UniProtKB - P19096 (FAS_MOUSE)
Protein
Fatty acid synthase
Gene
Fasn
Organism
Mus musculus (Mouse)
Status
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
Catalytic activityi
- acetyl-CoA + 2n H+ + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + n CO2 + (n+1) CoA + 2n NADP+1 PublicationEC:2.3.1.851 PublicationThis reaction proceeds in the forward1 Publication direction.
- EC:2.3.1.381 PublicationThis reaction proceeds in the forward1 Publication direction.
- EC:2.3.1.391 PublicationThis reaction proceeds in the forward1 Publication direction.
- EC:2.3.1.411 PublicationThis reaction proceeds in the forward1 Publication direction.
- EC:1.1.1.100By similarityThis reaction proceeds in the backwardBy similarity direction.
- EC:4.2.1.59By similarityThis reaction proceeds in the forwardBy similarity direction.
- EC:1.3.1.39By similarityThis reaction proceeds in the backwardBy similarity direction.
- EC:3.1.2.14By similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- EC:3.1.2.14By similarityThis reaction proceeds in the forwardBy similarity direction.
Kineticsi
- KM=1.28 µM for malonyl-CoA1 Publication
- KM=1.63 µM for acetyl-CoA1 Publication
: fatty acid biosynthesis Pathwayi
This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.1 PublicationView all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 161 | For beta-ketoacyl synthase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 581 | For malonyltransferase activityPROSITE-ProRule annotation | 1 | |
Binding sitei | 671 | Acyl-CoACombined sources1 Publication | 1 | |
Binding sitei | 773 | Acyl-CoACombined sources1 Publication | 1 | |
Active sitei | 878 | For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2301 | For thioesterase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2474 | For thioesterase activityPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1664 – 1681 | NADP (ER)By similarityAdd BLAST | 18 | |
Nucleotide bindingi | 1879 – 1894 | NADP (KR)By similarityAdd BLAST | 16 |
GO - Molecular functioni
- (3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
- [acyl-carrier-protein] S-acetyltransferase activity Source: UniProtKB-EC
- [acyl-carrier-protein] S-malonyltransferase activity Source: MGI
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
- 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
- 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
- 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB-EC
- 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: UniProtKB-EC
- 3-oxo-glutaryl-[acp] methyl ester reductase activity Source: UniProtKB-EC
- 3-oxo-pimeloyl-[acp] methyl ester reductase activity Source: UniProtKB-EC
- drug binding Source: MGI
- enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity Source: UniProtKB-EC
- fatty acid synthase activity Source: MGI
- identical protein binding Source: MGI
- myristoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
- NADPH binding Source: MGI
- oleoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
- palmitoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
- phosphopantetheine binding Source: InterPro
GO - Biological processi
- acetyl-CoA metabolic process Source: MGI
- cellular response to interleukin-4 Source: MGI
- fatty acid biosynthetic process Source: MGI
- mammary gland development Source: CACAO
Keywordsi
Molecular function | Hydrolase, Lyase, Multifunctional enzyme, Oxidoreductase, Transferase |
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Ligand | NAD, NADP, Pyridoxal phosphate |
Enzyme and pathway databases
Reactomei | R-MMU-163765, ChREBP activates metabolic gene expression R-MMU-199220, Vitamin B5 (pantothenate) metabolism R-MMU-75105, Fatty acyl-CoA biosynthesis |
UniPathwayi | UPA00094 |
Protein family/group databases
ESTHERi | mouse-FASN, Thioesterase |
Names & Taxonomyi
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) |
Gene namesi | Name:Fasn |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:95485, Fasn |
Subcellular locationi
Other locations
- Cytoplasm By similarity
- Melanosome By similarity
Cytosol
- cytosol Source: MGI
Golgi apparatus
- Golgi apparatus Source: MGI
Mitochondrion
- mitochondrion Source: MGI
Plasma Membrane
- plasma membrane Source: MGI
Other locations
- cytoplasm Source: MGI
- glycogen granule Source: MGI
- melanosome Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000180277 | 1 – 2504 | Fatty acid synthaseAdd BLAST | 2504 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionine1 Publication | 1 | |
Modified residuei | 59 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 63 | PhosphoserineBy similarity | 1 | |
Modified residuei | 70 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 207 | PhosphoserineBy similarity | 1 | |
Modified residuei | 298 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 528 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 673 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 725 | PhosphoserineCombined sources | 1 | |
Modified residuei | 790 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 993 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1071 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1276 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1464 | S-nitrosocysteineBy similarity | 1 | |
Modified residuei | 1577 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1587 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1697 | N6-(pyridoxal phosphate)lysine; alternateBy similarity | 1 | |
Modified residuei | 1697 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 1764 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 1840 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 1988 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 2084 | S-nitrosocysteineBy similarity | 1 | |
Modified residuei | 2150 | O-(pantetheine 4'-phosphoryl)serine; alternatePROSITE-ProRule annotation | 1 | |
Modified residuei | 2150 | Phosphoserine; alternateBy similarity | 1 | |
Modified residuei | 2190 | PhosphoserineCombined sources | 1 | |
Modified residuei | 2229 | PhosphoserineBy similarity | 1 | |
Modified residuei | 2384 | N6-acetyllysineCombined sources | 1 | |
Cross-linki | 2442 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity |
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 conjugationProteomic databases
CPTACi | non-CPTAC-3808 |
EPDi | P19096 |
jPOSTi | P19096 |
MaxQBi | P19096 |
PaxDbi | P19096 |
PeptideAtlasi | P19096 |
PRIDEi | P19096 |
PTM databases
iPTMneti | P19096 |
PhosphoSitePlusi | P19096 |
SwissPalmi | P19096 |
Expressioni
Inductioni
Up-regulated by endocannabinoid anandamide/AEA.1 Publication
Gene expression databases
Bgeei | ENSMUSG00000025153, Expressed in mammary gland and 350 other tissues |
ExpressionAtlasi | P19096, baseline and differential |
Genevisiblei | P19096, MM |
Interactioni
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 similarityGO - Molecular functioni
- identical protein binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 199596, 23 interactors |
IntActi | P19096, 11 interactors |
MINTi | P19096 |
STRINGi | 10090.ENSMUSP00000052872 |
Chemistry databases
BindingDBi | P19096 |
Miscellaneous databases
RNActi | P19096, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P19096 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2112 – 2192 | CarrierPROSITE-ProRule annotationAdd BLAST | 81 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 414 | Beta-ketoacyl synthaseAdd BLAST | 414 | |
Regioni | 429 – 817 | Acyl and malonyl transferasesAdd BLAST | 389 | |
Regioni | 647 – 648 | Acyl-CoA bindingCombined sources1 Publication | 2 | |
Regioni | 1628 – 1856 | Enoyl reductaseAdd BLAST | 229 | |
Regioni | 1857 – 2111 | Beta-ketoacyl reductaseAdd BLAST | 255 | |
Regioni | 2201 – 2504 | ThioesteraseAdd BLAST | 304 |
Phylogenomic databases
eggNOGi | KOG1202, Eukaryota |
GeneTreei | ENSGT00940000157276 |
HOGENOMi | CLU_000022_31_7_1 |
InParanoidi | P19096 |
OMAi | CKVYYAS |
OrthoDBi | 19161at2759 |
PhylomeDBi | P19096 |
TreeFami | TF300549 |
Family and domain databases
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 |
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 |
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 |
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 |
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 |
PROSITEi | View protein in PROSITE PS00606, B_KETOACYL_SYNTHASE, 1 hit PS50075, CARRIER, 1 hit PS00012, PHOSPHOPANTETHEINE, 1 hit |
(1+)i Sequence
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
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
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A0U1RNJ1 | A0A0U1RNJ1_MOUSE | 3-hydroxyacyl-[acyl-carrier-protein... | Fasn | 2,502 | Annotation score: | ||
A0A0U1RPP5 | A0A0U1RPP5_MOUSE | Fatty acid synthase | Fasn | 24 | Annotation score: |
Sequence cautioni
The sequence CAA31525 differs from that shown. Reason: Frameshift.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 1992 | T → N in CAA31525 (PubMed:2920037).Curated | 1 | |
Sequence conflicti | 2028 | G → C in CAA31525 (PubMed:2920037).Curated | 1 | |
Sequence conflicti | 2045 | G → V in CAA31525 (PubMed:2920037).Curated | 1 | |
Sequence conflicti | 2117 | T → N in CAA31525 (PubMed:2920037).Curated | 1 | |
Sequence conflicti | 2175 | Q → R in CAA31525 (PubMed:2920037).Curated | 1 | |
Sequence conflicti | 2295 | Y → H in CAA31525 (PubMed:2920037).Curated | 1 |
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. |
CCDSi | CCDS25759.1 |
PIRi | A32262 |
RefSeqi | NP_032014.3, NM_007988.3 |
Genome annotation databases
Ensembli | ENSMUST00000055655; ENSMUSP00000052872; ENSMUSG00000025153 |
GeneIDi | 14104 |
KEGGi | mmu:14104 |
UCSCi | uc007mut.1, mouse |
Similar proteinsi
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. |
CCDSi | CCDS25759.1 |
PIRi | A32262 |
RefSeqi | NP_032014.3, NM_007988.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5MY0 | X-ray | 2.94 | A/B/C/D | 2-852 | [»] | |
5MY2 | X-ray | 2.70 | A/B/C/D | 2-852 | [»] | |
6ROP | X-ray | 2.70 | A/B/C/D | 2-852 | [»] | |
SMRi | P19096 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 199596, 23 interactors |
IntActi | P19096, 11 interactors |
MINTi | P19096 |
STRINGi | 10090.ENSMUSP00000052872 |
Chemistry databases
BindingDBi | P19096 |
ChEMBLi | CHEMBL1795189 |
Protein family/group databases
ESTHERi | mouse-FASN, Thioesterase |
PTM databases
iPTMneti | P19096 |
PhosphoSitePlusi | P19096 |
SwissPalmi | P19096 |
Proteomic databases
CPTACi | non-CPTAC-3808 |
EPDi | P19096 |
jPOSTi | P19096 |
MaxQBi | P19096 |
PaxDbi | P19096 |
PeptideAtlasi | P19096 |
PRIDEi | P19096 |
Protocols and materials databases
Antibodypediai | 1650, 720 antibodies |
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 | KOG1202, Eukaryota |
GeneTreei | ENSGT00940000157276 |
HOGENOMi | CLU_000022_31_7_1 |
InParanoidi | P19096 |
OMAi | CKVYYAS |
OrthoDBi | 19161at2759 |
PhylomeDBi | P19096 |
TreeFami | TF300549 |
Enzyme and pathway databases
UniPathwayi | UPA00094 |
Reactomei | R-MMU-163765, ChREBP activates metabolic gene expression R-MMU-199220, Vitamin B5 (pantothenate) metabolism R-MMU-75105, Fatty acyl-CoA biosynthesis |
Miscellaneous databases
BioGRID-ORCSi | 14104, 9 hits in 17 CRISPR screens |
ChiTaRSi | Fasn, mouse |
PROi | PR:P19096 |
RNActi | P19096, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000025153, Expressed in mammary gland and 350 other tissues |
ExpressionAtlasi | P19096, baseline and differential |
Genevisiblei | P19096, MM |
Family and domain databases
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 |
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 |
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 |
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 |
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 |
PROSITEi | View protein in PROSITE PS00606, B_KETOACYL_SYNTHASE, 1 hit PS50075, CARRIER, 1 hit PS00012, PHOSPHOPANTETHEINE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | FAS_MOUSE | |
Accessioni | P19096Primary (citable) accession number: P19096 Secondary accession number(s): B1ATU8 Q9EQR0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1990 |
Last sequence update: | October 11, 2004 | |
Last modified: | December 2, 2020 | |
This is version 203 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references