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Reviewed (UniProtKB/Swiss-Prot)

Note: Proteins listed in ProtBank™ database are NOT off-the-shelf [catalog] proteins. Customized protein production request can be made for any protein in this database by clicking on the corresponding button under "Quick Quote". Please ensure sequence accuracy and/or make any necessary modifications prior to submitting your quote request

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Reviewed (UniProtKB/Swiss-Prot)


Name Gene Symbol Rec Full Name Protein Information Quick Quote  Price,
Turnaround
UGDH_MOUSE, Mus musculus (house mouse) Ugdh UDP-glucose 6-dehydrogenase Functions
wild_type
Starting from $1600,
4 weeks
Protein Domains
mutant
Quote

Protein Names | ProteinIDs  | Organism | Gene Names  | GeneID | Genome Annotation(Ensembl) |  Protein Sequence | 
General annotation |  References | Order
Protein Names
Recommended name:
 UDP-glucose 6-dehydrogenase;
Alternative name(s):
Protein IDs
(Accession numbers)
UniProtKB
 O70475
NCBI RefSeq

NP_033492.1, NM_009466.2.
Organism
Latin Name/
(Common Name)
Mus musculus (Mouse).
Taxonomic Identifier (NCBI)
 10090
Gene Names
 Ugdh [GenPool]
GeneID

22235
Genome
Annotation (Ensembl)

ENSMUST00000031103, ENSMUSP00000031103; ENSMUSG00000029201
Protein Sequence
 
SEQUENCE   493 AA;  54832 MW;  C6234F3C1D7480C7 CRC64;
MVEIKKICCI GAGYVGGPTC SVIAHMCPEI RVTVVDVNEA RINAWNSPTL PIYEPGLKEV
VESCRGKNLF FSTNIDDAIR EADLVFISVN TPTKTYGMGK GRAADLKYIE ACARRIVQNS
NGYKIVTEKS TVPVRAAESI RRIFDANTKP NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI
GGDETPEGQK AVRALCAVYE HWVPKEKILT TNTWSSELSK LAANAFLAQR ISSINSISAL
CEATGADVEE VATAIGMDQR IGNKFLKASV GFGGSCFQKD VLNLVYLCEA LNLPEVARYW
QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS IYISKYLMDE
GAHLHIYDPK VPREQIVVDL SHPGVSADDQ VSRLVTISKD PYEACDGAHA LVICTEWDMF
KELDYERIHK KMLKPAFIFD GRRVLDGLHS ELQTIGFQIE TIGKKVSSKR IPYTPGEIPK
FSLQDPPNKK PKV
General annotation
Function
 Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate.
Cofactor
Subunit structure
 Homohexamer (By similarity).
Subcellular location

Tissue specificity
Induction
Domain
Post-translational modification

Involvement in disease

References

  • "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)., PubMeb:9737970 DOI:10.1074/jbc.273.39.25117

  • "The status, quality, and expansion of the NIH full-length cDNAproject: the Mammalian Gene Collection (MGC).";,Genome Res. 14:2121-2127(2004).,PubMeb:15489334 DOI:10.1101/gr.2596504

  • "Large-scale phosphorylation analysis of mouse liver.";,Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;,Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).,PubMeb:17242355 DOI:10.1073/pnas.0609836104

  • "Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";,Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;,J. Proteome Res. 7:3957-3967(2008).,PubMeb:18630941 DOI:10.1021/pr800223m

  • "Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";,Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;,Mol. Cell. Proteomics 8:904-912(2009).,PubMeb:19131326 DOI:10.1074/mcp.M800451-MCP200

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Comparative Toxicogenomics Database | Order
Protein Domain Databases
InterPro

IPR008927, 6-PGluconate_DH_C-like.

IPR021157, Cyt_c1_TM_anchor_C.

IPR016040, NAD(P)-bd_dom.

IPR017476, Nucleotide_sugar_DH.

IPR014027, UDP-Glc/GDP-Man_DH_C.

IPR014026, UDP-Glc/GDP-Man_DH_dimer.

IPR001732, UDP-Glc/GDP-Man_DH_N.
Gene3D

G3DSA:1.20.5.100, Cyt_c1_TM_anchor_C; 1.

G3DSA:3.40.50.720, NAD(P)-bd; 2.
PANTHER
Pfam

PF00984, UDPG_MGDP_dh; 1.

PF03720, UDPG_MGDP_dh_C; 1.

PF03721, UDPG_MGDP_dh_N; 1.
PRINTS
SUPFAM

SSF48179, 6DGDH_C_like; 1.

SSF52413, UDP-Glc/GDP-Man_DH_C; 1.
PROSITE
3D Structure
Database (PDB)
Entry
Method
Resolution (A)
Chain
Positions
PDBsum
Sequence
Annotation
Feature key
Position(s)
Length
Description
Polypeptide chain 1 - 493 493 UDP-glucose 6-dehydrogenase. /FTId=PRO_0000074061.
Nucleotide phosphate-binding region 11 - 16 6 NAD (By similarity).
Nucleotide phosphate-binding region 89 - 93 5 NAD (By similarity).
Nucleotide phosphate-binding region 130 - 131 2 NAD (By similarity).
Nucleotide phosphate-binding region 276 - 279 4 NAD (By similarity).
Region 161 - 165 5 Substrate binding (By similarity).
Region 220 - 227 8 Substrate binding (By similarity).
Region 260 - 273 14 Substrate binding (By similarity).
Region 338 - 339 2 Substrate binding (By similarity).
Amino acid(s) 276 1 Nucleophile (By similarity).
Binding 36 1 NAD (By similarity).
Binding 41 1 NAD (By similarity).
Binding 165 1 NAD (By similarity).
Binding 346 1 NAD (By similarity).
Binding 442 1 Substrate (By similarity).
Posttranslational modification of a residue 107 1 N6-acetyllysine (By similarity).
Posttranslational modification of a residue 173 1 N6-acetyllysine (By similarity).
Posttranslational modification of a residue 434 1 N6-acetyllysine (By similarity).
Posttranslational modification of a residue 473 1 Phosphotyrosine.
Posttranslational modification of a residue 474 1 Phosphothreonine.
Protein-protein
Interaction
Databases
DIP
IntAct
MINT
STRING

O70475
Binary Interactions
With
Entry
#Exp.
IntAct
Enzyme and Pathway Databases
Pathway
Interaction DB
Reactome
Phylogenomic Database
HOVERGEN

HBG003512
InParanoid

O70475
OMA

ARINAWN
OrthoDB

EOG4N30NS
Proteomics
Database (PRIDE)

O70475
Comparative
Toxicogenomics
Database (CTD)

7358
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