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Entry version 204 (10 Feb 2021)
Sequence version 2 (11 Oct 2004)
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Protein

Fatty acid synthase

Gene

Fasn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.28 µM for malonyl-CoA1 Publication
  2. KM=1.63 µM for acetyl-CoA1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: fatty acid biosynthesis

    This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.1 Publication
    View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei161For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
    Active sitei581For malonyltransferase activityPROSITE-ProRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei671Acyl-CoACombined sources1 Publication1
    Binding sitei773Acyl-CoACombined sources1 Publication1
    Active sitei878For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation1
    Active sitei2301For thioesterase activityPROSITE-ProRule annotation1
    Active sitei2474For thioesterase activityPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi1664 – 1681NADP (ER)By similarityAdd BLAST18
    Nucleotide bindingi1879 – 1894NADP (KR)By similarityAdd BLAST16

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase, Lyase, Multifunctional enzyme, Oxidoreductase, Transferase
    Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
    LigandNAD, NADP, Pyridoxal phosphate

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-MMU-163765, ChREBP activates metabolic gene expression
    R-MMU-199220, Vitamin B5 (pantothenate) metabolism
    R-MMU-75105, Fatty acyl-CoA biosynthesis

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00094

    Protein family/group databases

    ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

    More...
    ESTHERi
    mouse-FASN, Thioesterase

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Fatty acid synthase (EC:2.3.1.851 Publication)
    Alternative name(s):
    Type I Fatty Acid Synthase1 Publication
    Including the following 7 domains:
    [Acyl-carrier-protein] S-acetyltransferase (EC:2.3.1.381 Publication)
    [Acyl-carrier-protein] S-malonyltransferase (EC:2.3.1.391 Publication)
    3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.411 Publication)
    3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.100By similarity)
    3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.59By similarity)
    Enoyl-[acyl-carrier-protein] reductase (EC:1.3.1.39By similarity)
    Acyl-[acyl-carrier-protein] hydrolase (EC:3.1.2.14By similarity)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:Fasn
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

    Organism-specific databases

    Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

    More...
    MGIi
    MGI:95485, Fasn

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL1795189

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001802771 – 2504Fatty acid synthaseAdd BLAST2504

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionine1 Publication1
    Modified residuei59N6-acetyllysineCombined sources1
    Modified residuei63PhosphoserineBy similarity1
    Modified residuei70N6-acetyllysineBy similarity1
    Modified residuei207PhosphoserineBy similarity1
    Modified residuei298N6-acetyllysineBy similarity1
    Modified residuei528N6-acetyllysineBy similarity1
    Modified residuei673N6-acetyllysineBy similarity1
    Modified residuei725PhosphoserineCombined sources1
    Modified residuei790N6-acetyllysineCombined sources1
    Modified residuei993N6-acetyllysineCombined sources1
    Modified residuei1071N6-acetyllysineCombined sources1
    Modified residuei1276N6-acetyllysineCombined sources1
    Modified residuei1464S-nitrosocysteineBy similarity1
    Modified residuei1577PhosphoserineCombined sources1
    Modified residuei1587PhosphoserineCombined sources1
    Modified residuei1697N6-(pyridoxal phosphate)lysine; alternateBy similarity1
    Modified residuei1697N6-acetyllysine; alternateBy similarity1
    Modified residuei1764N6-acetyllysineBy similarity1
    Modified residuei1840N6-acetyllysineCombined sources1
    Modified residuei1988N6-acetyllysineBy similarity1
    Modified residuei2084S-nitrosocysteineBy similarity1
    Modified residuei2150O-(pantetheine 4'-phosphoryl)serine; alternatePROSITE-ProRule annotation1
    Modified residuei2150Phosphoserine; alternateBy similarity1
    Modified residuei2190PhosphoserineCombined sources1
    Modified residuei2229PhosphoserineBy similarity1
    Modified residuei2384N6-acetyllysineCombined sources1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki2442Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    S-nitrosylation of Fatty acid synthase at cysteine residues Cys-1464 or Cys-2084 is important for the enzyme dimerization. In adipocytes, S-nitrosylation of Fatty acid synthase occurs under physiological conditions and gradually increases during adipogenesis.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphopantetheine, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    The CPTAC Assay portal

    More...
    CPTACi
    non-CPTAC-3808

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P19096

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P19096

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P19096

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P19096

    PeptideAtlas

    More...
    PeptideAtlasi
    P19096

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P19096

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P19096

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P19096

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P19096

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Up-regulated by endocannabinoid anandamide/AEA.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSMUSG00000025153, Expressed in mammary gland and 350 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P19096, baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P19096, MM

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer which is arranged in a head to tail fashion (By similarity).

    Interacts with CEACAM1; this interaction is insulin and phosphorylation-dependent; reduces fatty-acid synthase activity (By similarity).

    By similarity

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    199596, 23 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P19096, 11 interactors

    Molecular INTeraction database

    More...
    MINTi
    P19096

    STRING: functional protein association networks

    More...
    STRINGi
    10090.ENSMUSP00000052872

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P19096

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P19096, protein

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    12504
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P19096

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2112 – 2192CarrierPROSITE-ProRule annotationAdd BLAST81

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 414Beta-ketoacyl synthaseAdd BLAST414
    Regioni429 – 817Acyl and malonyl transferasesAdd BLAST389
    Regioni647 – 648Acyl-CoA bindingCombined sources1 Publication2
    Regioni1628 – 1856Enoyl reductaseAdd BLAST229
    Regioni1857 – 2111Beta-ketoacyl reductaseAdd BLAST255
    Regioni2201 – 2504ThioesteraseAdd BLAST304

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1202, Eukaryota

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000157276

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_000022_31_7_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P19096

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    CKVYYAS

    Database of Orthologous Groups

    More...
    OrthoDBi
    19161at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P19096

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF300549

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.1200.10, 1 hit
    1.10.1470.20, 1 hit
    3.10.129.110, 1 hit
    3.40.366.10, 1 hit
    3.40.47.10, 1 hit
    3.40.50.1820, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR029058, AB_hydrolase
    IPR001227, Ac_transferase_dom_sf
    IPR036736, ACP-like_sf
    IPR014043, Acyl_transferase
    IPR016035, Acyl_Trfase/lysoPLipase
    IPR013149, ADH_C
    IPR023102, Fatty_acid_synthase_dom_2
    IPR011032, GroES-like_sf
    IPR018201, Ketoacyl_synth_AS
    IPR014031, Ketoacyl_synth_C
    IPR014030, Ketoacyl_synth_N
    IPR016036, Malonyl_transacylase_ACP-bd
    IPR013217, Methyltransf_12
    IPR036291, NAD(P)-bd_dom_sf
    IPR032821, PKS_assoc
    IPR020841, PKS_Beta-ketoAc_synthase_dom
    IPR020807, PKS_dehydratase
    IPR042104, PKS_dehydratase_sf
    IPR020843, PKS_ER
    IPR013968, PKS_KR
    IPR020806, PKS_PP-bd
    IPR009081, PP-bd_ACP
    IPR006162, Ppantetheine_attach_site
    IPR029063, SAM-dependent_MTases
    IPR001031, Thioesterase
    IPR016039, Thiolase-like

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00698, Acyl_transf_1, 1 hit
    PF00107, ADH_zinc_N, 1 hit
    PF16197, KAsynt_C_assoc, 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
    PF14765, PS-DH, 1 hit
    PF00975, Thioesterase, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00827, PKS_AT, 1 hit
    SM00826, PKS_DH, 1 hit
    SM00829, PKS_ER, 1 hit
    SM00825, PKS_KS, 1 hit
    SM00823, PKS_PP, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF47336, SSF47336, 1 hit
    SSF50129, SSF50129, 1 hit
    SSF51735, SSF51735, 2 hits
    SSF52151, SSF52151, 1 hit
    SSF53335, SSF53335, 1 hit
    SSF53474, SSF53474, 1 hit
    SSF53901, SSF53901, 1 hit
    SSF55048, SSF55048, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00606, B_KETOACYL_SYNTHASE, 1 hit
    PS50075, CARRIER, 1 hit
    PS00012, PHOSPHOPANTETHEINE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

    P19096-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR
    60 70 80 90 100
    SGKLKDLSKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL
    110 120 130 140 150
    RGTNTGVWVG VSGSEASEAL SRDPETLLGY SMVGCQRAMM ANRLSFFFDF
    160 170 180 190 200
    KGPSIALDTA CSSSLLALQN AYQAIRSGEC PAALVGGINL LLKPNTSVQF
    210 220 230 240 250
    MKLGMLSPDG TCRSFDDSGS GYCRSEAVVA VLLTKKSLAR RVYATILNAG
    260 270 280 290 300
    TNTDGSKEQG VTFPSGEVQE QLICSLYQPA GLAPESLEYI EAHGTGTKVG
    310 320 330 340 350
    DPQELNGITR SLCAFRQAPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEH
    360 370 380 390 400
    GVWAPNLHFH NPNPEIPALL DGRLQVVDRP LPVRGGNVGI NSFGFGGSNV
    410 420 430 440 450
    HVILQPNTRQ APAPTAHAAL PHLLHASGRT LEAVQDLLEQ GRQHSQDLAF
    460 470 480 490 500
    VSMLNDIAAT PTAAMPFRGY TVLGVEGRVQ EVQQVSTNKR PLWFICSGMG
    510 520 530 540 550
    TQWRGMGLSL MRLDSFRESI LRSDEAVKPL GVKVSDLLLS TDERTFDDIV
    560 570 580 590 600
    HAFVSLTAIQ IALIDLLTSV GLKPDGIIGH SLGEVACGYA DGCLSQREAV
    610 620 630 640 650
    LAAYWRGQCI KDAHLPPGSM AAVGLSWEEC KQRCPAGVVP ACHNSEDTVT
    660 670 680 690 700
    ISGPQAAVNE FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK
    710 720 730 740 750
    VIREPRPRSA RWLSTSIPEA QWQSSLARTS SAEYNVNNLV SPVLFQEALW
    760 770 780 790 800
    HIPEHAVVLE IAPHALLQAV LKRGVKSSCT IIPLMKRDHK DNLEFFLTNL
    810 820 830 840 850
    GKVHLTGINV NPNALFPPVE FPAPRGTPLI SPHIKWDHSQ TWDVPVAEDF
    860 870 880 890 900
    PNGSSSSSAT VYSIDASPES PDHYLVDHCI DGRVIFPGTG YLCLVWKTLA
    910 920 930 940 950
    RSLGLSLEET PVVFENVSFH QATILPKTGT VALEVRLLEA SHAFEVSDTG
    960 970 980 990 1000
    NLIVSGKVYL WEDPNSKLFD HPEVPTPPES ASVSRLTQGE VYKELRLRGY
    1010 1020 1030 1040 1050
    DYGPQFQGIC EATLEGEQGK LLWKDNWVTF MDTMLQVSIL GSSQQSLQLP
    1060 1070 1080 1090 1100
    TRVTAIYIDP ATHRQKVYRL KEDTQVADVT TSRCLGITVS GGIHISRLQT
    1110 1120 1130 1140 1150
    TATSRRQQEQ LVPTLEKFVF TPHMEAECLS ESTALQKELQ LCKGLARALQ
    1160 1170 1180 1190 1200
    TKATQQGLKA AMLGQEDPPQ HGLPRLLAAA CQLQLNGNLQ LELGEALAQE
    1210 1220 1230 1240 1250
    RLLLPEDPLI SGLLNSQALK ACVDTALENL STLKMKVAEV LAGEGHLYSR
    1260 1270 1280 1290 1300
    IPALLNTQPM LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWNPSDPAPS
    1310 1320 1330 1340 1350
    SLGALDLLVC NCALATLGDP ALALDNMVAA LKEGGFLLVH TVLKGHALGE
    1360 1370 1380 1390 1400
    TLACLPSEVQ PAPSLLSQEE WESLFSRKAL HLVGLKRSFY GTALFLCRRA
    1410 1420 1430 1440 1450
    IPQEKPIFLS VEDTSFQWVD SLKSTLATSS SQPVWLTAMD CPTSGVVGLV
    1460 1470 1480 1490 1500
    NCLRKEPGGH RIRCILLSNL SNTSHAPKLD PGSPELQQVL KHDLVMNVYR
    1510 1520 1530 1540 1550
    DGAWGAFRHF QLEQDKPKEQ TAHAFVNVLT RGDLASIRWV SSPLKHTQPS
    1560 1570 1580 1590 1600
    SSGAQLCTVY YASLNFRDIM LATGKLSPDA IPGKWASRDC MLGMEFSGRD
    1610 1620 1630 1640 1650
    RCGRRVMGLV PAEGLATSVL LSSDFLWDVP SSWTLEEAAS VPVVYTTAYY
    1660 1670 1680 1690 1700
    SLVVRGRIQR GETVLIHSGS GGVGQAAISI ALSLGCRVFT TVGSAEKRAY
    1710 1720 1730 1740 1750
    LQARFPQLDD TSFANSRDTS FEQHVLLHTG GKGVDLVLNS LAEEKLQASV
    1760 1770 1780 1790 1800
    RCLAQHGRFL EIGKFDLSNN HPLGMAIFLK NVTFHGILLD ALFEEANDSW
    1810 1820 1830 1840 1850
    REVAALLKAG IRDGVVKPLK CTVFPKAQVE DAFRYMAQGK HIGKVLVQVR
    1860 1870 1880 1890 1900
    EEEPEAVLPG AQPTLISAIS KTFCPAHKSY IITGGLGGFG LELARWLVLR
    1910 1920 1930 1940 1950
    GAQRLVLTSR SGIRTGYQAK HIREWRRQGI QVLVSTSNVS SLEGARALIA
    1960 1970 1980 1990 2000
    EATKLGPVGG VFNLAMVLRD AMLENQTPEL FQDVNKPKYN GTLNLDRATR
    2010 2020 2030 2040 2050
    EACPELDYFV AFSSVSCGRG NAGQTNYGFA NSTMERICEQ RRHDGLPGLA
    2060 2070 2080 2090 2100
    VQWGAIGDVG IVLEAMGTND TVIGGTLPQR ISSCMEVLDL FLNQPHAVLS
    2110 2120 2130 2140 2150
    SFVLAEKKAV AHGDGDTQRD LVKAVAHILG IRDLAGINLD STLADLGLDS
    2160 2170 2180 2190 2200
    LMGVEVRQIL EREHDLVLPM REVRQLTLRK LQEMSSKTDS ATDTTAPKSR
    2210 2220 2230 2240 2250
    SDTSLKQNQL NLSTLLVNPE GPTLTQLNSV QSSERPLFLV HPIEGSTTVF
    2260 2270 2280 2290 2300
    HSLAAKLSVP TYGLQCTQAA PLDSIPNLAA YYIDCIKQVQ PEGPYRIAGY
    2310 2320 2330 2340 2350
    SFGACVAFEM CSQLQAQQGP APTHNNLFLF DGSHTYVLAY TQSYRAKMTP
    2360 2370 2380 2390 2400
    GCEAEAEAEA LCFFIKQFLD VEHSKVLEAL LPLKSLEDRV AASVDLITKS
    2410 2420 2430 2440 2450
    HHSLDRRELS FAAVSFYHKL RAADQYKPKA KYHGNVTLLR AKTGGTYGED
    2460 2470 2480 2490 2500
    LGADYNLSQV CDGKVSVHII EGDHRTLLEG SGLESIINII HSSLAEPRVS

    VREG
    Length:2,504
    Mass (Da):272,428
    Last modified:October 11, 2004 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2B48068B9D370C6F
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    A0A0U1RNJ1A0A0U1RNJ1_MOUSE
    3-hydroxyacyl-[acyl-carrier-protein...
    Fasn
    2,502Annotation score:

    Annotation score:5 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    A0A0U1RPP5A0A0U1RPP5_MOUSE
    Fatty acid synthase
    Fasn
    24Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence CAA31525 differs from that shown. Reason: Frameshift.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti1992T → N in CAA31525 (PubMed:2920037).Curated1
    Sequence conflicti2028G → C in CAA31525 (PubMed:2920037).Curated1
    Sequence conflicti2045G → V in CAA31525 (PubMed:2920037).Curated1
    Sequence conflicti2117T → N in CAA31525 (PubMed:2920037).Curated1
    Sequence conflicti2175Q → R in CAA31525 (PubMed:2920037).Curated1
    Sequence conflicti2295Y → H in CAA31525 (PubMed:2920037).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AF127033 mRNA Translation: AAG02285.1
    AL663090 Genomic DNA No translation available.
    BC046513 mRNA Translation: AAH46513.1
    BC059850 mRNA Translation: AAH59850.1
    AK080374 mRNA Translation: BAC37895.1
    X13135 mRNA Translation: CAA31525.1 Frameshift.

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS25759.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A32262

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_032014.3, NM_007988.3

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSMUST00000055655; ENSMUSP00000052872; ENSMUSG00000025153

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    14104

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mmu:14104

    UCSC genome browser

    More...
    UCSCi
    uc007mut.1, mouse

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF127033 mRNA Translation: AAG02285.1
    AL663090 Genomic DNA No translation available.
    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

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5MY0X-ray2.94A/B/C/D2-852[»]
    5MY2X-ray2.70A/B/C/D2-852[»]
    6ROPX-ray2.70A/B/C/D2-852[»]
    SMRiP19096
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi199596, 23 interactors
    IntActiP19096, 11 interactors
    MINTiP19096
    STRINGi10090.ENSMUSP00000052872

    Chemistry databases

    BindingDBiP19096
    ChEMBLiCHEMBL1795189

    Protein family/group databases

    ESTHERimouse-FASN, Thioesterase

    PTM databases

    iPTMnetiP19096
    PhosphoSitePlusiP19096
    SwissPalmiP19096

    Proteomic databases

    CPTACinon-CPTAC-3808
    EPDiP19096
    jPOSTiP19096
    MaxQBiP19096
    PaxDbiP19096
    PeptideAtlasiP19096
    PRIDEiP19096

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...
    Antibodypediai
    1650, 720 antibodies

    Genome annotation databases

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

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    2194
    MGIiMGI:95485, Fasn

    Phylogenomic databases

    eggNOGiKOG1202, Eukaryota
    GeneTreeiENSGT00940000157276
    HOGENOMiCLU_000022_31_7_1
    InParanoidiP19096
    OMAiCKVYYAS
    OrthoDBi19161at2759
    PhylomeDBiP19096
    TreeFamiTF300549

    Enzyme and pathway databases

    UniPathwayiUPA00094
    ReactomeiR-MMU-163765, ChREBP activates metabolic gene expression
    R-MMU-199220, Vitamin B5 (pantothenate) metabolism
    R-MMU-75105, Fatty acyl-CoA biosynthesis

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...
    BioGRID-ORCSi
    14104, 9 hits in 17 CRISPR screens

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    Fasn, mouse

    Protein Ontology

    More...
    PROi
    PR:P19096
    RNActiP19096, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSMUSG00000025153, Expressed in mammary gland and 350 other tissues
    ExpressionAtlasiP19096, baseline and differential
    GenevisibleiP19096, MM

    Family and domain databases

    Gene3Di1.10.1200.10, 1 hit
    1.10.1470.20, 1 hit
    3.10.129.110, 1 hit
    3.40.366.10, 1 hit
    3.40.47.10, 1 hit
    3.40.50.1820, 1 hit
    InterProiView protein in InterPro
    IPR029058, AB_hydrolase
    IPR001227, Ac_transferase_dom_sf
    IPR036736, ACP-like_sf
    IPR014043, Acyl_transferase
    IPR016035, Acyl_Trfase/lysoPLipase
    IPR013149, ADH_C
    IPR023102, Fatty_acid_synthase_dom_2
    IPR011032, GroES-like_sf
    IPR018201, Ketoacyl_synth_AS
    IPR014031, Ketoacyl_synth_C
    IPR014030, Ketoacyl_synth_N
    IPR016036, Malonyl_transacylase_ACP-bd
    IPR013217, Methyltransf_12
    IPR036291, NAD(P)-bd_dom_sf
    IPR032821, PKS_assoc
    IPR020841, PKS_Beta-ketoAc_synthase_dom
    IPR020807, PKS_dehydratase
    IPR042104, PKS_dehydratase_sf
    IPR020843, PKS_ER
    IPR013968, PKS_KR
    IPR020806, PKS_PP-bd
    IPR009081, PP-bd_ACP
    IPR006162, Ppantetheine_attach_site
    IPR029063, SAM-dependent_MTases
    IPR001031, Thioesterase
    IPR016039, Thiolase-like
    PfamiView protein in Pfam
    PF00698, Acyl_transf_1, 1 hit
    PF00107, ADH_zinc_N, 1 hit
    PF16197, KAsynt_C_assoc, 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
    PF14765, PS-DH, 1 hit
    PF00975, Thioesterase, 1 hit
    SMARTiView protein in SMART
    SM00827, PKS_AT, 1 hit
    SM00826, PKS_DH, 1 hit
    SM00829, PKS_ER, 1 hit
    SM00825, PKS_KS, 1 hit
    SM00823, PKS_PP, 1 hit
    SUPFAMiSSF47336, SSF47336, 1 hit
    SSF50129, SSF50129, 1 hit
    SSF51735, SSF51735, 2 hits
    SSF52151, SSF52151, 1 hit
    SSF53335, SSF53335, 1 hit
    SSF53474, SSF53474, 1 hit
    SSF53901, SSF53901, 1 hit
    SSF55048, SSF55048, 1 hit
    PROSITEiView protein in PROSITE
    PS00606, B_KETOACYL_SYNTHASE, 1 hit
    PS50075, CARRIER, 1 hit
    PS00012, PHOSPHOPANTETHEINE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFAS_MOUSE
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P19096
    Secondary accession number(s): B1ATU8
    , Q6PB72, Q8C4Z0, Q9EQR0
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: October 11, 2004
    Last modified: February 10, 2021
    This is version 204 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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