ACADM_MOUSE - dbPTM
ACADM_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACADM_MOUSE
UniProt AC P45952
Protein Name Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
Gene Name Acadm
Organism Mus musculus (Mouse).
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 MAAAFRRGCRVLRSVSHFECRTQHSKAAHKQEPGLGFSFELTEQQKEFQATARKFAREEIIPVAPEYDKSGEYPFPLIKRAWELGLINAHIPESCGGLGLGTFDACLITEELAYGCTGVQTAIEANSLGQMPVILAGNDQQKKKYLGRMTEQPMMCAYCVTEPSAGSDVAAIKTKAEKKGDEYVINGQKMWITNGGKANWYFLLARSNPDPKVPASKAFTGFIVEADTPGIHIGKKELNMGQRCSDTRGIAFEDVRVPKENVLIGEGAGFKIAMGAFDRTRPTVAAGAVGLAQRALDEATKYALDRKTFGKLLVEHQGVSFLLAEMAMKVELARLSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQIFGGYGFNTEYPVEKLMRDAKIYQIYEGTAQIQRLIIAREHIEKYKN
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
30AcetylationQHSKAAHKQEPGLGF
CCCHHHHCCCCCCCE		52.1823576753
30SuccinylationQHSKAAHKQEPGLGF
CCCHHHHCCCCCCCE		52.1823806337
30SuccinylationQHSKAAHKQEPGLGF
CCCHHHHCCCCCCCE		52.18-
46AcetylationFELTEQQKEFQATAR
EEECHHHHHHHHHHH		61.2623954790
69AcetylationPVAPEYDKSGEYPFP
CCCCCCCCCCCCCCH		60.5023576753
69SuccinylationPVAPEYDKSGEYPFP
CCCCCCCCCCCCCCH		60.5023806337
69SuccinylationPVAPEYDKSGEYPFP
CCCCCCCCCCCCCCH		60.50-
70PhosphorylationVAPEYDKSGEYPFPL
CCCCCCCCCCCCCHH		33.6822817900
79AcetylationEYPFPLIKRAWELGL
CCCCHHHHHHHHHCC		43.6923576753
79SuccinylationEYPFPLIKRAWELGL
CCCCHHHHHHHHHCC		43.69-
79UbiquitinationEYPFPLIKRAWELGL
CCCCHHHHHHHHHCC		43.69-
79GlutarylationEYPFPLIKRAWELGL
CCCCHHHHHHHHHCC		43.6924703693
158PhosphorylationEQPMMCAYCVTEPSA
CCCEEEEEEECCCCC		5.1928576409
173SuccinylationGSDVAAIKTKAEKKG
CCCEEEEEEHHHHCC		38.9726388266
173AcetylationGSDVAAIKTKAEKKG
CCCEEEEEEHHHHCC		38.9723864654
175AcetylationDVAAIKTKAEKKGDE
CEEEEEEHHHHCCCE		49.9323864654
178AcetylationAIKTKAEKKGDEYVI
EEEEHHHHCCCEEEE		67.9023864654
179SuccinylationIKTKAEKKGDEYVIN
EEEHHHHCCCEEEEC		64.2023806337
179GlutarylationIKTKAEKKGDEYVIN
EEEHHHHCCCEEEEC		64.2024703693
179SuccinylationIKTKAEKKGDEYVIN
EEEHHHHCCCEEEEC		64.20-
179AcetylationIKTKAEKKGDEYVIN
EEEHHHHCCCEEEEC		64.2024062335
212SuccinylationARSNPDPKVPASKAF
EECCCCCCCCHHHHC		69.1323806337
212GlutarylationARSNPDPKVPASKAF
EECCCCCCCCHHHHC		69.1324703693
212SuccinylationARSNPDPKVPASKAF
EECCCCCCCCHHHHC		69.13-
212MalonylationARSNPDPKVPASKAF
EECCCCCCCCHHHHC		69.1326320211
212AcetylationARSNPDPKVPASKAF
EECCCCCCCCHHHHC		69.1323576753
217SuccinylationDPKVPASKAFTGFIV
CCCCCHHHHCCEEEE		50.0223806337
217SuccinylationDPKVPASKAFTGFIV
CCCCCHHHHCCEEEE		50.02-
217AcetylationDPKVPASKAFTGFIV
CCCCCHHHHCCEEEE		50.0223576753
217GlutarylationDPKVPASKAFTGFIV
CCCCCHHHHCCEEEE		50.0224703693
235AcetylationTPGIHIGKKELNMGQ
CCCEEECCCCCCCCC		42.3323576753
235SuccinylationTPGIHIGKKELNMGQ
CCCEEECCCCCCCCC		42.33-
235SuccinylationTPGIHIGKKELNMGQ
CCCEEECCCCCCCCC		42.3323806337
235UbiquitinationTPGIHIGKKELNMGQ
CCCEEECCCCCCCCC		42.33-
236AcetylationPGIHIGKKELNMGQR
CCEEECCCCCCCCCC		63.3224062335
244S-nitrosylationELNMGQRCSDTRGIA
CCCCCCCCCCCCCCC		3.1221278135
244S-nitrosocysteineELNMGQRCSDTRGIA
CCCCCCCCCCCCCCC		3.12-
259MalonylationFEDVRVPKENVLIGE
CCCCCCCHHHEEEEC		60.0926320211
259GlutarylationFEDVRVPKENVLIGE
CCCCCCCHHHEEEEC		60.0924703693
259SuccinylationFEDVRVPKENVLIGE
CCCCCCCHHHEEEEC		60.09-
259SuccinylationFEDVRVPKENVLIGE
CCCCCCCHHHEEEEC		60.0923806337
259AcetylationFEDVRVPKENVLIGE
CCCCCCCHHHEEEEC		60.0923576753
271AcetylationIGEGAGFKIAMGAFD
EECCCCCEEEEECCC		28.7423576753
271SuccinylationIGEGAGFKIAMGAFD
EECCCCCEEEEECCC		28.7423806337
271SuccinylationIGEGAGFKIAMGAFD
EECCCCCEEEEECCC		28.74-
301AcetylationRALDEATKYALDRKT
HHHHHHHHHHHHHCC		35.2623576753
301UbiquitinationRALDEATKYALDRKT
HHHHHHHHHHHHHCC		35.2622790023
311SuccinylationLDRKTFGKLLVEHQG
HHHCCHHHHHHHHHC		34.1624315375
311AcetylationLDRKTFGKLLVEHQG
HHHCCHHHHHHHHHC		34.1624062335
351PhosphorylationVDSGRRNTYYASIAK
CCCCCCCCHHHHHHH		18.9827180971
352PhosphorylationDSGRRNTYYASIAKA
CCCCCCCHHHHHHHH		10.6923140645
353PhosphorylationSGRRNTYYASIAKAF
CCCCCCHHHHHHHHH		7.5823140645
395UbiquitinationEKLMRDAKIYQIYEG
HHHHHHCCEEEEEEC		46.3522790023
418AcetylationIAREHIEKYKN----
HHHHHHHHHCC----		62.0023864654
420AcetylationREHIEKYKN------
HHHHHHHCC------		68.222381229
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of ACADM_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ACADM_MOUSE

loading...

Related Literatures of Post-Translational Modification

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