CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018709
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Long-chain-fatty-acid--CoA ligase ACSBG1 
Protein Synonyms/Alias
 Acyl-CoA synthetase bubblegum family member 1; Gonadotropin-regulated long chain acyl CoA synthetase; GR-LACS 
Gene Name
 Acsbg1 
Gene Synonyms/Alias
 Grlacs 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
51IDGRTLSKESPSHGLacetylation[1]
65LELSAPEKARAASLDubiquitination[2]
211VIVVDTQKQLEKILKacetylation[1]
211VIVVDTQKQLEKILKubiquitination[2]
215DTQKQLEKILKIWKDacetylation[1]
218KQLEKILKIWKDLPHacetylation[1]
221EKILKIWKDLPHLKAacetylation[1]
238IYQEPPPKKMANVYTacetylation[1]
639FCQRVGSKASTVSEIubiquitination[2]
650VSEIVGQKDEAVYQAacetylation[1]
678ARPYHIQKWAILERDacetylation[1]
709LTVLEKYKDIIDSFYacetylation[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]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional Description
 Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Able to activate long-chain fatty acids. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids. 
Sequence Annotation
 NP_BIND 279 287 ATP (By similarity).
 NP_BIND 469 474 ATP (By similarity).
 BINDING 547 547 ATP (By similarity).
 BINDING 562 562 ATP (By similarity).
 BINDING 698 698 ATP (By similarity).
 MOD_RES 655 655 Phosphotyrosine (By similarity).  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism; Microsome; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 721 AA 
Protein Sequence
MPRSSEAGYC CLSRDSNMPD SRDDQQQGAS MGTSPDNSQT SSLIDGRTLS KESPSHGLEL 60
SAPEKARAAS LDASEEALWT TRADGRVRLR LEPFCTQLPY TVHQMFYEAL DKYGNLSALG 120
FKRKDKWERI SYYQYYLIAR KVAKGFLKLG LERAHSVAIL GFNSPEWFFS AVGTVFAGGI 180
VTGIYTTSSP EACQYIAHDC RANVIVVDTQ KQLEKILKIW KDLPHLKAVV IYQEPPPKKM 240
ANVYTMEELI ELGQEVPEEA LDAIIDTQQP NQCCVLVYTS GTTGNPKGVM LSQDNITWTA 300
RYGSQAGDIQ PAEVQQEVVV SYLPLSHIAA QIYDLWTGIQ WGAQVCFADP DALKGTLVNT 360
LREVEPTSHM GVPRVWEKIM ERIQEVAAQS GFIRRKMLLW AMSVTLEQNL TCPSNDLKPF 420
TSRLADYLVL ARVRQALGFA KCQKNFYGAA PMTAETQRFF LGLNIRLYAG YGLSESTGPH 480
FMSSPYNYRL YSSGRVVPGC RVKLVNQDAD GIGEICLWGR TIFMGYLNME DKTHEAIDSE 540
GWLHTGDMGR LDDDGFLYIT GRLKELIITA GGENVPPVPI EEAVKMELPI ISSAMLIGDQ 600
RKFLSMLLTL KCTLNPETSE PTDNLTEQAV EFCQRVGSKA STVSEIVGQK DEAVYQAIHE 660
GIQRVNANAA ARPYHIQKWA ILERDFSISG GELGPTMKLK RLTVLEKYKD IIDSFYQEQK 720
Q 721 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:RGD.
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004467; F:long-chain fatty acid-CoA ligase activity; ISS:HGNC.
 GO:0031957; F:very long-chain fatty acid-CoA ligase activity; ISS:HGNC.
 GO:0001552; P:ovarian follicle atresia; IEP:RGD.
 GO:0051384; P:response to glucocorticoid stimulus; IEA:Compara.
 GO:0000038; P:very long-chain fatty acid metabolic process; ISS:HGNC. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig. 
Pfam
 PF00501; AMP-binding 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS