UGDH_HUMAN - dbPTM
UGDH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UGDH_HUMAN
UniProt AC O60701
Protein Name UDP-glucose 6-dehydrogenase
Gene Name UGDH
Organism Homo sapiens (Human).
Sequence Length 494
Subcellular Localization
Protein Description Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate..
Protein Sequence MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDEGAHLHIYDPKVPREQIVVDLSHPGVSEDDQVSRLVTISKDPYEACDGAHAVVICTEWDMFKELDYERIHKKMLKPAFIFDGRRVLDGLHNELQTIGFQIETIGKKVSSKRIPYAPSGEIPKFSLQDPPNKKPKV
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
6Malonylation--MFEIKKICCIGAG
--CCCCEEEEEECCC
46.7926320211
10UbiquitinationEIKKICCIGAGYVGG
CCEEEEEECCCCCCC
3.5323000965
10AcetylationEIKKICCIGAGYVGG
CCEEEEEECCCCCCC
3.5319608861
27UbiquitinationCSVIAHMCPEIRVTV
HHHHHHHCCCCEEEE
1.6433845483
32UbiquitinationHMCPEIRVTVVDVNE
HHCCCCEEEEEECCH
6.1433845483
40PhosphorylationTVVDVNESRINAWNS
EEEECCHHHCCCCCC
33.0021712546
47PhosphorylationSRINAWNSPTLPIYE
HHCCCCCCCCCCCCC
14.4622199227
49PhosphorylationINAWNSPTLPIYEPG
CCCCCCCCCCCCCCC
45.0122199227
52UbiquitinationWNSPTLPIYEPGLKE
CCCCCCCCCCCCHHH
7.3722817900
53PhosphorylationNSPTLPIYEPGLKEV
CCCCCCCCCCCHHHH
17.7127259358
63O-linked_GlycosylationGLKEVVESCRGKNLF
CHHHHHHHCCCCCCE
9.4826853435
67UbiquitinationVVESCRGKNLFFSTN
HHHHCCCCCCEEECC
31.0033845483
672-HydroxyisobutyrylationVVESCRGKNLFFSTN
HHHHCCCCCCEEECC
31.00-
73UbiquitinationGKNLFFSTNIDDAIK
CCCCEEECCHHHHHH
30.9133845483
76UbiquitinationLFFSTNIDDAIKEAD
CEEECCHHHHHHHCC
41.1633845483
76AcetylationLFFSTNIDDAIKEAD
CEEECCHHHHHHHCC
41.1619608861
80UbiquitinationTNIDDAIKEADLVFI
CCHHHHHHHCCEEEE
48.8722817900
88PhosphorylationEADLVFISVNTPTKT
HCCEEEEECCCCCCC
9.6123663014
91PhosphorylationLVFISVNTPTKTYGM
EEEEECCCCCCCCCC
30.1330266825
93PhosphorylationFISVNTPTKTYGMGK
EEECCCCCCCCCCCC
33.7023663014
93UbiquitinationFISVNTPTKTYGMGK
EEECCCCCCCCCCCC
33.7022817900
94UbiquitinationISVNTPTKTYGMGKG
EECCCCCCCCCCCCC
40.7433845483
95PhosphorylationSVNTPTKTYGMGKGR
ECCCCCCCCCCCCCC
27.9923532336
96PhosphorylationVNTPTKTYGMGKGRA
CCCCCCCCCCCCCCH
13.4823532336
100UbiquitinationTKTYGMGKGRAADLK
CCCCCCCCCCHHHHH
36.0129967540
1002-HydroxyisobutyrylationTKTYGMGKGRAADLK
CCCCCCCCCCHHHHH
36.01-
103UbiquitinationYGMGKGRAADLKYIE
CCCCCCCHHHHHHHH
17.6222817900
106UbiquitinationGKGRAADLKYIEACA
CCCCHHHHHHHHHHH
3.7833845483
106AcetylationGKGRAADLKYIEACA
CCCCHHHHHHHHHHH
3.7819608861
107AcetylationKGRAADLKYIEACAR
CCCHHHHHHHHHHHH
44.7419608861
107UbiquitinationKGRAADLKYIEACAR
CCCHHHHHHHHHHHH
44.7423000965
1072-HydroxyisobutyrylationKGRAADLKYIEACAR
CCCHHHHHHHHHHHH
44.74-
107MalonylationKGRAADLKYIEACAR
CCCHHHHHHHHHHHH
44.7432601280
108PhosphorylationGRAADLKYIEACARR
CCHHHHHHHHHHHHH
15.99-
110UbiquitinationAADLKYIEACARRIV
HHHHHHHHHHHHHHH
34.3129967540
120UbiquitinationARRIVQNSNGYKIVT
HHHHHHCCCCCEEEE
17.9723000965
124UbiquitinationVQNSNGYKIVTEKST
HHCCCCCEEEECCCC
31.9033845483
129UbiquitinationGYKIVTEKSTVPVRA
CCEEEECCCCCCHHH
41.9033845483
1292-HydroxyisobutyrylationGYKIVTEKSTVPVRA
CCEEEECCCCCCHHH
41.90-
130PhosphorylationYKIVTEKSTVPVRAA
CEEEECCCCCCHHHH
28.5323403867
131PhosphorylationKIVTEKSTVPVRAAE
EEEECCCCCCHHHHH
39.6423403867
140UbiquitinationPVRAAESIRRIFDAN
CHHHHHHHHHHHCCC
2.3029967540
142UbiquitinationRAAESIRRIFDANTK
HHHHHHHHHHCCCCC
32.0527667366
149UbiquitinationRIFDANTKPNLNLQV
HHHCCCCCCCCCEEE
31.5422817900
162UbiquitinationQVLSNPEFLAEGTAI
EECCCHHHHHCCCCH
9.1522817900
167UbiquitinationPEFLAEGTAIKDLKN
HHHHHCCCCHHCCCC
19.4033845483
170UbiquitinationLAEGTAIKDLKNPDR
HHCCCCHHCCCCCCC
55.3233845483
173AcetylationGTAIKDLKNPDRVLI
CCCHHCCCCCCCEEE
76.2619608861
173UbiquitinationGTAIKDLKNPDRVLI
CCCHHCCCCCCCEEE
76.2622817900
1732-HydroxyisobutyrylationGTAIKDLKNPDRVLI
CCCHHCCCCCCCEEE
76.26-
183UbiquitinationDRVLIGGDETPEGQR
CCEEECCCCCHHHHH
51.9222817900
185PhosphorylationVLIGGDETPEGQRAV
EEECCCCCHHHHHHH
31.2321815630
186UbiquitinationLIGGDETPEGQRAVQ
EECCCCCHHHHHHHH
41.4922817900
197UbiquitinationRAVQALCAVYEHWVP
HHHHHHHHHHHHCCC
14.0533845483
199PhosphorylationVQALCAVYEHWVPRE
HHHHHHHHHHCCCHH
5.4227642862
200UbiquitinationQALCAVYEHWVPREK
HHHHHHHHHCCCHHH
25.3633845483
207UbiquitinationEHWVPREKILTTNTW
HHCCCHHHCCCCCCC
44.2729967540
2072-HydroxyisobutyrylationEHWVPREKILTTNTW
HHCCCHHHCCCCCCC
44.27-
232UbiquitinationAFLAQRISSINSISA
HHHHHHHHHHHHHHH
27.6233845483
233UbiquitinationFLAQRISSINSISAL
HHHHHHHHHHHHHHH
24.3433845483
242UbiquitinationNSISALCEATGADVE
HHHHHHHHHHCCCHH
50.5533845483
257SulfoxidationEVATAIGMDQRIGNK
HHHHHHCCCHHHCCH
3.0330846556
262UbiquitinationIGMDQRIGNKFLKAS
HCCCHHHCCHHHHHH
33.2033845483
263UbiquitinationGMDQRIGNKFLKASV
CCCHHHCCHHHHHHC
29.5433845483
264UbiquitinationMDQRIGNKFLKASVG
CCHHHCCHHHHHHCC
47.0333845483
267UbiquitinationRIGNKFLKASVGFGG
HHCCHHHHHHCCCCC
41.5733845483
269PhosphorylationGNKFLKASVGFGGSC
CCHHHHHHCCCCCCH
22.6120860994
272UbiquitinationFLKASVGFGGSCFQK
HHHHHCCCCCCHHHH
10.5733845483
273UbiquitinationLKASVGFGGSCFQKD
HHHHCCCCCCHHHHH
22.6029967540
275PhosphorylationASVGFGGSCFQKDVL
HHCCCCCCHHHHHHH
16.4925159151
286PhosphorylationKDVLNLVYLCEALNL
HHHHHHHHHHHHCCH
14.59-
303UbiquitinationVARYWQQVIDMNDYQ
HHHHHHHHCCCCHHH
2.1029967540
309PhosphorylationQVIDMNDYQRRRFAS
HHCCCCHHHHHHHHH
10.0227259358
316PhosphorylationYQRRRFASRIIDSLF
HHHHHHHHHHHHHHH
22.69-
321PhosphorylationFASRIIDSLFNTVTD
HHHHHHHHHHHHCCC
25.18-
327PhosphorylationDSLFNTVTDKKIAIL
HHHHHHCCCCEEEEE
39.81-
329UbiquitinationLFNTVTDKKIAILGF
HHHHCCCCEEEEEEE
36.3933845483
3292-HydroxyisobutyrylationLFNTVTDKKIAILGF
HHHHCCCCEEEEEEE
36.39-
330UbiquitinationFNTVTDKKIAILGFA
HHHCCCCEEEEEEEE
39.9333845483
3302-HydroxyisobutyrylationFNTVTDKKIAILGFA
HHHCCCCEEEEEEEE
39.93-
333UbiquitinationVTDKKIAILGFAFKK
CCCCEEEEEEEEEEC
4.3829967540
337UbiquitinationKIAILGFAFKKDTGD
EEEEEEEEEECCCCC
17.3533845483
337AcetylationKIAILGFAFKKDTGD
EEEEEEEEEECCCCC
17.3519608861
339AcetylationAILGFAFKKDTGDTR
EEEEEEEECCCCCCC
46.4319809299
339UbiquitinationAILGFAFKKDTGDTR
EEEEEEEECCCCCCC
46.4333845483
3392-HydroxyisobutyrylationAILGFAFKKDTGDTR
EEEEEEEECCCCCCC
46.43-
348PhosphorylationDTGDTRESSSIYISK
CCCCCCCCCEEEEEE
26.5421406692
349PhosphorylationTGDTRESSSIYISKY
CCCCCCCCEEEEEEE
18.9221406692
350PhosphorylationGDTRESSSIYISKYL
CCCCCCCEEEEEEEE
28.7921406692
352PhosphorylationTRESSSIYISKYLMD
CCCCCEEEEEEEECC
10.9028152594
354PhosphorylationESSSIYISKYLMDEG
CCCEEEEEEEECCCC
9.7728152594
363UbiquitinationYLMDEGAHLHIYDPK
EECCCCCCEEECCCC
28.8829967540
367UbiquitinationEGAHLHIYDPKVPRE
CCCCEEECCCCCCHH
18.5533845483
367AcetylationEGAHLHIYDPKVPRE
CCCCEEECCCCCCHH
18.5519608861
370UbiquitinationHLHIYDPKVPREQIV
CEEECCCCCCHHHEE
63.0729967540
3702-HydroxyisobutyrylationHLHIYDPKVPREQIV
CEEECCCCCCHHHEE
63.07-
379PhosphorylationPREQIVVDLSHPGVS
CHHHEEEECCCCCCC
31.4032142685
384UbiquitinationVVDLSHPGVSEDDQV
EEECCCCCCCCCCCE
30.1133845483
386PhosphorylationDLSHPGVSEDDQVSR
ECCCCCCCCCCCEEE
41.0227251275
393UbiquitinationSEDDQVSRLVTISKD
CCCCCEEEEEEEECC
34.0333845483
394UbiquitinationEDDQVSRLVTISKDP
CCCCEEEEEEEECCH
2.8729967540
397UbiquitinationQVSRLVTISKDPYEA
CEEEEEEEECCHHHH
3.6233845483
409PhosphorylationYEACDGAHAVVICTE
HHHCCCCCEEEEECC
25.2832142685
414UbiquitinationGAHAVVICTEWDMFK
CCCEEEEECCHHHHH
1.5833845483
419SulfoxidationVICTEWDMFKELDYE
EEECCHHHHHHCCHH
5.6130846556
423UbiquitinationEWDMFKELDYERIHK
CHHHHHHCCHHHHHH
9.7833845483
424UbiquitinationWDMFKELDYERIHKK
HHHHHHCCHHHHHHH
44.3229967540
430UbiquitinationLDYERIHKKMLKPAF
CCHHHHHHHHCCCEE
37.1929967540
431MalonylationDYERIHKKMLKPAFI
CHHHHHHHHCCCEEE
34.9926320211
434AcetylationRIHKKMLKPAFIFDG
HHHHHHCCCEEEECC
30.7019608861
434UbiquitinationRIHKKMLKPAFIFDG
HHHHHHCCCEEEECC
30.7033845483
461PhosphorylationTIGFQIETIGKKVSS
HHCEEEEECCCEECC
36.3422817900
464UbiquitinationFQIETIGKKVSSKRI
EEEEECCCEECCCCC
46.2633845483
473PhosphorylationVSSKRIPYAPSGEIP
ECCCCCCCCCCCCCC
28.8628152594
476PhosphorylationKRIPYAPSGEIPKFS
CCCCCCCCCCCCCCC
40.6722617229
481UbiquitinationAPSGEIPKFSLQDPP
CCCCCCCCCCCCCCC
53.9333845483
483PhosphorylationSGEIPKFSLQDPPNK
CCCCCCCCCCCCCCC
31.1128555341
490AcetylationSLQDPPNKKPKV---
CCCCCCCCCCCC---
75.9925953088
490UbiquitinationSLQDPPNKKPKV---
CCCCCCCCCCCC---
75.9933845483
491UbiquitinationLQDPPNKKPKV----
CCCCCCCCCCC----
57.6329967540
491MalonylationLQDPPNKKPKV----
CCCCCCCCCCC----
57.6326320211
491AcetylationLQDPPNKKPKV----
CCCCCCCCCCC----
57.6325953088

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
461TPhosphorylationKinaseCDK1P06493
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UGDH_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAD5_HUMANAK5physical
16169070
UD11_HUMANUGT1A1physical
21988832
METK2_HUMANMAT2Aphysical
22863883
MAOX_HUMANME1physical
22863883
RNH2A_HUMANRNASEH2Aphysical
22863883
SNX1_HUMANSNX1physical
22863883
UGDH_HUMANUGDHphysical
25416956
TPPC4_HUMANTRAPPC4physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UGDH_HUMAN

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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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