ACADM_HUMAN - dbPTM
ACADM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACADM_HUMAN
UniProt AC P11310
Protein Name Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Gene Name ACADM
Organism Homo sapiens (Human).
Sequence Length 421
Subcellular Localization Mitochondrion matrix.
Protein Description Acyl-CoA dehydrogenase specific for acyl chain lengths of 4 to 16 that catalyzes the initial step of fatty acid beta-oxidation. Utilizes the electron transfer flavoprotein (ETF) as an electron acceptor to transfer electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase)..
Protein Sequence MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYKN
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
42PhosphorylationLGFSFEFTEQQKEFQ
CCCEEEEHHHHHHHH		26.2020068231
69UbiquitinationPVAAEYDKTGEYPVP
HEEECCCCCCCCCHH		58.49-
692-HydroxyisobutyrylationPVAAEYDKTGEYPVP
HEEECCCCCCCCCHH		58.49-
69AcetylationPVAAEYDKTGEYPVP
HEEECCCCCCCCCHH		58.4925038526
69SuccinylationPVAAEYDKTGEYPVP
HEEECCCCCCCCCHH		58.49-
69SuccinylationPVAAEYDKTGEYPVP
HEEECCCCCCCCCHH		58.49-
70PhosphorylationVAAEYDKTGEYPVPL
EEECCCCCCCCCHHH		32.149414599
73PhosphorylationEYDKTGEYPVPLIRR
CCCCCCCCCHHHHHH		15.7546157395
73 (in isoform 2)Ubiquitination-15.75-
150PhosphorylationKKYLGRMTEEPLMCA
HHHHCCCCCCCEEEE		35.5220860994
173AcetylationGSDVAGIKTKAEKKG
CCCCCCCEECCHHCC		42.9525953088
178SuccinylationGIKTKAEKKGDEYII
CCEECCHHCCCEEEE		67.9027452117
179UbiquitinationIKTKAEKKGDEYIIN
CEECCHHCCCEEEEC		64.20-
179SuccinylationIKTKAEKKGDEYIIN
CEECCHHCCCEEEEC		64.20-
179SuccinylationIKTKAEKKGDEYIIN
CEECCHHCCCEEEEC		64.2027452117
183PhosphorylationAEKKGDEYIINGQKM
CHHCCCEEEECCEEE		16.3128152594
207PhosphorylationWYFLLARSDPDPKAP
EEEEEEECCCCCCCC		48.1446157383
212SuccinylationARSDPDPKAPANKAF
EECCCCCCCCCCCCC		74.51-
212SuccinylationARSDPDPKAPANKAF
EECCCCCCCCCCCCC		74.5123954790
212AcetylationARSDPDPKAPANKAF
EECCCCCCCCCCCCC		74.5123749302
216AcetylationPDPKAPANKAFTGFI
CCCCCCCCCCCCEEE		34.8219608861
217SuccinylationDPKAPANKAFTGFIV
CCCCCCCCCCCEEEE		47.16-
217AcetylationDPKAPANKAFTGFIV
CCCCCCCCCCCEEEE		47.16-
217SuccinylationDPKAPANKAFTGFIV
CCCCCCCCCCCEEEE		47.16-
217UbiquitinationDPKAPANKAFTGFIV
CCCCCCCCCCCEEEE		47.16-
2172-HydroxyisobutyrylationDPKAPANKAFTGFIV
CCCCCCCCCCCEEEE		47.16-
221 (in isoform 2)Ubiquitination-12.11-
228PhosphorylationGFIVEADTPGIQIGR
EEEEECCCCCEEECC		30.3869006573
236UbiquitinationPGIQIGRKELNMGQR
CCEEECCCCCCCCCC		62.43-
2362-HydroxyisobutyrylationPGIQIGRKELNMGQR
CCEEECCCCCCCCCC		62.43-
2562-HydroxyisobutyrylationGIVFEDVKVPKENVL
CCCEECEECCHHHEE		66.21-
256SuccinylationGIVFEDVKVPKENVL
CCCEECEECCHHHEE		66.2123954790
256AcetylationGIVFEDVKVPKENVL
CCCEECEECCHHHEE		66.2123236377
256UbiquitinationGIVFEDVKVPKENVL
CCCEECEECCHHHEE		66.21-
259SuccinylationFEDVKVPKENVLIGD
EECEECCHHHEEEEC		65.9827452117
259AcetylationFEDVKVPKENVLIGD
EECEECCHHHEEEEC		65.9825038526
259SuccinylationFEDVKVPKENVLIGD
EECEECCHHHEEEEC		65.98-
259UbiquitinationFEDVKVPKENVLIGD
EECEECCHHHEEEEC		65.98-
2592-HydroxyisobutyrylationFEDVKVPKENVLIGD
EECEECCHHHEEEEC		65.98-
260 (in isoform 2)Ubiquitination-46.64-
271UbiquitinationIGDGAGFKVAMGAFD
EECCCCCEEECCCCC		28.32-
271SuccinylationIGDGAGFKVAMGAFD
EECCCCCEEECCCCC		28.32-
271AcetylationIGDGAGFKVAMGAFD
EECCCCCEEECCCCC		28.3225038526
271SuccinylationIGDGAGFKVAMGAFD
EECCCCCEEECCCCC		28.3227452117
279SuccinylationVAMGAFDKTRPVVAA
EECCCCCCCCCHHHH		39.7227452117
2792-HydroxyisobutyrylationVAMGAFDKTRPVVAA
EECCCCCCCCCHHHH		39.72-
279MalonylationVAMGAFDKTRPVVAA
EECCCCCCCCCHHHH		39.7226320211
279UbiquitinationVAMGAFDKTRPVVAA
EECCCCCCCCCHHHH		39.72-
279AcetylationVAMGAFDKTRPVVAA
EECCCCCCCCCHHHH		39.7219608861
283AcetylationAFDKTRPVVAAGAVG
CCCCCCCHHHHHHHH		4.0519608861
300PhosphorylationQRALDEATKYALERK
HHHHHHHHHHHHHHC		23.6550563027
3012-HydroxyisobutyrylationRALDEATKYALERKT
HHHHHHHHHHHHHCC		35.26-
301AcetylationRALDEATKYALERKT
HHHHHHHHHHHHHCC		35.2619608861
301UbiquitinationRALDEATKYALERKT
HHHHHHHHHHHHHCC		35.26-
302PhosphorylationALDEATKYALERKTF
HHHHHHHHHHHHCCH		16.4430631047
305 (in isoform 2)Ubiquitination-43.91-
305AcetylationEATKYALERKTFGKL
HHHHHHHHHCCHHHH		43.9119608861
320PhosphorylationLVEHQAISFMLAEMA
HHHHHHHHHHHHHHH		13.9746157389
349MethylationWEVDSGRRNTYYASI
EECCCCCCCCHHHHH		43.28-
351PhosphorylationVDSGRRNTYYASIAK
CCCCCCCCHHHHHHH		18.989414609
352PhosphorylationDSGRRNTYYASIAKA
CCCCCCCHHHHHHHH		10.69110740699
353PhosphorylationSGRRNTYYASIAKAF
CCCCCCHHHHHHHHH		7.5869339323
395UbiquitinationEKLMRDAKIYQIYEG
HHHHHHCCEEEEEEC		46.35-
3952-HydroxyisobutyrylationEKLMRDAKIYQIYEG
HHHHHHCCEEEEEEC		46.35-
397PhosphorylationLMRDAKIYQIYEGTS
HHHHCCEEEEEECCH		6.5328152594
399 (in isoform 2)Ubiquitination-1.57-
400PhosphorylationDAKIYQIYEGTSQIQ
HCCEEEEEECCHHHH		7.8728152594
403PhosphorylationIYQIYEGTSQIQRLI
EEEEEECCHHHHHHH		12.9128152594
418AcetylationVAREHIDKYKN----
HHHHHHHHHCC----		58.4826210075
420AcetylationREHIDKYKN------
HHHHHHHCC------		63.022381231
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 ACADM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACADM_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 ACADM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STRAP_HUMANSTRAPphysical
22863883
AT1A1_HUMANATP1A1physical
26344197
ATPG_HUMANATP5C1physical
26344197
VATA_HUMANATP6V1Aphysical
26344197
CAND1_HUMANCAND1physical
26344197
CALX_HUMANCANXphysical
26344197
OST48_HUMANDDOSTphysical
26344197
DX39B_HUMANDDX39Bphysical
26344197
ETFA_HUMANETFAphysical
26344197
GFPT1_HUMANGFPT1physical
26344197
GFPT2_HUMANGFPT2physical
26344197
HIBCH_HUMANHIBCHphysical
26344197
IDH3A_HUMANIDH3Aphysical
26344197
2AAB_HUMANPPP2R1Bphysical
26344197
GLU2B_HUMANPRKCSHphysical
26344197
PRS7_HUMANPSMC2physical
26344197
RPN1_HUMANRPN1physical
26344197
SUCB1_HUMANSUCLA2physical
26344197
QCR2_HUMANUQCRC2physical
26344197
VDAC1_HUMANVDAC1physical
26344197
VDAC2_HUMANVDAC2physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
201450Acyl-CoA dehydrogenase medium-chain deficiency (ACADMD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB03147Flavin adenine dinucleotide
Regulatory Network of ACADM_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-212; LYS-279 AND LYS-301,AND MASS SPECTROMETRY.

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