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P19096 (FAS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid synthase

EC=2.3.1.85

Including the following 7 domains:

  1. [Acyl-carrier-protein] S-acetyltransferase
    EC=2.3.1.38
  2. [Acyl-carrier-protein] S-malonyltransferase
    EC=2.3.1.39
  3. 3-oxoacyl-[acyl-carrier-protein] synthase
    EC=2.3.1.41
  4. 3-oxoacyl-[acyl-carrier-protein] reductase
    EC=1.1.1.100
  5. 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
    EC=4.2.1.59
  6. Enoyl-[acyl-carrier-protein] reductase
    EC=1.3.1.39
  7. Oleoyl-[acyl-carrier-protein] hydrolase
    EC=3.1.2.14
Gene names
Name:Fasn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2504 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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 + [acyl-carrier-protein] = CoA + 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.

Subunit structure

Homodimer which is arranged in a head to tail fashion.

Subcellular location

Cytoplasm By similarity. Melanosome By similarity.

Sequence similarities

Contains 1 acyl carrier domain.

Sequence caution

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

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   LigandNAD
NADP
Pyridoxal phosphate
   Molecular functionHydrolase
Lyase
Oxidoreductase
Transferase
   PTMAcetylation
Phosphopantetheine
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processacetyl-CoA metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-4

Inferred from direct assay PubMed 9798653. Source: MGI

fatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

glycogen granule

Inferred from direct assay PubMed 15169678. Source: MGI

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_function3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity

Inferred from electronic annotation. Source: InterPro

3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity

Inferred from electronic annotation. Source: UniProtKB-EC

3-oxoacyl-[acyl-carrier-protein] synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

NADPH binding

Inferred from electronic annotation. Source: Ensembl

[acyl-carrier-protein] S-acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

[acyl-carrier-protein] S-malonyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

drug binding

Inferred from electronic annotation. Source: Ensembl

enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity

Inferred from electronic annotation. Source: UniProtKB-EC

enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity

Inferred from electronic annotation. Source: InterPro

myristoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

oleoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

palmitoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25042504Fatty acid synthase
PRO_0000180277

Regions

Domain2117 – 217357Acyl carrier
Nucleotide binding1664 – 168118NADP (ER) By similarity
Nucleotide binding1879 – 189416NADP (KR) By similarity
Region1 – 414414Beta-ketoacyl synthase
Region429 – 817389Acyl and malonyl transferases
Region1628 – 1856229Enoyl reductase
Region1857 – 2111255Beta-ketoacyl reductase
Region2201 – 2504304Thioesterase

Sites

Active site1611For beta-ketoacyl synthase activity By similarity
Active site5811For malonyltransferase activity By similarity
Active site8781For beta-hydroxyacyl dehydratase activity By similarity
Active site23011For thioesterase activity By similarity
Active site24741For thioesterase activity By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.4
Modified residue591N6-acetyllysine Ref.7
Modified residue701N6-acetyllysine By similarity
Modified residue2071Phosphoserine By similarity
Modified residue2981N6-acetyllysine By similarity
Modified residue5281N6-acetyllysine By similarity
Modified residue6731N6-acetyllysine By similarity
Modified residue7901N6-acetyllysine Ref.7
Modified residue9931N6-acetyllysine Ref.7
Modified residue10711N6-acetyllysine Ref.7
Modified residue12761N6-acetyllysine Ref.7
Modified residue16971N6-(pyridoxal phosphate)lysine; alternate By similarity
Modified residue16971N6-acetyllysine; alternate By similarity
Modified residue17641N6-acetyllysine By similarity
Modified residue18401N6-acetyllysine Ref.7
Modified residue19881N6-acetyllysine By similarity
Modified residue21501O-(pantetheine 4'-phosphoryl)serine By similarity
Modified residue22291Phosphoserine By similarity
Modified residue23841N6-acetyllysine Ref.7

Experimental info

Sequence conflict19921T → N in CAA31525. Ref.6
Sequence conflict20281G → C in CAA31525. Ref.6
Sequence conflict20451G → V in CAA31525. Ref.6
Sequence conflict21171T → N in CAA31525. Ref.6
Sequence conflict21751Q → R in CAA31525. Ref.6
Sequence conflict22951Y → H in CAA31525. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P19096 [UniParc].

Last modified October 11, 2004. Version 2.
Checksum: 2B48068B9D370C6F

FASTA2,504272,428
        10         20         30         40         50         60 
MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR SGKLKDLSKF 

        70         80         90        100        110        120 
DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL RGTNTGVWVG VSGSEASEAL 

       130        140        150        160        170        180 
SRDPETLLGY SMVGCQRAMM ANRLSFFFDF KGPSIALDTA CSSSLLALQN AYQAIRSGEC 

       190        200        210        220        230        240 
PAALVGGINL LLKPNTSVQF MKLGMLSPDG TCRSFDDSGS GYCRSEAVVA VLLTKKSLAR 

       250        260        270        280        290        300 
RVYATILNAG TNTDGSKEQG VTFPSGEVQE QLICSLYQPA GLAPESLEYI EAHGTGTKVG 

       310        320        330        340        350        360 
DPQELNGITR SLCAFRQAPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEH GVWAPNLHFH 

       370        380        390        400        410        420 
NPNPEIPALL DGRLQVVDRP LPVRGGNVGI NSFGFGGSNV HVILQPNTRQ APAPTAHAAL 

       430        440        450        460        470        480 
PHLLHASGRT LEAVQDLLEQ GRQHSQDLAF VSMLNDIAAT PTAAMPFRGY TVLGVEGRVQ 

       490        500        510        520        530        540 
EVQQVSTNKR PLWFICSGMG TQWRGMGLSL MRLDSFRESI LRSDEAVKPL GVKVSDLLLS 

       550        560        570        580        590        600 
TDERTFDDIV HAFVSLTAIQ IALIDLLTSV GLKPDGIIGH SLGEVACGYA DGCLSQREAV 

       610        620        630        640        650        660 
LAAYWRGQCI KDAHLPPGSM AAVGLSWEEC KQRCPAGVVP ACHNSEDTVT ISGPQAAVNE 

       670        680        690        700        710        720 
FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK VIREPRPRSA RWLSTSIPEA 

       730        740        750        760        770        780 
QWQSSLARTS SAEYNVNNLV SPVLFQEALW HIPEHAVVLE IAPHALLQAV LKRGVKSSCT 

       790        800        810        820        830        840 
IIPLMKRDHK DNLEFFLTNL GKVHLTGINV NPNALFPPVE FPAPRGTPLI SPHIKWDHSQ 

       850        860        870        880        890        900 
TWDVPVAEDF PNGSSSSSAT VYSIDASPES PDHYLVDHCI DGRVIFPGTG YLCLVWKTLA 

       910        920        930        940        950        960 
RSLGLSLEET PVVFENVSFH QATILPKTGT VALEVRLLEA SHAFEVSDTG NLIVSGKVYL 

       970        980        990       1000       1010       1020 
WEDPNSKLFD HPEVPTPPES ASVSRLTQGE VYKELRLRGY DYGPQFQGIC EATLEGEQGK 

      1030       1040       1050       1060       1070       1080 
LLWKDNWVTF MDTMLQVSIL GSSQQSLQLP TRVTAIYIDP ATHRQKVYRL KEDTQVADVT 

      1090       1100       1110       1120       1130       1140 
TSRCLGITVS GGIHISRLQT TATSRRQQEQ LVPTLEKFVF TPHMEAECLS ESTALQKELQ 

      1150       1160       1170       1180       1190       1200 
LCKGLARALQ TKATQQGLKA AMLGQEDPPQ HGLPRLLAAA CQLQLNGNLQ LELGEALAQE 

      1210       1220       1230       1240       1250       1260 
RLLLPEDPLI SGLLNSQALK ACVDTALENL STLKMKVAEV LAGEGHLYSR IPALLNTQPM 

      1270       1280       1290       1300       1310       1320 
LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWNPSDPAPS SLGALDLLVC NCALATLGDP 

      1330       1340       1350       1360       1370       1380 
ALALDNMVAA LKEGGFLLVH TVLKGHALGE TLACLPSEVQ PAPSLLSQEE WESLFSRKAL 

      1390       1400       1410       1420       1430       1440 
HLVGLKRSFY GTALFLCRRA IPQEKPIFLS VEDTSFQWVD SLKSTLATSS SQPVWLTAMD 

      1450       1460       1470       1480       1490       1500 
CPTSGVVGLV NCLRKEPGGH RIRCILLSNL SNTSHAPKLD PGSPELQQVL KHDLVMNVYR 

      1510       1520       1530       1540       1550       1560 
DGAWGAFRHF QLEQDKPKEQ TAHAFVNVLT RGDLASIRWV SSPLKHTQPS SSGAQLCTVY 

      1570       1580       1590       1600       1610       1620 
YASLNFRDIM LATGKLSPDA IPGKWASRDC MLGMEFSGRD RCGRRVMGLV PAEGLATSVL 

      1630       1640       1650       1660       1670       1680 
LSSDFLWDVP SSWTLEEAAS VPVVYTTAYY SLVVRGRIQR GETVLIHSGS GGVGQAAISI 

      1690       1700       1710       1720       1730       1740 
ALSLGCRVFT TVGSAEKRAY LQARFPQLDD TSFANSRDTS FEQHVLLHTG GKGVDLVLNS 

      1750       1760       1770       1780       1790       1800 
LAEEKLQASV RCLAQHGRFL EIGKFDLSNN HPLGMAIFLK NVTFHGILLD ALFEEANDSW 

      1810       1820       1830       1840       1850       1860 
REVAALLKAG IRDGVVKPLK CTVFPKAQVE DAFRYMAQGK HIGKVLVQVR EEEPEAVLPG 

      1870       1880       1890       1900       1910       1920 
AQPTLISAIS KTFCPAHKSY IITGGLGGFG LELARWLVLR GAQRLVLTSR SGIRTGYQAK 

      1930       1940       1950       1960       1970       1980 
HIREWRRQGI QVLVSTSNVS SLEGARALIA EATKLGPVGG VFNLAMVLRD AMLENQTPEL 

      1990       2000       2010       2020       2030       2040 
FQDVNKPKYN GTLNLDRATR EACPELDYFV AFSSVSCGRG NAGQTNYGFA NSTMERICEQ 

      2050       2060       2070       2080       2090       2100 
RRHDGLPGLA VQWGAIGDVG IVLEAMGTND TVIGGTLPQR ISSCMEVLDL FLNQPHAVLS 

      2110       2120       2130       2140       2150       2160 
SFVLAEKKAV AHGDGDTQRD LVKAVAHILG IRDLAGINLD STLADLGLDS LMGVEVRQIL 

      2170       2180       2190       2200       2210       2220 
EREHDLVLPM REVRQLTLRK LQEMSSKTDS ATDTTAPKSR SDTSLKQNQL NLSTLLVNPE 

      2230       2240       2250       2260       2270       2280 
GPTLTQLNSV QSSERPLFLV HPIEGSTTVF HSLAAKLSVP TYGLQCTQAA PLDSIPNLAA 

      2290       2300       2310       2320       2330       2340 
YYIDCIKQVQ PEGPYRIAGY SFGACVAFEM CSQLQAQQGP APTHNNLFLF DGSHTYVLAY 

      2350       2360       2370       2380       2390       2400 
TQSYRAKMTP GCEAEAEAEA LCFFIKQFLD VEHSKVLEAL LPLKSLEDRV AASVDLITKS 

      2410       2420       2430       2440       2450       2460 
HHSLDRRELS FAAVSFYHKL RAADQYKPKA KYHGNVTLLR AKTGGTYGED LGADYNLSQV 

      2470       2480       2490       2500 
CDGKVSVHII EGDHRTLLEG SGLESIINII HSSLAEPRVS VREG 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS25759.1.
PIRA32262.
RefSeqNP_032014.3. NM_007988.3.
UniGeneMm.236443.

3D structure databases

ProteinModelPortalP19096.
SMRP19096. Positions 2-853, 1215-2107, 2113-2201, 2211-2484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199596. 4 interactions.
IntActP19096. 8 interactions.
MINTMINT-2514287.

Chemistry

BindingDBP19096.
ChEMBLCHEMBL1795189.

PTM databases

PhosphoSiteP19096.

Proteomic databases

MaxQBP19096.
PaxDbP19096.
PRIDEP19096.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000055655; ENSMUSP00000052872; ENSMUSG00000025153.
GeneID14104.
KEGGmmu:14104.
UCSCuc007mut.1. mouse.

Organism-specific databases

CTD2194.
MGIMGI:95485. Fasn.

Phylogenomic databases

eggNOGCOG3319.
GeneTreeENSGT00530000063309.
HOGENOMHOG000019642.
HOVERGENHBG005640.
InParanoidB1ATU8.
KOK00665.
OMARRCNERS.
OrthoDBEOG71K623.
PhylomeDBP19096.
TreeFamTF300549.

Gene expression databases

BgeeP19096.
CleanExMM_FASN.
GenevestigatorP19096.

Family and domain databases

Gene3D1.10.1200.10. 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.
InterProIPR029058. 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]
PfamPF00698. 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]
SMARTSM00829. PKS_ER. 1 hit.
SM00822. PKS_KR. 1 hit.
[Graphical view]
SUPFAMSSF47336. 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.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285138.
PROP19096.
SOURCESearch...

Entry information

Entry nameFAS_MOUSE
AccessionPrimary (citable) accession number: P19096
Secondary accession number(s): B1ATU8 expand/collapse secondary AC list , Q6PB72, Q8C4Z0, Q9EQR0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot