ACSM4_HUMAN - dbPTM
ACSM4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ACSM4_HUMAN
UniProt AC P0C7M7
Protein Name Acyl-coenzyme A synthetase ACSM4, mitochondrial
Gene Name ACSM4
Organism Homo sapiens (Human).
Sequence Length 580
Subcellular Localization Mitochondrion matrix.
Protein Description Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro) (By similarity)..
Protein Sequence MKIFFRYQTFRFIWLTKPPGRRLHKDHQLWTPLTLADFEAINRCNRPLPKNFNFAADVLDQWSQKEKTGERPANPALWWVNGKGDEVKWSFRELGSLSRKAANVLTKPCGLQRGDRLAVILPRIPEWWLVNVACIRTGIIFMPGTIQLTAKDILYRLRASKAKCIVASEEVAPAVESIVLECPDLKTKLLVSPQSWNGWLSFQELFQFASEEHSCVETGSQEPMTIYFTSGTTGFPKMAQHSQSSLGIGFTLCGRYWLDLKSSDIIWNMSDTGWVKAAIGSVFSSWLCGACVFVHRMAQFDTDTFLDTLTTYPITTLCSPPTVYRMLVQKDLKRYKFKSLRHCLTGGEPLNPEVLEQWRVQTGLELYEGYGQTEVGMICANQKGQEIKPGSMGKGMLPYDVQIIDENGNVLPPGKEGEIALRLKPTRPFCFFSKYVDNPQKTAATIRGDFYVTGDRGVMDSDGYFWFVGRADDVIISSGYRIGPFEVESALIEHPAVVESAVVSSPDQIRGEVVKAFVVLAAPFKSYNPEKLTLELQDHVKKSTAPYKYPRKVEFVQELPKTITGKIKRNVLRDQEWRGR
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
90O-linked_GlycosylationKGDEVKWSFRELGSL
CCCEEEEEHHHHHHC
14.5430379171
98PhosphorylationFRELGSLSRKAANVL
HHHHHHCCHHHHHHH
33.1724260401
177PhosphorylationEVAPAVESIVLECPD
HHHHHHHHHEEECCC
16.0546158175
262PhosphorylationRYWLDLKSSDIIWNM
CEEEECCCCCEEEEC
40.3122210691
272PhosphorylationIIWNMSDTGWVKAAI
EEEECCCCCHHHHHH
26.1522210691
316PhosphorylationLTTYPITTLCSPPTV
CCCCCCCCCCCCHHH
26.8746158181
339PhosphorylationLKRYKFKSLRHCLTG
HHHHCCCCHHHHHHC
33.4924719451
533PhosphorylationSYNPEKLTLELQDHV
CCCHHHEEEEHHHHH
29.2946158187
547PhosphorylationVKKSTAPYKYPRKVE
HHHCCCCCCCCCCCH
22.2314890153

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 ACSM4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ACSM4_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 ACSM4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ACSM4_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 ACSM4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-547, AND MASSSPECTROMETRY.

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