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P19096

- FAS_MOUSE

UniProt

P19096 - FAS_MOUSE

Protein

Fatty acid synthase

Gene

Fasn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (11 Oct 2004)
      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+.
    Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].
    Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].
    Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].
    (3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
    A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.
    An acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH.
    Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.

    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 sitei2301 – 23011For thioesterase activityPROSITE-ProRule annotation
    Active sitei2474 – 24741For thioesterase activityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1664 – 168118NADP (ER)By similarityAdd
    BLAST
    Nucleotide bindingi1879 – 189416NADP (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. myristoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
    11. NADPH binding Source: Ensembl
    12. oleoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
    13. palmitoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
    14. zinc ion binding Source: InterPro

    GO - Biological processi

    1. acetyl-CoA metabolic process Source: Ensembl
    2. cellular response to interleukin-4 Source: MGI
    3. fatty acid biosynthetic process Source: UniProtKB-KW

    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

    ReactomeiREACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_221573. Vitamin B5 (pantothenate) metabolism.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:95485. Fasn.

    Subcellular locationi

    Cytoplasm By similarity. Melanosome By similarity

    GO - Cellular componenti

    1. glycogen granule Source: MGI
    2. Golgi apparatus Source: Ensembl
    3. melanosome Source: UniProtKB-SubCell
    4. mitochondrion Source: MGI
    5. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25042504Fatty acid synthasePRO_0000180277Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei59 – 591N6-acetyllysine1 Publication
    Modified residuei70 – 701N6-acetyllysineBy similarity
    Modified residuei207 – 2071PhosphoserineBy similarity
    Modified residuei298 – 2981N6-acetyllysineBy similarity
    Modified residuei528 – 5281N6-acetyllysineBy similarity
    Modified residuei673 – 6731N6-acetyllysineBy similarity
    Modified residuei790 – 7901N6-acetyllysine1 Publication
    Modified residuei993 – 9931N6-acetyllysine1 Publication
    Modified residuei1071 – 10711N6-acetyllysine1 Publication
    Modified residuei1276 – 12761N6-acetyllysine1 Publication
    Modified residuei1697 – 16971N6-(pyridoxal phosphate)lysine; alternateBy similarity
    Modified residuei1697 – 16971N6-acetyllysine; alternateBy similarity
    Modified residuei1764 – 17641N6-acetyllysineBy similarity
    Modified residuei1840 – 18401N6-acetyllysine1 Publication
    Modified residuei1988 – 19881N6-acetyllysineBy similarity
    Modified residuei2150 – 21501O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
    Modified residuei2229 – 22291PhosphoserineBy similarity
    Modified residuei2384 – 23841N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphopantetheine, Phosphoprotein

    Proteomic databases

    MaxQBiP19096.
    PaxDbiP19096.
    PRIDEiP19096.

    PTM databases

    PhosphoSiteiP19096.

    Expressioni

    Gene expression databases

    BgeeiP19096.
    CleanExiMM_FASN.
    GenevestigatoriP19096.

    Interactioni

    Subunit structurei

    Homodimer which is arranged in a head to tail fashion.

    Protein-protein interaction databases

    BioGridi199596. 4 interactions.
    IntActiP19096. 8 interactions.
    MINTiMINT-2514287.

    Structurei

    3D structure databases

    ProteinModelPortaliP19096.
    SMRiP19096. Positions 2-853, 1215-2107, 2113-2201, 2211-2484.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2117 – 217357Acyl carrierPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 414414Beta-ketoacyl synthaseAdd
    BLAST
    Regioni429 – 817389Acyl and malonyl transferasesAdd
    BLAST
    Regioni1628 – 1856229Enoyl reductaseAdd
    BLAST
    Regioni1857 – 2111255Beta-ketoacyl reductaseAdd
    BLAST
    Regioni2201 – 2504304ThioesteraseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 acyl carrier domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3319.
    GeneTreeiENSGT00530000063309.
    HOGENOMiHOG000019642.
    HOVERGENiHBG005640.
    InParanoidiB1ATU8.
    KOiK00665.
    OMAiRRCNERS.
    OrthoDBiEOG71K623.
    PhylomeDBiP19096.
    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.
    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.
    IPR029063. SAM-dependent_MTases-like.
    IPR001031. Thioesterase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view]
    PfamiPF00698. Acyl_transf_1. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    PF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    PF08659. KR. 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.

    P19096-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR     50
    SGKLKDLSKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL 100
    RGTNTGVWVG VSGSEASEAL SRDPETLLGY SMVGCQRAMM ANRLSFFFDF 150
    KGPSIALDTA CSSSLLALQN AYQAIRSGEC PAALVGGINL LLKPNTSVQF 200
    MKLGMLSPDG TCRSFDDSGS GYCRSEAVVA VLLTKKSLAR RVYATILNAG 250
    TNTDGSKEQG VTFPSGEVQE QLICSLYQPA GLAPESLEYI EAHGTGTKVG 300
    DPQELNGITR SLCAFRQAPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEH 350
    GVWAPNLHFH NPNPEIPALL DGRLQVVDRP LPVRGGNVGI NSFGFGGSNV 400
    HVILQPNTRQ APAPTAHAAL PHLLHASGRT LEAVQDLLEQ GRQHSQDLAF 450
    VSMLNDIAAT PTAAMPFRGY TVLGVEGRVQ EVQQVSTNKR PLWFICSGMG 500
    TQWRGMGLSL MRLDSFRESI LRSDEAVKPL GVKVSDLLLS TDERTFDDIV 550
    HAFVSLTAIQ IALIDLLTSV GLKPDGIIGH SLGEVACGYA DGCLSQREAV 600
    LAAYWRGQCI KDAHLPPGSM AAVGLSWEEC KQRCPAGVVP ACHNSEDTVT 650
    ISGPQAAVNE FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK 700
    VIREPRPRSA RWLSTSIPEA QWQSSLARTS SAEYNVNNLV SPVLFQEALW 750
    HIPEHAVVLE IAPHALLQAV LKRGVKSSCT IIPLMKRDHK DNLEFFLTNL 800
    GKVHLTGINV NPNALFPPVE FPAPRGTPLI SPHIKWDHSQ TWDVPVAEDF 850
    PNGSSSSSAT VYSIDASPES PDHYLVDHCI DGRVIFPGTG YLCLVWKTLA 900
    RSLGLSLEET PVVFENVSFH QATILPKTGT VALEVRLLEA SHAFEVSDTG 950
    NLIVSGKVYL WEDPNSKLFD HPEVPTPPES ASVSRLTQGE VYKELRLRGY 1000
    DYGPQFQGIC EATLEGEQGK LLWKDNWVTF MDTMLQVSIL GSSQQSLQLP 1050
    TRVTAIYIDP ATHRQKVYRL KEDTQVADVT TSRCLGITVS GGIHISRLQT 1100
    TATSRRQQEQ LVPTLEKFVF TPHMEAECLS ESTALQKELQ LCKGLARALQ 1150
    TKATQQGLKA AMLGQEDPPQ HGLPRLLAAA CQLQLNGNLQ LELGEALAQE 1200
    RLLLPEDPLI SGLLNSQALK ACVDTALENL STLKMKVAEV LAGEGHLYSR 1250
    IPALLNTQPM LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWNPSDPAPS 1300
    SLGALDLLVC NCALATLGDP ALALDNMVAA LKEGGFLLVH TVLKGHALGE 1350
    TLACLPSEVQ PAPSLLSQEE WESLFSRKAL HLVGLKRSFY GTALFLCRRA 1400
    IPQEKPIFLS VEDTSFQWVD SLKSTLATSS SQPVWLTAMD CPTSGVVGLV 1450
    NCLRKEPGGH RIRCILLSNL SNTSHAPKLD PGSPELQQVL KHDLVMNVYR 1500
    DGAWGAFRHF QLEQDKPKEQ TAHAFVNVLT RGDLASIRWV SSPLKHTQPS 1550
    SSGAQLCTVY YASLNFRDIM LATGKLSPDA IPGKWASRDC MLGMEFSGRD 1600
    RCGRRVMGLV PAEGLATSVL LSSDFLWDVP SSWTLEEAAS VPVVYTTAYY 1650
    SLVVRGRIQR GETVLIHSGS GGVGQAAISI ALSLGCRVFT TVGSAEKRAY 1700
    LQARFPQLDD TSFANSRDTS FEQHVLLHTG GKGVDLVLNS LAEEKLQASV 1750
    RCLAQHGRFL EIGKFDLSNN HPLGMAIFLK NVTFHGILLD ALFEEANDSW 1800
    REVAALLKAG IRDGVVKPLK CTVFPKAQVE DAFRYMAQGK HIGKVLVQVR 1850
    EEEPEAVLPG AQPTLISAIS KTFCPAHKSY IITGGLGGFG LELARWLVLR 1900
    GAQRLVLTSR SGIRTGYQAK HIREWRRQGI QVLVSTSNVS SLEGARALIA 1950
    EATKLGPVGG VFNLAMVLRD AMLENQTPEL FQDVNKPKYN GTLNLDRATR 2000
    EACPELDYFV AFSSVSCGRG NAGQTNYGFA NSTMERICEQ RRHDGLPGLA 2050
    VQWGAIGDVG IVLEAMGTND TVIGGTLPQR ISSCMEVLDL FLNQPHAVLS 2100
    SFVLAEKKAV AHGDGDTQRD LVKAVAHILG IRDLAGINLD STLADLGLDS 2150
    LMGVEVRQIL EREHDLVLPM REVRQLTLRK LQEMSSKTDS ATDTTAPKSR 2200
    SDTSLKQNQL NLSTLLVNPE GPTLTQLNSV QSSERPLFLV HPIEGSTTVF 2250
    HSLAAKLSVP TYGLQCTQAA PLDSIPNLAA YYIDCIKQVQ PEGPYRIAGY 2300
    SFGACVAFEM CSQLQAQQGP APTHNNLFLF DGSHTYVLAY TQSYRAKMTP 2350
    GCEAEAEAEA LCFFIKQFLD VEHSKVLEAL LPLKSLEDRV AASVDLITKS 2400
    HHSLDRRELS FAAVSFYHKL RAADQYKPKA KYHGNVTLLR AKTGGTYGED 2450
    LGADYNLSQV CDGKVSVHII EGDHRTLLEG SGLESIINII HSSLAEPRVS 2500
    VREG 2504
    Length:2,504
    Mass (Da):272,428
    Last modified:October 11, 2004 - v2
    Checksum:i2B48068B9D370C6F
    GO

    Sequence cautioni

    The sequence CAA31525.1 differs from that shown. Reason: Frameshift at positions 1842, 1855, 1863, 1964 and 1967.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1992 – 19921T → N in CAA31525. (PubMed:2920037)Curated
    Sequence conflicti2028 – 20281G → C in CAA31525. (PubMed:2920037)Curated
    Sequence conflicti2045 – 20451G → V in CAA31525. (PubMed:2920037)Curated
    Sequence conflicti2117 – 21171T → N in CAA31525. (PubMed:2920037)Curated
    Sequence conflicti2175 – 21751Q → R in CAA31525. (PubMed:2920037)Curated
    Sequence conflicti2295 – 22951Y → H in CAA31525. (PubMed:2920037)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF127033 mRNA. Translation: AAG02285.1.
    AL663090 Genomic DNA. Translation: CAM27545.1.
    BC046513 mRNA. Translation: AAH46513.1.
    BC059850 mRNA. Translation: AAH59850.1.
    AK080374 mRNA. Translation: BAC37895.1.
    X13135 mRNA. Translation: CAA31525.1. Frameshift.
    CCDSiCCDS25759.1.
    PIRiA32262.
    RefSeqiNP_032014.3. NM_007988.3.
    UniGeneiMm.236443.

    Genome annotation databases

    EnsembliENSMUST00000055655; ENSMUSP00000052872; ENSMUSG00000025153.
    GeneIDi14104.
    KEGGimmu:14104.
    UCSCiuc007mut.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF127033 mRNA. Translation: AAG02285.1 .
    AL663090 Genomic DNA. Translation: CAM27545.1 .
    BC046513 mRNA. Translation: AAH46513.1 .
    BC059850 mRNA. Translation: AAH59850.1 .
    AK080374 mRNA. Translation: BAC37895.1 .
    X13135 mRNA. Translation: CAA31525.1 . Frameshift.
    CCDSi CCDS25759.1.
    PIRi A32262.
    RefSeqi NP_032014.3. NM_007988.3.
    UniGenei Mm.236443.

    3D structure databases

    ProteinModelPortali P19096.
    SMRi P19096. Positions 2-853, 1215-2107, 2113-2201, 2211-2484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199596. 4 interactions.
    IntActi P19096. 8 interactions.
    MINTi MINT-2514287.

    Chemistry

    BindingDBi P19096.
    ChEMBLi CHEMBL1795189.

    PTM databases

    PhosphoSitei P19096.

    Proteomic databases

    MaxQBi P19096.
    PaxDbi P19096.
    PRIDEi P19096.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000055655 ; ENSMUSP00000052872 ; ENSMUSG00000025153 .
    GeneIDi 14104.
    KEGGi mmu:14104.
    UCSCi uc007mut.1. mouse.

    Organism-specific databases

    CTDi 2194.
    MGIi MGI:95485. Fasn.

    Phylogenomic databases

    eggNOGi COG3319.
    GeneTreei ENSGT00530000063309.
    HOGENOMi HOG000019642.
    HOVERGENi HBG005640.
    InParanoidi B1ATU8.
    KOi K00665.
    OMAi RRCNERS.
    OrthoDBi EOG71K623.
    PhylomeDBi P19096.
    TreeFami TF300549.

    Enzyme and pathway databases

    Reactomei REACT_198969. Activation of gene expression by SREBF (SREBP).
    REACT_221573. Vitamin B5 (pantothenate) metabolism.

    Miscellaneous databases

    NextBioi 285138.
    PROi P19096.
    SOURCEi Search...

    Gene expression databases

    Bgeei P19096.
    CleanExi MM_FASN.
    Genevestigatori P19096.

    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.
    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.
    IPR029063. SAM-dependent_MTases-like.
    IPR001031. Thioesterase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view ]
    Pfami PF00698. Acyl_transf_1. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    PF00109. ketoacyl-synt. 1 hit.
    PF02801. Ketoacyl-synt_C. 1 hit.
    PF08659. KR. 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. "Involvement of fatty acid synthase in axonal development in mouse embryos."
      Ueno K.
      Genes Cells 5:859-869(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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].
      Strain: FVB/N.
      Tissue: Brain and Liver.
    4. Bienvenut W.V.
      Submitted (JUL-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-12; 225-235; 299-310; 385-409; 469-478; 1252-1270; 1333-1344; 1388-1398; 1501-1508; 1705-1717; 1733-1745; 2124-2132; 2376-2384 AND 2476-2498, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Liver.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1527-2504.
      Strain: C57BL/6J.
      Tissue: Thymus.
    6. "Structure of mouse fatty acid synthase mRNA. Identification of the two NADPH binding sites."
      Paulauskis J.D., Sul H.S.
      Biochem. Biophys. Res. Commun. 158:690-695(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1666-2504.
      Strain: CD-1.
      Tissue: Liver.
    7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-790; LYS-993; LYS-1071; LYS-1276; LYS-1840 AND LYS-2384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiFAS_MOUSE
    AccessioniPrimary (citable) accession number: P19096
    Secondary accession number(s): B1ATU8
    , Q6PB72, Q8C4Z0, Q9EQR0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3