MAOX_HUMAN - dbPTM
MAOX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MAOX_HUMAN
UniProt AC P48163
Protein Name NADP-dependent malic enzyme
Gene Name ME1
Organism Homo sapiens (Human).
Sequence Length 572
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MEPEAPRRRHTHQRGYLLTRNPHLNKDLAFTLEERQQLNIHGLLPPSFNSQEIQVLRVVKNFEHLNSDFDRYLLLMDLQDRNEKLFYRVLTSDIEKFMPIVYTPTVGLACQQYSLVFRKPRGLFITIHDRGHIASVLNAWPEDVIKAIVVTDGERILGLGDLGCNGMGIPVGKLALYTACGGMNPQECLPVILDVGTENEELLKDPLYIGLRQRRVRGSEYDDFLDEFMEAVSSKYGMNCLIQFEDFANVNAFRLLNKYRNQYCTFNDDIQGTASVAVAGLLAALRITKNKLSDQTILFQGAGEAALGIAHLIVMALEKEGLPKEKAIKKIWLVDSKGLIVKGRASLTQEKEKFAHEHEEMKNLEAIVQEIKPTALIGVAAIGGAFSEQILKDMAAFNERPIIFALSNPTSKAECSAEQCYKITKGRAIFASGSPFDPVTLPNGQTLYPGQGNNSYVFPGVALGVVACGLRQITDNIFLTTAEVIAQQVSDKHLEEGRLYPPLNTIRDVSLKIAEKIVKDAYQEKTATVYPEPQNKEAFVRSQMYSTDYDQILPDCYSWPEEVQKIQTKVDQ
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
1Acetylation-------MEPEAPRR
-------CCCCCCCC		20.4819413330
9UbiquitinationEPEAPRRRHTHQRGY
CCCCCCCCCCHHHCE		40.09-
9AcetylationEPEAPRRRHTHQRGY
CCCCCCCCCCHHHCE		40.09-
9UbiquitinationEPEAPRRRHTHQRGY
CCCCCCCCCCHHHCE		40.0924816145
26UbiquitinationTRNPHLNKDLAFTLE
CCCCCCCCCCCCCHH		61.5521906983
26UbiquitinationTRNPHLNKDLAFTLE
CCCCCCCCCCCCCHH		61.5521890473
60AcetylationIQVLRVVKNFEHLNS
HHHEEEECCHHHCCC		53.7319608861
60UbiquitinationIQVLRVVKNFEHLNS
HHHEEEECCHHHCCC		53.7327667366
60UbiquitinationIQVLRVVKNFEHLNS
HHHEEEECCHHHCCC		53.7321890473
67PhosphorylationKNFEHLNSDFDRYLL
CCHHHCCCHHHHEEE		46.12-
84AcetylationDLQDRNEKLFYRVLT
EHHHHCHHHHHHHHH		47.6623749302
84UbiquitinationDLQDRNEKLFYRVLT
EHHHHCHHHHHHHHH		47.6627667366
92PhosphorylationLFYRVLTSDIEKFMP
HHHHHHHHHHHHHCC		32.22-
113PhosphorylationVGLACQQYSLVFRKP
HHHCCEEEEEEEECC		4.33-
151PhosphorylationVIKAIVVTDGERILG
HEEEEEEECCCEEEC		27.65-
208PhosphorylationELLKDPLYIGLRQRR
HHHCCCCCHHHCCCC		9.79-
219PhosphorylationRQRRVRGSEYDDFLD
CCCCCCCCCHHHHHH		23.5526657352
221PhosphorylationRRVRGSEYDDFLDEF
CCCCCCCHHHHHHHH		23.6222617229
229SulfoxidationDDFLDEFMEAVSSKY
HHHHHHHHHHHHHHH		2.8030846556
262UbiquitinationLLNKYRNQYCTFNDD
HHHHHHCCCCCCCCC		26.19-
262UbiquitinationLLNKYRNQYCTFNDD
HHHHHHCCCCCCCCC		26.1922817900
267UbiquitinationRNQYCTFNDDIQGTA
HCCCCCCCCCCCCHH		28.0822817900
276UbiquitinationDIQGTASVAVAGLLA
CCCCHHHHHHHHHHH		4.6322817900
276UbiquitinationDIQGTASVAVAGLLA
CCCCHHHHHHHHHHH		4.63-
278UbiquitinationQGTASVAVAGLLAAL
CCHHHHHHHHHHHHH		3.9922817900
336PhosphorylationKKIWLVDSKGLIVKG
CEEEEECCCCEEEEC		22.5722617229
337UbiquitinationKIWLVDSKGLIVKGR
EEEEECCCCEEEECC		53.9621906983
337AcetylationKIWLVDSKGLIVKGR
EEEEECCCCEEEECC		53.96-
337UbiquitinationKIWLVDSKGLIVKGR
EEEEECCCCEEEECC		53.96-
342UbiquitinationDSKGLIVKGRASLTQ
CCCCEEEECCCCCCH		35.3722817900
346PhosphorylationLIVKGRASLTQEKEK
EEEECCCCCCHHHHH		30.5026437602
347UbiquitinationIVKGRASLTQEKEKF
EEECCCCCCHHHHHH		5.8221963094
347UbiquitinationIVKGRASLTQEKEKF
EEECCCCCCHHHHHH		5.82-
350UbiquitinationGRASLTQEKEKFAHE
CCCCCCHHHHHHHHH		58.9322817900
351UbiquitinationRASLTQEKEKFAHEH
CCCCCHHHHHHHHHH		57.2821906983
353UbiquitinationSLTQEKEKFAHEHEE
CCCHHHHHHHHHHHH		59.9422817900
361SulfoxidationFAHEHEEMKNLEAIV
HHHHHHHHHCHHHHH		2.9630846556
412UbiquitinationALSNPTSKAECSAEQ
EECCCCCCCCCCHHH		51.1621963094
422AcetylationCSAEQCYKITKGRAI
CCHHHHHHHHCCCEE		52.0726051181
422UbiquitinationCSAEQCYKITKGRAI
CCHHHHHHHHCCCEE		52.0727667366
425UbiquitinationEQCYKITKGRAIFAS
HHHHHHHCCCEEEEC		50.2822817900
437UbiquitinationFASGSPFDPVTLPNG
EECCCCCCCEECCCC		39.8922817900
437UbiquitinationFASGSPFDPVTLPNG
EECCCCCCCEECCCC		39.89-
441UbiquitinationSPFDPVTLPNGQTLY
CCCCCEECCCCCEEC		2.9422817900
444UbiquitinationDPVTLPNGQTLYPGQ
CCEECCCCCEECCCC		21.6523503661
450UbiquitinationNGQTLYPGQGNNSYV
CCCEECCCCCCCCCC		34.1821963094
450UbiquitinationNGQTLYPGQGNNSYV
CCCEECCCCCCCCCC		34.18-
461UbiquitinationNSYVFPGVALGVVAC
CCCCCCHHHHHHHHH		3.96-
461UbiquitinationNSYVFPGVALGVVAC
CCCCCCHHHHHHHHH		3.9622817900
474PhosphorylationACGLRQITDNIFLTT
HHCCHHHCCCCCCCH		18.04-
492UbiquitinationIAQQVSDKHLEEGRL
HHHHHCHHHHHCCCC		42.4529967540
494UbiquitinationQQVSDKHLEEGRLYP
HHHCHHHHHCCCCCC		8.69-
510PhosphorylationLNTIRDVSLKIAEKI
CCHHHHHHHHHHHHH		28.38-
512UbiquitinationTIRDVSLKIAEKIVK
HHHHHHHHHHHHHHH		32.1521906983
516UbiquitinationVSLKIAEKIVKDAYQ
HHHHHHHHHHHHHHH		43.7227667366
519UbiquitinationKIAEKIVKDAYQEKT
HHHHHHHHHHHHHCC		39.8623503661
525UbiquitinationVKDAYQEKTATVYPE
HHHHHHHCCCEECCC		28.1221906983
528PhosphorylationAYQEKTATVYPEPQN
HHHHCCCEECCCCCC		26.2928152594
530PhosphorylationQEKTATVYPEPQNKE
HHCCCEECCCCCCHH		9.4928152594
536UbiquitinationVYPEPQNKEAFVRSQ
ECCCCCCHHHHHHHH		45.2121906983
569SumoylationEVQKIQTKVDQ----
HHHHHHHHCCC----		27.69-
569SumoylationEVQKIQTKVDQ----
HHHHHHHHCCC----		27.69-
569UbiquitinationEVQKIQTKVDQ----
HHHHHHHHCCC----		27.6921906983
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
336SPhosphorylationKinaseNEK1Q96PY6
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MAOX_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 MAOX_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRC8_HUMANCTTNphysical
22863883
NMI_HUMANNMIphysical
22863883
TBCD_HUMANTBCDphysical
22863883
GSTK1_HUMANGSTK1physical
26344197
MOES_HUMANMSNphysical
26344197
PPCE_HUMANPREPphysical
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 MAOX_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
"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-60 AND LYS-84, AND MASSSPECTROMETRY.

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