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Q00796

- DHSO_HUMAN

UniProt

Q00796 - DHSO_HUMAN

Protein

Sorbitol dehydrogenase

Gene

SORD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 4 (23 Mar 2010)
      Previous versions | rss
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    Functioni

    Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm By similarity.By similarity

    Catalytic activityi

    L-iditol + NAD+ = L-sorbose + NADH.

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi45 – 451Zinc; catalytic
    Binding sitei51 – 511SubstrateBy similarity
    Metal bindingi70 – 701Zinc; catalytic
    Metal bindingi71 – 711Zinc; catalytic
    Binding sitei156 – 1561SubstrateBy similarity
    Binding sitei299 – 2991SubstrateBy similarity
    Binding sitei300 – 3001SubstrateBy similarity

    GO - Molecular functioni

    1. carbohydrate binding Source: UniProtKB
    2. L-iditol 2-dehydrogenase activity Source: UniProtKB
    3. NAD binding Source: UniProtKB
    4. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. fructose biosynthetic process Source: UniProtKB
    2. glucose metabolic process Source: UniProtKB
    3. L-xylitol catabolic process Source: UniProtKB
    4. L-xylitol metabolic process Source: UniProtKB
    5. sorbitol catabolic process Source: UniProtKB
    6. sperm motility Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    SABIO-RKQ00796.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sorbitol dehydrogenase (EC:1.1.1.14)
    Alternative name(s):
    L-iditol 2-dehydrogenase
    Gene namesi
    Name:SORD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:11184. SORD.

    Subcellular locationi

    Mitochondrion membrane; Peripheral membrane protein. Cell projectionciliumflagellum
    Note: Associated with mitochondria of the midpiece and near the plasma membrane in the principal piece of the flagellum. Also found in the epididymosome, secreted by the epididymal epithelium and that transfers proteins from the epididymal fluid to the sperm surface By similarity.By similarity

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProtKB
    3. membrane Source: UniProtKB
    4. mitochondrial membrane Source: UniProtKB-SubCell
    5. motile cilium Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cilium, Flagellum, Membrane, Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36021.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 357356Sorbitol dehydrogenasePRO_0000160817Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ00796.
    PaxDbiQ00796.
    PRIDEiQ00796.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00216057.

    PTM databases

    PhosphoSiteiQ00796.

    Expressioni

    Tissue specificityi

    Expressed in kidney and epithelial cells of both benign and malignant prostate tissue. Expressed in epididymis (at protein level).3 Publications

    Inductioni

    Up-regulated by androgens and down-regulated by castration.1 Publication

    Gene expression databases

    ArrayExpressiQ00796.
    BgeeiQ00796.
    CleanExiHS_SORD.
    GenevestigatoriQ00796.

    Organism-specific databases

    HPAiHPA040260.
    HPA040621.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi112535. 33 interactions.
    IntActiQ00796. 1 interaction.
    MINTiMINT-5004436.
    STRINGi9606.ENSP00000267814.

    Structurei

    Secondary structure

    1
    357
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 167
    Beta strandi19 – 246
    Beta strandi34 – 4411
    Helixi46 – 549
    Beta strandi55 – 573
    Beta strandi71 – 799
    Beta strandi91 – 944
    Beta strandi96 – 983
    Helixi104 – 1074
    Helixi111 – 1133
    Beta strandi130 – 1367
    Helixi137 – 1393
    Beta strandi140 – 1423
    Helixi149 – 16820
    Beta strandi175 – 1795
    Helixi183 – 19412
    Beta strandi198 – 2058
    Helixi207 – 2159
    Beta strandi219 – 2235
    Helixi229 – 24012
    Beta strandi245 – 2495
    Helixi254 – 26310
    Beta strandi269 – 2724
    Helixi284 – 2896
    Beta strandi293 – 2964
    Helixi304 – 3129
    Helixi319 – 3213
    Beta strandi322 – 3276
    Helixi328 – 3303
    Helixi331 – 3399
    Beta strandi344 – 3496

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PL6X-ray2.00A/B/C/D2-357[»]
    1PL7X-ray2.20A/B/C/D2-357[»]
    1PL8X-ray1.90A/B/C/D2-357[»]
    ProteinModelPortaliQ00796.
    SMRiQ00796. Positions 2-357.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00796.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1063.
    HOGENOMiHOG000294670.
    HOVERGENiHBG005484.
    InParanoidiQ00796.
    KOiK00008.
    OMAiGPMIVEG.
    OrthoDBiEOG7DRJ36.
    PhylomeDBiQ00796.
    TreeFamiTF313060.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_GroES-like.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q00796-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' 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

    MAAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH    50
    YWEYGRIGNF IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR 100
    ENDEFCKMGR YNLSPSIFFC ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE 150
    EGALIEPLSV GIHACRRGGV TLGHKVLVCG AGPIGMVTLL VAKAMGAAQV 200
    VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGQL GCKPEVTIEC 250
    TGAEASIQAG IYATRSGGNL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY 300
    CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC 350
    DPSDQNP 357
    Length:357
    Mass (Da):38,325
    Last modified:March 23, 2010 - v4
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51Missing AA sequence (PubMed:2691249)Curated
    Sequence conflicti59 – 591N → D AA sequence (PubMed:2691249)Curated
    Sequence conflicti186 – 1861M → E AA sequence (PubMed:2691249)Curated
    Sequence conflicti281 – 2811T → S AA sequence (PubMed:2691249)Curated
    Sequence conflicti289 – 2891I → T AA sequence (PubMed:2691249)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti239 – 2391Q → L.1 Publication
    Corresponds to variant rs55739437 [ dbSNP | Ensembl ].
    VAR_000430
    Natural varianti269 – 2691N → T.5 Publications
    Corresponds to variant rs2229659 [ dbSNP | Ensembl ].
    VAR_060351

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei90 – 9910DRVAIEPGAP → FLTMSPLRKA in isoform 2. 1 PublicationVSP_056353
    Alternative sequencei100 – 356257Missing in isoform 2. 1 PublicationVSP_056354Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    PIRiA54674.
    RefSeqiNP_003095.2. NM_003104.5.
    UniGeneiHs.878.

    Genome annotation databases

    EnsembliENST00000267814; ENSP00000267814; ENSG00000140263.
    ENST00000558789; ENSP00000453904; ENSG00000140263.
    GeneIDi6652.
    KEGGihsa:6652.
    UCSCiuc001zul.4. human.

    Polymorphism databases

    DMDMi292495088.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS10116.1.
    PIRi A54674.
    RefSeqi NP_003095.2. NM_003104.5.
    UniGenei Hs.878.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PL6 X-ray 2.00 A/B/C/D 2-357 [» ]
    1PL7 X-ray 2.20 A/B/C/D 2-357 [» ]
    1PL8 X-ray 1.90 A/B/C/D 2-357 [» ]
    ProteinModelPortali Q00796.
    SMRi Q00796. Positions 2-357.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112535. 33 interactions.
    IntActi Q00796. 1 interaction.
    MINTi MINT-5004436.
    STRINGi 9606.ENSP00000267814.

    Chemistry

    ChEMBLi CHEMBL2275.

    PTM databases

    PhosphoSitei Q00796.

    Polymorphism databases

    DMDMi 292495088.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00216057.

    Proteomic databases

    MaxQBi Q00796.
    PaxDbi Q00796.
    PRIDEi Q00796.

    Protocols and materials databases

    DNASUi 6652.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267814 ; ENSP00000267814 ; ENSG00000140263 .
    ENST00000558789 ; ENSP00000453904 ; ENSG00000140263 .
    GeneIDi 6652.
    KEGGi hsa:6652.
    UCSCi uc001zul.4. human.

    Organism-specific databases

    CTDi 6652.
    GeneCardsi GC15P045315.
    HGNCi HGNC:11184. SORD.
    HPAi HPA040260.
    HPA040621.
    MIMi 182500. gene.
    neXtProti NX_Q00796.
    PharmGKBi PA36021.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1063.
    HOGENOMi HOG000294670.
    HOVERGENi HBG005484.
    InParanoidi Q00796.
    KOi K00008.
    OMAi GPMIVEG.
    OrthoDBi EOG7DRJ36.
    PhylomeDBi Q00796.
    TreeFami TF313060.

    Enzyme and pathway databases

    SABIO-RK Q00796.

    Miscellaneous databases

    EvolutionaryTracei Q00796.
    GeneWikii SORD.
    GenomeRNAii 6652.
    NextBioi 25929.
    PROi Q00796.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00796.
    Bgeei Q00796.
    CleanExi HS_SORD.
    Genevestigatori Q00796.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProi IPR013149. ADH_C.
    IPR013154. ADH_GroES-like.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11695. PTHR11695. 1 hit.
    Pfami PF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50129. SSF50129. 1 hit.
    PROSITEi PS00059. ADH_ZINC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human sorbitol dehydrogenase gene: cDNA cloning, sequence determination, and mapping by fluorescence in situ hybridization."
      Lee F.K., Cheung M.C., Chung S.
      Genomics 21:354-358(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-269.
      Tissue: Liver.
    2. "Structural organization of the human sorbitol dehydrogenase gene (SORD)."
      Iwata T., Popescu N.C., Zimonjic D.B., Karlsson C., Hoeoeg J.-O., Vaca G., Rodriguez I.R., Carper D.
      Genomics 26:55-62(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS LEU-239 AND THR-269.
    3. "Identification and characterisation of a sequence related to human sorbitol dehydrogenase."
      Carr I.M., Markham A.F., Coletta P.L.
      Eur. J. Biochem. 245:760-767(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-269.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT THR-269.
      Tissue: Brain and Hippocampus.
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-269.
      Tissue: Brain and Lymph.
    7. "Variability within mammalian sorbitol dehydrogenases. The primary structure of the human liver enzyme."
      Karlsson C., Maret W., Auld D.S., Hoeoeg J.-O., Joernvall H.
      Eur. J. Biochem. 186:543-550(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-357.
      Tissue: Liver.
    8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21.
      Tissue: Platelet.
    9. "Polyol pathway in human epididymis and semen."
      Frenette G., Thabet M., Sullivan R.
      J. Androl. 27:233-239(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "Sorbitol dehydrogenase expression is regulated by androgens in the human prostate."
      Szabo Z., Hamalainen J., Loikkanen I., Moilanen A.M., Hirvikoski P., Vaisanen T., Paavonen T.K., Vaarala M.H.
      Oncol. Rep. 23:1233-1239(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    12. "ZAC1 is up-regulated by hypertonicity and decreases sorbitol dehydrogenase expression, allowing accumulation of sorbitol in kidney cells."
      Lanaspa M.A., Andres-Hernando A., Rivard C.J., Dai Y., Li N., Berl T.
      J. Biol. Chem. 284:19974-19981(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiDHSO_HUMAN
    AccessioniPrimary (citable) accession number: Q00796
    Secondary accession number(s): B2R655
    , B7Z3A6, J3JZZ5, Q16682, Q9UMD6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: March 23, 2010
    Last modified: October 1, 2014
    This is version 161 of the entry and version 4 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Miscellaneous

    The polyol pathway is proposed to be involved the cellular toxicity of diabetic hyperglycemia.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3