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Entry version 208 (16 Oct 2019)
Sequence version 4 (23 Mar 2010)
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Protein

Sorbitol dehydrogenase

Gene

SORD

Organism
Homo sapiens (Human)
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

Polyol dehydrogenase that catalyzes the reversible NAD+-dependent oxidation of various sugar alcohols. Is mostly active with D-sorbitol (D-glucitol), L-threitol, xylitol and ribitol as substrates, leading to the C2-oxidized products D-fructose, L-erythrulose, D-xylulose, and D-ribulose, respectively (PubMed:3365415). Is a key enzyme in the polyol pathway that interconverts glucose and fructose via sorbitol, which constitutes an important alternate route for glucose metabolism. The polyol pathway is believed to be involved in the etiology of diabetic complications, such as diabetic neuropathy and retinopathy, induced by hyperglycemia (PubMed:12962626, PubMed:29966615, PubMed:25105142). May play a role in sperm motility by using sorbitol as an alternative energy source for sperm motility (PubMed:16278369). May have a more general function in the metabolism of secondary alcohols since it also catalyzes the stereospecific oxidation of (2R,3R)-2,3-butanediol. To a lesser extent, can also oxidize L-arabinitol, galactitol and D-mannitol and glycerol in vitro. Oxidizes neither ethanol nor other primary alcohols. Cannot use NADP+ as the electron acceptor (PubMed:3365415).2 Publications1 Publication2 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 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

Zn2+2 PublicationsNote: Binds 1 zinc ion per subunit.2 Publications

<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 CP-166,572, an inhibitor that is competitive with fructose (PubMed:12962626). Also competitively inhibited by phenanthroline and 4-methylpyrazole in vitro (PubMed:3365415).2 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 1.7 sec(-1) for the oxidation of D-sorbitol at pH 7.1, and 5.2 sec(-1) at pH 10.0. kcat is 5.9 sec(-1) the oxidation of xylitol as substrate at pH 10.0. kcat is 5.3 sec(-1) the oxidation of L-threitol as substrate at pH 10.0. kcat is 4.2 sec(-1) the oxidation of (2R,3R)-2,3-butanediol as substrate at pH 10.0. kcat is 45 sec(-1) for the reduction of D-fructose at pH 7.1.1 Publication
  1. KM=1.5 mM for sorbitol1 Publication
  2. KM=225 µM for NAD+1 Publication
  3. KM=210 µM for NADH1 Publication
  4. KM=0.62 mM for D-sorbitol (at pH 7.1)1 Publication
  5. KM=0.67 mM for D-sorbitol (at pH 10.0)1 Publication
  6. KM=0.22 mM for xylitol (at pH 10.0)1 Publication
  7. KM=2.7 mM for L-threitol (at pH 10.0)1 Publication
  8. KM=9.5 mM for (2R,3R)-2,3-butanediol (at pH 10.0)1 Publication
  9. KM=0.14 M for D-fructose (at pH 7.1)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi45Zinc; catalyticCombined sources1 Publication1
    <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 sitei51SubstrateBy similarity1
    Metal bindingi70Zinc; catalyticCombined sources1 Publication1
    Metal bindingi71Zinc; catalyticCombined sources1 Publication1
    Binding sitei156SubstrateBy similarity1
    Binding sitei184NAD; via amide nitrogenCombined sources1 Publication1
    Binding sitei204NADCombined sources1 Publication1
    Binding sitei209NADCombined sources1 Publication1
    Binding sitei299SubstrateBy similarity1
    Binding sitei300SubstrateBy 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 bindingi273 – 275NADCombined sources1 Publication3
    Nucleotide bindingi297 – 299NADCombined sources1 Publication3

    <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
    LigandMetal-binding, NAD, Zinc

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.1.1.14 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-5652227 Fructose biosynthesis
    R-HSA-5661270 Formation of xylulose-5-phosphate

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q00796

    <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:
    Sorbitol dehydrogenase3 Publications (EC:1.1.1.-2 Publications)
    Short name:
    SDH1 Publication
    Alternative name(s):
    (R,R)-butanediol dehydrogenase1 Publication (EC:1.1.1.41 Publication)
    L-iditol 2-dehydrogenase (EC:1.1.1.14By similarity)
    Polyol dehydrogenase1 Publication
    Ribitol dehydrogenase1 Publication (EC:1.1.1.561 Publication)
    Short name:
    RDH
    Xylitol dehydrogenase1 Publication (EC:1.1.1.91 Publication)
    Short name:
    XDH
    <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:SORD
    <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>OrganismiHomo sapiens (Human)
    <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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <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
    • UP000005640 <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 15

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:11184 SORD

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    182500 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q00796

    <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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell projection, Cilium, Flagellum, Membrane, Mitochondrion

    <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

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    6652

    Open Targets

    More...
    OpenTargetsi
    ENSG00000140263

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA36021

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    Q00796

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2275

    Drug and drug target database

    More...
    DrugBanki
    DB04478 Cp-166572, 2-Hydroxymethyl-4-(4-N,N-Dimethylaminosulfonyl-1-Piperazino)-Pyrimidine
    DB00157 NADH

    DrugCentral

    More...
    DrugCentrali
    Q00796

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    SORD

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    292495088

    <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 sources2 Publications
    <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_00001608172 – 357Sorbitol dehydrogenaseAdd BLAST356

    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-acetylalanineCombined sources1
    Modified residuei211PhosphoserineCombined sources1
    Modified residuei225PhosphoserineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q00796

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q00796

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    Q00796

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q00796

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

    More...
    PaxDbi
    Q00796

    PeptideAtlas

    More...
    PeptideAtlasi
    Q00796

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q00796

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    57873 [Q00796-1]
    6501

    2D gel databases

    REPRODUCTION-2DPAGE

    More...
    REPRODUCTION-2DPAGEi
    IPI00216057

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q00796

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    Q00796

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    Q00796

    <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 liver (PubMed:3365415). Expressed in kidney and epithelial cells of both benign and malignant prostate tissue. Expressed in epididymis (at protein level).4 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 androgens and down-regulated by castration.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000140263 Expressed in 137 organ(s), highest expression level in left lobe of thyroid gland

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q00796 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q00796 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA040260
    HPA040621

    <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

    Homotetramer.

    2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-750068,EBI-750068

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    112535, 61 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    Q00796, 9 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q00796

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000267814

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    Q00796

    <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

    1357
    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
    Q00796

    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
    Q00796

    <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
    KOG0024 Eukaryota
    COG1063 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00550000074781

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000294670

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q00796

    KEGG Orthology (KO)

    More...
    KOi
    K00008

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    ETWYAMS

    Database of Orthologous Groups

    More...
    OrthoDBi
    1019156at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q00796

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF313060

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR013149 ADH_C
    IPR013154 ADH_N
    IPR002328 ADH_Zn_CS
    IPR011032 GroES-like_sf
    IPR036291 NAD(P)-bd_dom_sf
    IPR020843 PKS_ER

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF08240 ADH_N, 1 hit
    PF00107 ADH_zinc_N, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00829 PKS_ER, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF50129 SSF50129, 1 hit
    SSF51735 SSF51735, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00059 ADH_ZINC, 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

    This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q00796-1) [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
    MAAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH
    60 70 80 90 100
    YWEYGRIGNF IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR
    110 120 130 140 150
    ENDEFCKMGR YNLSPSIFFC ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE
    160 170 180 190 200
    EGALIEPLSV GIHACRRGGV TLGHKVLVCG AGPIGMVTLL VAKAMGAAQV
    210 220 230 240 250
    VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGQL GCKPEVTIEC
    260 270 280 290 300
    TGAEASIQAG IYATRSGGNL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY
    310 320 330 340 350
    CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC

    DPSDQNP
    Length:357
    Mass (Da):38,325
    Last modified:March 23, 2010 - v4
    <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:iFF13DDD5EBE47754
    GO
    Isoform 2 (identifier: Q00796-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         90-99: DRVAIEPGAP → FLTMSPLRKA
         100-356: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:100
    Mass (Da):10,812
    Checksum:iC02F3F45EE9F6D11
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    H0YLA4H0YLA4_HUMAN
    Sorbitol dehydrogenase
    SORD
    336Annotation score:

    Annotation score:1 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>
    H0YKB3H0YKB3_HUMAN
    Sorbitol dehydrogenase
    SORD
    117Annotation score:

    Annotation score:1 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 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 conflicti5Missing AA sequence (PubMed:2691249).Curated1
    Sequence conflicti59N → D AA sequence (PubMed:2691249).Curated1
    Sequence conflicti186M → E AA sequence (PubMed:2691249).Curated1
    Sequence conflicti281T → S AA sequence (PubMed:2691249).Curated1
    Sequence conflicti289I → T AA sequence (PubMed:2691249).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_000430239Q → L1 PublicationCorresponds to variant dbSNP:rs1042079Ensembl.1
    Natural variantiVAR_060351269N → T5 PublicationsCorresponds to variant dbSNP:rs930337Ensembl.1

    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_05635390 – 99DRVAIEPGAP → FLTMSPLRKA in isoform 2. 1 Publication10
    Alternative sequenceiVSP_056354100 – 356Missing in isoform 2. 1 PublicationAdd BLAST257

    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
    U07361 mRNA Translation: AAA66064.1
    L29008 mRNA Translation: AAA80565.1
    L29254
    , L29249, L29250, L29251, L29252, L29253 Genomic DNA Translation: AAA80566.1
    U67243
    , U67236, U67237, U67238, U67239, U67240, U67241, U67242 Genomic DNA Translation: AAB61898.1
    AK295656 mRNA Translation: BAH12142.1
    AK312444 mRNA Translation: BAG35352.1
    AC090888 Genomic DNA No translation available.
    AC091117 Genomic DNA No translation available.
    BC021085 mRNA Translation: AAH21085.1
    BC025295 mRNA Translation: AAH25295.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS10116.1 [Q00796-1]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A54674

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_003095.2, NM_003104.5 [Q00796-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000267814; ENSP00000267814; ENSG00000140263 [Q00796-1]
    ENST00000558789; ENSP00000453904; ENSG00000140263 [Q00796-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    6652

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:6652

    UCSC genome browser

    More...
    UCSCi
    uc001zul.5 human [Q00796-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    <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
    U07361 mRNA Translation: AAA66064.1
    L29008 mRNA Translation: AAA80565.1
    L29254
    , L29249, L29250, L29251, L29252, L29253 Genomic DNA Translation: AAA80566.1
    U67243
    , U67236, U67237, U67238, U67239, U67240, U67241, U67242 Genomic DNA Translation: AAB61898.1
    AK295656 mRNA Translation: BAH12142.1
    AK312444 mRNA Translation: BAG35352.1
    AC090888 Genomic DNA No translation available.
    AC091117 Genomic DNA No translation available.
    BC021085 mRNA Translation: AAH21085.1
    BC025295 mRNA Translation: AAH25295.1
    CCDSiCCDS10116.1 [Q00796-1]
    PIRiA54674
    RefSeqiNP_003095.2, NM_003104.5 [Q00796-1]

    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
    1PL6X-ray2.00A/B/C/D2-357[»]
    1PL7X-ray2.20A/B/C/D2-357[»]
    1PL8X-ray1.90A/B/C/D2-357[»]
    SMRiQ00796
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi112535, 61 interactors
    IntActiQ00796, 9 interactors
    MINTiQ00796
    STRINGi9606.ENSP00000267814

    Chemistry databases

    BindingDBiQ00796
    ChEMBLiCHEMBL2275
    DrugBankiDB04478 Cp-166572, 2-Hydroxymethyl-4-(4-N,N-Dimethylaminosulfonyl-1-Piperazino)-Pyrimidine
    DB00157 NADH
    DrugCentraliQ00796

    PTM databases

    iPTMnetiQ00796
    PhosphoSitePlusiQ00796
    SwissPalmiQ00796

    Polymorphism and mutation databases

    BioMutaiSORD
    DMDMi292495088

    2D gel databases

    REPRODUCTION-2DPAGEiIPI00216057

    Proteomic databases

    EPDiQ00796
    jPOSTiQ00796
    MassIVEiQ00796
    MaxQBiQ00796
    PaxDbiQ00796
    PeptideAtlasiQ00796
    PRIDEiQ00796
    ProteomicsDBi57873 [Q00796-1]
    6501

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    6652

    Genome annotation databases

    EnsembliENST00000267814; ENSP00000267814; ENSG00000140263 [Q00796-1]
    ENST00000558789; ENSP00000453904; ENSG00000140263 [Q00796-2]
    GeneIDi6652
    KEGGihsa:6652
    UCSCiuc001zul.5 human [Q00796-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    6652
    DisGeNETi6652

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    SORD
    HGNCiHGNC:11184 SORD
    HPAiHPA040260
    HPA040621
    MIMi182500 gene
    neXtProtiNX_Q00796
    OpenTargetsiENSG00000140263
    PharmGKBiPA36021

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0024 Eukaryota
    COG1063 LUCA
    GeneTreeiENSGT00550000074781
    HOGENOMiHOG000294670
    InParanoidiQ00796
    KOiK00008
    OMAiETWYAMS
    OrthoDBi1019156at2759
    PhylomeDBiQ00796
    TreeFamiTF313060

    Enzyme and pathway databases

    BRENDAi1.1.1.14 2681
    ReactomeiR-HSA-5652227 Fructose biosynthesis
    R-HSA-5661270 Formation of xylulose-5-phosphate
    SABIO-RKiQ00796

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    SORD human
    EvolutionaryTraceiQ00796

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    SORD

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    6652
    PharosiQ00796

    Protein Ontology

    More...
    PROi
    PR:Q00796

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000140263 Expressed in 137 organ(s), highest expression level in left lobe of thyroid gland
    ExpressionAtlasiQ00796 baseline and differential
    GenevisibleiQ00796 HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR013149 ADH_C
    IPR013154 ADH_N
    IPR002328 ADH_Zn_CS
    IPR011032 GroES-like_sf
    IPR036291 NAD(P)-bd_dom_sf
    IPR020843 PKS_ER
    PfamiView protein in Pfam
    PF08240 ADH_N, 1 hit
    PF00107 ADH_zinc_N, 1 hit
    SMARTiView protein in SMART
    SM00829 PKS_ER, 1 hit
    SUPFAMiSSF50129 SSF50129, 1 hit
    SSF51735 SSF51735, 1 hit
    PROSITEiView protein in PROSITE
    PS00059 ADH_ZINC, 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 nameiDHSO_HUMAN
    <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: Q00796
    Secondary accession number(s): B2R655
    , B7Z3A6, J3JZZ5, Q16682, Q9UMD6
    <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: April 1, 1993
    Last sequence update: March 23, 2010
    Last modified: October 16, 2019
    This is version 208 of the entry and version 4 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 programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <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, Direct protein sequencing, 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. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    6. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
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