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Reviewed, UniProtKB/Swiss-Prot Q00796 (DHSO_HUMAN)

Last modified November 25, 2008. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Sorbitol dehydrogenase
    EC=1.1.1.14
Alternative name(s):
    L-iditol 2-dehydrogenase
Gene names
Name: SORD
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length357 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 357356Sorbitol dehydrogenase
PRO_0000160817

Sites

Metal binding451Zinc; catalytic
Metal binding701Zinc; catalytic
Metal binding711Zinc; catalytic

Amino acid modifications

Modified residue21N-acetylalanine

Natural variations

Natural variant2391L → Q
VAR_000430

Experimental info

Sequence conflict51Missing AA sequence Ref.5
Sequence conflict591N → D AA sequence Ref.5
Sequence conflict1861M → E AA sequence Ref.5
Sequence conflict2811T → S AA sequence Ref.5
Sequence conflict2891I → T AA sequence Ref.5

Secondary structure

............................................................ 357
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00796-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 99A9C6744CFFC4C6

FASTA35738,297
        10         20         30         40         50         60 
MAAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH YWEYGRIGNF 

        70         80         90        100        110        120 
IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR ENDEFCKMGR YNLSPSIFFC 

       130        140        150        160        170        180 
ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE EGALIEPLSV GIHACRRGGV TLGHKVLVCG 

       190        200        210        220        230        240 
AGPIGMVTLL VAKAMGAAQV VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGLL 

       250        260        270        280        290        300 
GCKPEVTIEC TGAEASIQAG IYATRSGGTL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY 

       310        320        330        340        350 
CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC DPSDQNP 

« Hide

References

« Hide 'large scale' references
[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: 8088829] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 7782086] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[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: 9183016] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-239.
Tissue: Brain and Lymph.
[5]"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: 2691249] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-357.
Tissue: Liver.
[6]"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: 12665801] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
Tissue: Platelet.
[7]"X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase."
Pauly T.A., Ekstrom J.L., Beebe D.A., Chrunyk B., Cunningham D., Griffor M., Kamath A., Lee S.E., Madura R., Mcguire D., Subashi T., Wasilko D., Watts P., Mylari B.L., Oates P.J., Adams P.D., Rath V.L.
Structure 11:1071-1085(2003) [PubMed: 12962626] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

U07361 mRNA. Translation: AAA66064.1.
L29008 mRNA. Translation: AAA80565.1.
L29254 expand/collapse EMBL AC list , L29249, L29250, L29251, L29252, L29253 Genomic DNA. Translation: AAA80566.1.
U67243 expand/collapse EMBL AC list , U67236, U67237, U67238, U67239, U67240, U67241, U67242 Genomic DNA. Translation: AAB61898.1.
BC021085 mRNA. Translation: AAH21085.1.
BC025295 mRNA. Translation: AAH25295.1.
PIRA54674.
RefSeqNP_003095.2.
UniGeneHs.878

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1PL6X-ray2.00A/B/C/D1-357[»]
1PL7X-ray2.20A/B/C/D1-357[»]
1PL8X-ray1.90A/B/C/D1-357[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ00796.

PTM databases

PhosphoSiteQ00796.

2-D gel databases

REPRODUCTION-2DPAGEIPI00216057.

Genome annotation databases

EnsemblENSG00000140263. Homo sapiens. [Contig view]
GeneID6652.
KEGGhsa:6652.

Organism-specific databases

H-InvDBHIX0012204.
HGNCHGNC:11184. SORD.
MIM182500. gene.
PharmGKBPA36021.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ00796.
HOVERGENQ00796.

Gene expression databases

ArrayExpressQ00796.
CleanExHS_SORD.
GermOnlineENSG00000140263. Homo sapiens.

Family and domain databases

InterProIPR013154. AlcDHase_GroES-like.
IPR002085. AlcDHase_SF_Zn.
IPR013149. AlcDHase_Zn-bd.
IPR002328. AlcDHase_Zn_CS.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00157. NADH.
LinkHubQ00796.
NextBio25929.
SOURCESearch...

Entry information

Entry nameDHSO_HUMAN
AccessionPrimary (citable) accession number: Q00796
Secondary accession number(s): Q16682, Q9UMD6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: November 25, 2008
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents