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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 catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities as an acyl carrier protein.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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
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 ‘Function’ 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

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_and_taxonomy_section">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:2.3.1.85)
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)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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; 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.<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 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 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_processing_section">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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphopantetheine, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
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

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PRIDEi
P19096

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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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 335 organ(s), highest expression level in mammary gland

CleanEx database of gene expression profiles

More...
CleanExi
MM_FASN

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P19096 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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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_section">'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_section">'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)

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BioGridi
199596, 6 interactors

Protein interaction database and analysis system

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IntActi
P19096, 11 interactors

Molecular INTeraction database

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MINTi
P19096

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000052872

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P19096

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P19096

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

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SMRi
P19096

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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_and_domains_section">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
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
COG3321 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157276

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000019642

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG005640

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P19096

KEGG Orthology (KO)

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KOi
K00665

Identification of Orthologs from Complete Genome Data

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OMAi
TEALCAF

Database of Orthologous Groups

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OrthoDBi
EOG091G003K

Database for complete collections of gene phylogenies

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PhylomeDBi
P19096

TreeFam database of animal gene trees

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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
3.40.366.10, 1 hit
3.40.47.10, 1 hit
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

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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
IPR032821 KAsynt_C_assoc
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
IPR020801 PKS_acyl_transferase
IPR020841 PKS_Beta-ketoAc_synthase_dom
IPR020807 PKS_dehydratase
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

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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

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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
Fatty acid synthase
Fasn
2,502Annotation score:

Annotation score:2 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:2 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 at positions 1842, 1855, 1863, 1964 and 1967.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

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EMBLi

GenBank nucleotide sequence database

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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

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CCDSi
CCDS25759.1

Protein sequence database of the Protein Information Resource

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PIRi
A32262

NCBI Reference Sequences

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RefSeqi
NP_032014.3, NM_007988.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.236443

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000055655; ENSMUSP00000052872; ENSMUSG00000025153

Database of genes from NCBI RefSeq genomes

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GeneIDi
14104

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:14104

UCSC genome browser

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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
UniGeneiMm.236443

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5MY0X-ray2.94A/B/C/D2-852[»]
5MY2X-ray2.70A/B/C/D2-852[»]
ProteinModelPortaliP19096
SMRiP19096
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199596, 6 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

EPDiP19096
MaxQBiP19096
PaxDbiP19096
PeptideAtlasiP19096
PRIDEiP19096

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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
COG3321 LUCA
GeneTreeiENSGT00940000157276
HOGENOMiHOG000019642
HOVERGENiHBG005640
InParanoidiP19096
KOiK00665
OMAiTEALCAF
OrthoDBiEOG091G003K
PhylomeDBiP19096
TreeFamiTF300549

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

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PROi
PR:P19096

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000025153 Expressed in 335 organ(s), highest expression level in mammary gland
CleanExiMM_FASN
ExpressionAtlasiP19096 baseline and differential
GenevisibleiP19096 MM

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
1.10.1470.20, 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
IPR032821 KAsynt_C_assoc
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
IPR020801 PKS_acyl_transferase
IPR020841 PKS_Beta-ketoAc_synthase_dom
IPR020807 PKS_dehydratase
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...

<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_and_isoforms">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: December 5, 2018
This is version 190 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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