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P19096

- FAS_MOUSE

UniProt

P19096 - FAS_MOUSE

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Protein
Fatty acid synthase
Gene
Fasn
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei161 – 1611For beta-ketoacyl synthase activity By similarity
Active sitei581 – 5811For malonyltransferase activity By similarity
Active sitei878 – 8781For beta-hydroxyacyl dehydratase activity By similarity
Active sitei2301 – 23011For thioesterase activity By similarity
Active sitei2474 – 24741For thioesterase activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1664 – 168118NADP (ER) By similarity
Add
BLAST
Nucleotide bindingi1879 – 189416NADP (KR) By similarity
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Lyase, Oxidoreductase, Transferase

Keywords - Biological processi

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

Keywords - Ligandi

NAD, NADP, Pyridoxal phosphate

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid synthase (EC:2.3.1.85)
Including the following 7 domains:
[Acyl-carrier-protein] S-acetyltransferase (EC:2.3.1.38)
[Acyl-carrier-protein] S-malonyltransferase (EC:2.3.1.39)
3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.41)
3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.100)
3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.59)
Enoyl-[acyl-carrier-protein] reductase (EC:1.3.1.39)
Oleoyl-[acyl-carrier-protein] hydrolase (EC:3.1.2.14)
Gene namesi
Name:Fasn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:95485. Fasn.

Subcellular locationi

Cytoplasm By similarity. Melanosome By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25042504Fatty acid synthase
PRO_0000180277Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation, Phosphopantetheine, Phosphoprotein

Proteomic databases

MaxQBiP19096.
PaxDbiP19096.
PRIDEiP19096.

PTM databases

PhosphoSiteiP19096.

Expressioni

Gene expression databases

BgeeiP19096.
CleanExiMM_FASN.
GenevestigatoriP19096.

Interactioni

Subunit structurei

Homodimer which is arranged in a head to tail fashion.

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2117 – 217357Acyl carrier
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 414414Beta-ketoacyl synthase
Add
BLAST
Regioni429 – 817389Acyl and malonyl transferases
Add
BLAST
Regioni1628 – 1856229Enoyl reductase
Add
BLAST
Regioni1857 – 2111255Beta-ketoacyl reductase
Add
BLAST
Regioni2201 – 2504304Thioesterase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3319.
GeneTreeiENSGT00530000063309.
HOGENOMiHOG000019642.
HOVERGENiHBG005640.
InParanoidiB1ATU8.
KOiK00665.
OMAiRRCNERS.
OrthoDBiEOG71K623.
PhylomeDBiP19096.
TreeFamiTF300549.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
1.10.1470.20. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.150. 1 hit.
3.40.50.1820. 2 hits.
3.40.50.720. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR023102. Fatty_acid_synthase_dom_2.
IPR011032. GroES-like.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR013217. Methyltransf_12.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR006162. PPantetheine_attach_site.
IPR029063. SAM-dependent_MTases-like.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF08242. Methyltransf_12. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
SM00822. PKS_KR. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF53474. SSF53474. 1 hit.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19096-1 [UniParc]FASTAAdd to Basket

« Hide

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

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1992 – 19921T → N in CAA31525. 1 Publication
Sequence conflicti2028 – 20281G → C in CAA31525. 1 Publication
Sequence conflicti2045 – 20451G → V in CAA31525. 1 Publication
Sequence conflicti2117 – 21171T → N in CAA31525. 1 Publication
Sequence conflicti2175 – 21751Q → R in CAA31525. 1 Publication
Sequence conflicti2295 – 22951Y → H in CAA31525. 1 Publication

Sequence databases

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

Genome annotation databases

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

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBi P19096.
ChEMBLi CHEMBL1795189.

PTM databases

PhosphoSitei P19096.

Proteomic databases

MaxQBi P19096.
PaxDbi P19096.
PRIDEi P19096.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

CTDi 2194.
MGIi MGI:95485. Fasn.

Phylogenomic databases

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

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi 285138.
PROi P19096.
SOURCEi Search...

Gene expression databases

Bgeei P19096.
CleanExi MM_FASN.
Genevestigatori P19096.

Family and domain databases

Gene3Di 1.10.1200.10. 1 hit.
1.10.1470.20. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.150. 1 hit.
3.40.50.1820. 2 hits.
3.40.50.720. 2 hits.
InterProi IPR029058. AB_hydrolase.
IPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR023102. Fatty_acid_synthase_dom_2.
IPR011032. GroES-like.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR013217. Methyltransf_12.
IPR016040. NAD(P)-bd_dom.
IPR020842. PKS/FAS_KR.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR006162. PPantetheine_attach_site.
IPR029063. SAM-dependent_MTases-like.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF00698. Acyl_transf_1. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF08242. Methyltransf_12. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view ]
SMARTi SM00829. PKS_ER. 1 hit.
SM00822. PKS_KR. 1 hit.
[Graphical view ]
SUPFAMi SSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF53474. SSF53474. 1 hit.
SSF53901. SSF53901. 2 hits.
SSF55048. SSF55048. 1 hit.
PROSITEi PS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Involvement of fatty acid synthase in axonal development in mouse embryos."
    Ueno K.
    Genes Cells 5:859-869(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Brain and Liver.
  4. Bienvenut W.V.
    Submitted (JUL-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-12; 225-235; 299-310; 385-409; 469-478; 1252-1270; 1333-1344; 1388-1398; 1501-1508; 1705-1717; 1733-1745; 2124-2132; 2376-2384 AND 2476-2498, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Liver.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1527-2504.
    Strain: C57BL/6J.
    Tissue: Thymus.
  6. "Structure of mouse fatty acid synthase mRNA. Identification of the two NADPH binding sites."
    Paulauskis J.D., Sul H.S.
    Biochem. Biophys. Res. Commun. 158:690-695(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1666-2504.
    Strain: CD-1.
    Tissue: Liver.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59; LYS-790; LYS-993; LYS-1071; LYS-1276; LYS-1840 AND LYS-2384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiFAS_MOUSE
AccessioniPrimary (citable) accession number: P19096
Secondary accession number(s): B1ATU8
, Q6PB72, Q8C4Z0, Q9EQR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 11, 2004
Last modified: September 3, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3

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