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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
90 | O-linked_Glycosylation | KGDEVKWSFRELGSL CCCEEEEEHHHHHHC | 14.54 | 30379171 | |
98 | Phosphorylation | FRELGSLSRKAANVL HHHHHHCCHHHHHHH | 33.17 | 24260401 | |
177 | Phosphorylation | EVAPAVESIVLECPD HHHHHHHHHEEECCC | 16.05 | 46158175 | |
262 | Phosphorylation | RYWLDLKSSDIIWNM CEEEECCCCCEEEEC | 40.31 | 22210691 | |
272 | Phosphorylation | IIWNMSDTGWVKAAI EEEECCCCCHHHHHH | 26.15 | 22210691 | |
316 | Phosphorylation | LTTYPITTLCSPPTV CCCCCCCCCCCCHHH | 26.87 | 46158181 | |
339 | Phosphorylation | LKRYKFKSLRHCLTG HHHHCCCCHHHHHHC | 33.49 | 24719451 | |
533 | Phosphorylation | SYNPEKLTLELQDHV CCCHHHEEEEHHHHH | 29.29 | 46158187 | |
547 | Phosphorylation | VKKSTAPYKYPRKVE HHHCCCCCCCCCCCH | 22.23 | 14890153 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACSM4_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ACSM4_HUMAN !! |
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. |
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Phosphorylation | |
Reference | PubMed |
"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. |