Fasn
entrez
50671
canonical
uniprot
P12785
canonical
ensembl
ENSRNOG00000045636
resolver
ensembl
ENSRNOG00055032554
resolver
ensembl
ENSRNOG00060009215
resolver
ensembl
ENSRNOG00065004831
resolver
ensp
ENSRNOP00000064445
resolver
ensp
ENSRNOP00055046446
resolver
ensp
ENSRNOP00060012144
resolver
ensp
ENSRNOP00065004819
resolver
enst
ENSRNOT00000073321
resolver
enst
ENSRNOT00055056294
resolver
enst
ENSRNOT00060015551
resolver
enst
ENSRNOT00065007006
resolver
genesymbol
Fasn
resolver
uniprot
O09187
resolver
uniprot
O09190
resolver
uniprot
Q63577
resolver
uniprot
Q64717
resolver
uniprot_entry
FAS_RAT
resolver
uniprot_sec
O09187
resolver
uniprot_sec
O09190
resolver
uniprot_sec
Q63577
resolver
uniprot_sec
Q64717
resolver
activity_regulation
ACTIVITY REGULATION: Cerulenin, a potent non-competitive pharmacological inhibitor of FAS, binds covalently to the active site of the condensing enzyme region, inactivating a key enzyme step in fatty acid synthesis (PubMed:16969344). Another inhibitor, though less efficient, is C75, a member of the alpha-methylene-gamma-butyrolactone chemical class, also proposed as an antitumour and anti-obesity agent (PubMed:15715522). {ECO:0000269|PubMed:15715522, ECO:0000269|PubMed:16969344}.
uniprot
proteins
amino_acid_sequence
MEEVVIAGMSGKLPESENLQEFWANLIGGVDMVTDDDRRWKAGLYGLPKRSGKLKDLSKFDASFFGVHPKQAHTMDPQLRLLLEVSYEAIVDGGINPASLRGTNTGVWVGVSGSEASEALSRDPETLLGYSMVGCQRAMMANRLSFFFDFKGPSIALDTACSSSLLALQNAYQAIRSGECPAAIVGGINLLLKPNTSVQFMKLGMLSPDGTCRSFDDSGNGYCRAEAVVAVLLTKKSLARRVYATILNAGTNTDGCKEQGVTFPSGEAQEQLIRSLYQPGGVAPESLEYIEAHGTGTKVGDPQELNGITRSLCAFRQSPLLIGSTKSNMGHPEPASGLAALTKVLLSLENGVWAPNLHFHNPNPEIPALLDGRLQVVDRPLPVRGGIVGINSFGFGGANVHVILQPNTQQAPAPAPHAALPHLLHASGRTMEAVQGLLEQGRQHSQDLAFVSMLNDIAATPTAAMPFRGYTVLGVEGHVQEVQQVPASQRPLWFICSGMGTQWRGMGLSLMRLDSFRESILRSDEALKPLGVKVSDLLLSTDEHTFDDIVHSFVSLTAIQIALIDLLTSMGLKPDGIIGHSLGEVACGYADGCLSQREAVLAAYWRGQCIKDANLPAGSMAAVGLSWEECKQRCPPGVVPACHNSEDTVTISGPQAAVNEFVEQLKQEGVFAKEVRTGGLAFHSYFMEGIAPTLLQALKKVIREPRPRSARWLSTSIPEAQWQSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGVKPSCTIIPLMKRDHKDNLEFFLTNLGKVHLTGIDINPNALFPPVEFPVPRGTPLISPHIKWDHSQTWDIPVAEDFPNGSSSSSATVYNIDASSESSDHYLVDHCIDGRVLFPGTGYLYLVWKTLARSLSLSLEETPVVFENVTFHQATILPRTGTVPLEVRLLEASHAFEVSDSGNLIVSGKVYQWEDPDSKLFDHPEVPIPAESESVSRLTQGEVYKELRLRGYDYGPHFQGVYEATLEGEQGKLLWKDNWVTFMDTMLQISILGFSKQSLQLPTRVTAIYIDPATHLQKVYMLEGDTQVADVTTSRCLGVTVSGGVYISRLQTTATSRRQQEQLVPTLEKFVFTPHVEPECLSESAILQKELQLCKGLAKALQTKATQQGLKMTVPGLEDLPQHGLPRLLAAACQLQLNGNLQLELGEVLARERLLLPEDPLISGLLNSQALKACIDTALENLSTLKMKVVEVLAGEGHLYSHISALLNTQPMLQLEYTATDRHPQALKDVQTKLQQHDVAQGQWDPSGPAPTNLGALDLVVCNCALATLGDPALALDNMVAALKDGGFLLMHTVLKGHALGETLACLPSEVQPGPSFLSQEEWESLFSRKALHLVGLKKSFYGTALFLCRRLSPQDKPIFLPVEDTSFQWVDSLKSILATSSSQPVWLTAMNCPTSGVVGLVNCLRKEPGGHRIRCILLSNLSSTSHVPKLDPGSSELQKVLESDLVMNVYRDGAWGAFRHFQLEQDKPEEQTAHAFVNVLTRGDLASIRWVSSPLKHMQPPSSSGAQLCTVYYASLNFRDIMLATGKLSPDAIPGKWASRDCMLGMEFSGRDKCGRRVMGLVPAEGLATSVLLSPDFLWDVPSSWTLEEAASVPVVYTTAYYSLVVRGRIQHGETVLIHSGSGGVGQAAISIALSLGCRVFTTVGSAEKRAYLQARFPQLDDTSFANSRDTSFEQHVLLHTGGKGVDLVLNSLAEEKLQASVRCLAQHGRFLEIGKFDLSNNHPLGMAIFLKNVTFHGILLDALFEGANDSWREVAELLKAGIRDGVVKPLKCTVFPKAQVEDAFRYMAQGKHIGKVLVQVREEEPEAMLPGAQPTLISAISKTFCPEHKSYIITGGLGGFGLELARWLVLRGAQRLVLTSRSGIRTGYQAKHVREWRRQGIHVLVSTSNVSSLEGARALIAEATKLGPVGGVFNLAMVLRDAMLENQTPELFQDVNKPKYNGTLNLDRATREACPELDYFVAFSSVSCGRGNAGQSNYGFANSTMERICEQRRHDGLPGLAVQWGAIGDVGIILEAMGTNDTVVGGTLPQRISSCMEVLDLFLNQPHAVLSSFVLAEKKAVAHGDGEAQRDLVKAVAHILGIRDLAGINLDSSLADLGLDSLMGVEVRQILEREHDLVLPIREVRQLTLRKLQEMSSKAGSDTELAAPKSKNDTSLKQAQLNLSILLVNPEGPTLTRLNSVQSSERPLFLVHPIEGSITVFHSLAAKLSVPTYGLQCTQAAPLDSIPNLAAYYIDCIKQVQPEGPYRVAGYSFGACVAFEMCSQLQAQQGPAPAHNNLFLFDGSHTYVLAYTQSYRAKLTPGCEAEAEAEAICFFIKQFVDAEHSKVLEALLPLKSLEDRVAAAVDLITRSHQSLDRRDLSFAAVSFYYKLRAADQYKPKAKYHGNVILLRAKTGGTYGEDLGADYNLSQVCDGKVSVHIIEGDHRTLLEGRGLESIINIIHSSLAEPRVSVREG
uniprot
proteins
ec_number
1.1.1.100
uniprot
proteins
ec_number
1.3.1.39
uniprot
proteins
ec_number
2.3.1.38
uniprot
proteins
ec_number
2.3.1.39
uniprot
proteins
ec_number
2.3.1.41
uniprot
proteins
ec_number
2.3.1.85
uniprot
proteins
ec_number
3.1.2.14
uniprot
proteins
ec_number
4.2.1.59
uniprot
proteins
function
FUNCTION: Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain. {ECO:0000269|PubMed:15715522, ECO:0000269|PubMed:18096506, ECO:0000269|PubMed:8250834, ECO:0000269|PubMed:8756713, ECO:0000305|PubMed:9405069}.
uniprot
proteins
mass_dalton
272650
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000269|PubMed:15715522, ECO:0000269|PubMed:8250834, ECO:0000269|PubMed:8756713}.
uniprot
proteins
post_translational_modification
PTM: S-nitrosylation of Fatty acid synthase at cysteine residues Cys-1464 or Cys-2085 is important for the enzyme dimerization. In adipocytes, S-nitrosylation of Fatty acid synthase occurs under physiological conditions and gradually increases during adipogenesis. {ECO:0000250|UniProtKB:P49327}.
uniprot
proteins
pubmed
12926246
uniprot
proteins
pubmed
1339331
uniprot
proteins
pubmed
15715522
uniprot
proteins
pubmed
16054098
uniprot
proteins
pubmed
16969344
uniprot
proteins
pubmed
1736293
uniprot
proteins
pubmed
18096506
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2313386
uniprot
proteins
pubmed
2717611
uniprot
proteins
pubmed
2891707
uniprot
proteins
pubmed
2915923
uniprot
proteins
pubmed
3109907
uniprot
proteins
pubmed
8250834
uniprot
proteins
pubmed
8756713
uniprot
proteins
pubmed
9405069
uniprot
proteins
sequence_length
2505
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}.
uniprot
proteins