MAOM_HUMAN - dbPTM
MAOM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAOM_HUMAN
UniProt AC P23368
Protein Name NAD-dependent malic enzyme, mitochondrial
Gene Name ME2
Organism Homo sapiens (Human).
Sequence Length 584
Subcellular Localization Mitochondrion matrix.
Protein Description
Protein Sequence MLSRLRVVSTTCTLACRHLHIKEKGKPLMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFYRILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGMGIPVGKLCLYTACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGRNTLIQFEDFGNHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEAQKKIWMFDKYGLLVKGRKAKIDSYQEPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPTAQAECTAEEAYTLTEGRCLFASGSPFGPVKLTDGRVFTPGQGNNVYIFPGVALAVILCNTRHISDSVFLEAAKALTSQLTDEELAQGRLYPPLANIQEVSINIAIKVTEYLYANKMAFRYPEPEDKAKYVKERTWRSEYDSLLPDVYEWPESASSPPVITE
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
24MalonylationRHLHIKEKGKPLMLN
HHCCHHHCCCCCEEC		68.2026320211
24AcetylationRHLHIKEKGKPLMLN
HHCCHHHCCCCCEEC		68.2023749302
26MalonylationLHIKEKGKPLMLNPR
CCHHHCCCCCEECCC		46.1526320211
38SulfoxidationNPRTNKGMAFTLQER
CCCCCCCCCEEHHHH		2.7121406390
67MethylationTQDIQALRFHRNLKK
HHHHHHHHHHHHHHH		28.48115483085
74AcetylationRFHRNLKKMTSPLEK
HHHHHHHHCCCCHHH		51.0525038526
74MalonylationRFHRNLKKMTSPLEK
HHHHHHHHCCCCHHH		51.0526320211
77PhosphorylationRNLKKMTSPLEKYIY
HHHHHCCCCHHHHHH		24.8024719451
81AcetylationKMTSPLEKYIYIMGI
HCCCCHHHHHHEEEC		44.6325038526
94AcetylationGIQERNEKLFYRILQ
ECHHHCHHHHHHHHH		47.6619608861
94UbiquitinationGIQERNEKLFYRILQ
ECHHHCHHHHHHHHH		47.6624816145
106PhosphorylationILQDDIESLMPIVYT
HHHHHHHHHCCCEEC		30.24-
113O-linked_GlycosylationSLMPIVYTPTVGLAC
HHCCCEECCCCCCHH		11.1129351928
115O-linked_GlycosylationMPIVYTPTVGLACSQ
CCCEECCCCCCHHHH		21.2929351928
156MalonylationNWPENHVKAVVVTDG
CCCCCCCEEEEEECC		28.1026320211
156AcetylationNWPENHVKAVVVTDG
CCCCCCCEEEEEECC		28.1019608861
156SuccinylationNWPENHVKAVVVTDG
CCCCCCCEEEEEECC		28.1027452117
175PhosphorylationGLGDLGVYGMGIPVG
CCCCCCCCCCCCCHH		10.29-
222PhosphorylationDPFYMGLYQKRDRTQ
CCCHHHHHCCCCCCH		13.27-
224AcetylationFYMGLYQKRDRTQQY
CHHHHHCCCCCCHHH		42.5919608861
224SuccinylationFYMGLYQKRDRTQQY
CHHHHHCCCCCCHHH		42.5927452117
240AcetylationDLIDEFMKAITDRYG
HHHHHHHHHHHHHHC		41.7919608861
240SuccinylationDLIDEFMKAITDRYG
HHHHHHHHHHHHHHC		41.7927452117
269PhosphorylationAFRFLRKYREKYCTF
HHHHHHHHHHHHCCC		19.99-
272AcetylationFLRKYREKYCTFNDD
HHHHHHHHHCCCCCC		36.3119608861
272SuccinylationFLRKYREKYCTFNDD
HHHHHHHHHCCCCCC		36.3127452117
283PhosphorylationFNDDIQGTAAVALAG
CCCCCHHHHHHHHHH		8.62-
339AcetylationLSEQEAQKKIWMFDK
CCHHHHHHHHHCHHH		53.9630582819
346UbiquitinationKKIWMFDKYGLLVKG
HHHHCHHHCCEEECC		29.9219608861
346AcetylationKKIWMFDKYGLLVKG
HHHHCHHHCCEEECC		29.9219608861
347PhosphorylationKIWMFDKYGLLVKGR
HHHCHHHCCEEECCC		18.17-
352AcetylationDKYGLLVKGRKAKID
HHCCEEECCCCCCCC		53.6325953088
400PhosphorylationAGAGRLFTPDVIRAM
ECCCCCCCHHHHHHH		24.15-
441S-nitrosylationYTLTEGRCLFASGSP
EECCCCCEEEECCCC		5.5719483679
441S-nitrosocysteineYTLTEGRCLFASGSP
EECCCCCEEEECCCC		5.57-
445PhosphorylationEGRCLFASGSPFGPV
CCCEEEECCCCCCCE		32.2521406692
447PhosphorylationRCLFASGSPFGPVKL
CEEEECCCCCCCEEC		17.9821406692
453AcetylationGSPFGPVKLTDGRVF
CCCCCCEECCCCCEE		49.1325953088
453UbiquitinationGSPFGPVKLTDGRVF
CCCCCCEECCCCCEE		49.13-
461PhosphorylationLTDGRVFTPGQGNNV
CCCCCEECCCCCCCE		24.5324043423
469PhosphorylationPGQGNNVYIFPGVAL
CCCCCCEEECCCCCE		10.0424043423
483PhosphorylationLAVILCNTRHISDSV
EEHHHHCCCCCCHHH		23.7224043423
503PhosphorylationKALTSQLTDEELAQG
HHHHHCCCHHHHHCC		33.46-
513PhosphorylationELAQGRLYPPLANIQ
HHHCCCCCCCCCCCE		11.0526546556
533PhosphorylationIAIKVTEYLYANKMA
EEEHHHHHHHHCCCC		8.81-
538AcetylationTEYLYANKMAFRYPE
HHHHHHCCCCCCCCC		24.3523236377
538UbiquitinationTEYLYANKMAFRYPE
HHHHHHCCCCCCCCC		24.3529967540
543PhosphorylationANKMAFRYPEPEDKA
HCCCCCCCCCHHHHH		12.90-
554UbiquitinationEDKAKYVKERTWRSE
HHHHHHHHHHHHHHH		38.0924816145
575PhosphorylationDVYEWPESASSPPVI
CHHCCCCCCCCCCCC		29.3928348404
577PhosphorylationYEWPESASSPPVITE
HCCCCCCCCCCCCCC		53.2928348404
578PhosphorylationEWPESASSPPVITE-
CCCCCCCCCCCCCC-		32.7028348404
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 MAOM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of MAOM_HUMAN !!
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 MAOM_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-156; LYS-224; LYS-240;LYS-272 AND LYS-346, AND MASS SPECTROMETRY.

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