DHE4_HUMAN - dbPTM
DHE4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DHE4_HUMAN
UniProt AC P49448
Protein Name Glutamate dehydrogenase 2, mitochondrial
Gene Name GLUD2
Organism Homo sapiens (Human).
Sequence Length 558
Subcellular Localization Mitochondrion matrix .
Protein Description Important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission..
Protein Sequence MYRYLAKALLPSRAGPAALGSAANHSAALLGRGRGQPAAASQPGLALAARRHYSELVADREDDPNFFKMVEGFFDRGASIVEDKLVKDLRTQESEEQKRNRVRGILRIIKPCNHVLSLSFPIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFGGAKAGVKINPKNYTENELEKITRRFTMELAKKGFIGPGVDVPAPDMNTGEREMSWIADTYASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFRDKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILGFPKAKPYEGSILEVDCDILIPAATEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLERNILVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLLSVQESLERKFGKHGGTIPIVPTAEFQDSISGASEKDIVHSALAYTMERSARQIMHTAMKYNLGLDLRTAAYVNAIEKVFKVYSEAGVTFT
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
12PhosphorylationLAKALLPSRAGPAAL
HHHHHCCCCCCHHHH		34.4322199227
53PhosphorylationALAARRHYSELVADR
HHHHHHHHHHHHCCC		11.30-
54PhosphorylationLAARRHYSELVADRE
HHHHHHHHHHHCCCC		20.52-
68SuccinylationEDDPNFFKMVEGFFD
CCCCCHHHHHHCHHH		37.59-
76MethylationMVEGFFDRGASIVED
HHHCHHHCCCHHHHH		37.10-
79PhosphorylationGFFDRGASIVEDKLV
CHHHCCCHHHHHHHH		29.9520166139
84SuccinylationGASIVEDKLVKDLRT
CCHHHHHHHHHHHHC		41.49-
84AcetylationGASIVEDKLVKDLRT
CCHHHHHHHHHHHHC		41.4923236377
110AcetylationRGILRIIKPCNHVLS
HHHHHHHHCCCEEEE		40.94-
110SuccinylationRGILRIIKPCNHVLS
HHHHHHHHCCCEEEE		40.94-
112S-nitrosylationILRIIKPCNHVLSLS
HHHHHHCCCEEEEEE		4.7024105792
128PhosphorylationPIRRDDGSWEVIEGY
EEECCCCCEEEEEEE		27.3623927012
135PhosphorylationSWEVIEGYRAQHSQH
CEEEEEEEECCCCCC		7.0323927012
152PhosphorylationPCKGGIRYSTDVSVD
CCCCCCCCCCCCCHH		17.6328152594
153PhosphorylationCKGGIRYSTDVSVDE
CCCCCCCCCCCCHHH		14.3228152594
154PhosphorylationKGGIRYSTDVSVDEV
CCCCCCCCCCCHHHH		31.3323927012
157PhosphorylationIRYSTDVSVDEVKAL
CCCCCCCCHHHHHHH		27.0223927012
162AcetylationDVSVDEVKALASLMT
CCCHHHHHHHHHHHH		35.32-
162SuccinylationDVSVDEVKALASLMT
CCCHHHHHHHHHHHH		35.32-
162UbiquitinationDVSVDEVKALASLMT
CCCHHHHHHHHHHHH		35.32-
162SuccinylationDVSVDEVKALASLMT
CCCHHHHHHHHHHHH		35.3221890473
170PhosphorylationALASLMTYKCAVVDV
HHHHHHHCEEEEEEC		7.07-
171AcetylationLASLMTYKCAVVDVP
HHHHHHCEEEEEECC		13.42-
171MethylationLASLMTYKCAVVDVP
HHHHHHCEEEEEECC		13.42-
172ADP-ribosylationASLMTYKCAVVDVPF
HHHHHCEEEEEECCC		2.15-
172ADP-ribosylationASLMTYKCAVVDVPF
HHHHHCEEEEEECCC		2.1516023112
183AcetylationDVPFGGAKAGVKINP
ECCCCCCCCCCCCCC		49.28-
183SuccinylationDVPFGGAKAGVKINP
ECCCCCCCCCCCCCC		49.28-
183UbiquitinationDVPFGGAKAGVKINP
ECCCCCCCCCCCCCC		49.28-
187UbiquitinationGGAKAGVKINPKNYT
CCCCCCCCCCCCCCC		35.53-
187AcetylationGGAKAGVKINPKNYT
CCCCCCCCCCCCCCC		35.53-
191AcetylationAGVKINPKNYTENEL
CCCCCCCCCCCHHHH		59.0925953088
191SuccinylationAGVKINPKNYTENEL
CCCCCCCCCCCHHHH		59.09-
200SuccinylationYTENELEKITRRFTM
CCHHHHHHHHHHHHH		63.10-
206PhosphorylationEKITRRFTMELAKKG
HHHHHHHHHHHHHCC		14.13-
211AcetylationRFTMELAKKGFIGPG
HHHHHHHHCCCCCCC		67.0824886821
211UbiquitinationRFTMELAKKGFIGPG
HHHHHHHHCCCCCCC		67.0821890473
272PhosphorylationIHGRISATGRGVFHG
CCCCCCCCCCCHHHC		22.1828857561
288PhosphorylationENFINEASYMSILGM
HHHHCHHHHHHHHCC		18.3928857561
289PhosphorylationNFINEASYMSILGMT
HHHCHHHHHHHHCCC		11.2628857561
316PhosphorylationFGNVGLHSMRYLHRF
CCCCCHHHHHHHHHC		15.2527251275
326AcetylationYLHRFGAKCIAVGES
HHHHCCCEEEEECCC		26.93-
333PhosphorylationKCIAVGESDGSIWNP
EEEEECCCCCCCCCC		41.1525072903
336PhosphorylationAVGESDGSIWNPDGI
EECCCCCCCCCCCCC		29.4425072903
346SuccinylationNPDGIDPKELEDFKL
CCCCCCHHHHHHHCC		71.79-
346AcetylationNPDGIDPKELEDFKL
CCCCCCHHHHHHHCC		71.7912634863
352SuccinylationPKELEDFKLQHGSIL
HHHHHHHCCCCCCCC		60.61-
352AcetylationPKELEDFKLQHGSIL
HHHHHHHCCCCCCCC		60.6124885283
352UbiquitinationPKELEDFKLQHGSIL
HHHHHHHCCCCCCCC		60.61-
352SuccinylationPKELEDFKLQHGSIL
HHHHHHHCCCCCCCC		60.6121890473
357PhosphorylationDFKLQHGSILGFPKA
HHCCCCCCCCCCCCC		16.7123312004
363AcetylationGSILGFPKAKPYEGS
CCCCCCCCCCCCCCC		67.77-
363UbiquitinationGSILGFPKAKPYEGS
CCCCCCCCCCCCCCC		67.77-
363SuccinylationGSILGFPKAKPYEGS
CCCCCCCCCCCCCCC		67.77-
365SuccinylationILGFPKAKPYEGSIL
CCCCCCCCCCCCCEE		55.01-
365AcetylationILGFPKAKPYEGSIL
CCCCCCCCCCCCCEE		55.01-
370PhosphorylationKAKPYEGSILEVDCD
CCCCCCCCEEEEECC		16.44-
386AcetylationLIPAATEKQLTKSNA
EEECCCHHHHCCCCC		46.37-
390SuccinylationATEKQLTKSNAPRVK
CCHHHHCCCCCCCCE		50.75-
390UbiquitinationATEKQLTKSNAPRVK
CCHHHHCCCCCCCCE		50.75-
390AcetylationATEKQLTKSNAPRVK
CCHHHHCCCCCCCCE		50.757675233
391PhosphorylationTEKQLTKSNAPRVKA
CHHHHCCCCCCCCEE		32.7524247654
399AcetylationNAPRVKAKIIAEGAN
CCCCCEEEEEECCCC		29.00-
399UbiquitinationNAPRVKAKIIAEGAN
CCCCCEEEEEECCCC		29.0021890473
409PhosphorylationAEGANGPTTPEADKI
ECCCCCCCCHHHHHH		57.2830266825
410PhosphorylationEGANGPTTPEADKIF
CCCCCCCCHHHHHHH		23.4330266825
415AcetylationPTTPEADKIFLERNI
CCCHHHHHHHHHCCE		42.2612634871
415SuccinylationPTTPEADKIFLERNI
CCCHHHHHHHHHCCE		42.26-
415SuccinylationPTTPEADKIFLERNI
CCCHHHHHHHHHCCE		42.2621890473
415UbiquitinationPTTPEADKIFLERNI
CCCHHHHHHHHHCCE		42.26-
438PhosphorylationNAGGVTVSYFEWLKN
CCCCEEEEHHHHHHC		18.10-
439PhosphorylationAGGVTVSYFEWLKNL
CCCEEEEHHHHHHCC		10.94-
450PhosphorylationLKNLNHVSYGRLTFK
HHCCCCCEEEEEEEE		17.8323401153
451PhosphorylationKNLNHVSYGRLTFKY
HCCCCCEEEEEEEEE		12.7428450419
457SuccinylationSYGRLTFKYERDSNY
EEEEEEEEEECCCCE		40.75-
457AcetylationSYGRLTFKYERDSNY
EEEEEEEEEECCCCE		40.7510929529
458PhosphorylationYGRLTFKYERDSNYH
EEEEEEEEECCCCEE		16.4128152594
477SuccinylationVQESLERKFGKHGGT
HHHHHHHHHHCCCCC		49.44-
477AcetylationVQESLERKFGKHGGT
HHHHHHHHHHCCCCC		49.44-
480SuccinylationSLERKFGKHGGTIPI
HHHHHHHCCCCCCCE		42.06-
480AcetylationSLERKFGKHGGTIPI
HHHHHHHCCCCCCCE		42.06-
503SuccinylationSISGASEKDIVHSAL
CCCCCCHHHHHHHHH		50.70-
503AcetylationSISGASEKDIVHSAL
CCCCCCHHHHHHHHH		50.70-
524PhosphorylationSARQIMHTAMKYNLG
HHHHHHHHHHHHCCC		15.8620068231
527UbiquitinationQIMHTAMKYNLGLDL
HHHHHHHHHCCCCCH		28.64-
527SuccinylationQIMHTAMKYNLGLDL
HHHHHHHHHCCCCCH		28.64-
527AcetylationQIMHTAMKYNLGLDL
HHHHHHHHHCCCCCH		28.6410929537
528PhosphorylationIMHTAMKYNLGLDLR
HHHHHHHHCCCCCHH		11.52-
539PhosphorylationLDLRTAAYVNAIEKV
CCHHHHHHHHHHHHH		7.5628152594
545SuccinylationAYVNAIEKVFKVYSE
HHHHHHHHHHHHHHH		47.0221890473
545AcetylationAYVNAIEKVFKVYSE
HHHHHHHHHHHHHHH		47.027214687
545UbiquitinationAYVNAIEKVFKVYSE
HHHHHHHHHHHHHHH		47.02-
545SuccinylationAYVNAIEKVFKVYSE
HHHHHHHHHHHHHHH		47.02-
548AcetylationNAIEKVFKVYSEAGV
HHHHHHHHHHHHCCC		43.16-
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 DHE4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DHE4_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 DHE4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TM1L1_HUMANTOM1L1physical
16169070
DHE3_HUMANGLUD1physical
26186194
DHE3_HUMANGLUD1physical
28514442
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 DHE4_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-415; LYS-457; LYS-527 ANDLYS-545, AND MASS SPECTROMETRY.

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