CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-032012
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Long-chain-fatty-acid--CoA ligase 1 
Protein Synonyms/Alias
 cDNA FLJ53511, highly similar to Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) 
Gene Name
 ACSL1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
36VDKPEKAKLLLEGVEubiquitination[1]
45LLEGVENKLIPGLKIubiquitination[1, 2, 3]
185RLLMDDLKVLQPTVFubiquitination[1, 4, 5]
224WLLDFASKRKEAELRubiquitination[2, 4]
248WDRLIFHKVQSSLGGubiquitination[2, 3, 4]
350NVFQGYLKDPAKTAEubiquitination[5]
361KTAEALDKDGWLHTGubiquitination[2]
461CRNKDVKKAILEDMVubiquitination[1]
472EDMVRLGKDSGLKPFubiquitination[1]
477LGKDSGLKPFEQVKGubiquitination[1]
526DDLYSTIKV******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]
 [2] 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]
 [3] 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]
 [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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Ligase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 527 AA 
Protein Sequence
MVIVPLYDTL GNEAITYIVN KAELSLVFVD KPEKAKLLLE GVENKLIPGL KIIVVMDAYG 60
SELVERGQRC GVEVTSMKAM EDLGRANRRK PKPPAPEDLA VICFTSGTTG NPKGAMVTHR 120
NIVSDCSAFV KATENTVNPC PDDTLISFLP LAHMFERVVE CVMLCHGAKI GFFQGDIRLL 180
MDDLKVLQPT VFPVVPRLLN RMFDRIFGQA NTTLKRWLLD FASKRKEAEL RSGIIRNNSL 240
WDRLIFHKVQ SSLGGRVRLM VTGAAPVSAT VLTFLRAALG CQFYEGYGQT ECTAGCCLTM 300
PGDWTAGHVG APMPCNLIKL VDVEEMNYMA AEGEGEVCVK GPNVFQGYLK DPAKTAEALD 360
KDGWLHTGDI GKWLPNGTLK IIDRKKHIFK LAQGEYIAPE KIENIYMRSE PVAQVFVHGE 420
SLQAFLIAIV VPDVETLCSW AQKRGFEGSF EELCRNKDVK KAILEDMVRL GKDSGLKPFE 480
QVKGITLHPE LFSIDNGLLT PTMKAKRPEL RNYFRSQIDD LYSTIKV 527 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IEA:Compara.
 GO:0005741; C:mitochondrial outer membrane; IEA:Compara.
 GO:0005778; C:peroxisomal membrane; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:Compara.
 GO:0033211; P:adiponectin-mediated signaling pathway; IEA:Compara.
 GO:0015908; P:fatty acid transport; IEA:Compara.
 GO:0001676; P:long-chain fatty acid metabolic process; IEA:GOC.
 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:0006641; P:triglyceride metabolic process; IEA:Compara.
 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