T in CAA68126 (PubMed:9085278).Curated1
    Sequence conflicti359S → R in CAA68126 (PubMed:9085278).Curated1

    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_04436813Missing in isoform 2. 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
    X99793 Genomic DNA Translation: CAA68126.1 Frameshift.
    EF579963 mRNA Translation: ABU55811.1
    AL078637 Genomic DNA Translation: CAB45057.1
    AL161561 Genomic DNA Translation: CAB79332.1
    CP002687 Genomic DNA Translation: AEE84868.1
    CP002687 Genomic DNA Translation: AEE84869.1
    AY062451 mRNA Translation: AAL32529.1
    BT008479 mRNA Translation: AAP37838.1
    AY087323 mRNA Translation: AAM64873.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    T09885

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001078438.1, NM_001084969.1 [Q9STX2-2]
    NP_194153.1, NM_118555.4 [Q9STX2-1]

    Genome annotation databases

    Ensembl plant genome annotation project

    More...
    EnsemblPlantsi
    AT4G24220.1; AT4G24220.1; AT4G24220 [Q9STX2-1]
    AT4G24220.2; AT4G24220.2; AT4G24220 [Q9STX2-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    828523

    Gramene; a comparative resource for plants

    More...
    Gramenei
    AT4G24220.1; AT4G24220.1; AT4G24220 [Q9STX2-1]
    AT4G24220.2; AT4G24220.2; AT4G24220 [Q9STX2-2]

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ath:AT4G24220

    Keywords - Coding sequence diversityi

    Alternative splicing

    <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
    X99793 Genomic DNA Translation: CAA68126.1 Frameshift.
    EF579963 mRNA Translation: ABU55811.1
    AL078637 Genomic DNA Translation: CAB45057.1
    AL161561 Genomic DNA Translation: CAB79332.1
    CP002687 Genomic DNA Translation: AEE84868.1
    CP002687 Genomic DNA Translation: AEE84869.1
    AY062451 mRNA Translation: AAL32529.1
    BT008479 mRNA Translation: AAP37838.1
    AY087323 mRNA Translation: AAM64873.1
    PIRiT09885
    RefSeqiNP_001078438.1, NM_001084969.1 [Q9STX2-2]
    NP_194153.1, NM_118555.4 [Q9STX2-1]

    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
    6EL3X-ray1.90A/B/C/D/E/F17-388[»]
    SMRiQ9STX2
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi13812, 1 interactor
    STRINGi3702.AT4G24220.1

    PTM databases

    iPTMnetiQ9STX2

    Proteomic databases

    PaxDbiQ9STX2
    PRIDEiQ9STX2

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G24220.1; AT4G24220.1; AT4G24220 [Q9STX2-1]
    AT4G24220.2; AT4G24220.2; AT4G24220 [Q9STX2-2]
    GeneIDi828523
    GrameneiAT4G24220.1; AT4G24220.1; AT4G24220 [Q9STX2-1]
    AT4G24220.2; AT4G24220.2; AT4G24220 [Q9STX2-2]
    KEGGiath:AT4G24220

    Organism-specific databases

    AraportiAT4G24220
    TAIRilocus:2135932 AT4G24220

    Phylogenomic databases

    eggNOGiENOG410IH3A Eukaryota
    ENOG410XPIJ LUCA
    HOGENOMiHOG000216741
    InParanoidiQ9STX2
    KOiK22419
    OMAiLGNAMNM
    OrthoDBi588707at2759
    PhylomeDBiQ9STX2

    Enzyme and pathway databases

    BioCyciMetaCyc:AT4G24220-MONOMER
    BRENDAi1.3.1.3 399

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:Q9STX2

    Gene expression databases

    ExpressionAtlasiQ9STX2 baseline and differential
    GenevisibleiQ9STX2 AT

    Family and domain databases

    InterProiView protein in InterPro
    IPR036291 NAD(P)-bd_dom_sf
    SUPFAMiSSF51735 SSF51735, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
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    MobiDB: a database of protein disorder and mobility annotations

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    MobiDBi
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    <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 nameiVEP1_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: Q9STX2
    Secondary accession number(s): A8MRU3, Q39171
    <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: October 31, 2012
    Last sequence update: May 1, 2000
    Last modified: May 8, 2019
    This is version 115 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
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