CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001075
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; Kidney-specific protein KS; Middle-chain acyl-CoA synthetase 2 
Gene Name
 Acsm2 
Gene Synonyms/Alias
 Ks 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
59DHWASLEKAGKRSPGacetylation[1]
141MPGTTQMKSTDILYRacetylation[1]
180DCSFLKIKLLVSEKNacetylation[1]
186IKLLVSEKNREGWLNacetylation[1]
195REGWLNFKALLKDASacetylation[1]
406GNVLPPGKEGDMALRacetylation[1]
415GDMALRVKPIRPIGMacetylation[1]
450LLGDRGIKDTEGYFHacetylation[1]
532KVLQEHVKSVTAPYKacetylation[1]
557LPKTITGKIERAKLRacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
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 359 364 ATP (By similarity).
 REGION 469 471 Coenzyme A binding (By similarity).
 REGION 540 542 Coenzyme A binding (By similarity).
 BINDING 139 139 Coenzyme A (By similarity).
 BINDING 364 364 Substrate (By similarity).
 BINDING 446 446 ATP (By similarity).
 BINDING 461 461 ATP (By similarity).
 BINDING 472 472 Substrate (By similarity).
 BINDING 501 501 Coenzyme A (By similarity).
 BINDING 532 532 Coenzyme A (By similarity).
 BINDING 557 557 ATP (By similarity).  
Keyword
 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
 572 AA 
Protein Sequence
MHWLWKIPRL CTFWGTEMFH RTFHMNIKKL MPIQWGHQEV PAKFNFASDV IDHWASLEKA 60
GKRSPGPALW WMNGSGEELK WNFRELSEIS KQTANVLTGA CGLQRGDRVA VVLPRVPEWW 120
LVTLGCMRSG LVFMPGTTQM KSTDILYRLQ SSKARAIVAG DEVVQEVDAV APDCSFLKIK 180
LLVSEKNREG WLNFKALLKD ASPIHQCVET VSQESAAIYF TSGTSGPPKM AEHSHCSLGL 240
KAKMDAGWTG LGPSDTMWTI SDTGWILNIL GSFLEPWVLG TCIFVHLLPK FDPQTVLKVL 300
SSYPINTLLG APLIYRMLLQ QDLSSYKFPH LHSCFSGGET LLPETLESWK AKTGLEIREI 360
YGQTETGITC RVSRTMKVKP GYLGTAIVPY DVQVIDEQGN VLPPGKEGDM ALRVKPIRPI 420
GMFSGYVDNP KKTQANIRGD FWLLGDRGIK DTEGYFHFMG RTDDIINSSG YRIGPSEVEN 480
ALMEHPAVVE TAVISSPDPI RREVVKAFVV LAPEFLSHDQ DQLTKVLQEH VKSVTAPYKY 540
PRKVEFVLDL PKTITGKIER AKLRAKEWKT SG 572 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 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
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig.
 IPR025110; DUF4009. 
Pfam
 PF00501; AMP-binding
 PF13193; DUF4009 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS