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Reviewed, UniProtKB/Swiss-Prot O60701 (UGDH_HUMAN)

Last modified November 3, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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

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Names and origin

Protein namesRecommended name:
    UDP-glucose 6-dehydrogenase
      Short name=UDP-Glc dehydrogenase
      Short name=UDP-GlcDH
      Short name=UDPGDH
    EC=1.1.1.22
Gene names
Name: UGDH
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate.

Catalytic activity

UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH.

Pathway

Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.

Subunit structure

Homohexamer By similarity.

Sequence similarities

Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494UDP-glucose 6-dehydrogenase
PRO_0000074060

Regions

Nucleotide binding6 – 2318NAD By similarity
Region162 – 1654Substrate binding By similarity

Sites

Active site2761Nucleophile By similarity
Binding site361NAD By similarity
Binding site411NAD By similarity
Binding site931NAD By similarity
Binding site1311NAD; via amide nitrogen By similarity
Binding site1651NAD By similarity
Binding site2201Substrate By similarity
Binding site2731Substrate; via amide nitrogen By similarity
Binding site2791NAD By similarity
Binding site3391Substrate By similarity
Binding site3461NAD By similarity

Amino acid modifications

Modified residue1071N6-acetyllysine Ref.7
Modified residue1731N6-acetyllysine Ref.7
Modified residue4341N6-acetyllysine Ref.7
Modified residue4731Phosphotyrosine By similarity

Experimental info

Sequence conflict3381F → V in AAC05135. Ref.5
Sequence conflict3771V → A in AAC05135. Ref.5

Secondary structure

1 ..................................................................................... 494
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O60701-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 9C9DA5E1227D65CC

FASTA49455,024
        10         20         30         40         50         60 
MFEIKKICCI GAGYVGGPTC SVIAHMCPEI RVTVVDVNES RINAWNSPTL PIYEPGLKEV 

        70         80         90        100        110        120 
VESCRGKNLF FSTNIDDAIK EADLVFISVN TPTKTYGMGK GRAADLKYIE ACARRIVQNS 

       130        140        150        160        170        180 
NGYKIVTEKS TVPVRAAESI RRIFDANTKP NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI 

       190        200        210        220        230        240 
GGDETPEGQR AVQALCAVYE HWVPREKILT TNTWSSELSK LAANAFLAQR ISSINSISAL 

       250        260        270        280        290        300 
CEATGADVEE VATAIGMDQR IGNKFLKASV GFGGSCFQKD VLNLVYLCEA LNLPEVARYW 

       310        320        330        340        350        360 
QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS IYISKYLMDE 

       370        380        390        400        410        420 
GAHLHIYDPK VPREQIVVDL SHPGVSEDDQ VSRLVTISKD PYEACDGAHA VVICTEWDMF 

       430        440        450        460        470        480 
KELDYERIHK KMLKPAFIFD GRRVLDGLHN ELQTIGFQIE TIGKKVSSKR IPYAPSGEIP 

       490 
KFSLQDPPNK KPKV

« Hide

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References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the human and mouse UDP-glucose dehydrogenase genes."
Spicer A.P., Kaback L.A., Smith T.J., Seldin M.F.
J. Biol. Chem. 273:25117-25124(1998) [PubMed: 9737970] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"cDNA cloning and expression analysis of the human UDPglucose dehydrogenase."
Peng H.L., Lou M.D., Chang M.L., Chang H.Y.
Proc. Natl. Sci. Counc. Repub. China, B, Life Sci. 22:166-172(1998) [PubMed: 9850599] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Characterization of human gene encoding UDP-glucose dehydrogenase."
Chang M.L., Chang H.Y., Peng H.L.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
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].
Tissue: Skin.
[5]Raghuram V., Foskett J.K.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 214-388.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-107; LYS-173 AND LYS-434, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF061016 mRNA. Translation: AAC36095.1.
AJ007702 mRNA. Translation: CAA07609.1.
AJ272274 expand/collapse EMBL AC list , AJ272275, AJ272276, AJ272277, AJ272278, AJ272279, AJ272280, AJ272281 Genomic DNA. Translation: CAB75891.1.
BC022781 mRNA. Translation: AAH22781.1.
AF049126 mRNA. Translation: AAC05135.1.
IPIIPI00031420.
PIRJE0353.
RefSeqNP_003350.1.
UniGeneHs.572518

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2Q3EX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L1-466[»]
2QG4X-ray2.10A/B/C/D/E/F/G/H1-466[»]
3ITKX-ray2.40A/B/C/D/E/F1-466[»]
ModBaseSearch...

Protein-protein interaction databases

IntActO60701. 3 interactions.
STRINGO60701.

PTM databases

PhosphoSiteO60701.

2-D gel databases

REPRODUCTION-2DPAGEO60701.

Proteomic databases

PeptideAtlasO60701.
PRIDEO60701.

Genome annotation databases

EnsemblENST00000316423; ENSP00000319501; ENSG00000109814; Homo sapiens. [Genome view]
GeneID7358.
KEGGhsa:7358.
NMPDRfig|9606.3.peg.24043.
UCSCuc003guk.1. human.

Organism-specific databases

CTD7358.
GeneCardsGC04M039176.
H-InvDBHIX0004163.
HGNCHGNC:12525. UGDH.
MIM603370. gene.
PharmGKBPA37170.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO60701.
HOVERGENO60701.
OMAQMCPEIR.

Enzyme and pathway databases

BRENDA1.1.1.22. 247.
ReactomeREACT_13433. Biological oxidations.

Gene expression databases

ArrayExpressO60701.
BgeeO60701.
CleanExHS_UGDH.
GenevestigatorO60701.
GermOnlineENSG00000109814. Homo sapiens.

Family and domain databases

InterProIPR016040. NAD(P)-bd_dom.
IPR017476. Nucleotide_sugar_DH.
IPR014027. UDP-Glc/GDP-Man_DH_C.
IPR014026. UDP-Glc/GDP-Man_DH_dimer.
IPR014028. UDP-Glc/GDP-Man_DH_dimer-bd.
IPR001732. UDP-Glc/GDP-Man_DH_N.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:3.40.50.1870. UDP-Glc/GDP-Man_DH_C. 1 hit.
PANTHERPTHR11374. UDPG_MGDP_DH_Creg. 1 hit.
PfamPF00984. UDPG_MGDP_dh. 1 hit.
PF03720. UDPG_MGDP_dh_C. 1 hit.
PF03721. UDPG_MGDP_dh_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR03026. NDP-sugDHase. 1 hit.
ProtoNetSearch...

Other Resources

DrugBankDB00157. NADH.
NextBio28812.
SOURCESearch...

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Entry information

Entry nameUGDH_HUMAN
AccessionPrimary (citable) accession number: O60701
Secondary accession number(s): O60589
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: November 3, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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