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P49327

- FAS_HUMAN

UniProt

P49327 - FAS_HUMAN

Protein

Fatty acid synthase

Gene

FASN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 3 (24 Nov 2009)
      Previous versions | rss
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    Functioni

    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.

    Catalytic activityi

    Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) CoA + n CO2 + 2n NADP+.1 Publication
    Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].1 Publication
    Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].1 Publication
    Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].1 Publication
    (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.1 Publication
    A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.1 Publication
    An acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH.1 Publication
    Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei161 – 1611For beta-ketoacyl synthase activityPROSITE-ProRule annotation
    Active sitei581 – 5811For malonyltransferase activityPROSITE-ProRule annotation
    Active sitei878 – 8781For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation
    Active sitei2308 – 23081For thioesterase activity1 PublicationPROSITE-ProRule annotation
    Active sitei2481 – 24811For thioesterase activityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1671 – 168818NADP (ER)By similarityAdd
    BLAST
    Nucleotide bindingi1886 – 190116NADP (KR)By similarityAdd
    BLAST

    GO - Molecular functioni

    1. [acyl-carrier-protein] S-acetyltransferase activity Source: UniProtKB-EC
    2. [acyl-carrier-protein] S-malonyltransferase activity Source: UniProtKB-EC
    3. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
    4. 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Source: InterPro
    5. 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB-EC
    6. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: UniProtKB-EC
    7. drug binding Source: Ensembl
    8. enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity Source: UniProtKB-EC
    9. enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Source: InterPro
    10. fatty acid synthase activity Source: Reactome
    11. myristoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
    12. NADPH binding Source: Ensembl
    13. oleoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
    14. palmitoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
    15. poly(A) RNA binding Source: UniProtKB
    16. protein binding Source: UniProtKB
    17. zinc ion binding Source: InterPro

    GO - Biological processi

    1. acetyl-CoA metabolic process Source: Ensembl
    2. cellular lipid metabolic process Source: Reactome
    3. cellular response to interleukin-4 Source: Ensembl
    4. energy reserve metabolic process Source: Reactome
    5. fatty acid biosynthetic process Source: UniProtKB-KW
    6. fatty acid metabolic process Source: ProtInc
    7. long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
    8. osteoblast differentiation Source: UniProt
    9. pantothenate metabolic process Source: Reactome
    10. positive regulation of cellular metabolic process Source: Reactome
    11. small molecule metabolic process Source: Reactome
    12. triglyceride biosynthetic process Source: Reactome
    13. vitamin metabolic process Source: Reactome
    14. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Lyase, Oxidoreductase, Transferase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    NAD, NADP, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09992-MONOMER.
    ReactomeiREACT_11172. Vitamin B5 (pantothenate) metabolism.
    REACT_1319. Fatty Acyl-CoA Biosynthesis.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_2122. ChREBP activates metabolic gene expression.
    SABIO-RKP49327.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid synthase (EC:2.3.1.85)
    Including the following 7 domains:
    [Acyl-carrier-protein] S-acetyltransferase (EC:2.3.1.38)
    [Acyl-carrier-protein] S-malonyltransferase (EC:2.3.1.39)
    3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.41)
    3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.100)
    3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.59)
    Enoyl-[acyl-carrier-protein] reductase (EC:1.3.1.39)
    Oleoyl-[acyl-carrier-protein] hydrolase (EC:3.1.2.14)
    Gene namesi
    Name:FASN
    Synonyms:FAS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:3594. FASN.

    Subcellular locationi

    Cytoplasm 1 Publication. Melanosome 1 Publication
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. glycogen granule Source: Ensembl
    5. Golgi apparatus Source: HPA
    6. melanosome Source: UniProtKB-SubCell
    7. membrane Source: UniProtKB
    8. mitochondrion Source: Ensembl
    9. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28006.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25112511Fatty acid synthasePRO_0000180276Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei70 – 701N6-acetyllysine1 Publication
    Modified residuei207 – 2071Phosphoserine1 Publication
    Modified residuei298 – 2981N6-acetyllysine1 Publication
    Modified residuei436 – 4361N6-acetyllysine1 Publication
    Modified residuei528 – 5281N6-acetyllysine1 Publication
    Modified residuei673 – 6731N6-acetyllysine1 Publication
    Modified residuei992 – 9921N6-acetyllysineBy similarity
    Modified residuei1704 – 17041N6-(pyridoxal phosphate)lysine; alternateBy similarity
    Modified residuei1704 – 17041N6-acetyllysine; alternate1 Publication
    Modified residuei1771 – 17711N6-acetyllysine1 Publication
    Modified residuei1847 – 18471N6-acetyllysine1 Publication
    Modified residuei1995 – 19951N6-acetyllysine1 Publication
    Modified residuei2156 – 21561O-(pantetheine 4'-phosphoryl)serine1 PublicationPROSITE-ProRule annotation
    Modified residuei2198 – 21981Phosphoserine2 Publications
    Modified residuei2204 – 22041Phosphothreonine3 Publications
    Modified residuei2236 – 22361Phosphoserine1 Publication
    Modified residuei2391 – 23911N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphopantetheine, Phosphoprotein

    Proteomic databases

    MaxQBiP49327.
    PaxDbiP49327.
    PRIDEiP49327.

    PTM databases

    PhosphoSiteiP49327.

    Expressioni

    Tissue specificityi

    Ubiquitous. Prominent expression in brain, lung, and liver.2 Publications

    Gene expression databases

    BgeeiP49327.
    CleanExiHS_FAS.
    HS_FASN.
    GenevestigatoriP49327.

    Organism-specific databases

    HPAiCAB005192.
    CAB015417.
    HPA006461.

    Interactioni

    Subunit structurei

    Homodimer which is arranged in a head to tail fashion.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q99IB86EBI-356658,EBI-6927928From a different organism.

    Protein-protein interaction databases

    BioGridi108488. 51 interactions.
    DIPiDIP-33681N.
    IntActiP49327. 27 interactions.
    MINTiMINT-1146154.

    Structurei

    Secondary structure

    1
    2511
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1310
    Beta strandi16 – 183
    Helixi19 – 279
    Beta strandi36 – 405
    Helixi44 – 463
    Turni62 – 665
    Helixi69 – 735
    Helixi77 – 9216
    Helixi97 – 1004
    Beta strandi106 – 1105
    Helixi115 – 1206
    Turni124 – 1263
    Helixi130 – 1356
    Helixi139 – 14810
    Beta strandi154 – 1585
    Helixi160 – 1623
    Helixi163 – 17614
    Beta strandi181 – 1899
    Helixi194 – 2029
    Beta strandi227 – 2359
    Helixi236 – 2383
    Beta strandi243 – 25311
    Helixi266 – 27914
    Helixi284 – 2863
    Beta strandi287 – 2915
    Helixi300 – 31213
    Beta strandi320 – 3234
    Helixi326 – 3294
    Helixi333 – 3353
    Helixi336 – 35015
    Helixi367 – 3704
    Beta strandi373 – 3764
    Beta strandi387 – 3937
    Beta strandi397 – 40610
    Helixi416 – 4194
    Beta strandi422 – 4309
    Helixi431 – 44313
    Turni444 – 4463
    Helixi448 – 45710
    Turni462 – 4643
    Beta strandi467 – 47711
    Beta strandi481 – 4844
    Beta strandi492 – 4965
    Turni504 – 5096
    Helixi510 – 5123
    Helixi514 – 52714
    Helixi528 – 5303
    Helixi534 – 5396
    Helixi545 – 5473
    Helixi549 – 56921
    Beta strandi575 – 5795
    Helixi583 – 5908
    Helixi596 – 61116
    Beta strandi618 – 6258
    Helixi627 – 6337
    Beta strandi639 – 6457
    Beta strandi648 – 6547
    Helixi655 – 66713
    Beta strandi672 – 6754
    Beta strandi677 – 6793
    Helixi685 – 6906
    Helixi691 – 70111
    Beta strandi702 – 7043
    Beta strandi715 – 7173
    Helixi719 – 7213
    Helixi725 – 7284
    Helixi732 – 7409
    Helixi745 – 7495
    Beta strandi757 – 7648
    Helixi768 – 7747
    Beta strandi780 – 7834
    Helixi792 – 80514
    Helixi812 – 8154
    Helixi831 – 8333
    Helixi847 – 8493
    Helixi2127 – 21348
    Turni2149 – 21535
    Helixi2156 – 217015
    Helixi2176 – 21805
    Helixi2184 – 21929
    Helixi2219 – 22224
    Beta strandi2230 – 22334
    Beta strandi2239 – 22413
    Beta strandi2244 – 22474
    Helixi2255 – 22573
    Helixi2258 – 22636
    Beta strandi2268 – 22714
    Helixi2282 – 229312
    Turni2294 – 22963
    Beta strandi2303 – 23075
    Helixi2309 – 232517
    Beta strandi2333 – 23386
    Helixi2343 – 235210
    Helixi2360 – 237516
    Helixi2380 – 23878
    Beta strandi2390 – 23923
    Helixi2393 – 240715
    Helixi2413 – 243220
    Beta strandi2443 – 24475
    Turni2459 – 24635
    Helixi2464 – 24663
    Beta strandi2472 – 24765
    Helixi2483 – 24853
    Helixi2487 – 249913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XKTX-ray2.60A/B2218-2502[»]
    2CG5X-ray2.70B2119-2207[»]
    2JFDX-ray2.81A/B/C/D422-823[»]
    2JFKX-ray2.40A/B/C/D422-831[»]
    2PX6X-ray2.30A/B2200-2511[»]
    3HHDX-ray2.15A/B/C/D2-963[»]
    3TJMX-ray1.48A2218-2500[»]
    ProteinModelPortaliP49327.
    SMRiP49327. Positions 2-853, 1220-2114, 2124-2194, 2218-2491.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49327.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2123 – 217957Acyl carrierPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 414414Beta-ketoacyl synthaseBy similarityAdd
    BLAST
    Regioni429 – 817389Acyl and malonyl transferasesBy similarityAdd
    BLAST
    Regioni1635 – 1863229Enoyl reductaseBy similarityAdd
    BLAST
    Regioni1864 – 2118255Beta-ketoacyl reductaseBy similarityAdd
    BLAST
    Regioni2207 – 2511305ThioesteraseBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 acyl carrier domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3319.
    HOVERGENiHBG005640.
    InParanoidiP49327.
    KOiK00665.
    OMAiGPGPHWD.
    OrthoDBiEOG71K623.
    PhylomeDBiP49327.
    TreeFamiTF300549.

    Family and domain databases

    Gene3Di1.10.1200.10. 1 hit.
    1.10.1470.20. 1 hit.
    3.40.366.10. 2 hits.
    3.40.47.10. 2 hits.
    3.40.50.150. 1 hit.
    3.40.50.1820. 2 hits.
    3.40.50.720. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR001227. Ac_transferase_dom.
    IPR009081. Acyl_carrier_prot-like.
    IPR014043. Acyl_transferase.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR013149. ADH_C.
    IPR002198. DH_sc/Rdtase_SDR.
    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.
    IPR006162. PPantetheine_attach_site.
    IPR029063. SAM-dependent_MTases-like.
    IPR001031. Thioesterase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view]
    PfamiPF00698. Acyl_transf_1. 1 hit.
    PF00106. adh_short. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    PF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    PF08242. Methyltransf_12. 1 hit.
    PF00550. PP-binding. 1 hit.
    PF00975. Thioesterase. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    SM00822. PKS_KR. 1 hit.
    [Graphical view]
    SUPFAMiSSF47336. SSF47336. 1 hit.
    SSF50129. SSF50129. 1 hit.
    SSF52151. SSF52151. 2 hits.
    SSF53335. SSF53335. 1 hit.
    SSF53474. SSF53474. 1 hit.
    SSF53901. SSF53901. 2 hits.
    SSF55048. SSF55048. 1 hit.
    PROSITEiPS50075. ACP_DOMAIN. 1 hit.
    PS00606. B_KETOACYL_SYNTHASE. 1 hit.
    PS00012. PHOSPHOPANTETHEINE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P49327-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEEVVIAGMS GKLPESENLQ EFWDNLIGGV DMVTDDDRRW KAGLYGLPRR     50
    SGKLKDLSRF DASFFGVHPK QAHTMDPQLR LLLEVTYEAI VDGGINPDSL 100
    RGTHTGVWVG VSGSETSEAL SRDPETLVGY SMVGCQRAMM ANRLSFFFDF 150
    RGPSIALDTA CSSSLMALQN AYQAIHSGQC PAAIVGGINV LLKPNTSVQF 200
    LRLGMLSPEG TCKAFDTAGN GYCRSEGVVA VLLTKKSLAR RVYATILNAG 250
    TNTDGFKEQG VTFPSGDIQE QLIRSLYQSA GVAPESFEYI EAHGTGTKVG 300
    DPQELNGITR ALCATRQEPL LIGSTKSNMG HPEPASGLAA LAKVLLSLEH 350
    GLWAPNLHFH SPNPEIPALL DGRLQVVDQP LPVRGGNVGI NSFGFGGSNV 400
    HIILRPNTQP PPAPAPHATL PRLLRASGRT PEAVQKLLEQ GLRHSQDLAF 450
    LSMLNDIAAV PATAMPFRGY AVLGGERGGP EVQQVPAGER PLWFICSGMG 500
    TQWRGMGLSL MRLDRFRDSI LRSDEAVKPF GLKVSQLLLS TDESTFDDIV 550
    HSFVSLTAIQ IGLIDLLSCM GLRPDGIVGH SLGEVACGYA DGCLSQEEAV 600
    LAAYWRGQCI KEAHLPPGAM AAVGLSWEEC KQRCPPGVVP ACHNSKDTVT 650
    ISGPQAPVFE FVEQLRKEGV FAKEVRTGGM AFHSYFMEAI APPLLQELKK 700
    VIREPKPRSA RWLSTSIPEA QWHSSLARTS SAEYNVNNLV SPVLFQEALW 750
    HVPEHAVVLE IAPHALLQAV LKRGLKPSCT IIPLMKKDHR DNLEFFLAGI 800
    GRLHLSGIDA NPNALFPPVE FPAPRGTPLI SPLIKWDHSL AWDVPAAEDF 850
    PNGSGSPSAA IYNIDTSSES PDHYLVDHTL DGRVLFPATG YLSIVWKTLA 900
    RALGLGVEQL PVVFEDVVLH QATILPKTGT VSLEVRLLEA SRAFEVSENG 950
    NLVVSGKVYQ WDDPDPRLFD HPESPTPNPT EPLFLAQAEV YKELRLRGYD 1000
    YGPHFQGILE ASLEGDSGRL LWKDNWVSFM DTMLQMSILG SAKHGLYLPT 1050
    RVTAIHIDPA THRQKLYTLQ DKAQVADVVV SRWLRVTVAG GVHISGLHTE 1100
    SAPRRQQEQQ VPILEKFCFT PHTEEGCLSE RAALQEELQL CKGLVQALQT 1150
    KVTQQGLKMV VPGLDGAQIP RDPSQQELPR LLSAACRLQL NGNLQLELAQ 1200
    VLAQERPKLP EDPLLSGLLD SPALKACLDT AVENMPSLKM KVVEVLAGHG 1250
    HLYSRIPGLL SPHPLLQLSY TATDRHPQAL EAAQAELQQH DVAQGQWDPA 1300
    DPAPSALGSA DLLVCNCAVA ALGDPASALS NMVAALREGG FLLLHTLLRG 1350
    HPLGDIVAFL TSTEPQYGQG ILSQDAWESL FSRVSLRLVG LKKSFYGSTL 1400
    FLCRRPTPQD SPIFLPVDDT SFRWVESLKG ILADEDSSRP VWLKAINCAT 1450
    SGVVGLVNCL RREPGGNRLR CVLLSNLSST SHVPEVDPGS AELQKVLQGD 1500
    LVMNVYRDGA WGAFRHFLLE EDKPEEPTAH AFVSTLTRGD LSSIRWVCSS 1550
    LRHAQPTCPG AQLCTVYYAS LNFRDIMLAT GKLSPDAIPG KWTSQDSLLG 1600
    MEFSGRDASG KRVMGLVPAK GLATSVLLSP DFLWDVPSNW TLEEAASVPV 1650
    VYSTAYYALV VRGRVRPGET LLIHSGSGGV GQAAIAIALS LGCRVFTTVG 1700
    SAEKRAYLQA RFPQLDSTSF ANSRDTSFEQ HVLWHTGGKG VDLVLNSLAE 1750
    EKLQASVRCL ATHGRFLEIG KFDLSQNHPL GMAIFLKNVT FHGVLLDAFF 1800
    NESSADWREV WALVQAGIRD GVVRPLKCTV FHGAQVEDAF RYMAQGKHIG 1850
    KVVVQVLAEE PEAVLKGAKP KLMSAISKTF CPAHKSYIIA GGLGGFGLEL 1900
    AQWLIQRGVQ KLVLTSRSGI RTGYQAKQVR RWRRQGVQVQ VSTSNISSLE 1950
    GARGLIAEAA QLGPVGGVFN LAVVLRDGLL ENQTPEFFQD VCKPKYSGTL 2000
    NLDRVTREAC PELDYFVVFS SVSCGRGNAG QSNYGFANSA MERICEKRRH 2050
    EGLPGLAVQW GAIGDVGILV ETMSTNDTIV SGTLPQRMAS CLEVLDLFLN 2100
    QPHMVLSSFV LAEKAAAYRD RDSQRDLVEA VAHILGIRDL AAVNLDSSLA 2150
    DLGLDSLMSV EVRQTLEREL NLVLSVREVR QLTLRKLQEL SSKADEASEL 2200
    ACPTPKEDGL AQQQTQLNLR SLLVNPEGPT LMRLNSVQSS ERPLFLVHPI 2250
    EGSTTVFHSL ASRLSIPTYG LQCTRAAPLD SIHSLAAYYI DCIRQVQPEG 2300
    PYRVAGYSYG ACVAFEMCSQ LQAQQSPAPT HNSLFLFDGS PTYVLAYTQS 2350
    YRAKLTPGCE AEAETEAICF FVQQFTDMEH NRVLEALLPL KGLEERVAAA 2400
    VDLIIKSHQG LDRQELSFAA RSFYYKLRAA EQYTPKAKYH GNVMLLRAKT 2450
    GGAYGEDLGA DYNLSQVCDG KVSVHVIEGD HRTLLEGSGL ESIISIIHSS 2500
    LAEPRVSVRE G 2511
    Length:2,511
    Mass (Da):273,427
    Last modified:November 24, 2009 - v3
    Checksum:i7A07171FEFA3287B
    GO

    Sequence cautioni

    The sequence AAC50259.1 differs from that shown. Reason: Several sequencing errors.
    The sequence AAB35516.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE06070.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti459 – 4624AVPA → LSPT in AAA73576. 1 PublicationCurated
    Sequence conflicti528 – 5292KP → NR in AAA73576. 1 PublicationCurated
    Sequence conflicti637 – 6371G → A in AAA73576. 1 PublicationCurated
    Sequence conflicti801 – 8011G → R in AAA73576. 1 PublicationCurated
    Sequence conflicti902 – 9021A → P in AAA73576. 1 PublicationCurated
    Sequence conflicti958 – 9581V → M in AAS09886. 1 PublicationCurated
    Sequence conflicti1121 – 11211P → S in AAA73576. 1 PublicationCurated
    Sequence conflicti1121 – 11211P → S in AAS09886. 1 PublicationCurated
    Sequence conflicti1151 – 11511K → T in AAH63242. (PubMed:15489334)Curated
    Sequence conflicti1353 – 13564LGDI → SGH in AAA73576. 1 PublicationCurated
    Sequence conflicti1386 – 13861L → V in AAA73576. 1 PublicationCurated
    Sequence conflicti1467 – 14682NR → T in AAA73576. 1 PublicationCurated
    Sequence conflicti1827 – 18271K → E in AAS09886. 1 PublicationCurated
    Sequence conflicti1934 – 19341R → A in AAA73576. 1 PublicationCurated
    Sequence conflicti2065 – 20651D → H in AAB35516. (PubMed:7595075)Curated
    Sequence conflicti2087 – 20871R → A in AAA73576. 1 PublicationCurated
    Sequence conflicti2363 – 23631A → P in AAB35516. (PubMed:7595075)Curated
    Sequence conflicti2428 – 24281R → G in AAA73576. 1 PublicationCurated
    Sequence conflicti2453 – 24531A → T in AAB35516. (PubMed:7595075)Curated
    Sequence conflicti2456 – 24561E → Q in AAB35516. (PubMed:7595075)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1483 – 14831V → I.
    Corresponds to variant rs2228305 [ dbSNP | Ensembl ].
    VAR_055479
    Natural varianti1694 – 16941R → H.
    Corresponds to variant rs2229424 [ dbSNP | Ensembl ].
    VAR_055480
    Natural varianti1888 – 18881I → V.
    Corresponds to variant rs2228307 [ dbSNP | Ensembl ].
    VAR_055481

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26644 mRNA. Translation: AAC50259.1. Sequence problems.
    U29344 mRNA. Translation: AAA73576.1.
    AY451392 mRNA. Translation: AAS09886.1.
    AB209988 mRNA. Translation: BAE06070.1. Different initiation.
    AC135056 Genomic DNA. No translation available.
    BC007267 mRNA. Translation: AAH07267.1.
    BC007909 mRNA. Translation: AAH07909.1.
    BC014634 mRNA. Translation: AAH14634.2.
    BC063242 mRNA. Translation: AAH63242.1.
    S80437 mRNA. Translation: AAB35516.1. Different initiation.
    CCDSiCCDS11801.1.
    PIRiA57788.
    G01880.
    RefSeqiNP_004095.4. NM_004104.4.
    UniGeneiHs.83190.

    Genome annotation databases

    EnsembliENST00000306749; ENSP00000304592; ENSG00000169710.
    GeneIDi2194.
    KEGGihsa:2194.
    UCSCiuc002kdu.3. human.

    Polymorphism databases

    DMDMi269849686.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26644 mRNA. Translation: AAC50259.1 . Sequence problems.
    U29344 mRNA. Translation: AAA73576.1 .
    AY451392 mRNA. Translation: AAS09886.1 .
    AB209988 mRNA. Translation: BAE06070.1 . Different initiation.
    AC135056 Genomic DNA. No translation available.
    BC007267 mRNA. Translation: AAH07267.1 .
    BC007909 mRNA. Translation: AAH07909.1 .
    BC014634 mRNA. Translation: AAH14634.2 .
    BC063242 mRNA. Translation: AAH63242.1 .
    S80437 mRNA. Translation: AAB35516.1 . Different initiation.
    CCDSi CCDS11801.1.
    PIRi A57788.
    G01880.
    RefSeqi NP_004095.4. NM_004104.4.
    UniGenei Hs.83190.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XKT X-ray 2.60 A/B 2218-2502 [» ]
    2CG5 X-ray 2.70 B 2119-2207 [» ]
    2JFD X-ray 2.81 A/B/C/D 422-823 [» ]
    2JFK X-ray 2.40 A/B/C/D 422-831 [» ]
    2PX6 X-ray 2.30 A/B 2200-2511 [» ]
    3HHD X-ray 2.15 A/B/C/D 2-963 [» ]
    3TJM X-ray 1.48 A 2218-2500 [» ]
    ProteinModelPortali P49327.
    SMRi P49327. Positions 2-853, 1220-2114, 2124-2194, 2218-2491.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108488. 51 interactions.
    DIPi DIP-33681N.
    IntActi P49327. 27 interactions.
    MINTi MINT-1146154.

    Chemistry

    ChEMBLi CHEMBL4158.
    DrugBanki DB01034. Cerulenin.
    DB01083. Orlistat.

    PTM databases

    PhosphoSitei P49327.

    Polymorphism databases

    DMDMi 269849686.

    Proteomic databases

    MaxQBi P49327.
    PaxDbi P49327.
    PRIDEi P49327.

    Protocols and materials databases

    DNASUi 2194.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306749 ; ENSP00000304592 ; ENSG00000169710 .
    GeneIDi 2194.
    KEGGi hsa:2194.
    UCSCi uc002kdu.3. human.

    Organism-specific databases

    CTDi 2194.
    GeneCardsi GC17M080037.
    H-InvDB HIX0014269.
    HGNCi HGNC:3594. FASN.
    HPAi CAB005192.
    CAB015417.
    HPA006461.
    MIMi 600212. gene.
    neXtProti NX_P49327.
    PharmGKBi PA28006.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3319.
    HOVERGENi HBG005640.
    InParanoidi P49327.
    KOi K00665.
    OMAi GPGPHWD.
    OrthoDBi EOG71K623.
    PhylomeDBi P49327.
    TreeFami TF300549.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS09992-MONOMER.
    Reactomei REACT_11172. Vitamin B5 (pantothenate) metabolism.
    REACT_1319. Fatty Acyl-CoA Biosynthesis.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_2122. ChREBP activates metabolic gene expression.
    SABIO-RK P49327.

    Miscellaneous databases

    ChiTaRSi FASN. human.
    EvolutionaryTracei P49327.
    GeneWikii Fatty_acid_synthase.
    GenomeRNAii 2194.
    NextBioi 8869.
    PROi P49327.
    SOURCEi Search...

    Gene expression databases

    Bgeei P49327.
    CleanExi HS_FAS.
    HS_FASN.
    Genevestigatori P49327.

    Family and domain databases

    Gene3Di 1.10.1200.10. 1 hit.
    1.10.1470.20. 1 hit.
    3.40.366.10. 2 hits.
    3.40.47.10. 2 hits.
    3.40.50.150. 1 hit.
    3.40.50.1820. 2 hits.
    3.40.50.720. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR001227. Ac_transferase_dom.
    IPR009081. Acyl_carrier_prot-like.
    IPR014043. Acyl_transferase.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR013149. ADH_C.
    IPR002198. DH_sc/Rdtase_SDR.
    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.
    IPR006162. PPantetheine_attach_site.
    IPR029063. SAM-dependent_MTases-like.
    IPR001031. Thioesterase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view ]
    Pfami PF00698. Acyl_transf_1. 1 hit.
    PF00106. adh_short. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    PF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    PF08242. Methyltransf_12. 1 hit.
    PF00550. PP-binding. 1 hit.
    PF00975. Thioesterase. 1 hit.
    [Graphical view ]
    SMARTi SM00829. PKS_ER. 1 hit.
    SM00822. PKS_KR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47336. SSF47336. 1 hit.
    SSF50129. SSF50129. 1 hit.
    SSF52151. SSF52151. 2 hits.
    SSF53335. SSF53335. 1 hit.
    SSF53474. SSF53474. 1 hit.
    SSF53901. SSF53901. 2 hits.
    SSF55048. SSF55048. 1 hit.
    PROSITEi PS50075. ACP_DOMAIN. 1 hit.
    PS00606. B_KETOACYL_SYNTHASE. 1 hit.
    PS00012. PHOSPHOPANTETHEINE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, PHOSPHOPANTETHEINYLATION AT SER-2156, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "Molecular cloning of tumor-associated human fatty acid synthase."
      Hennigar R.A., Jenner K.H., Heine H.S., Kayler A.E., Wood F.D., Kuhajda F.P., Pasternack G.R.
      Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Recharacterization of the human fatty acid synthase (FAS) gene."
      Mao J., Wakil S.J.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
      Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      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.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Eye.
    7. Bienvenut W.V.
      Submitted (JUL-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-12; 647-666; 791-802; 1242-1255; 1338-1349 AND 2126-2138, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    8. "Fatty acid synthesis: a potential selective target for antineoplastic therapy."
      Kuhajda F.P., Jenner K., Wood F.D., Hennigar R.A., Jacobs L.B., Dick J.D., Pasternack G.R.
      Proc. Natl. Acad. Sci. U.S.A. 91:6379-6383(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 753-758 AND 1285-1297.
    9. "Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation."
      Semenkovich C.F., Coleman T., Fiedorek F.T. Jr.
      J. Lipid Res. 36:1507-1521(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2047-2511, TISSUE SPECIFICITY.
    10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2198 AND THR-2204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-2198; THR-2204 AND SER-2236, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-298; LYS-436; LYS-528; LYS-673; LYS-1704; LYS-1771; LYS-1847 AND LYS-1995, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Quaternary structure of human fatty acid synthase by electron cryomicroscopy."
      Brink J., Ludtke S.J., Yang C.Y., Gu Z.-W., Wakil S.J., Chiu W.
      Proc. Natl. Acad. Sci. U.S.A. 99:138-143(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING, STRUCTURE BY ELECTRON CRYOMICROSCOPY.
    20. "Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain."
      Chakravarty B., Gu Z., Chirala S.S., Wakil S.J., Quiocho F.A.
      Proc. Natl. Acad. Sci. U.S.A. 101:15567-15572(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2218-2502.
    21. "Mechanism and substrate recognition of human holo ACP synthase."
      Bunkoczi G., Pasta S., Joshi A., Wu X., Kavanagh K.L., Smith S., Oppermann U.
      Chem. Biol. 14:1243-1253(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2119-2207 IN COMPLEX WITH AASDHPPT AND COENZYME A.
    22. "Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat."
      Pemble C.W. IV, Johnson L.C., Kridel S.J., Lowther W.T.
      Nat. Struct. Mol. Biol. 14:704-709(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2200-2511 IN COMPLEX WITH ORLISTAT, ACTIVE SITE FOR THIOESTERASE ACTIVITY.
    23. "Structure of the MAT domain of human FAS with malonyl-CoA."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 422-831 IN COMPLEX WITH MALONYL-COENZYME A.

    Entry informationi

    Entry nameiFAS_HUMAN
    AccessioniPrimary (citable) accession number: P49327
    Secondary accession number(s): Q13479
    , Q16702, Q4LE83, Q6P4U5, Q6SS02, Q969R1, Q96C68, Q96IT0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 165 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    The relatively low beta-ketoacyl synthase activity may be attributable to the low 4'-phosphopantetheine content of the protein.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3