UGDH_MOUSE - dbPTM
UGDH_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UGDH_MOUSE
UniProt AC O70475
Protein Name UDP-glucose 6-dehydrogenase
Gene Name Ugdh
Organism Mus musculus (Mouse).
Sequence Length 493
Subcellular Localization
Protein Description Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate..
Protein Sequence MVEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIREADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQKAVRALCAVYEHWVPKEKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSADDQVSRLVTISKDPYEACDGAHALVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHSELQTIGFQIETIGKKVSSKRIPYTPGEIPKFSLQDPPNKKPKV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
6Acetylation--MVEIKKICCIGAG
--CCCCEEEEEECCC		46.7922826441
47PhosphorylationARINAWNSPTLPIYE
HHCCCCCCCCCCCCC		14.4623984901
49PhosphorylationINAWNSPTLPIYEPG
CCCCCCCCCCCCCCC		45.0124719451
53PhosphorylationNSPTLPIYEPGLKEV
CCCCCCCCCCCHHHH		17.7122817900
67UbiquitinationVVESCRGKNLFFSTN
HHHHCCCCCCEEECC		31.0022790023
88PhosphorylationEADLVFISVNTPTKT
HCCEEEEECCCCCCC		9.6127087446
91PhosphorylationLVFISVNTPTKTYGM
EEEEECCCCCCCCCC		30.1327087446
93PhosphorylationFISVNTPTKTYGMGK
EEECCCCCCCCCCCC		33.7023649490
94UbiquitinationISVNTPTKTYGMGKG
EECCCCCCCCCCCCC		40.7422790023
100UbiquitinationTKTYGMGKGRAADLK
CCCCCCCCCCHHHHH		36.01-
100MalonylationTKTYGMGKGRAADLK
CCCCCCCCCCHHHHH		36.0126320211
107UbiquitinationKGRAADLKYIEACAR
CCCHHHHHHHHHHHH		44.74-
107AcetylationKGRAADLKYIEACAR
CCCHHHHHHHHHHHH		44.7423806337
107MalonylationKGRAADLKYIEACAR
CCCHHHHHHHHHHHH		44.7426320211
124UbiquitinationVQNSNGYKIVTEKST
HHCCCCCEEEECCCC		31.9022790023
129AcetylationGYKIVTEKSTVPVRA
CCEEEECCCCCCHHH		41.9022826441
149UbiquitinationRIFDANTKPNLNLQV
HHHCCCCCCCCCEEE		31.54-
149SuccinylationRIFDANTKPNLNLQV
HHHCCCCCCCCCEEE		31.5423954790
173AcetylationGTAIKDLKNPDRVLI
CCCHHCCCCCCCEEE		76.2623201123
185PhosphorylationVLIGGDETPEGQKAV
EEECCCCCHHHHHHH		31.2329233185
190UbiquitinationDETPEGQKAVRALCA
CCCHHHHHHHHHHHH		60.76-
190AcetylationDETPEGQKAVRALCA
CCCHHHHHHHHHHHH		60.7623954790
190MalonylationDETPEGQKAVRALCA
CCCHHHHHHHHHHHH		60.7626320211
205UbiquitinationVYEHWVPKEKILTTN
HHHHCCCHHHEECCC		63.1222790023
207UbiquitinationEHWVPKEKILTTNTW
HHCCCHHHEECCCCC		49.4922790023
207AcetylationEHWVPKEKILTTNTW
HHCCCHHHEECCCCC		49.4922826441
241S-palmitoylationINSISALCEATGADV
HHHHHHHHHHHCCCH		3.1528526873
264MalonylationMDQRIGNKFLKASVG
CCHHHCCHHHHHHCC		47.0326320211
267AcetylationRIGNKFLKASVGFGG
HHCCHHHHHHCCCCC		41.5722826441
269PhosphorylationGNKFLKASVGFGGSC
CCHHHHHHCCCCCCH		22.6125521595
275PhosphorylationASVGFGGSCFQKDVL
HHCCCCCCHHHHHHH		16.4930352176
288S-palmitoylationVLNLVYLCEALNLPE
HHHHHHHHHHCCHHH		1.2528526873
329AcetylationLFNTVTDKKIAILGF
HHHHCCCCEEEEEEE		36.3922826441
329UbiquitinationLFNTVTDKKIAILGF
HHHHCCCCEEEEEEE		36.3922790023
330AcetylationFNTVTDKKIAILGFA
HHHCCCCEEEEEEEE		39.9322826441
339AcetylationAILGFAFKKDTGDTR
EEEEEEEECCCCCCC		46.4322826441
352PhosphorylationTRESSSIYISKYLMD
CCCCCEEEEEEEECC		10.9025195567
355AcetylationSSSIYISKYLMDEGA
CCEEEEEEEECCCCC		32.6123954790
355UbiquitinationSSSIYISKYLMDEGA
CCEEEEEEEECCCCC		32.6122790023
370AcetylationHLHIYDPKVPREQIV
CEEECCCCCCHHHEE		63.0723954790
370UbiquitinationHLHIYDPKVPREQIV
CEEECCCCCCHHHEE		63.0722790023
386PhosphorylationDLSHPGVSADDQVSR
ECCCCCCCHHHHHHH		31.7125338131
399MalonylationSRLVTISKDPYEACD
HHEEEECCCHHHHCC		59.8926073543
431AcetylationDYERIHKKMLKPAFI
CHHHHHHHHCCCEEE		34.9922826441
434UbiquitinationRIHKKMLKPAFIFDG
HHHHHHCCCEEEECC		30.7022790023
434AcetylationRIHKKMLKPAFIFDG
HHHHHHCCCEEEECC		30.7023806337
464UbiquitinationFQIETIGKKVSSKRI
EEEEECCCEECCCCC		46.2622790023
473PhosphorylationVSSKRIPYTPGEIPK
ECCCCCCCCCCCCCC		24.1621082442
474PhosphorylationSSKRIPYTPGEIPKF
CCCCCCCCCCCCCCC		21.3327087446
480UbiquitinationYTPGEIPKFSLQDPP
CCCCCCCCCCCCCCC		53.9322790023
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
474TPhosphorylationKinaseMAPK1P63085
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UGDH_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of UGDH_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UGDH_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UGDH_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-474, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-474, AND MASSSPECTROMETRY.
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-473 AND THR-474, ANDMASS SPECTROMETRY.

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