Sequence of FAS_HUMAN
EC Number:2.3.1.39
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
malonyl-CoA + an [acyl-carrier protein] = CoA + a malonyl-[acyl-carrier protein]
Other sequences found for EC No. 2.3.1.39
General information:
Sequence
0 MEEVVIAGMS GKLPESENLQ EFWDNLIGGV DMVTDDDRRW KAGLYGLPRR SGKLKDLSRF
60 DASFFGVHPK QAHTMDPQLR LLLEVTYEAI VDGGINPDSL RGTHTGVWVG VSGSETSEAL
120 SRDPETLVGY SMVGCQRAMM ANRLSFFFDF RGPSIALDTA CSSSLMALQN AYQAIHSGQC
180 PAAIVGGINV LLKPNTSVQF LRLGMLSPEG TCKAFDTAGN GYCRSEGVVA VLLTKKSLAR
240 RVYATILNAG TNTDGFKEQG VTFPSGDIQE QLIRSLYQSA GVAPESFEYI EAHGTGTKVG
300 DPQELNGITR ALCATRQEPL LIGSTKSNMG HPEPASGLAA LAKVLLSLEH GLWAPNLHFH
360 SPNPEIPALL DGRLQVVDQP LPVRGGNVGI NSFGFGGSNV HIILRPNTQP PPAPAPHATL
420 PRLLRASGRT PEAVQKLLEQ GLRHSQDLAF LSMLNDIAAV PATAMPFRGY AVLGGERGGP
480 EVQQVPAGER PLWFICSGMG TQWRGMGLSL MRLDRFRDSI LRSDEAVKPF GLKVSQLLLS
540 TDESTFDDIV HSFVSLTAIQ IGLIDLLSCM GLRPDGIVGH SLGEVACGYA DGCLSQEEAV
600 LAAYWRGQCI KEAHLPPGAM AAVGLSWEEC KQRCPPGVVP ACHNSKDTVT ISGPQAPVFE
660 FVEQLRKEGV FAKEVRTGGM AFHSYFMEAI APPLLQELKK VIREPKPRSA RWLSTSIPEA
720 QWHSSLARTS SAEYNVNNLV SPVLFQEALW HVPEHAVVLE IAPHALLQAV LKRGLKPSCT
780 IIPLMKKDHR DNLEFFLAGI GRLHLSGIDA NPNALFPPVE FPAPRGTPLI SPLIKWDHSL
840 AWDVPAAEDF PNGSGSPSAA IYNIDTSSES PDHYLVDHTL DGRVLFPATG YLSIVWKTLA
900 RALGLGVEQL PVVFEDVVLH QATILPKTGT VSLEVRLLEA SRAFEVSENG NLVVSGKVYQ
960 WDDPDPRLFD HPESPTPNPT EPLFLAQAEV YKELRLRGYD YGPHFQGILE ASLEGDSGRL
1020 LWKDNWVSFM DTMLQMSILG SAKHGLYLPT RVTAIHIDPA THRQKLYTLQ DKAQVADVVV
1080 SRWLRVTVAG GVHISGLHTE SAPRRQQEQQ VPILEKFCFT PHTEEGCLSE RAALQEELQL
1140 CKGLVQALQT KVTQQGLKMV VPGLDGAQIP RDPSQQELPR LLSAACRLQL NGNLQLELAQ
1200 VLAQERPKLP EDPLLSGLLD SPALKACLDT AVENMPSLKM KVVEVLAGHG HLYSRIPGLL
1260 SPHPLLQLSY TATDRHPQAL EAAQAELQQH DVAQGQWDPA DPAPSALGSA DLLVCNCAVA
1320 ALGDPASALS NMVAALREGG FLLLHTLLRG HPLGDIVAFL TSTEPQYGQG ILSQDAWESL
1380 FSRVSLRLVG LKKSFYGSTL FLCRRPTPQD SPIFLPVDDT SFRWVESLKG ILADEDSSRP
1440 VWLKAINCAT SGVVGLVNCL RREPGGNRLR CVLLSNLSST SHVPEVDPGS AELQKVLQGD
1500 LVMNVYRDGA WGAFRHFLLE EDKPEEPTAH AFVSTLTRGD LSSIRWVCSS LRHAQPTCPG
1560 AQLCTVYYAS LNFRDIMLAT GKLSPDAIPG KWTSQDSLLG MEFSGRDASG KRVMGLVPAK
1620 GLATSVLLSP DFLWDVPSNW TLEEAASVPV VYSTAYYALV VRGRVRPGET LLIHSGSGGV
1680 GQAAIAIALS LGCRVFTTVG SAEKRAYLQA RFPQLDSTSF ANSRDTSFEQ HVLWHTGGKG
1740 VDLVLNSLAE EKLQASVRCL ATHGRFLEIG KFDLSQNHPL GMAIFLKNVT FHGVLLDAFF
1800 NESSADWREV WALVQAGIRD GVVRPLKCTV FHGAQVEDAF RYMAQGKHIG KVVVQVLAEE
1860 PEAVLKGAKP KLMSAISKTF CPAHKSYIIA GGLGGFGLEL AQWLIQRGVQ KLVLTSRSGI
1920 RTGYQAKQVR RWRRQGVQVQ VSTSNISSLE GARGLIAEAA QLGPVGGVFN LAVVLRDGLL
1980 ENQTPEFFQD VCKPKYSGTL NLDRVTREAC PELDYFVVFS SVSCGRGNAG QSNYGFANSA
2040 MERICEKRRH EGLPGLAVQW GAIGDVGILV ETMSTNDTIV SGTLPQRMAS CLEVLDLFLN
2100 QPHMVLSSFV LAEKAAAYRD RDSQRDLVEA VAHILGIRDL AAVNLDSSLA DLGLDSLMSV
2160 EVRQTLEREL NLVLSVREVR QLTLRKLQEL SSKADEASEL ACPTPKEDGL AQQQTQLNLR
2220 SLLVNPEGPT LMRLNSVQSS ERPLFLVHPI EGSTTVFHSL ASRLSIPTYG LQCTRAAPLD
2280 SIHSLAAYYI DCIRQVQPEG PYRVAGYSYG ACVAFEMCSQ LQAQQSPAPT HNSLFLFDGS
2340 PTYVLAYTQS YRAKLTPGCE AEAETEAICF FVQQFTDMEH NRVLEALLPL KGLEERVAAA
2400 VDLIIKSHQG LDRQELSFAA RSFYYKLRAA EQYTPKAKYH GNVMLLRAKT GGAYGEDLGA
2460 DYNLSQVCDG KVSVHVIEGD HRTLLEGSGL ESIISIIHSS LAEPRVSVRE G
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1057472
Jayakumar A.,Tai M.-H.,Huang W.-Y.,Al-Feel W.,Hsu M.,Abu-Elheiga L.,Chirala S.S.,Wakil S.J.
Human fatty acid synthase: properties and molecular cloning.
Proc. Natl. Acad. Sci. U.S.A.
92
8695-8699
1995
1057476
Zody M.C.,Garber M.,Adams D.J.,Sharpe T.,Harrow J.,Lupski J.R.,Nicholson C.,Searle S.M.,Wilming L.,Young S.K.,Abouelleil A.,Allen N.R.,Bi W.,Bloom T.,Borowsky M.L.,Bugalter B.E.,Butler J.,Chang J.L.,Chen C.-K.,Cook A.,Corum B.,Cuomo C.A.,de Jong P.J.,DeCaprio D.,Dewar K.,FitzGerald M.,Gilbert J.,Gibson R.,Gnerre S.,Goldstein S.,Grafham D.V.,Grocock R.,Hafez N.,Hagopian D.S.,Hart E.,Norman C.H.,Humphray S.,Jaffe D.B.,Jones M.,Kamal M.,Khodiyar V.K.,LaButti K.,Laird G.,Lehoczky J.,Liu X.,Lokyitsang T.,Loveland J.,Lui A.,Macdonald P.,Major J.E.,Matthews L.,Mauceli E.,McCarroll S.A.,Mihalev A.H.,Mudge J.,Nguyen C.,Nicol R.,O'Leary S.B.,Osoegawa K.,Schwartz D.C.,Shaw-Smith C.,Stankiewicz P.,Steward C.,Swarbreck D.,Venkataraman V.,Whittaker C.A.,Yang X.,Zimmer A.R.,Bradley A.,Hubbard T.,Birren B.W.,Rogers J.,Lander E.S.,Nusbaum C.
DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.
Nature
440
1045-1049
2006
1057477
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
1057479
Kuhajda F.P.,Jenner K.,Wood F.D.,Hennigar R.A.,Jacobs L.B.,Dick J.D.,Pasternack G.R.
Fatty acid synthesis: a potential selective target for antineoplastic therapy.
Proc. Natl. Acad. Sci. U.S.A.
91
6379-6383
1994
1057480
Semenkovich C.F.,Coleman T.,Fiedorek F.T. Jr.
Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation.
J. Lipid Res.
36
1507-1521
1995
1057481
Jayakumar A.,Huang W.Y.,Raetz B.,Chirala S.S.,Wakil S.J.
Cloning and expression of the multifunctional human fatty acid synthase and its subdomains in Escherichia coli.
Proc. Natl. Acad. Sci. U.S.A.
93
14509-14514
1996
1057482
Jayakumar A.,Chirala S.S.,Wakil S.J.
Human fatty acid synthase: assembling recombinant halves of the fatty acid synthase subunit protein reconstitutes enzyme activity.
Proc. Natl. Acad. Sci. U.S.A.
94
12326-12330
1997
1057483
Carlisle-Moore L.,Gordon C.R.,Machutta C.A.,Miller W.T.,Tonge P.J.
Substrate recognition by the human fatty-acid synthase.
J. Biol. Chem.
280
42612-42618
2005
1057484
Zhao W.,Kridel S.,Thorburn A.,Kooshki M.,Little J.,Hebbar S.,Robbins M.
Fatty acid synthase: a novel target for antiglioma therapy.
Br. J. Cancer
95
869-878
2006
1057485
Choi M.S.,Jung J.Y.,Kim H.J.,Ham M.R.,Lee T.R.,Shin D.W.
S-nitrosylation of fatty acid synthase regulates its activity through dimerization.
J. Lipid Res.
57
607-615
2016
1057486
Andersen J.S.,Wilkinson C.J.,Mayor T.,Mortensen P.,Nigg E.A.,Mann M.
Proteomic characterization of the human centrosome by protein correlation profiling.
Nature
426
570-574
2003
1057487
Chi A.,Valencia J.C.,Hu Z.-Z.,Watabe H.,Yamaguchi H.,Mangini N.J.,Huang H.,Canfield V.A.,Cheng K.C.,Yang F.,Abe R.,Yamagishi S.,Shabanowitz J.,Hearing V.J.,Wu C.,Appella E.,Hunt D.F.
Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.
J. Proteome Res.
5
3135-3144
2006
1057488
Beausoleil S.A.,Villen J.,Gerber S.A.,Rush J.,Gygi S.P.
A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
Nat. Biotechnol.
24
1285-1292
2006
1057489
Dephoure N.,Zhou C.,Villen J.,Beausoleil S.A.,Bakalarski C.E.,Elledge S.J.,Gygi S.P.
A quantitative atlas of mitotic phosphorylation.
Proc. Natl. Acad. Sci. U.S.A.
105
10762-10767
2008
1057490
Gauci S.,Helbig A.O.,Slijper M.,Krijgsveld J.,Heck A.J.,Mohammed S.
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
Anal. Chem.
81
4493-4501
2009
1057491
Oppermann F.S.,Gnad F.,Olsen J.V.,Hornberger R.,Greff Z.,Keri G.,Mann M.,Daub H.
Large-scale proteomics analysis of the human kinome.
Mol. Cell. Proteomics
8
1751-1764
2009
1057492
Choudhary C.,Kumar C.,Gnad F.,Nielsen M.L.,Rehman M.,Walther T.C.,Olsen J.V.,Mann M.
Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Science
325
834-840
2009
1057493
Olsen J.V.,Vermeulen M.,Santamaria A.,Kumar C.,Miller M.L.,Jensen L.J.,Gnad F.,Cox J.,Jensen T.S.,Nigg E.A.,Brunak S.,Mann M.
Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
Sci. Signal.
3
0-0
2010
1057494
Burkard T.R.,Planyavsky M.,Kaupe I.,Breitwieser F.P.,Buerckstuemmer T.,Bennett K.L.,Superti-Furga G.,Colinge J.
Initial characterization of the human central proteome.
BMC Syst. Biol.
5
17-17
2011
1057495
Bienvenut W.V.,Sumpton D.,Martinez A.,Lilla S.,Espagne C.,Meinnel T.,Giglione C.
Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.
Mol. Cell. Proteomics
11
0-0
2012
1057496
Zhou H.,Di Palma S.,Preisinger C.,Peng M.,Polat A.N.,Heck A.J.,Mohammed S.
Toward a comprehensive characterization of a human cancer cell phosphoproteome.
J. Proteome Res.
12
260-271
2013
1057497
Bian Y.,Song C.,Cheng K.,Dong M.,Wang F.,Huang J.,Sun D.,Wang L.,Ye M.,Zou H.
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
J. Proteomics
96
253-262
2014
1057498
Impens F.,Radoshevich L.,Cossart P.,Ribet D.
Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
Proc. Natl. Acad. Sci. U.S.A.
111
12432-12437
2014
1057499
Vaca Jacome A.S.,Rabilloud T.,Schaeffer-Reiss C.,Rompais M.,Ayoub D.,Lane L.,Bairoch A.,Van Dorsselaer A.,Carapito C.
N-terminome analysis of the human mitochondrial proteome.
Proteomics
15
2519-2524
2015
1057500
Williams C.G.,Jureka A.S.,Silvas J.A.,Nicolini A.M.,Chvatal S.A.,Carlson-Stevermer J.,Oki J.,Holden K.,Basler C.F.
Inhibitors of VPS34 and fatty-acid metabolism suppress SARS-CoV-2 replication.
Cell Rep.
36
109479-109479
2021
1057501
Brink J.,Ludtke S.J.,Yang C.Y.,Gu Z.-W.,Wakil S.J.,Chiu W.
Quaternary structure of human fatty acid synthase by electron cryomicroscopy.
Proc. Natl. Acad. Sci. U.S.A.
99
138-143
2002
1057502
Chakravarty B.,Gu Z.,Chirala S.S.,Wakil S.J.,Quiocho F.A.
Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain.
Proc. Natl. Acad. Sci. U.S.A.
101
15567-15572
2004
1057503
Bunkoczi G.,Pasta S.,Joshi A.,Wu X.,Kavanagh K.L.,Smith S.,Oppermann U.
Mechanism and substrate recognition of human holo ACP synthase.
Chem. Biol.
14
1243-1253
2007
1057504
Pemble C.W. IV,Johnson L.C.,Kridel S.J.,Lowther W.T.
Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat.
Nat. Struct. Mol. Biol.
14
704-709
2007
1057506
Pinggera A.,Mackenroth L.,Rump A.,Schallner J.,Beleggia F.,Wollnik B.,Striessnig J.
New gain-of-function mutation shows CACNA1D as recurrently mutated gene in autism spectrum disorders and epilepsy.
Hum. Mol. Genet.
26
2923-2932
2017
