CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004046
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
41TDDDRRWKAGLYGLPacetylation[1]
49AGLYGLPKRSGKLKDacetylation[1]
59GKLKDLSKFDASFFGacetylation[1]
70SFFGVHPKQAHTMDPacetylation[1]
298EAHGTGTKVGDPQELacetylation[1]
528LRSDEALKPLGVKVSacetylation[1]
673KQEGVFAKEVRTGGLacetylation[1]
786CTIIPLMKRDHKDNLacetylation[1]
790PLMKRDHKDNLEFFLacetylation[1]
967QWEDPDSKLFDHPEVacetylation[1]
993LTQGEVYKELRLRGYacetylation[1]
1234LENLSTLKMKVVEVLacetylation[1]
1276DRHPQALKDVQTKLQacetylation[1]
1386ALHLVGLKKSFYGTAacetylation[1]
1405RRLSPQDKPIFLPVEacetylation[1]
1488PGSSELQKVLESDLVacetylation[1]
1516HFQLEQDKPEEQTAHacetylation[1]
1576DIMLATGKLSPDAIPacetylation[1]
1585SPDAIPGKWASRDCMacetylation[1]
1698TTVGSAEKRAYLQARacetylation[1]
1746LNSLAEEKLQASVRCacetylation[1]
1765GRFLEIGKFDLSNNHacetylation[1]
1818GIRDGVVKPLKCTVFacetylation[1]
1841FRYMAQGKHIGKVLVacetylation[1]
1921IRTGYQAKHVREWRRacetylation[1]
1987ELFQDVNKPKYNGTLacetylation[1]
1989FQDVNKPKYNGTLNLacetylation[1]
2124EAQRDLVKAVAHILGacetylation[1]
2188KLQEMSSKAGSDTELubiquitination[2]
2376FVDAEHSKVLEALLPacetylation[1]
2385LEALLPLKSLEDRVAacetylation[1]
2428LRAADQYKPKAKYHGacetylation[1]
2432DQYKPKAKYHGNVILacetylation[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
 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 2118 2174 Acyl carrier.
 NP_BIND 1665 1682 NADP (ER).
 NP_BIND 1765 1780 NADP (KR).
 REGION 1 413 Beta-ketoacyl synthase.
 REGION 429 817 Acyl and malonyl transferases.
 REGION 1629 1857 Enoyl reductase.
 REGION 1858 2113 Beta-ketoacyl reductase.
 REGION 2202 2505 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 2302 2302 For thioesterase activity (By
 ACT_SITE 2475 2475 For thioesterase activity (By
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 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 1698 1698 N6-(pyridoxal phosphate)lysine; alternate
 MOD_RES 1698 1698 N6-acetyllysine; alternate (By
 MOD_RES 1765 1765 N6-acetyllysine (By similarity).
 MOD_RES 1841 1841 N6-acetyllysine (By similarity).
 MOD_RES 1989 1989 N6-acetyllysine (By similarity).
 MOD_RES 2151 2151 O-(pantetheine 4'-phosphoryl)serine (By
 MOD_RES 2230 2230 Phosphoserine (By similarity).  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; 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
 2505 AA 
Protein Sequence
MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR SGKLKDLSKF 60
DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL RGTNTGVWVG VSGSEASEAL 120
SRDPETLLGY SMVGCQRAMM ANRLSFFFDF KGPSIALDTA CSSSLLALQN AYQAIRSGEC 180
PAAIVGGINL LLKPNTSVQF MKLGMLSPDG TCRSFDDSGN GYCRAEAVVA VLLTKKSLAR 240
RVYATILNAG TNTDGCKEQG VTFPSGEAQE QLIRSLYQPG GVAPESLEYI EAHGTGTKVG 300
DPQELNGITR SLCAFRQSPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEN GVWAPNLHFH 360
NPNPEIPALL DGRLQVVDRP LPVRGGIVGI NSFGFGGANV HVILQPNTQQ APAPAPHAAL 420
PHLLHASGRT MEAVQGLLEQ GRQHSQDLAF VSMLNDIAAT PTAAMPFRGY TVLGVEGHVQ 480
EVQQVPASQR PLWFICSGMG TQWRGMGLSL MRLDSFRESI LRSDEALKPL GVKVSDLLLS 540
TDEHTFDDIV HSFVSLTAIQ IALIDLLTSM GLKPDGIIGH SLGEVACGYA DGCLSQREAV 600
LAAYWRGQCI KDANLPAGSM AAVGLSWEEC KQRCPPGVVP ACHNSEDTVT ISGPQAAVNE 660
FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK VIREPRPRSA RWLSTSIPEA 720
QWQSSLARTS SAEYNVNNLV SPVLFQEALW HVPEHAVVLE IAPHALLQAV LKRGVKPSCT 780
IIPLMKRDHK DNLEFFLTNL GKVHLTGIDI NPNALFPPVE FPVPRGTPLI SPHIKWDHSQ 840
TWDIPVAEDF PNGSSSSSAT VYNIDASSES SDHYLVDHCI DGRVLFPGTG YLYLVWKTLA 900
RSLSLSLEET PVVFENVTFH QATILPRTGT VPLEVRLLEA SHAFEVSDSG NLIVSGKVYQ 960
WEDPDSKLFD HPEVPIPAES ESVSRLTQGE VYKELRLRGY DYGPHFQGVY EATLEGEQGK 1020
LLWKDNWVTF MDTMLQISIL GFSKQSLQLP TRVTAIYIDP ATHLQKVYML EGDTQVADVT 1080
TSRCLGVTVS GGVYISRLQT TATSRRQQEQ LVPTLEKFVF TPHVEPECLS ESAILQKELQ 1140
LCKGLAKALQ TKATQQGLKM TVPGLEDLPQ HGLPRLLAAA CQLQLNGNLQ LELGEVLARE 1200
RLLLPEDPLI SGLLNSQALK ACIDTALENL STLKMKVVEV LAGEGHLYSH ISALLNTQPM 1260
LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWDPSGPAPT NLGALDLVVC NCALATLGDP 1320
ALALDNMVAA LKDGGFLLMH TVLKGHALGE TLACLPSEVQ PGPSFLSQEE WESLFSRKAL 1380
HLVGLKKSFY GTALFLCRRL SPQDKPIFLP VEDTSFQWVD SLKSILATSS SQPVWLTAMN 1440
CPTSGVVGLV NCLRKEPGGH RIRCILLSNL SSTSHVPKLD PGSSELQKVL ESDLVMNVYR 1500
DGAWGAFRHF QLEQDKPEEQ TAHAFVNVLT RGDLASIRWV SSPLKHMQPP SSSGAQLCTV 1560
YYASLNFRDI MLATGKLSPD AIPGKWASRD CMLGMEFSGR DKCGRRVMGL VPAEGLATSV 1620
LLSPDFLWDV PSSWTLEEAA SVPVVYTTAY YSLVVRGRIQ HGETVLIHSG SGGVGQAAIS 1680
IALSLGCRVF TTVGSAEKRA YLQARFPQLD DTSFANSRDT SFEQHVLLHT GGKGVDLVLN 1740
SLAEEKLQAS VRCLAQHGRF LEIGKFDLSN NHPLGMAIFL KNVTFHGILL DALFEGANDS 1800
WREVAELLKA GIRDGVVKPL KCTVFPKAQV EDAFRYMAQG KHIGKVLVQV REEEPEAMLP 1860
GAQPTLISAI SKTFCPEHKS YIITGGLGGF GLELARWLVL RGAQRLVLTS RSGIRTGYQA 1920
KHVREWRRQG IHVLVSTSNV SSLEGARALI AEATKLGPVG GVFNLAMVLR DAMLENQTPE 1980
LFQDVNKPKY NGTLNLDRAT REACPELDYF VAFSSVSCGR GNAGQSNYGF ANSTMERICE 2040
QRRHDGLPGL AVQWGAIGDV GIILEAMGTN DTVVGGTLPQ RISSCMEVLD LFLNQPHAVL 2100
SSFVLAEKKA VAHGDGEAQR DLVKAVAHIL GIRDLAGINL DSSLADLGLD SLMGVEVRQI 2160
LEREHDLVLP IREVRQLTLR KLQEMSSKAG SDTELAAPKS KNDTSLKQAQ LNLSILLVNP 2220
EGPTLTRLNS VQSSERPLFL VHPIEGSITV FHSLAAKLSV PTYGLQCTQA APLDSIPNLA 2280
AYYIDCIKQV QPEGPYRVAG YSFGACVAFE MCSQLQAQQG PAPAHNNLFL FDGSHTYVLA 2340
YTQSYRAKLT PGCEAEAEAE AICFFIKQFV DAEHSKVLEA LLPLKSLEDR VAAAVDLITR 2400
SHQSLDRRDL SFAAVSFYYK LRAADQYKPK AKYHGNVILL RAKTGGTYGE DLGADYNLSQ 2460
VCDGKVSVHI IEGDHRTLLE GRGLESIINI IHSSLAEPRV SVREG 2505 
Gene Ontology
 GO:0042587; C:glycogen granule; IEA:Compara.
 GO:0005794; C:Golgi apparatus; IEA:Compara.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IEA:Compara.
 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; IDA:RGD.
 GO:0004319; F:enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity; IEA:EC.
 GO:0004312; F:fatty acid synthase activity; IDA:RGD.
 GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:EC.
 GO:0070402; F:NADPH binding; IDA:RGD.
 GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:EC.
 GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:EC.
 GO:0042803; F:protein homodimerization activity; IDA:RGD.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006084; P:acetyl-CoA metabolic process; IDA:RGD.
 GO:0006633; P:fatty acid biosynthetic process; IMP:RGD. 
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