Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 116 (26 Feb 2020)
Sequence version 1 (01 Oct 2000)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Aspartate-semialdehyde dehydrogenase 1

Gene

asd1

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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 NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 S-methyl-L-cysteine sulfoxide in vitro, via the formation of a covalently bound cysteine at the active site Cys-134.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.19 mM for L-aspartate 4-semialdehyde1 Publication
  2. KM=0.32 mM for NADP+1 Publication
  3. KM=1.1 mM for phosphate1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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 2 of the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate.UniRule annotation
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. Aspartokinase (VC_0547), Bifunctional aspartokinase/homoserine dehydrogenase (VC_2364), Aspartokinase (VC_0391), Bifunctional aspartokinase/homoserine dehydrogenase (VC_2684)
    2. Aspartate-semialdehyde dehydrogenase 2 (asd2), Aspartate-semialdehyde dehydrogenase 1 (asd1)
    3. 4-hydroxy-tetrahydrodipicolinate synthase (dapA)
    4. 4-hydroxy-tetrahydrodipicolinate reductase (dapB)
    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 2 of the subpathway that synthesizes L-homoserine from L-aspartate.UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Aspartokinase (VC_0547), Bifunctional aspartokinase/homoserine dehydrogenase (VC_2364), Aspartokinase (VC_0391), Bifunctional aspartokinase/homoserine dehydrogenase (VC_2684)
    2. Aspartate-semialdehyde dehydrogenase 2 (asd2), Aspartate-semialdehyde dehydrogenase 1 (asd1)
    3. Bifunctional aspartokinase/homoserine dehydrogenase (VC_2684), Bifunctional aspartokinase/homoserine dehydrogenase (VC_2364)
    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 2 of the subpathway that synthesizes L-threonine from L-aspartate.UniRule annotation
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Aspartokinase (VC_0547), Bifunctional aspartokinase/homoserine dehydrogenase (VC_2364), Aspartokinase (VC_0391), Bifunctional aspartokinase/homoserine dehydrogenase (VC_2684)
    2. Aspartate-semialdehyde dehydrogenase 2 (asd2), Aspartate-semialdehyde dehydrogenase 1 (asd1)
    3. Bifunctional aspartokinase/homoserine dehydrogenase (VC_2684), Bifunctional aspartokinase/homoserine dehydrogenase (VC_2364)
    4. Homoserine kinase (thrB)
    5. no protein annotated in this organism
    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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei72NADP1 Publication1
    Binding sitei101PhosphateUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei134Acyl-thioester intermediate1 Publication1
    Binding sitei161Substrate1 Publication1
    Binding sitei192NADP; via carbonyl oxygen1 Publication1
    Binding sitei240Substrate1 Publication1
    Binding sitei243PhosphateUniRule annotation1
    Binding sitei267Substrate1 Publication1
    Active sitei274Proton acceptor1 Publication1
    Binding sitei350NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi9 – 12NADP1 Publication4
    Nucleotide bindingi36 – 37NADP1 Publication2
    Nucleotide bindingi164 – 165NADP1 Publication2

    <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 functionOxidoreductase
    Biological processAmino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis, Methionine biosynthesis, Threonine biosynthesis
    LigandNADP

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-15807
    VCHO:VC2036-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.2.1.11 6626

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q9KQG2

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

    More...
    UniPathwayi
    UPA00034;UER00016
    UPA00050;UER00463
    UPA00051;UER00464

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Aspartate-semialdehyde dehydrogenase 1 (EC:1.2.1.111 Publication)
    Short name:
    ASA dehydrogenase 1
    Short name:
    ASADH 1
    Alternative name(s):
    Aspartate-beta-semialdehyde dehydrogenase 1
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:asd1
    Ordered Locus Names:VC_2036
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri243277 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000584 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 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_00004111261 – 370Aspartate-semialdehyde dehydrogenase 1Add BLAST370

    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 residuei134S-cysteinyl cysteine; in inhibited form1

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    UniRule annotation1 Publication

    GO - Molecular functioni

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    243277.VC_2036

    <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

    1370
    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
    Q9KQG2

    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
    Q9KQG2

    <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 aspartate-semialdehyde dehydrogenase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CM3 Bacteria
    COG0136 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_066397_0_0_6

    KEGG Orthology (KO)

    More...
    KOi
    K00133

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    VGTDPTW

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_02121 ASADH, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000319 Asp-semialdehyde_DH_CS
    IPR011534 Asp_ADH_gamma-type
    IPR012080 Asp_semialdehyde_DH
    IPR036291 NAD(P)-bd_dom_sf
    IPR000534 Semialdehyde_DH_NAD-bd
    IPR012280 Semialdhyde_DH_dimer_dom

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR46278:SF4 PTHR46278:SF4, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01118 Semialdhyde_dh, 1 hit
    PF02774 Semialdhyde_dhC, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00859 Semialdhyde_dh, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735 SSF51735, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01745 asd_gamma, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS01103 ASD, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    Q9KQG2-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MRVGLVGWRG MVGSVLMQRM VEERDFDLIE PVFFSTSQIG VPAPNFGKDA
    60 70 80 90 100
    GMLHDAFDIE SLKQLDAVIT CQGGSYTEKV YPALRQAGWK GYWIDAASTL
    110 120 130 140 150
    RMDKEAIITL DPVNLKQILH GIHHGTKTFV GGNCTVSLML MALGGLYERG
    160 170 180 190 200
    LVEWMSAMTY QAASGAGAQN MRELISQMGV INDAVSSELA NPASSILDID
    210 220 230 240 250
    KKVAETMRSG SFPTDNFGVP LAGSLIPWID VKRDNGQSKE EWKAGVEANK
    260 270 280 290 300
    ILGLQDSPVP IDGTCVRIGA MRCHSQALTI KLKQNIPLDE IEEMIATHND
    310 320 330 340 350
    WVKVIPNERD ITARELTPAK VTGTLSVPVG RLRKMAMGDD FLNAFTVGDQ
    360 370
    LLWGAAEPLR RTLRIILAEK
    Length:370
    Mass (Da):40,498
    Last modified:October 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:i52F936ACCB4FBA84
    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
    AE003852 Genomic DNA Translation: AAF95184.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    F82125

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_231670.1, NC_002505.1
    WP_001263690.1, NZ_LT906614.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAF95184; AAF95184; VC_2036

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    2613415

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    vch:VC2036

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|243277.26.peg.1944

    <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
    AE003852 Genomic DNA Translation: AAF95184.1
    PIRiF82125
    RefSeqiNP_231670.1, NC_002505.1
    WP_001263690.1, NZ_LT906614.1

    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
    1MB4X-ray1.84A/B1-370[»]
    1MC4X-ray2.77A1-370[»]
    3PZRX-ray1.75A/B1-370[»]
    3Q0EX-ray1.80A/B1-370[»]
    4R5MX-ray1.89A/B1-370[»]
    SMRiQ9KQG2
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi243277.VC_2036

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    2613415

    Genome annotation databases

    EnsemblBacteriaiAAF95184; AAF95184; VC_2036
    GeneIDi2613415
    KEGGivch:VC2036
    PATRICifig|243277.26.peg.1944

    Phylogenomic databases

    eggNOGiENOG4105CM3 Bacteria
    COG0136 LUCA
    HOGENOMiCLU_066397_0_0_6
    KOiK00133
    OMAiVGTDPTW

    Enzyme and pathway databases

    UniPathwayiUPA00034;UER00016
    UPA00050;UER00463
    UPA00051;UER00464
    BioCyciMetaCyc:MONOMER-15807
    VCHO:VC2036-MONOMER
    BRENDAi1.2.1.11 6626
    SABIO-RKiQ9KQG2

    Miscellaneous databases

    EvolutionaryTraceiQ9KQG2

    Family and domain databases

    HAMAPiMF_02121 ASADH, 1 hit
    InterProiView protein in InterPro
    IPR000319 Asp-semialdehyde_DH_CS
    IPR011534 Asp_ADH_gamma-type
    IPR012080 Asp_semialdehyde_DH
    IPR036291 NAD(P)-bd_dom_sf
    IPR000534 Semialdehyde_DH_NAD-bd
    IPR012280 Semialdhyde_DH_dimer_dom
    PANTHERiPTHR46278:SF4 PTHR46278:SF4, 1 hit
    PfamiView protein in Pfam
    PF01118 Semialdhyde_dh, 1 hit
    PF02774 Semialdhyde_dhC, 1 hit
    SMARTiView protein in SMART
    SM00859 Semialdhyde_dh, 1 hit
    SUPFAMiSSF51735 SSF51735, 1 hit
    TIGRFAMsiTIGR01745 asd_gamma, 1 hit
    PROSITEiView protein in PROSITE
    PS01103 ASD, 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 nameiDHAS1_VIBCH
    <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: Q9KQG2
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 27, 2011
    Last sequence update: October 1, 2000
    Last modified: February 26, 2020
    This is version 116 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. 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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again