M2GD_HUMAN - dbPTM
M2GD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID M2GD_HUMAN
UniProt AC Q9UI17
Protein Name Dimethylglycine dehydrogenase, mitochondrial
Gene Name DMGDH
Organism Homo sapiens (Human).
Sequence Length 866
Subcellular Localization Mitochondrion.
Protein Description Catalyzes the demethylation of N,N-dimethylglycine to sarcosine. Also has activity with sarcosine in vitro..
Protein Sequence MLRPGAQLLRGLLLRSCPLQGSPGRPRSVCGREGEEKPPLSAETQWKDRAETVIIGGGCVGVSLAYHLAKAGMKDVVLLEKSELTAGSTWHAAGLTTYFHPGINLKKIHYDSIKLYEKLEEETGQVVGFHQPGSIRLATTPVRVDEFKYQMTRTGWHATEQYLIEPEKIQEMFPLLNMNKVLAGLYNPGDGHIDPYSLTMALAAGARKCGALLKYPAPVTSLKARSDGTWDVETPQGSMRANRIVNAAGFWAREVGKMIGLEHPLIPVQHQYVVTSTISEVKALKRELPVLRDLEGSYYLRQERDGLLFGPYESQEKMKVQDSWVTNGVPPGFGKELFESDLDRIMEHIKAAMEMVPVLKKADIINVVNGPITYSPDILPMVGPHQGVRNYWVAIGFGYGIIHAGGVGKYLSDWILHGEPPFDLIELDPNRYGKWTTTQYTEAKARESYGFNNIVGYPKEERFAGRPTQRVSGLYQRLESKCSMGFHAGWEQPHWFYKPGQDTQYRPSFRRTNWFEPVGSEYKQVMQRVAVTDLSPFGKFNIKGQDSIRLLDHLFANVIPKVGFTNISHMLTPKGRVYAELTVSHQSPGEFLLITGSGSELHDLRWIEEEAVKGGYDVEIKNITDELGVLGVAGPQARKVLQKLTSEDLSDDVFKFLQTKSLKVSNIPVTAIRISYTGELGWELYHRREDSVALYDAIMNAGQEEGIDNFGTYAMNALRLEKAFRAWGLEMNCDTNPLEAGLEYFVKLNKPADFIGKQALKQIKAKGLKRRLVCLTLATDDVDPEGNESIWYNGKVVGNTTSGSYSYSIQKSLAFAYVPVQLSEVGQQVEVELLGKNYPAVIIQEPLVLTEPTRNRLQKKGGKDKT
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
37AcetylationCGREGEEKPPLSAET
CCCCCCCCCCCCCCC		47.8620167786
91Tele-8alpha-FAD histidineLTAGSTWHAAGLTTY
CCCCCCCCCCCCCCE		13.04-
91OtherLTAGSTWHAAGLTTY
CCCCCCCCCCCCCCE		13.0427486859
110PhosphorylationINLKKIHYDSIKLYE
CCCEEEEHHHHHHHH		18.1727732954
112PhosphorylationLKKIHYDSIKLYEKL
CEEEEHHHHHHHHHH		17.9227732954
114AcetylationKIHYDSIKLYEKLEE
EEEHHHHHHHHHHHH		49.30-
116PhosphorylationHYDSIKLYEKLEEET
EHHHHHHHHHHHHHH		13.1527732954
118AcetylationDSIKLYEKLEEETGQ
HHHHHHHHHHHHHCC		47.8720167786
140PhosphorylationGSIRLATTPVRVDEF
CCEEEECCCEEEHHH		17.7424961811
148SuccinylationPVRVDEFKYQMTRTG
CEEEHHHEEEECCCC		32.31-
148SuccinylationPVRVDEFKYQMTRTG
CEEEHHHEEEECCCC		32.31-
148AcetylationPVRVDEFKYQMTRTG
CEEEHHHEEEECCCC		32.31-
168AcetylationQYLIEPEKIQEMFPL
EEEECHHHHHHHHHH		61.48-
215PhosphorylationKCGALLKYPAPVTSL
HHCCCCCCCCCCCEE		12.4720886841
220PhosphorylationLKYPAPVTSLKARSD
CCCCCCCCEEEECCC		27.5520886841
223AcetylationPAPVTSLKARSDGTW
CCCCCEEEECCCCCC		41.33-
226PhosphorylationVTSLKARSDGTWDVE
CCEEEECCCCCCCCC		45.3024275569
234PhosphorylationDGTWDVETPQGSMRA
CCCCCCCCCCCCHHH		22.2926074081
238PhosphorylationDVETPQGSMRANRIV
CCCCCCCCHHHHHHH		10.3926074081
317SuccinylationGPYESQEKMKVQDSW
CCCCCCCCCCCCCCH		36.06-
317SuccinylationGPYESQEKMKVQDSW
CCCCCCCCCCCCCCH		36.06-
319SuccinylationYESQEKMKVQDSWVT
CCCCCCCCCCCCHHH		48.05-
319SuccinylationYESQEKMKVQDSWVT
CCCCCCCCCCCCHHH		48.05-
335AcetylationGVPPGFGKELFESDL
CCCCCCCHHHHHHHH		49.32-
360AcetylationMEMVPVLKKADIINV
HHHHHHHHHCCEEEE		46.2624885481
373PhosphorylationNVVNGPITYSPDILP
EECCCCCCCCCCCCC		22.53-
374PhosphorylationVVNGPITYSPDILPM
ECCCCCCCCCCCCCC		20.94-
434SuccinylationLDPNRYGKWTTTQYT
CCCCCCCCCCCCCCC		32.22-
434AcetylationLDPNRYGKWTTTQYT
CCCCCCCCCCCCCCC		32.22-
434SuccinylationLDPNRYGKWTTTQYT
CCCCCCCCCCCCCCC		32.22-
437PhosphorylationNRYGKWTTTQYTEAK
CCCCCCCCCCCCHHH		15.7029759185
438PhosphorylationRYGKWTTTQYTEAKA
CCCCCCCCCCCHHHH		16.5329759185
440PhosphorylationGKWTTTQYTEAKARE
CCCCCCCCCHHHHHH		12.4029759185
441PhosphorylationKWTTTQYTEAKARES
CCCCCCCCHHHHHHH		21.4629759185
508PhosphorylationQDTQYRPSFRRTNWF
CCCCCCCCCCCCCCC		23.5324719451
520PhosphorylationNWFEPVGSEYKQVMQ
CCCCCCCHHHHHHHH		37.6824719451
523SuccinylationEPVGSEYKQVMQRVA
CCCCHHHHHHHHHHC		32.15-
523SuccinylationEPVGSEYKQVMQRVA
CCCCHHHHHHHHHHC		32.15-
523AcetylationEPVGSEYKQVMQRVA
CCCCHHHHHHHHHHC		32.15-
574AcetylationISHMLTPKGRVYAEL
CHHCCCCCCEEEEEE		54.8624885489
597PhosphorylationEFLLITGSGSELHDL
CEEEEECCCHHCEEC		30.42-
645PhosphorylationRKVLQKLTSEDLSDD
HHHHHHHCCCCCCHH		36.7924275569
646PhosphorylationKVLQKLTSEDLSDDV
HHHHHHCCCCCCHHH		39.2828857561
655SuccinylationDLSDDVFKFLQTKSL
CCCHHHHHHHHCCCC		45.04-
655AcetylationDLSDDVFKFLQTKSL
CCCHHHHHHHHCCCC		45.04-
655SuccinylationDLSDDVFKFLQTKSL
CCCHHHHHHHHCCCC		45.04-
695PhosphorylationREDSVALYDAIMNAG
CCCHHHHHHHHHHCC		8.13-
764AcetylationKQALKQIKAKGLKRR
HHHHHHHHCCCCCCE		41.36-
795SuccinylationESIWYNGKVVGNTTS
CEEEECCEEEEECCC		30.06-
795SuccinylationESIWYNGKVVGNTTS
CEEEECCEEEEECCC		30.06-
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 M2GD_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of M2GD_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 M2GD_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of M2GD_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
605850DMGDH deficiency (DMGDHD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of M2GD_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory