CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007971
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Long-chain-fatty-acid--CoA ligase 4 
Protein Synonyms/Alias
 Fatty acid activator 4; Long-chain acyl-CoA synthetase 4 
Gene Name
 FAA4 
Gene Synonyms/Alias
 YMR246W; YM9408.08 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
83KRVDGKDKPIEKTWLubiquitination[1]
192SKLAVPLKTAKNVKFubiquitination[1]
397FWTVYALKERNIPCSubiquitination[1]
413LLSGLIFKRIREATGubiquitination[1]
496EDLGYFAKNNQGELLubiquitination[1, 2]
505NQGELLFKGAPICSEubiquitination[1]
515PICSEYYKNPEETAAubiquitination[1, 2]
541DIAEWTPKGQVKIIDubiquitination[1]
626ESYIHEKKLQDAVCKubiquitination[1]
633KLQDAVCKDMLSTAKubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047] 
Functional Description
 Esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Contributes, with FAA1, to the activation of imported myristate. 
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 694 AA 
Protein Sequence
MTEQYSVAVG EAANEHETAP RRNIRVKDQP LIRPINSSAS TLYEFALECF TKGGKRDGMA 60
WRDIIDIHET KKTIVKRVDG KDKPIEKTWL YYELTPYITM TYEEMICVMH DIGRGLIKIG 120
VKPNGENKFH IFASTSHKWM KTFLGCMSQG IPVVTAYDTL GESGLIHSMV ETDSVAIFTD 180
NQLLSKLAVP LKTAKNVKFV IHNEPIDPSD KRQNGKLYKA AKDAVDKIKE VRPDIKIYSF 240
DEIIEIGKKA KDEVELHFPK PEDPACIMYT SGSTGTPKGV VLTHYNIVAG IGGVGHNVIG 300
WIGPTDRIIA FLPLAHIFEL TFEFEAFYWN GILGYANVKT LTPTSTRNCQ GDLMEFKPTV 360
MVGVAAVWET VRKGILAKIN ELPGWSQTLF WTVYALKERN IPCSGLLSGL IFKRIREATG 420
GNLRFILNGG SAISIDAQKF LSNLLCPMLI GYGLTEGVAN ACVLEPEHFD YGIAGDLVGT 480
ITAKLVDVED LGYFAKNNQG ELLFKGAPIC SEYYKNPEET AAAFTDDGWF RTGDIAEWTP 540
KGQVKIIDRK KNLVKTLNGE YIALEKLESI YRSNPYVQNI CVYADENKVK PVGIVVPNLG 600
HLSKLAIELG IMVPGEDVES YIHEKKLQDA VCKDMLSTAK SQGLNGIELL CGIVFFEEEW 660
TPENGLVTSA QKLKRRDILA AVKPDVERVY KENT 694 
Gene Ontology
 GO:0005811; C:lipid particle; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:SGD.
 GO:0015909; P:long-chain fatty acid transport; IGI:SGD.
 GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IMP:SGD. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig. 
Pfam
 PF00501; AMP-binding 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS