[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Placenta; DOI=10.1074/jbc.273.39.25117; PubMed=9737970 [NCBI, ExPASy, EBI, Israel, Japan] Spicer A.P., Kaback L.A., Smith T.J., Seldin M.F.; "Molecular cloning and characterization of the human and mouse UDP-glucose dehydrogenase genes."; J. Biol. Chem. 273:25117-25124(1998).
[2]	NUCLEOTIDE SEQUENCE. TISSUE=Liver; PubMed=9850599 [NCBI, ExPASy, EBI, Israel, Japan] Peng H.L., Lou M.D., Chang M.L., Chang H.Y.; "cDNA cloning and expression analysis of the human UDPglucose dehydrogenase."; Proc. Natl. Sci. Counc. Repub. China, B, Life Sci. 22:166-172(1998).
[3]	NUCLEOTIDE SEQUENCE. Chang M.L., Chang H.Y., Peng H.L.; "Characterization of human gene encoding UDP-glucose dehydrogenase."; Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 214-388. Raghuram V., Foskett J.K.; Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.

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-glucuronate biosynthesis; UDP-glucuronate from UDP-glucose: step 1/1 .
SUBUNIT: Homohexamer (By similarity).
SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF061016; AAC36095.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ007702; CAA07609.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ272274; CAB75891.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ272275; CAB75891.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ272276; CAB75891.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ272277; CAB75891.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ272278; CAB75891.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ272279; CAB75891.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ272280; CAB75891.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ272281; CAB75891.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022781; AAH22781.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF049126; AAC05135.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JE0353; JE0353.

NP_003350.1; -.

3D structure databases

PDB

2Q3E; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-466.	[ExPASy / RCSB / EBI]
2QG4; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-466.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2Q3E; -.
2QG4; -.

ModBase

O60701.

Protein-protein interaction databases

IntAct

O60701; 2.

PTM databases

PhosphoSite

O60701; -.

Enzyme and pathway databases

Reactome

REACT_2063; Metabolism of xenobiotics.

2D gel databases

REPRODUCTION-2DPAGE

O60701; -.

Organism-specific databases

GC04M039176; -.

HIX0004163; -.

HGNC:12525; UGDH.

603370; gene. [NCBI / EBI]

PharmGKB

PA37170; -.

GeneCards

O60701.

Gene expression databases

ArrayExpress

O60701; -.

CleanEx

HS_UGDH; -.

GermOnline

ENSG00000109814; Homo sapiens.

Ontologies

GO:0009055;	Molecular function: electron carrier activity (traceable author statement from UniProtKB).
GO:0051287;	Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0003979;	Molecular function: UDP-glucose 6-dehydrogenase activity (traceable author statement from ProtInc).
GO:0006024;	Biological process: glycosaminoglycan biosynthetic process (traceable author statement from ProtInc).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006011;	Biological process: UDP-glucose metabolic process (traceable author statement from ProtInc).
GO:0006065;	Biological process: UDP-glucuronate biosynthetic process (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR016040; NAD(P)-bd.
IPR017476; Nucleotide_sugar_DH.
IPR014027; UDP-Glc/GDP-Man_DHase_C.
IPR014026; UDP-Glc/GDP-Man_DHase_dimer.
IPR014028; UDP-Glc/GDP-Man_DHase_dimer-bd.
IPR001732; UDP-Glc/GDP-Man_DHase_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.
G3DSA:3.40.50.1870; UDP-Glc/GDP-Man_DH_C; 1.

PANTHER

PTHR11374; UDPG_MGDP_DH_Creg; 1.

Pfam

PF00984; UDPG_MGDP_dh; 1.
PF03720; UDPG_MGDP_dh_C; 1.
PF03721; UDPG_MGDP_dh_N; 1.
Pfam graphical view of domain structure.

Proteomic databases

PeptideAtlas

O60701; -.

Proteomics databases

PRIDE

O60701; -.

Genome annotation databases

Ensembl

ENSG00000109814; Homo sapiens. [Contig view]

GeneID

7358; -.

KEGG

hsa:7358; -.

NMPDR

fig|9606.3.peg.24043; -.

Phylogenomic databases

HOGENOM

O60701; -.

HOVERGEN

O60701; -.

Other

DB00157; NADH.

28812; -.

UGDH; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; NAD; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 494`	`494`	`UDP-glucose 6-dehydrogenase.`	`PRO_0000074060`
`NP_BIND`	`6 23`	`18`	`NAD (By similarity).`
`REGION`	`162 165`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`276 276`		`Nucleophile (By similarity).`
`BINDING`	`36 36`		`NAD (By similarity).`
`BINDING`	`41 41`		`NAD (By similarity).`
`BINDING`	`93 93`		`NAD (By similarity).`
`BINDING`	`131 131`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`165 165`		`NAD (By similarity).`
`BINDING`	`220 220`		`Substrate (By similarity).`
`BINDING`	`273 273`		`Substrate; via amide nitrogen (By similarity).`
`BINDING`	`279 279`		`NAD (By similarity).`
`BINDING`	`339 339`		`Substrate (By similarity).`
`BINDING`	`346 346`		`NAD (By similarity).`
`MOD_RES`	`473 473`		`Phosphotyrosine (By similarity).`
`CONFLICT`	`338 338`		`F -> V (in Ref. 5; AAC05135).`
`CONFLICT`	`377 377`		`V -> A (in Ref. 5; AAC05135).`
`STRAND`	`6 10`	`5`
`HELIX`	`16 26`	`11`
`STRAND`	`30 35`	`6`
`HELIX`	`39 45`	`7`
`STRAND`	`47 49`	`3`
`HELIX`	`57 64`	`8`
`TURN`	`66 68`	`3`
`STRAND`	`69 73`	`5`
`HELIX`	`75 81`	`7`
`STRAND`	`83 87`	`5`
`TURN`	`98 102`	`5`
`HELIX`	`107 118`	`12`
`STRAND`	`122 128`	`7`
`HELIX`	`136 146`	`11`
`STRAND`	`153 158`	`6`
`HELIX`	`168 173`	`6`
`STRAND`	`178 181`	`4`
`HELIX`	`186 199`	`14`
`TURN`	`200 202`	`3`
`HELIX`	`205 207`	`3`
`STRAND`	`208 211`	`4`
`HELIX`	`213 244`	`32`
`HELIX`	`248 256`	`9`
`TURN`	`259 261`	`3`
`STRAND`	`263 265`	`3`
`STRAND`	`274 276`	`3`
`HELIX`	`277 290`	`14`
`HELIX`	`294 321`	`28`
`TURN`	`322 324`	`3`
`STRAND`	`330 334`	`5`
`STRAND`	`337 339`	`3`
`HELIX`	`349 359`	`11`
`STRAND`	`363 367`	`5`
`STRAND`	`369 371`	`3`
`HELIX`	`373 380`	`8`
`HELIX`	`390 394`	`5`
`STRAND`	`395 397`	`3`
`HELIX`	`401 405`	`5`
`STRAND`	`409 413`	`5`
`HELIX`	`418 422`	`5`
`HELIX`	`425 431`	`7`
`STRAND`	`437 442`	`6`
`TURN`	`444 447`	`4`
`HELIX`	`449 455`	`7`
`STRAND`	`458 461`	`4`

Sequence information

Length: 494 AA [This is the length of the unprocessed precursor]

Molecular weight: 55024 Da [This is the MW of the unprocessed precursor]

CRC64: 9C9DA5E1227D65CC [This is a checksum on the sequence]

        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

O60701 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools