CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006270
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Long-chain-fatty-acid--CoA ligase 1 
Protein Synonyms/Alias
 Acyl-CoA synthetase 1; ACS1; Long-chain acyl-CoA synthetase 1; LACS 1; Long-chain acyl-CoA synthetase 2; LACS 2; Long-chain fatty acid-CoA ligase 2; Palmitoyl-CoA ligase 1; Palmitoyl-CoA ligase 2 
Gene Name
 ACSL1 
Gene Synonyms/Alias
 FACL1; FACL2; LACS; LACS1; LACS2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
207VDKPEKAKLLLEGVEubiquitination[1]
216LLEGVENKLIPGLKIubiquitination[1]
356RLLMDDLKVLQPTVFubiquitination[1]
622CRNKDVKKAILEDMVubiquitination[1]
633EDMVRLGKDSGLKPFubiquitination[1]
638LGKDSGLKPFEQVKGubiquitination[1]
687DDLYSTIKV******ubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
 Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate. 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 9 9 Nitrated tyrosine (By similarity).
 MOD_RES 84 84 Phosphotyrosine (By similarity).
 MOD_RES 543 543 N6-acetyllysine (By similarity).
 MOD_RES 632 632 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane; Microsome; Mitochondrion; Mitochondrion outer membrane; Nitration; Nucleotide-binding; Peroxisome; Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 698 AA 
Protein Sequence
MQAHELFRYF RMPELVDFRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKP LKPPCDLSMQ 60
SVEVAGSGGA RRSALLDSDE PLVYFYDDVT TLYEGFQRGI QVSNNGPCLG SRKPDQPYEW 120
LSYKQVAELS ECIGSALIQK GFKTAPDQFI GIFAQNRPEW VIIEQGCFAY SMVIVPLYDT 180
LGNEAITYIV NKAELSLVFV DKPEKAKLLL EGVENKLIPG LKIIVVMDAY GSELVERGQR 240
CGVEVTSMKA MEDLGRANRR KPKPPAPEDL AVICFTSGTT GNPKGAMVTH RNIVSDCSAF 300
VKATENTVNP CPDDTLISFL PLAHMFERVV ECVMLCHGAK IGFFQGDIRL LMDDLKVLQP 360
TVFPVVPRLL NRMFDRIFGQ ANTTLKRWLL DFASKRKEAE LRSGIIRNNS LWDRLIFHKV 420
QSSLGGRVRL MVTGAAPVSA TVLTFLRAAL GCQFYEGYGQ TECTAGCCLT MPGDWTAGHV 480
GAPMPCNLIK LVDVEEMNYM AAEGEGEGYL KDPAKTAEAL DKDGWLHTGD IGKWLPNGTL 540
KIIDRKKHIF KLAQGEYIAP EKIENIYMRS EPVAQVFVHG ESLQAFLIAI VVPDVETLCS 600
WAQKRGFEGS FEELCRNKDV KKAILEDMVR LGKDSGLKPF EQVKGITLHP ELFSIDNGLL 660
TPTMKAKRPE LRNYFRSQID DLYSTIKV 688 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
 GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
 GO:0033211; P:adiponectin-mediated signaling pathway; IEA:Compara.
 GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
 GO:0043651; P:linoleic acid metabolic process; TAS:Reactome.
 GO:0044539; P:long-chain fatty acid import; IDA:UniProtKB.
 GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
 GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0007584; P:response to nutrient; IEA:Compara.
 GO:0034201; P:response to oleic acid; IEA:Compara.
 GO:0014070; P:response to organic cyclic compound; IEA:Compara.
 GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome.
 GO:0042178; P:xenobiotic catabolic process; IEA:Compara. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig. 
Pfam
 PF00501; AMP-binding 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS