CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004735
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fatty acid synthase subunit alpha 
Protein Synonyms/Alias
 Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase; Beta-ketoacyl reductase; 3-oxoacyl-[acyl-carrier-protein] synthase; Beta-ketoacyl synthase 
Gene Name
 FAS2 
Gene Synonyms/Alias
 YPL231W; P1409 
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
37ETQDVFLKDFNTERVacetylation[1]
37ETQDVFLKDFNTERVubiquitination[2, 3]
64AQRTLKNKYESYDAAacetylation[1]
64AQRTLKNKYESYDAAubiquitination[3]
83REILCYSKDAKEIYYacetylation[1]
83REILCYSKDAKEIYYubiquitination[3]
86LCYSKDAKEIYYTPDacetylation[1]
86LCYSKDAKEIYYTPDubiquitination[3]
100DPSELAAKEEPAKEEacetylation[1]
105AAKEEPAKEEAPAPTubiquitination[3]
158LHVLVAHKLKKSLDSubiquitination[3]
161LVAHKLKKSLDSIPMubiquitination[3]
170LDSIPMSKTIKDLVGacetylation[1]
170LDSIPMSKTIKDLVGubiquitination[3]
173IPMSKTIKDLVGGKSacetylation[1]
236LSRLISSKMPGGFTIubiquitination[3]
284LGSEADAKAFLDSMAacetylation[1]
351QVLARYLKMDLDNGEacetylation[1]
351QVLARYLKMDLDNGEubiquitination[3]
462ISNTDETKGENYQLVubiquitination[3]
481EQLIENCKQVLDVDPubiquitination[3]
491LDVDPVYKDVAKPTGubiquitination[3]
495PVYKDVAKPTGPKTAubiquitination[3]
505GPKTAIDKNGNITYSacetylation[1]
505GPKTAIDKNGNITYSubiquitination[3]
521EPREKVRKLSQYVQEacetylation[1]
521EPREKVRKLSQYVQEubiquitination[3]
537ALGGPITKESQPTIEubiquitination[3]
552EDLTRVYKAISAQADacetylation[1]
552EDLTRVYKAISAQADubiquitination[3]
560AISAQADKQDISSSTacetylation[1]
560AISAQADKQDISSSTubiquitination[3]
573STRVEFEKLYSDLMKubiquitination[3]
580KLYSDLMKFLESSKEacetylation[1]
580KLYSDLMKFLESSKEubiquitination[3]
607DVEDALDKDSTKEVAubiquitination[3]
619EVASLPNKSTISKTVubiquitination[3]
624PNKSTISKTVSSTIPacetylation[1]
624PNKSTISKTVSSTIPubiquitination[3]
650KTPAGDWKYDRQLSSacetylation[1]
650KTPAGDWKYDRQLSSubiquitination[3]
665LFLDGLEKAAFNGVTubiquitination[3]
674AFNGVTFKDKYVLITacetylation[1]
674AFNGVTFKDKYVLITubiquitination[3]
676NGVTFKDKYVLITGAacetylation[1]
712VTTSRFSKQVTDYYQacetylation[1]
712VTTSRFSKQVTDYYQubiquitination[3]
724YYQSIYAKYGAKGSTubiquitination[3]
728IYAKYGAKGSTLIVVubiquitination[3]
807LRMMGCVKKQKSARGubiquitination[3]
890IIAEGIEKMGVRTFSacetylation[1]
899GVRTFSQKEMAFNLLubiquitination[3]
937LQFVPELKEFTAKLRacetylation[1]
945EFTAKLRKELVETSEacetylation[1]
955VETSEVRKAVSIETAacetylation[1]
996QLDFPELKPYKQVKQacetylation[1]
999FPELKPYKQVKQIAPubiquitination[3]
1002LKPYKQVKQIAPAELubiquitination[3]
1079YTGWVDSKTKEPVDDacetylation[1]
1087TKEPVDDKDVKAKYEacetylation[1]
1092DDKDVKAKYETSILEacetylation[1]
1118FNGYNPEKKEMIQEVacetylation[1]
1145KETAEQFKHQHGDKVacetylation[1]
1151FKHQHGDKVDIFEIPacetylation[1]
1166ETGEYSVKLLKGATLacetylation[1]
1169EYSVKLLKGATLYIPacetylation[1]
1177GATLYIPKALRFDRLacetylation[1]
1177GATLYIPKALRFDRLubiquitination[3]
1323VETILSGKARICIVGacetylation[1]
1413MAATATDKIGRSVPAacetylation[1]
1413MAATATDKIGRSVPAubiquitination[3]
1423RSVPAPGKGILTTARacetylation[1]
1423RSVPAPGKGILTTARubiquitination[3]
1437REHHSSVKYASPNLNacetylation[1]
1446ASPNLNMKYRKRQLVacetylation[1]
1446ASPNLNMKYRKRQLVubiquitination[3]
1514QWGNDFYKRDPRIAPacetylation[1]
1514QWGNDFYKRDPRIAPubiquitination[3]
1551TSTKANDKNESATINacetylation[1]
1551TSTKANDKNESATINubiquitination[3]
1562ATINEMMKHLGRSEGacetylation[1]
1585KFLTGHPKGAAGAWMubiquitination[3]
1629EYVLYPSKTLKTDGVacetylation[1]
1632LYPSKTLKTDGVRAVacetylation[1]
1632LYPSKTLKTDGVRAVubiquitination[3]
1676RYNEYVAKVSAREKSacetylation[1]
1686AREKSAYKFFHNGMIacetylation[1]
1686AREKSAYKFFHNGMIubiquitination[3]
1696HNGMIYNKLFVSKEHubiquitination[3]
1701YNKLFVSKEHAPYTDubiquitination[3]
1727ARVSKDKKSGSLTFNubiquitination[3]
1736GSLTFNSKNIQSKDSacetylation[1]
1736GSLTFNSKNIQSKDSubiquitination[3]
1741NSKNIQSKDSYINANacetylation[1]
1741NSKNIQSKDSYINANubiquitination[3]
1754ANTIETAKMIENMTKubiquitination[3]
1761KMIENMTKEKVSNGGubiquitination[3]
1821SAKEAVFKSLGVKSLacetylation[1]
1826VFKSLGVKSLGGGAAacetylation[1]
1826VFKSLGVKSLGGGAAubiquitination[3]
1835LGGGAALKDIEIVRVacetylation[1]
1844IEIVRVNKNAPAVELubiquitination[3]
1857ELHGNAKKAAEEAGVubiquitination[3]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [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]
 [3] 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] 
Functional Description
 Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3- oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl- carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex. 
Sequence Annotation
 DOMAIN 140 301 Acyl carrier.
 REGION 675 874 Beta-ketoacyl reductase.
 REGION 1149 1363 Beta-ketoacyl synthase.
 REGION 1772 1774 Acetyl-CoA binding.
 REGION 1817 1833 Acetyl-CoA binding.
 REGION 1841 1844 Acetyl-CoA binding.
 REGION 1871 1873 Acetyl-CoA binding.
 ACT_SITE 1305 1305 For beta-ketoacyl synthase activity.
 METAL 1772 1772 Magnesium.
 METAL 1773 1773 Magnesium; via carbonyl oxygen.
 METAL 1774 1774 Magnesium.
 METAL 1872 1872 Magnesium.
 METAL 1873 1873 Magnesium; via carbonyl oxygen.
 BINDING 1798 1798 Acetyl-CoA.
 BINDING 1808 1808 Acetyl-CoA.
 MOD_RES 180 180 O-(pantetheine 4'-phosphoryl)serine.
 MOD_RES 523 523 Phosphoserine.
 MOD_RES 958 958 Phosphoserine.
 MOD_RES 1440 1440 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding; Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1887 AA 
Protein Sequence
MKPEVEQELA HILLTELLAY QFASPVRWIE TQDVFLKDFN TERVVEIGPS PTLAGMAQRT 60
LKNKYESYDA ALSLHREILC YSKDAKEIYY TPDPSELAAK EEPAKEEAPA PTPAASAPAP 120
AAAAPAPVAA AAPAAAAAEI ADEPVKASLL LHVLVAHKLK KSLDSIPMSK TIKDLVGGKS 180
TVQNEILGDL GKEFGTTPEK PEETPLEELA ETFQDTFSGA LGKQSSSLLS RLISSKMPGG 240
FTITVARKYL QTRWGLPSGR QDGVLLVALS NEPAARLGSE ADAKAFLDSM AQKYASIVGV 300
DLSSAASASG AAGAGAAAGA AMIDAGALEE ITKDHKVLAR QQLQVLARYL KMDLDNGERK 360
FLKEKDTVAE LQAQLDYLNA ELGEFFVNGV ATSFSRKKAR TFDSSWNWAK QSLLSLYFEI 420
IHGVLKNVDR EVVSEAINIM NRSNDALIKF MEYHISNTDE TKGENYQLVK TLGEQLIENC 480
KQVLDVDPVY KDVAKPTGPK TAIDKNGNIT YSEEPREKVR KLSQYVQEMA LGGPITKESQ 540
PTIEEDLTRV YKAISAQADK QDISSSTRVE FEKLYSDLMK FLESSKEIDP SQTTQLAGMD 600
VEDALDKDST KEVASLPNKS TISKTVSSTI PRETIPFLHL RKKTPAGDWK YDRQLSSLFL 660
DGLEKAAFNG VTFKDKYVLI TGAGKGSIGA EVLQGLLQGG AKVVVTTSRF SKQVTDYYQS 720
IYAKYGAKGS TLIVVPFNQG SKQDVEALIE FIYDTEKNGG LGWDLDAIIP FAAIPEQGIE 780
LEHIDSKSEF AHRIMLTNIL RMMGCVKKQK SARGIETRPA QVILPMSPNH GTFGGDGMYS 840
ESKLSLETLF NRWHSESWAN QLTVCGAIIG WTRGTGLMSA NNIIAEGIEK MGVRTFSQKE 900
MAFNLLGLLT PEVVELCQKS PVMADLNGGL QFVPELKEFT AKLRKELVET SEVRKAVSIE 960
TALEHKVVNG NSADAAYAQV EIQPRANIQL DFPELKPYKQ VKQIAPAELE GLLDLERVIV 1020
VTGFAEVGPW GSARTRWEME AFGEFSLEGC VEMAWIMGFI SYHNGNLKGR PYTGWVDSKT 1080
KEPVDDKDVK AKYETSILEH SGIRLIEPEL FNGYNPEKKE MIQEVIVEED LEPFEASKET 1140
AEQFKHQHGD KVDIFEIPET GEYSVKLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI 1200
SDDIISQVDP ITLFVLVSVV EAFIASGITD PYEMYKYVHV SEVGNCSGSG MGGVSALRGM 1260
FKDRFKDEPV QNDILQESFI NTMSAWVNML LISSSGPIKT PVGACATSVE SVDIGVETIL 1320
SGKARICIVG GYDDFQEEGS FEFGNMKATS NTLEEFEHGR TPAEMSRPAT TTRNGFMEAQ 1380
GAGIQIIMQA DLALKMGVPI YGIVAMAATA TDKIGRSVPA PGKGILTTAR EHHSSVKYAS 1440
PNLNMKYRKR QLVTREAQIK DWVENELEAL KLEAEEIPSE DQNEFLLERT REIHNEAESQ 1500
LRAAQQQWGN DFYKRDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND KNESATINEM 1560
MKHLGRSEGN PVIGVFQKFL TGHPKGAAGA WMMNGALQIL NSGIIPGNRN ADNVDKILEQ 1620
FEYVLYPSKT LKTDGVRAVS ITSFGFGQKG GQAIVVHPDY LYGAITEDRY NEYVAKVSAR 1680
EKSAYKFFHN GMIYNKLFVS KEHAPYTDEL EEDVYLDPLA RVSKDKKSGS LTFNSKNIQS 1740
KDSYINANTI ETAKMIENMT KEKVSNGGVG VDVELITSIN VENDTFIERN FTPQEIEYCS 1800
AQPSVQSSFA GTWSAKEAVF KSLGVKSLGG GAALKDIEIV RVNKNAPAVE LHGNAKKAAE 1860
EAGVTDVKVS ISHDDLQAVA VAVSTKK 1887 
Gene Ontology
 GO:0005835; C:fatty acid synthase complex; IDA:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IDA:SGD.
 GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IMP:SGD.
 GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:EC.
 GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IGI:SGD.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0006633; P:fatty acid biosynthetic process; IMP:SGD.
 GO:0009059; P:macromolecule biosynthetic process; IEA:InterPro. 
Interpro
 IPR008278; 4-PPantetheinyl_Trfase_SF.
 IPR001227; Ac_transferase_dom.
 IPR002582; ACPS.
 IPR016035; Acyl_Trfase/lysoPLipase.
 IPR026025; FAS_alpha_yeast.
 IPR018201; Ketoacyl_synth_AS.
 IPR014031; Ketoacyl_synth_C.
 IPR014030; Ketoacyl_synth_N.
 IPR016040; NAD(P)-bd_dom.
 IPR004568; PPantethiene-prot_Trfase_dom.
 IPR016039; Thiolase-like.
 IPR016038; Thiolase-like_subgr. 
Pfam
 PF01648; ACPS
 PF00109; ketoacyl-synt
 PF02801; Ketoacyl-synt_C 
SMART
  
PROSITE
 PS50075; ACP_DOMAIN
 PS00606; B_KETOACYL_SYNTHASE
 PS00012; PHOSPHOPANTETHEINE 
PRINTS