Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  UDP-glucose 6-dehydrogenase  

UniProtKB / Swiss-Prot ID :  UGDH_HUMAN

Gene Name (Synonyms) : 
UGDH  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

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

Protein Sequence MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLF...
Predicted Secondary Structure CCCCEEEEEEECCHHHHHHHHHHHHHCCCCEEEEEECCHHHHHHHHCCCCCCCCCCHHHHHHHHCCCCEE...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
53PhosphotyrosineTLPIYEPGL
CCCCCCCCH
17.71Phosphositeplus
Link
80Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DDAIKEADL
CHHHHHCCE
48.87Phosphositeplus
Link
91PhosphothreonineISVNTPTKT
EEECCCCCC
30.13HPRD
Link
107N6-acetyllysineAADLKYIEA
CCCHHHHHH
44.74HPRD
Link
107N6-acetyllysineAADLKYIEA
CCCHHHHHH
44.74Phosphositeplus
Link
107N6-acetyllysine.AADLKYIEA
CCCHHHHHH
44.74UniProtKB
Link
149Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DANTKPNLN
HHCCCCCCE
31.54Phosphositeplus
Link
173Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IKDLKNPDR
HHHCCCCCE
76.26Phosphositeplus
Link
173N6-acetyllysineIKDLKNPDR
HHHCCCCCE
76.26HPRD
Link
173N6-acetyllysineIKDLKNPDR
HHHCCCCCE
76.26Phosphositeplus
Link
173N6-acetyllysine.IKDLKNPDR
HHHCCCCCE
76.26UniProtKB
Link
434N6-acetyllysineKKMLKPAFI
HHCCCCCEE
30.70HPRD
Link
434N6-acetyllysineKKMLKPAFI
HHCCCCCEE
30.70Phosphositeplus
Link
434N6-acetyllysine.KKMLKPAFI
HHCCCCCEE
30.70UniProtKB
Link
476PhosphoserinePYAPSGEIP
CCCCHHHHC
40.67HPRD
Link-
476PhosphoserinePYAPSGEIP
CCCCHHHHC
40.67Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
Q8N291_HUMANphysical interactionMINT-63178MINT16169070
KAD5_HUMANphysical interactionEBI-736148
intact16169070
KAD5_HUMANyeast 2-hybridHPRD:04535HPRD16169070
GYS2_HUMANENSP00000319501STRING
UDB10_HUMANENSP00000319501STRING
UXS1_HUMANENSP00000319501STRING
UD2A1_HUMANENSP00000319501STRING
UDB11_HUMANENSP00000319501STRING
UD2B7_HUMANENSP00000319501STRING
UD2B4_HUMANENSP00000319501STRING
UDB15_HUMANENSP00000319501STRING
GALE_HUMANENSP00000319501STRING
GYS1_HUMANENSP00000319501STRING
UDB17_HUMANENSP00000319501STRING
UD14_HUMANENSP00000319501STRING
UDB28_HUMANENSP00000319501STRING
UGPA_HUMANENSP00000319501STRING
ENPP3_HUMANENSP00000319501STRING
ENPP1_HUMANENSP00000319501STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-107; LYS-173 AND LYS-434,AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures