DHE3_MOUSE - dbPTM
DHE3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DHE3_MOUSE
UniProt AC P26443
Protein Name Glutamate dehydrogenase 1, mitochondrial
Gene Name Glud1
Organism Mus musculus (Mouse).
Sequence Length 558
Subcellular Localization Mitochondrion matrix.
Protein Description Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate..
Protein Sequence MYRRLGEALLLSRAGPAALGSAAADSAALLGWARGQPSAAPQPGLTPVARRHYSEAAADREDDPNFFKMVEGFFDRGASIVEDKLVEDLKTRESEEQKRNRVRGILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFGDKTFVVQGFGNVGLHSMRYLHRFGAKCVGVGESDGSIWNPDGIDPKELEDFKLQHGSILGFPKAKVYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGKHGGTIPVVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYVNAIEKVFKVYNEAGVTFT
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
21PhosphorylationAGPAALGSAAADSAA
CCHHHHCHHHHHHHH
18.6522817900
68AcetylationEDDPNFFKMVEGFFD
CCCCCHHHHHHCHHH
37.5923954790
68SuccinylationEDDPNFFKMVEGFFD
CCCCCHHHHHHCHHH
37.59-
68SuccinylationEDDPNFFKMVEGFFD
CCCCCHHHHHHCHHH
37.5923806337
79PhosphorylationGFFDRGASIVEDKLV
CHHHCCCHHHHHHHH
29.9525521595
84AcetylationGASIVEDKLVEDLKT
CCHHHHHHHHHHHHC
40.7123806337
84GlutarylationGASIVEDKLVEDLKT
CCHHHHHHHHHHHHC
40.7124703693
84MalonylationGASIVEDKLVEDLKT
CCHHHHHHHHHHHHC
40.7126320211
84SuccinylationGASIVEDKLVEDLKT
CCHHHHHHHHHHHHC
40.71-
84SuccinylationGASIVEDKLVEDLKT
CCHHHHHHHHHHHHC
40.7123806337
90AcetylationDKLVEDLKTRESEEQ
HHHHHHHHCCCCHHH
58.8323576753
90GlutarylationDKLVEDLKTRESEEQ
HHHHHHHHCCCCHHH
58.8324703693
90MalonylationDKLVEDLKTRESEEQ
HHHHHHHHCCCCHHH
58.8326073543
90SuccinylationDKLVEDLKTRESEEQ
HHHHHHHHCCCCHHH
58.83-
90UbiquitinationDKLVEDLKTRESEEQ
HHHHHHHHCCCCHHH
58.83-
94PhosphorylationEDLKTRESEEQKRNR
HHHHCCCCHHHHHHH
43.0423140645
98AcetylationTRESEEQKRNRVRGI
CCCCHHHHHHHHHHH
55.7223864654
110AcetylationRGILRIIKPCNHVLS
HHHHHHHHCCCEEEE
40.9423576753
110SuccinylationRGILRIIKPCNHVLS
HHHHHHHHCCCEEEE
40.94-
110SuccinylationRGILRIIKPCNHVLS
HHHHHHHHCCCEEEE
40.9424315375
112S-nitrosocysteineILRIIKPCNHVLSLS
HHHHHHCCCEEEEEE
4.70-
112S-nitrosylationILRIIKPCNHVLSLS
HHHHHHCCCEEEEEE
4.7022178444
112S-palmitoylationILRIIKPCNHVLSLS
HHHHHHCCCEEEEEE
4.7028526873
117PhosphorylationKPCNHVLSLSFPIRR
HCCCEEEEEECEEEC
22.3723140645
128PhosphorylationPIRRDDGSWEVIEGY
EEECCCCCEEEEEEE
27.3625521595
135PhosphorylationSWEVIEGYRAQHSQH
CEEEEEEEECCCCCC
7.0325619855
147AcetylationSQHRTPCKGGIRYST
CCCCCCCCCCCCCCC
62.4723806337
147MalonylationSQHRTPCKGGIRYST
CCCCCCCCCCCCCCC
62.4726320211
147SuccinylationSQHRTPCKGGIRYST
CCCCCCCCCCCCCCC
62.47-
147UbiquitinationSQHRTPCKGGIRYST
CCCCCCCCCCCCCCC
62.47-
152PhosphorylationPCKGGIRYSTDVSVD
CCCCCCCCCCCCCHH
17.6323984901
153PhosphorylationCKGGIRYSTDVSVDE
CCCCCCCCCCCCHHH
14.3225521595
154PhosphorylationKGGIRYSTDVSVDEV
CCCCCCCCCCCHHHH
31.3323140645
157PhosphorylationIRYSTDVSVDEVKAL
CCCCCCCCHHHHHHH
27.0225521595
162AcetylationDVSVDEVKALASLMT
CCCHHHHHHHHHHHH
35.3223576753
162SuccinylationDVSVDEVKALASLMT
CCCHHHHHHHHHHHH
35.32-
162SuccinylationDVSVDEVKALASLMT
CCCHHHHHHHHHHHH
35.3223806337
162UbiquitinationDVSVDEVKALASLMT
CCCHHHHHHHHHHHH
35.32-
171AcetylationLASLMTYKCAVVDVP
HHHHHHCEEEEEECC
13.4223576753
171UbiquitinationLASLMTYKCAVVDVP
HHHHHHCEEEEEECC
13.4222790023
172ADP-ribosylationASLMTYKCAVVDVPF
HHHHHCEEEEEECCC
2.15-
172ADP-ribosylationASLMTYKCAVVDVPF
HHHHHCEEEEEECCC
2.15-
172S-nitrosylationASLMTYKCAVVDVPF
HHHHHCEEEEEECCC
2.1522178444
172S-palmitoylationASLMTYKCAVVDVPF
HHHHHCEEEEEECCC
2.1528526873
183AcetylationDVPFGGAKAGVKINP
ECCCCCCCCCCCCCC
49.2823806337
183SuccinylationDVPFGGAKAGVKINP
ECCCCCCCCCCCCCC
49.28-
183SuccinylationDVPFGGAKAGVKINP
ECCCCCCCCCCCCCC
49.2823806337
183UbiquitinationDVPFGGAKAGVKINP
ECCCCCCCCCCCCCC
49.28-
187AcetylationGGAKAGVKINPKNYT
CCCCCCCCCCCCCCC
35.5323576753
187MalonylationGGAKAGVKINPKNYT
CCCCCCCCCCCCCCC
35.5326320211
187SuccinylationGGAKAGVKINPKNYT
CCCCCCCCCCCCCCC
35.5323806337
191AcetylationAGVKINPKNYTDNEL
CCCCCCCCCCCHHHH
59.0923576753
191MalonylationAGVKINPKNYTDNEL
CCCCCCCCCCCHHHH
59.0926320211
191SuccinylationAGVKINPKNYTDNEL
CCCCCCCCCCCHHHH
59.09-
191SuccinylationAGVKINPKNYTDNEL
CCCCCCCCCCCHHHH
59.0923806337
191UbiquitinationAGVKINPKNYTDNEL
CCCCCCCCCCCHHHH
59.09-
193PhosphorylationVKINPKNYTDNELEK
CCCCCCCCCHHHHHH
22.9225195567
200AcetylationYTDNELEKITRRFTM
CCHHHHHHHHHHHHH
63.1023864654
200SuccinylationYTDNELEKITRRFTM
CCHHHHHHHHHHHHH
63.10-
200SuccinylationYTDNELEKITRRFTM
CCHHHHHHHHHHHHH
63.1023806337
200UbiquitinationYTDNELEKITRRFTM
CCHHHHHHHHHHHHH
63.10-
211AcetylationRFTMELAKKGFIGPG
HHHHHHHHCCCCCCC
67.0823576753
211SuccinylationRFTMELAKKGFIGPG
HHHHHHHHCCCCCCC
67.0823806337
212UbiquitinationFTMELAKKGFIGPGI
HHHHHHHCCCCCCCC
54.1422790023
226OxidationIDVPAPDMSTGEREM
CCCCCCCCCCCHHHH
3.6317242355
227PhosphorylationDVPAPDMSTGEREMS
CCCCCCCCCCHHHHH
40.4122324799
228PhosphorylationVPAPDMSTGEREMSW
CCCCCCCCCHHHHHH
36.1022817900
254S-nitrosylationYDINAHACVTGKPIS
CEECCCEEEECCCCC
1.7022178444
261PhosphorylationCVTGKPISQGGIHGR
EEECCCCCCCCCCCC
31.1622324799
270PhosphorylationGGIHGRISATGRGVF
CCCCCCCCCCCCCHH
20.5829899451
272PhosphorylationIHGRISATGRGVFHG
CCCCCCCCCCCHHHC
22.1822324799
326AcetylationYLHRFGAKCVGVGES
HHHHCCCEEEEECCC
29.8123576753
326SuccinylationYLHRFGAKCVGVGES
HHHHCCCEEEEECCC
29.8123806337
326UbiquitinationYLHRFGAKCVGVGES
HHHHCCCEEEEECCC
29.81-
327S-nitrosocysteineLHRFGAKCVGVGESD
HHHCCCEEEEECCCC
2.97-
327S-nitrosylationLHRFGAKCVGVGESD
HHHCCCEEEEECCCC
2.9724895380
333PhosphorylationKCVGVGESDGSIWNP
EEEEECCCCCCCCCC
41.1523984901
336PhosphorylationGVGESDGSIWNPDGI
EECCCCCCCCCCCCC
29.4423140645
346AcetylationNPDGIDPKELEDFKL
CCCCCCHHHHHHCCC
71.7923576753
346MalonylationNPDGIDPKELEDFKL
CCCCCCHHHHHHCCC
71.7926073543
346SuccinylationNPDGIDPKELEDFKL
CCCCCCHHHHHHCCC
71.79-
346SuccinylationNPDGIDPKELEDFKL
CCCCCCHHHHHHCCC
71.7923806337
352AcetylationPKELEDFKLQHGSIL
HHHHHHCCCCCCCCC
60.6123576753
352SuccinylationPKELEDFKLQHGSIL
HHHHHHCCCCCCCCC
60.61-
352SuccinylationPKELEDFKLQHGSIL
HHHHHHCCCCCCCCC
60.6123806337
352UbiquitinationPKELEDFKLQHGSIL
HHHHHHCCCCCCCCC
60.61-
357PhosphorylationDFKLQHGSILGFPKA
HCCCCCCCCCCCCCC
16.7123140645
363AcetylationGSILGFPKAKVYEGS
CCCCCCCCCEEECCC
59.5923576753
363GlutarylationGSILGFPKAKVYEGS
CCCCCCCCCEEECCC
59.5924703693
363SuccinylationGSILGFPKAKVYEGS
CCCCCCCCCEEECCC
59.59-
363SuccinylationGSILGFPKAKVYEGS
CCCCCCCCCEEECCC
59.5923806337
363UbiquitinationGSILGFPKAKVYEGS
CCCCCCCCCEEECCC
59.59-
365AcetylationILGFPKAKVYEGSIL
CCCCCCCEEECCCCE
52.0223576753
365SuccinylationILGFPKAKVYEGSIL
CCCCCCCEEECCCCE
52.02-
365SuccinylationILGFPKAKVYEGSIL
CCCCCCCEEECCCCE
52.0223806337
367PhosphorylationGFPKAKVYEGSILEA
CCCCCEEECCCCEEE
17.5423984901
370PhosphorylationKAKVYEGSILEADCD
CCEEECCCCEEECCC
16.4419060867
376GlutathionylationGSILEADCDILIPAA
CCCEEECCCEEEECC
4.5224333276
376S-nitrosylationGSILEADCDILIPAA
CCCEEECCCEEEECC
4.5222588120
384PhosphorylationDILIPAASEKQLTKS
CEEEECCCHHHCCCC
47.6423140645
386AcetylationLIPAASEKQLTKSNA
EEECCCHHHCCCCCC
48.3823864654
389PhosphorylationAASEKQLTKSNAPRV
CCCHHHCCCCCCCHH
29.9029550500
390AcetylationASEKQLTKSNAPRVK
CCHHHCCCCCCCHHE
50.7523576753
390GlutarylationASEKQLTKSNAPRVK
CCHHHCCCCCCCHHE
50.7524703693
390MalonylationASEKQLTKSNAPRVK
CCHHHCCCCCCCHHE
50.7526320211
390SuccinylationASEKQLTKSNAPRVK
CCHHHCCCCCCCHHE
50.75-
390SuccinylationASEKQLTKSNAPRVK
CCHHHCCCCCCCHHE
50.7523806337
391PhosphorylationSEKQLTKSNAPRVKA
CHHHCCCCCCCHHEE
32.7529550500
397AcetylationKSNAPRVKAKIIAEG
CCCCCHHEEEEEECC
45.2923201123
399AcetylationNAPRVKAKIIAEGAN
CCCHHEEEEEECCCC
29.0023576753
399GlutarylationNAPRVKAKIIAEGAN
CCCHHEEEEEECCCC
29.0024703693
399MalonylationNAPRVKAKIIAEGAN
CCCHHEEEEEECCCC
29.0026320211
399UbiquitinationNAPRVKAKIIAEGAN
CCCHHEEEEEECCCC
29.00-
409PhosphorylationAEGANGPTTPEADKI
ECCCCCCCCHHHHHH
57.2821082442
410PhosphorylationEGANGPTTPEADKIF
CCCCCCCCHHHHHHH
23.4325521595
415AcetylationPTTPEADKIFLERNI
CCCHHHHHHHHHCCE
42.2623576753
415SuccinylationPTTPEADKIFLERNI
CCCHHHHHHHHHCCE
42.26-
415SuccinylationPTTPEADKIFLERNI
CCCHHHHHHHHHCCE
42.2623806337
415UbiquitinationPTTPEADKIFLERNI
CCCHHHHHHHHHCCE
42.26-
444AcetylationVSYFEWLKNLNHVSY
EEHHHHHHCCCCCEE
61.5323576753
450PhosphorylationLKNLNHVSYGRLTFK
HHCCCCCEEEEEEEE
17.8326824392
451PhosphorylationKNLNHVSYGRLTFKY
HCCCCCEEEEEEEEE
12.7426032504
457N6-malonyllysineSYGRLTFKYERDSNY
EEEEEEEEEECCCCC
40.75-
457AcetylationSYGRLTFKYERDSNY
EEEEEEEEEECCCCC
40.7523576753
457MalonylationSYGRLTFKYERDSNY
EEEEEEEEEECCCCC
40.7526320211
457SuccinylationSYGRLTFKYERDSNY
EEEEEEEEEECCCCC
40.75-
457UbiquitinationSYGRLTFKYERDSNY
EEEEEEEEEECCCCC
40.75-
473PhosphorylationLLMSVQESLERKFGK
EEEEHHHHHHHHHHC
20.5922942356
477AcetylationVQESLERKFGKHGGT
HHHHHHHHHHCCCCC
49.4423576753
477SuccinylationVQESLERKFGKHGGT
HHHHHHHHHHCCCCC
49.44-
477SuccinylationVQESLERKFGKHGGT
HHHHHHHHHHCCCCC
49.4423806337
477UbiquitinationVQESLERKFGKHGGT
HHHHHHHHHHCCCCC
49.44-
480AcetylationSLERKFGKHGGTIPV
HHHHHHHCCCCCCCC
42.0623576753
480GlutarylationSLERKFGKHGGTIPV
HHHHHHHCCCCCCCC
42.0624703693
480MalonylationSLERKFGKHGGTIPV
HHHHHHHCCCCCCCC
42.0626320211
480SuccinylationSLERKFGKHGGTIPV
HHHHHHHCCCCCCCC
42.06-
480SuccinylationSLERKFGKHGGTIPV
HHHHHHHCCCCCCCC
42.0623806337
480UbiquitinationSLERKFGKHGGTIPV
HHHHHHHCCCCCCCC
42.06-
484PhosphorylationKFGKHGGTIPVVPTA
HHHCCCCCCCCCCCH
27.05-
490PhosphorylationGTIPVVPTAEFQDRI
CCCCCCCCHHHHHHC
27.4923140645
498PhosphorylationAEFQDRISGASEKDI
HHHHHHCCCCCHHHH
29.2423140645
501PhosphorylationQDRISGASEKDIVHS
HHHCCCCCHHHHCHH
49.0219060867
503N6-malonyllysineRISGASEKDIVHSGL
HCCCCCHHHHCHHHH
50.70-
503AcetylationRISGASEKDIVHSGL
HCCCCCHHHHCHHHH
50.7023806337
503GlutarylationRISGASEKDIVHSGL
HCCCCCHHHHCHHHH
50.7024703693
503MalonylationRISGASEKDIVHSGL
HCCCCCHHHHCHHHH
50.7026073543
503PhosphoglycerylationRISGASEKDIVHSGL
HCCCCCHHHHCHHHH
50.70-
503SuccinylationRISGASEKDIVHSGL
HCCCCCHHHHCHHHH
50.7023806337
503UbiquitinationRISGASEKDIVHSGL
HCCCCCHHHHCHHHH
50.70-
508PhosphorylationSEKDIVHSGLAYTME
CHHHHCHHHHHHHHH
25.3025521595
512PhosphorylationIVHSGLAYTMERSAR
HCHHHHHHHHHHHHH
16.2116873679
513PhosphorylationVHSGLAYTMERSARQ
CHHHHHHHHHHHHHH
13.6222817900
527N6-malonyllysineQIMRTAMKYNLGLDL
HHHHHHHHHCCCCCH
28.64-
527AcetylationQIMRTAMKYNLGLDL
HHHHHHHHHCCCCCH
28.6423806337
527GlutarylationQIMRTAMKYNLGLDL
HHHHHHHHHCCCCCH
28.6424703693
527MalonylationQIMRTAMKYNLGLDL
HHHHHHHHHCCCCCH
28.6426320211
527SuccinylationQIMRTAMKYNLGLDL
HHHHHHHHHCCCCCH
28.6423806337
528PhosphorylationIMRTAMKYNLGLDLR
HHHHHHHHCCCCCHH
11.5229514104
545AcetylationAYVNAIEKVFKVYNE
HHHHHHHHHHHHHHH
47.0223806337
545GlutarylationAYVNAIEKVFKVYNE
HHHHHHHHHHHHHHH
47.0224703693
545SuccinylationAYVNAIEKVFKVYNE
HHHHHHHHHHHHHHH
47.02-
545SuccinylationAYVNAIEKVFKVYNE
HHHHHHHHHHHHHHH
47.0223806337
545UbiquitinationAYVNAIEKVFKVYNE
HHHHHHHHHHHHHHH
47.02-
548AcetylationNAIEKVFKVYNEAGV
HHHHHHHHHHHHCCC
46.9623576753
548SuccinylationNAIEKVFKVYNEAGV
HHHHHHHHHHHHCCC
46.9624315375

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

Oops, there are no upstream regulatory protein records of DHE3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
84KAcetylation

23806337

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 DHE3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DHE3_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DHE3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, 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 SER-227, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-135 AND TYR-512, ANDMASS SPECTROMETRY.

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