CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004734
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fatty acid synthase 
Protein Synonyms/Alias
 [Acyl-carrier-protein] S-acetyltransferase; [Acyl-carrier-protein] S-malonyltransferase; 3-oxoacyl-[acyl-carrier-protein] synthase; 3-oxoacyl-[acyl-carrier-protein] reductase; 3-hydroxyacyl-[acyl-carrier-protein] dehydratase; Enoyl-[acyl-carrier-protein] reductase; Oleoyl-[acyl-carrier-protein] hydrolase 
Gene Name
 Fasn 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
41TDDDRRWKAGLYGLPubiquitination[1]
59GKLKDLSKFDASFFGacetylation[2, 3, 4, 5, 6]
59GKLKDLSKFDASFFGubiquitination[1]
70SFFGVHPKQAHTMDPacetylation[3, 5, 6]
70SFFGVHPKQAHTMDPubiquitination[1]
193GGINLLLKPNTSVQFubiquitination[1]
202NTSVQFMKLGMLSPDacetylation[5]
326PLLIGSTKSNMGHPEubiquitination[1]
528LRSDEAVKPLGVKVSacetylation[4, 6]
528LRSDEAVKPLGVKVSubiquitination[1]
533AVKPLGVKVSDLLLSubiquitination[1]
673KQEGVFAKEVRTGGLacetylation[3, 4, 5, 6, 7]
673KQEGVFAKEVRTGGLsuccinylation[6]
673KQEGVFAKEVRTGGLubiquitination[1]
776AVLKRGVKSSCTIIPacetylation[6]
776AVLKRGVKSSCTIIPubiquitination[1]
786CTIIPLMKRDHKDNLacetylation[2, 3, 4, 5, 6, 8]
786CTIIPLMKRDHKDNLubiquitination[1]
790PLMKRDHKDNLEFFLacetylation[4, 6]
790PLMKRDHKDNLEFFLubiquitination[1]
967LWEDPNSKLFDHPEVacetylation[4, 5]
967LWEDPNSKLFDHPEVubiquitination[1]
993LTQGEVYKELRLRGYacetylation[3, 4, 5, 6]
993LTQGEVYKELRLRGYubiquitination[1]
1020TLEGEQGKLLWKDNWubiquitination[1]
1071RQKVYRLKEDTQVADacetylation[6]
1071RQKVYRLKEDTQVADubiquitination[1]
1117QLVPTLEKFVFTPHMubiquitination[1]
1137SESTALQKELQLCKGubiquitination[1]
1143QKELQLCKGLARALQacetylation[3]
1143QKELQLCKGLARALQubiquitination[1]
1152LARALQTKATQQGLKubiquitination[1]
1159KATQQGLKAAMLGQEubiquitination[1]
1234LENLSTLKMKVAEVLacetylation[2, 3, 4, 5, 6]
1234LENLSTLKMKVAEVLubiquitination[1]
1236NLSTLKMKVAEVLAGacetylation[3]
1236NLSTLKMKVAEVLAGubiquitination[1]
1276DRHPQALKDVQTKLQacetylation[3, 5, 6]
1276DRHPQALKDVQTKLQubiquitination[1]
1378WESLFSRKALHLVGLubiquitination[1]
1478SNTSHAPKLDPGSPEubiquitination[1]
1491PELQQVLKHDLVMNVacetylation[4]
1491PELQQVLKHDLVMNVubiquitination[1]
1516HFQLEQDKPKEQTAHacetylation[3, 4, 6]
1518QLEQDKPKEQTAHAFacetylation[3]
1575DIMLATGKLSPDAIPacetylation[2, 3, 4, 5, 6, 9]
1575DIMLATGKLSPDAIPubiquitination[1]
1584SPDAIPGKWASRDCMacetylation[3]
1584SPDAIPGKWASRDCMubiquitination[1]
1697TTVGSAEKRAYLQARacetylation[6]
1745LNSLAEEKLQASVRCacetylation[4, 5]
1745LNSLAEEKLQASVRCubiquitination[1]
1817GIRDGVVKPLKCTVFubiquitination[1]
1820DGVVKPLKCTVFPKAubiquitination[1]
1826LKCTVFPKAQVEDAFacetylation[5]
1826LKCTVFPKAQVEDAFubiquitination[1]
1840FRYMAQGKHIGKVLVacetylation[4, 6]
1871TLISAISKTFCPAHKubiquitination[1]
1986ELFQDVNKPKYNGTLacetylation[2, 4, 5, 6]
1986ELFQDVNKPKYNGTLubiquitination[1]
1988FQDVNKPKYNGTLNLubiquitination[1]
2123DTQRDLVKAVAHILGubiquitination[1]
2187KLQEMSSKTDSATDTubiquitination[1]
2198ATDTTAPKSRSDTSLubiquitination[1]
2375FLDVEHSKVLEALLPacetylation[5]
2375FLDVEHSKVLEALLPubiquitination[1]
2384LEALLPLKSLEDRVAacetylation[6]
2384LEALLPLKSLEDRVAubiquitination[1]
2419AAVSFYHKLRAADQYacetylation[5]
2427LRAADQYKPKAKYHGacetylation[4]
2429AADQYKPKAKYHGNVacetylation[4]
2431DQYKPKAKYHGNVTLacetylation[3]
2431DQYKPKAKYHGNVTLubiquitination[1]
2442NVTLLRAKTGGTYGEubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [5] 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]
 [6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [7] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [8] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [9] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599] 
Functional Description
 Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein. 
Sequence Annotation
 DOMAIN 2117 2173 Acyl carrier.
 NP_BIND 1664 1681 NADP (ER) (By similarity).
 NP_BIND 1879 1894 NADP (KR) (By similarity).
 REGION 1 414 Beta-ketoacyl synthase.
 REGION 429 817 Acyl and malonyl transferases.
 REGION 1628 1856 Enoyl reductase.
 REGION 1857 2111 Beta-ketoacyl reductase.
 REGION 2201 2504 Thioesterase.
 ACT_SITE 161 161 For beta-ketoacyl synthase activity (By
 ACT_SITE 581 581 For malonyltransferase activity (By
 ACT_SITE 878 878 For beta-hydroxyacyl dehydratase activity
 ACT_SITE 2301 2301 For thioesterase activity (By
 ACT_SITE 2474 2474 For thioesterase activity (By
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 70 70 N6-acetyllysine (By similarity).
 MOD_RES 207 207 Phosphoserine (By similarity).
 MOD_RES 298 298 N6-acetyllysine (By similarity).
 MOD_RES 528 528 N6-acetyllysine (By similarity).
 MOD_RES 673 673 N6-acetyllysine (By similarity).
 MOD_RES 1697 1697 N6-(pyridoxal phosphate)lysine; alternate
 MOD_RES 1697 1697 N6-acetyllysine; alternate (By
 MOD_RES 1764 1764 N6-acetyllysine (By similarity).
 MOD_RES 1840 1840 N6-acetyllysine (By similarity).
 MOD_RES 1988 1988 N6-acetyllysine (By similarity).
 MOD_RES 2150 2150 O-(pantetheine 4'-phosphoryl)serine (By
 MOD_RES 2229 2229 Phosphoserine (By similarity).  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase; Lipid biosynthesis; Lipid metabolism; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein; Pyridoxal phosphate; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2504 AA 
Protein Sequence
MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR SGKLKDLSKF 60
DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL RGTNTGVWVG VSGSEASEAL 120
SRDPETLLGY SMVGCQRAMM ANRLSFFFDF KGPSIALDTA CSSSLLALQN AYQAIRSGEC 180
PAALVGGINL LLKPNTSVQF MKLGMLSPDG TCRSFDDSGS GYCRSEAVVA VLLTKKSLAR 240
RVYATILNAG TNTDGSKEQG VTFPSGEVQE QLICSLYQPA GLAPESLEYI EAHGTGTKVG 300
DPQELNGITR SLCAFRQAPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEH GVWAPNLHFH 360
NPNPEIPALL DGRLQVVDRP LPVRGGNVGI NSFGFGGSNV HVILQPNTRQ APAPTAHAAL 420
PHLLHASGRT LEAVQDLLEQ GRQHSQDLAF VSMLNDIAAT PTAAMPFRGY TVLGVEGRVQ 480
EVQQVSTNKR PLWFICSGMG TQWRGMGLSL MRLDSFRESI LRSDEAVKPL GVKVSDLLLS 540
TDERTFDDIV HAFVSLTAIQ IALIDLLTSV GLKPDGIIGH SLGEVACGYA DGCLSQREAV 600
LAAYWRGQCI KDAHLPPGSM AAVGLSWEEC KQRCPAGVVP ACHNSEDTVT ISGPQAAVNE 660
FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK VIREPRPRSA RWLSTSIPEA 720
QWQSSLARTS SAEYNVNNLV SPVLFQEALW HIPEHAVVLE IAPHALLQAV LKRGVKSSCT 780
IIPLMKRDHK DNLEFFLTNL GKVHLTGINV NPNALFPPVE FPAPRGTPLI SPHIKWDHSQ 840
TWDVPVAEDF PNGSSSSSAT VYSIDASPES PDHYLVDHCI DGRVIFPGTG YLCLVWKTLA 900
RSLGLSLEET PVVFENVSFH QATILPKTGT VALEVRLLEA SHAFEVSDTG NLIVSGKVYL 960
WEDPNSKLFD HPEVPTPPES ASVSRLTQGE VYKELRLRGY DYGPQFQGIC EATLEGEQGK 1020
LLWKDNWVTF MDTMLQVSIL GSSQQSLQLP TRVTAIYIDP ATHRQKVYRL KEDTQVADVT 1080
TSRCLGITVS GGIHISRLQT TATSRRQQEQ LVPTLEKFVF TPHMEAECLS ESTALQKELQ 1140
LCKGLARALQ TKATQQGLKA AMLGQEDPPQ HGLPRLLAAA CQLQLNGNLQ LELGEALAQE 1200
RLLLPEDPLI SGLLNSQALK ACVDTALENL STLKMKVAEV LAGEGHLYSR IPALLNTQPM 1260
LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWNPSDPAPS SLGALDLLVC NCALATLGDP 1320
ALALDNMVAA LKEGGFLLVH TVLKGHALGE TLACLPSEVQ PAPSLLSQEE WESLFSRKAL 1380
HLVGLKRSFY GTALFLCRRA IPQEKPIFLS VEDTSFQWVD SLKSTLATSS SQPVWLTAMD 1440
CPTSGVVGLV NCLRKEPGGH RIRCILLSNL SNTSHAPKLD PGSPELQQVL KHDLVMNVYR 1500
DGAWGAFRHF QLEQDKPKEQ TAHAFVNVLT RGDLASIRWV SSPLKHTQPS SSGAQLCTVY 1560
YASLNFRDIM LATGKLSPDA IPGKWASRDC MLGMEFSGRD RCGRRVMGLV PAEGLATSVL 1620
LSSDFLWDVP SSWTLEEAAS VPVVYTTAYY SLVVRGRIQR GETVLIHSGS GGVGQAAISI 1680
ALSLGCRVFT TVGSAEKRAY LQARFPQLDD TSFANSRDTS FEQHVLLHTG GKGVDLVLNS 1740
LAEEKLQASV RCLAQHGRFL EIGKFDLSNN HPLGMAIFLK NVTFHGILLD ALFEEANDSW 1800
REVAALLKAG IRDGVVKPLK CTVFPKAQVE DAFRYMAQGK HIGKVLVQVR EEEPEAVLPG 1860
AQPTLISAIS KTFCPAHKSY IITGGLGGFG LELARWLVLR GAQRLVLTSR SGIRTGYQAK 1920
HIREWRRQGI QVLVSTSNVS SLEGARALIA EATKLGPVGG VFNLAMVLRD AMLENQTPEL 1980
FQDVNKPKYN GTLNLDRATR EACPELDYFV AFSSVSCGRG NAGQTNYGFA NSTMERICEQ 2040
RRHDGLPGLA VQWGAIGDVG IVLEAMGTND TVIGGTLPQR ISSCMEVLDL FLNQPHAVLS 2100
SFVLAEKKAV AHGDGDTQRD LVKAVAHILG IRDLAGINLD STLADLGLDS LMGVEVRQIL 2160
EREHDLVLPM REVRQLTLRK LQEMSSKTDS ATDTTAPKSR SDTSLKQNQL NLSTLLVNPE 2220
GPTLTQLNSV QSSERPLFLV HPIEGSTTVF HSLAAKLSVP TYGLQCTQAA PLDSIPNLAA 2280
YYIDCIKQVQ PEGPYRIAGY SFGACVAFEM CSQLQAQQGP APTHNNLFLF DGSHTYVLAY 2340
TQSYRAKMTP GCEAEAEAEA LCFFIKQFLD VEHSKVLEAL LPLKSLEDRV AASVDLITKS 2400
HHSLDRRELS FAAVSFYHKL RAADQYKPKA KYHGNVTLLR AKTGGTYGED LGADYNLSQV 2460
CDGKVSVHII EGDHRTLLEG SGLESIINII HSSLAEPRVS VREG 2504 
Gene Ontology
 GO:0042587; C:glycogen granule; IDA:MGI.
 GO:0005794; C:Golgi apparatus; IEA:Compara.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:EC.
 GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro.
 GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:EC.
 GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:EC.
 GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:EC.
 GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:EC.
 GO:0008144; F:drug binding; IEA:Compara.
 GO:0004319; F:enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity; IEA:EC.
 GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:EC.
 GO:0070402; F:NADPH binding; IEA:Compara.
 GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:EC.
 GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:EC.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006084; P:acetyl-CoA metabolic process; IEA:Compara.
 GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
 GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. 
Interpro
 IPR001227; Ac_transferase_dom.
 IPR009081; Acyl_carrier_prot-like.
 IPR014043; Acyl_transferase.
 IPR016035; Acyl_Trfase/lysoPLipase.
 IPR013149; ADH_C.
 IPR023102; Fatty_acid_synthase_dom_2.
 IPR011032; GroES-like.
 IPR018201; Ketoacyl_synth_AS.
 IPR014031; Ketoacyl_synth_C.
 IPR014030; Ketoacyl_synth_N.
 IPR016036; Malonyl_transacylase_ACP-bd.
 IPR013217; Methyltransf_12.
 IPR016040; NAD(P)-bd_dom.
 IPR020842; PKS/FAS_KR.
 IPR020843; PKS_ER.
 IPR013968; PKS_KR.
 IPR006162; PPantetheine_attach_site.
 IPR001031; Thioesterase.
 IPR016039; Thiolase-like.
 IPR016038; Thiolase-like_subgr. 
Pfam
 PF00698; Acyl_transf_1
 PF00107; ADH_zinc_N
 PF00109; ketoacyl-synt
 PF02801; Ketoacyl-synt_C
 PF08659; KR
 PF08242; Methyltransf_12
 PF00550; PP-binding
 PF00975; Thioesterase 
SMART
 SM00829; PKS_ER
 SM00822; PKS_KR 
PROSITE
 PS50075; ACP_DOMAIN
 PS00606; B_KETOACYL_SYNTHASE
 PS00012; PHOSPHOPANTETHEINE 
PRINTS