| Tag | Content |
|---|
| CPLM ID | CPLM-011662 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Acyl-coenzyme A synthetase ACSM2A, mitochondrial |
Protein Synonyms/Alias | Acyl-CoA synthetase medium-chain family member 2A; Butyrate--CoA ligase 2A; Butyryl-coenzyme A synthetase 2A; Middle-chain acyl-CoA synthetase 2A |
Gene Name | ACSM2A |
Gene Synonyms/Alias | ACSM2; MACS2 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 298 | FDPLVILKTLSSYPI | acetylation | [1] |
|
Reference | [1] Regulation of cellular metabolism by protein lysine acetylation. Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL. Science. 2010 Feb 19;327(5968):1000-4. [ PMID: 20167786] |
Functional 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). |
Sequence Annotation | NP_BIND 221 229 ATP.
NP_BIND 359 364 ATP.
REGION 469 471 Coenzyme A binding.
REGION 540 542 Coenzyme A binding.
BINDING 139 139 Coenzyme A.
BINDING 364 364 Substrate.
BINDING 446 446 ATP.
BINDING 461 461 ATP.
BINDING 472 472 Substrate.
BINDING 501 501 Coenzyme A.
BINDING 532 532 Coenzyme A.
BINDING 557 557 ATP. |
Keyword | 3D-structure; ATP-binding; Complete proteome; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding; Polymorphism; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 577 AA |
Protein Sequence | MHWLRKVQGL CTLWGTQMSS RTLYINSRQL VSLQWGHQEV PAKFNFASDV LDHWADMEKA 60
GKRLPSPALW WVNGKGKELM WNFRELSENS QQAANVLSGA CGLQRGDRVA VVLPRVPEWW 120
LVILGCIRAG LIFMPGTIQM KSTDILYRLQ MSKAKAIVAG DEVIQEVDTV ASECPSLRIK 180
LLVSEKSCDG WLNFKKLLNE ASTTHHCVET GSQEASAIYF TSGTSGLPKM AEHSYSSLGL 240
KAKMDAGWTG LQASDIMWTI SDTGWILNIL CSLMEPWALG ACTFVHLLPK FDPLVILKTL 300
SSYPIKSMMG APIVYRMLLQ QDLSSYKFPH LQNCVTVGES LLPETLENWR AQTGLDIRES 360
YGQTETGLTC MVSKTMKIKP GYMGTAASCY DVQIIDDKGN VLPPGTEGDI GIRVKPIRPI 420
GIFSGYVDNP DKTAANIRGD FWLLGDRGIK DEDGYFQFMG RANDIINSSG YRIGPSEVEN 480
ALMEHPAVVE TAVISSPDPV RGEVVKAFVV LASQFLSHDP EQLTKELQQH VKSVTAPYKY 540
PRKIEFVLNL PKTVTGKIQR AKLRDKEWKM SGKARAQ 577 |
Gene Ontology | GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. GO:0005739; C:mitochondrion; NAS:BHF-UCL. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0047760; F:butyrate-CoA ligase activity; IDA:BHF-UCL. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. GO:0042593; P:glucose homeostasis; NAS:BHF-UCL. GO:0036112; P:medium-chain fatty-acyl-CoA metabolic process; IDA:BHF-UCL. GO:0070328; P:triglyceride homeostasis; NAS:BHF-UCL. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |