CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001623
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Long-chain-fatty-acid--CoA ligase 3 
Protein Synonyms/Alias
 Long-chain acyl-CoA synthetase 3; LACS 3 
Gene Name
 ACSL3 
Gene Synonyms/Alias
 ACS3; FACL3; LACS3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
13SSKPSTMKLKHTINPubiquitination[1]
63KAKPVNSKPDSAYRSubiquitination[2]
122DEVQPNGKIFKKVILubiquitination[1, 3, 4, 5]
157GLQMLGQKPKTNIAIubiquitination[1, 2, 4]
220SKELLQTKLKDIVSLubiquitination[2, 4]
222ELLQTKLKDIVSLVPubiquitination[2]
240HIITVDGKPPTWSEFubiquitination[2]
363TLADQSSKIKKGSKGubiquitination[1, 2, 4]
376KGDTSMLKPTLMAAVubiquitination[4]
392EIMDRIYKNVMNKVSubiquitination[2]
397IYKNVMNKVSEMSSFubiquitination[1, 2, 4]
507PLVCCEIKLKNWEEGubiquitination[2]
509VCCEIKLKNWEEGGYubiquitination[2]
547YKNEAKTKADFFEDEubiquitination[1, 2, 4, 6]
673AISASLEKFEIPVKIacetylation[7]
679EKFEIPVKIRLSPEPubiquitination[1, 3, 4, 5]
706KLKRKELKTHYQADIacetylation[7]
706KLKRKELKTHYQADIubiquitination[4]
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]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 mediates hepatic lipogenesis (By similarity). Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates (By similarity). Has mainly an anabolic role in energy metabolism. Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins). 
Sequence Annotation
 MOD_RES 683 683 Phosphoserine.  
Keyword
 ATP-binding; Complete proteome; Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane; Microsome; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding; Peroxisome; Phosphoprotein; Polymorphism; Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 720 AA 
Protein Sequence
MNNHVSSKPS TMKLKHTINP ILLYFIHFLI SLYTILTYIP FYFFSESRQE KSNRIKAKPV 60
NSKPDSAYRS VNSLDGLASV LYPGCDTLDK VFTYAKNKFK NKRLLGTREV LNEEDEVQPN 120
GKIFKKVILG QYNWLSYEDV FVRAFNFGNG LQMLGQKPKT NIAIFCETRA EWMIAAQACF 180
MYNFQLVTLY ATLGGPAIVH ALNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK 240
PPTWSEFPKG IIVHTMAAVE ALGAKASMEN QPHSKPLPSD IAVIMYTSGS TGLPKGVMIS 300
HSNIIAGITG MAERIPELGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG YSSPQTLADQ 360
SSKIKKGSKG DTSMLKPTLM AAVPEIMDRI YKNVMNKVSE MSSFQRNLFI LAYNYKMEQI 420
SKGRNTPLCD SFVFRKVRSL LGGNIRLLLC GGAPLSATTQ RFMNICFCCP VGQGYGLTES 480
AGAGTISEVW DYNTGRVGAP LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQSVTMGYY 540
KNEAKTKADF FEDENGQRWL CTGDIGEFEP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA 600
LKNLPLVDNI CAYANSYHSY VIGFVVPNQK ELTELARKKG LKGTWEELCN SCEMENEVLK 660
VLSEAAISAS LEKFEIPVKI RLSPEPWTPE TGLVTDAFKL KRKELKTHYQ ADIERMYGRK 720 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005811; C:lipid particle; IDA:UniProtKB.
 GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004467; F:long-chain fatty acid-CoA ligase activity; IMP:UniProtKB.
 GO:0007420; P:brain development; IEA:Compara.
 GO:0006633; P:fatty acid biosynthetic process; IEA:Compara.
 GO:0044539; P:long-chain fatty acid import; IDA:UniProtKB.
 GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; IMP:UniProtKB.
 GO:2001247; P:positive regulation of phosphatidylcholine biosynthetic process; IMP:UniProtKB.
 GO:0051047; P:positive regulation of secretion; IMP:UniProtKB.
 GO:0007584; P:response to nutrient; IEA:Compara.
 GO:0014070; P:response to organic cyclic compound; IEA:Compara.
 GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:UniProtKB. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig. 
Pfam
 PF00501; AMP-binding 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS