ACDSB_HUMAN - dbPTM
ACDSB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACDSB_HUMAN
UniProt AC P45954
Protein Name Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
Gene Name ACADSB
Organism Homo sapiens (Human).
Sequence Length 432
Subcellular Localization Mitochondrion matrix.
Protein Description Has greatest activity toward short branched chain acyl-CoA derivative such as (s)-2-methylbutyryl-CoA, isobutyryl-CoA, and 2-methylhexanoyl-CoA as well as toward short straight chain acyl-CoAs such as butyryl-CoA and hexanoyl-CoA. Can use valproyl-CoA as substrate and may play a role in controlling the metabolic flux of valproic acid in the development of toxicity of this agent..
Protein Sequence MEGLAVRLLRGSRLLRRNFLTCLSSWKIPPHVSKSSQSEALLNITNNGIHFAPLQTFTDEEMMIKSSVKKFAQEQIAPLVSTMDENSKMEKSVIQGLFQQGLMGIEVDPEYGGTGASFLSTVLVIEELAKVDASVAVFCEIQNTLINTLIRKHGTEEQKATYLPQLTTEKVGSFCLSEAGAGSDSFALKTRADKEGDYYVLNGSKMWISSAEHAGLFLVMANVDPTIGYKGITSFLVDRDTPGLHIGKPENKLGLRASSTCPLTFENVKVPEANILGQIGHGYKYAIGSLNEGRIGIAAQMLGLAQGCFDYTIPYIKERIQFGKRLFDFQGLQHQVAHVATQLEAARLLTYNAARLLEAGKPFIKEASMAKYYASEIAGQTTSKCIEWMGGVGYTKDYPVEKYFRDAKIGTIYEGASNIQLNTIAKHIDAEY
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
35PhosphorylationIPPHVSKSSQSEALL
CCCCCCCCCCCHHHH
26.5527251275
36PhosphorylationPPHVSKSSQSEALLN
CCCCCCCCCCHHHHH
41.2727251275
70UbiquitinationMIKSSVKKFAQEQIA
HHHHHHHHHHHHHHH
43.7221890473
70UbiquitinationMIKSSVKKFAQEQIA
HHHHHHHHHHHHHHH
43.7221890473
70UbiquitinationMIKSSVKKFAQEQIA
HHHHHHHHHHHHHHH
43.7221890473
70AcetylationMIKSSVKKFAQEQIA
HHHHHHHHHHHHHHH
43.7225953088
70SuccinylationMIKSSVKKFAQEQIA
HHHHHHHHHHHHHHH
43.7221890473
70SuccinylationMIKSSVKKFAQEQIA
HHHHHHHHHHHHHHH
43.72-
81PhosphorylationEQIAPLVSTMDENSK
HHHHHHHHCCCCCCH
26.2046157407
82PhosphorylationQIAPLVSTMDENSKM
HHHHHHHCCCCCCHH
22.5946157413
182UbiquitinationCLSEAGAGSDSFALK
ECCCCCCCCCCEEEE
30.94-
182AcetylationCLSEAGAGSDSFALK
ECCCCCCCCCCEEEE
30.94-
183PhosphorylationLSEAGAGSDSFALKT
CCCCCCCCCCEEEEE
29.5527251275
185PhosphorylationEAGAGSDSFALKTRA
CCCCCCCCEEEEECC
17.7069000345
198PhosphorylationRADKEGDYYVLNGSK
CCCCCCCEEEECCCE
13.3175089
199PhosphorylationADKEGDYYVLNGSKM
CCCCCCEEEECCCEE
11.8222817900
226PhosphorylationVMANVDPTIGYKGIT
EEECCCCCCCCCCHH
23.6728258704
229PhosphorylationNVDPTIGYKGITSFL
CCCCCCCCCCHHEEE
11.3728258704
259PhosphorylationKLGLRASSTCPLTFE
CCCCCCCCCCCCEEC
32.8026503514
284UbiquitinationGQIGHGYKYAIGSLN
EEECCHHHHEEECCC
32.5721890473
284UbiquitinationGQIGHGYKYAIGSLN
EEECCHHHHEEECCC
32.5721890473
284UbiquitinationGQIGHGYKYAIGSLN
EEECCHHHHEEECCC
32.5721890473
284SuccinylationGQIGHGYKYAIGSLN
EEECCHHHHEEECCC
32.5721890473
284AcetylationGQIGHGYKYAIGSLN
EEECCHHHHEEECCC
32.5719608861
284SuccinylationGQIGHGYKYAIGSLN
EEECCHHHHEEECCC
32.57-
285PhosphorylationQIGHGYKYAIGSLNE
EECCHHHHEEECCCC
8.5828258704
289PhosphorylationGYKYAIGSLNEGRIG
HHHHEEECCCCCCHH
23.1669008769
365AcetylationEAGKPFIKEASMAKY
HCCCCCHHHHHHHHH
47.837462021
371AcetylationIKEASMAKYYASEIA
HHHHHHHHHHHHHHC
30.1025038526
372PhosphorylationKEASMAKYYASEIAG
HHHHHHHHHHHHHCC
8.5028152594
373PhosphorylationEASMAKYYASEIAGQ
HHHHHHHHHHHHCCC
11.7128152594
413PhosphorylationDAKIGTIYEGASNIQ
CCCCCCEEECCCCCC
14.247105053
426AcetylationIQLNTIAKHIDAEY-
CCHHHHHHHHCCCC-
36.92-

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 ACDSB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACDSB_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 ACDSB_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YTHD1_HUMANYTHDF1physical
26186194
ACTZ_HUMANACTR1Aphysical
26344197
KDSR_HUMANKDSRphysical
26344197
PXDN_HUMANPXDNphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610006Short/branched-chain acyl-CoA dehydrogenase deficiency (SBCADD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00167L-Isoleucine
DB00313Valproic Acid
Regulatory Network of ACDSB_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-284, AND MASS SPECTROMETRY.

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