| Tag | Content |
|---|
| CPLM ID | CPLM-017192 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Acyl-coenzyme A synthetase ACSM2, mitochondrial |
Protein Synonyms/Alias | Acyl-CoA synthetase medium-chain family member 2; Butyrate--CoA ligase 2; Butyryl-coenzyme A synthetase 2; Middle-chain acyl-CoA synthetase 2 |
Gene Name | Acsm2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 84 | DHWASVEKAGKRSSG | ubiquitination | [1] | | 203 | APDCSFLKIKLLVSE | ubiquitination | [1] | | 205 | DCSFLKIKLLVSENS | ubiquitination | [1] | | 224 | LNFKALLKEASTIHQ | ubiquitination | [1] | | 378 | TLENWKAKTGLEIRE | ubiquitination | [1] | | 476 | LMGDRGIKDPEGYFH | ubiquitination | [1] | | 583 | LPKTVTGKIERAKLR | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
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 (By similarity).
NP_BIND 360 365 ATP (By similarity).
REGION 470 472 Coenzyme A binding (By similarity).
REGION 541 543 Coenzyme A binding (By similarity).
BINDING 139 139 Coenzyme A (By similarity).
BINDING 365 365 Substrate (By similarity).
BINDING 447 447 ATP (By similarity).
BINDING 462 462 ATP (By similarity).
BINDING 473 473 Substrate (By similarity).
BINDING 502 502 Coenzyme A (By similarity).
BINDING 533 533 Coenzyme A (By similarity).
BINDING 558 558 ATP (By similarity). |
Keyword | Alternative splicing; ATP-binding; Complete proteome; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Metal-binding; Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 575 AA |
Protein Sequence | MTTGSLDLPF VGSHRWIKWT TASLTMHHLW KIPRLFTLWG NEISCRTFHM NIKKLIPIQW 60
GHQEAPAKFN FASDVIDHWA SVEKAGKRSS GPALWWMNGS GKEIKWSFRE LSEASKQTAN 120
VLSGACGLHR GDRVAVVLPR IPEWWLMILG CMRTGLVFMP GTIQMRSSDI LYRLQASKAR 180
AIVAGDEVAQ EVDAVAPDCS FLKIKLLVSE NSREGWLNFK ALLKEASTIH QCVETESRES 240
AAIYFTSGTS GPPKMAEHSH CSLGIKAKMD AASWTGLSTS DIIWTISDTA WIMNILGAFL 300
EPWVLGACIF VHLLPKFDSQ TVLKVLSSYP INTLVGAPII YRMLLQQDLS SYKFPHLHSC 360
FSGGETLLPE TLENWKAKTG LEIREIYGQT ETGLICRVSR TMKVKPGYLG TAFAHYDVQV 420
IDEQGNVLPP GKEGDIAIRV KPIWPIGMFS GYVDNPKKTQ DNIRGDFWLM GDRGIKDPEG 480
YFHFIGRSDD IINSSGYRIG PSEVENALME HPAVSETAVI SSPDPSRGEV VKAFVVLAPE 540
FLSHDRDQLT KVLQEHVKSV TAPYKYPRKV EFVLDLPKTV TGKIERAKLR AKEWKTSGRA 600 |
Gene Ontology | GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. GO:0005739; C:mitochondrion; IDA:MGI. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0047760; F:butyrate-CoA ligase activity; IEA:EC. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |