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P49327 (FAS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Synonyms:FAS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2511 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+. Ref.1

Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein]. Ref.1

Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein]. Ref.1

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein]. Ref.1

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH. Ref.1

A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O. Ref.1

An acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH. Ref.1

Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate. Ref.1

Subunit structure

Homodimer which is arranged in a head to tail fashion.

Subcellular location

Cytoplasm. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.10

Tissue specificity

Ubiquitous. Prominent expression in brain, lung, and liver. Ref.1 Ref.9

Miscellaneous

The relatively low beta-ketoacyl synthase activity may be attributable to the low 4'-phosphopantetheine content of the protein.

Sequence similarities

Contains 1 acyl carrier domain.

Sequence caution

The sequence AAB35516.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAC50259.1 differs from that shown. Reason: Several sequencing errors.

The sequence BAE06070.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandNAD
NADP
Pyridoxal phosphate
   Molecular functionHydrolase
Lyase
Oxidoreductase
Transferase
   PTMAcetylation
Phosphopantetheine
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processacetyl-CoA metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cellular response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

energy reserve metabolic process

Traceable author statement. Source: Reactome

fatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

fatty acid metabolic process

Traceable author statement PubMed 7835891. Source: ProtInc

long-chain fatty-acyl-CoA biosynthetic process

Traceable author statement. Source: Reactome

pantothenate metabolic process

Traceable author statement. Source: Reactome

positive regulation of cellular metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride biosynthetic process

Traceable author statement. Source: Reactome

vitamin metabolic process

Traceable author statement. Source: Reactome

water-soluble vitamin metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

glycogen granule

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay. Source: HPA

   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

fatty acid synthase activity

Traceable author statement. Source: Reactome

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

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q99IB86EBI-356658,EBI-6927928From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25112511Fatty acid synthase
PRO_0000180276

Regions

Domain2123 – 217957Acyl carrier
Nucleotide binding1671 – 168818NADP (ER) By similarity
Nucleotide binding1886 – 190116NADP (KR) By similarity
Region1 – 414414Beta-ketoacyl synthase By similarity
Region429 – 817389Acyl and malonyl transferases By similarity
Region1635 – 1863229Enoyl reductase By similarity
Region1864 – 2118255Beta-ketoacyl reductase By similarity
Region2207 – 2511305Thioesterase By similarity

Sites

Active site1611For beta-ketoacyl synthase activity By similarity
Active site5811For malonyltransferase activity By similarity
Active site8781For beta-hydroxyacyl dehydratase activity By similarity
Active site23081For thioesterase activity Ref.22
Active site24811For thioesterase activity By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.13 Ref.18
Modified residue701N6-acetyllysine Ref.15
Modified residue2071Phosphoserine Ref.12
Modified residue2981N6-acetyllysine Ref.15
Modified residue4361N6-acetyllysine Ref.15
Modified residue5281N6-acetyllysine Ref.15
Modified residue6731N6-acetyllysine Ref.15
Modified residue9921N6-acetyllysine By similarity
Modified residue17041N6-(pyridoxal phosphate)lysine; alternate By similarity
Modified residue17041N6-acetyllysine; alternate Ref.15
Modified residue17711N6-acetyllysine Ref.15
Modified residue18471N6-acetyllysine Ref.15
Modified residue19951N6-acetyllysine Ref.15
Modified residue21561O-(pantetheine 4'-phosphoryl)serine
Modified residue21981Phosphoserine Ref.11 Ref.12
Modified residue22041Phosphothreonine Ref.11 Ref.12 Ref.14
Modified residue22361Phosphoserine Ref.12
Modified residue23911N6-acetyllysine By similarity

Natural variations

Natural variant14831V → I.
Corresponds to variant rs2228305 [ dbSNP | Ensembl ].
VAR_055479
Natural variant16941R → H.
Corresponds to variant rs2229424 [ dbSNP | Ensembl ].
VAR_055480
Natural variant18881I → V.
Corresponds to variant rs2228307 [ dbSNP | Ensembl ].
VAR_055481

Experimental info

Sequence conflict459 – 4624AVPA → LSPT in AAA73576. Ref.2
Sequence conflict528 – 5292KP → NR in AAA73576. Ref.2
Sequence conflict6371G → A in AAA73576. Ref.2
Sequence conflict8011G → R in AAA73576. Ref.2
Sequence conflict9021A → P in AAA73576. Ref.2
Sequence conflict9581V → M in AAS09886. Ref.3
Sequence conflict11211P → S in AAA73576. Ref.2
Sequence conflict11211P → S in AAS09886. Ref.3
Sequence conflict11511K → T in AAH63242. Ref.6
Sequence conflict1353 – 13564LGDI → SGH in AAA73576. Ref.2
Sequence conflict13861L → V in AAA73576. Ref.2
Sequence conflict1467 – 14682NR → T in AAA73576. Ref.2
Sequence conflict18271K → E in AAS09886. Ref.3
Sequence conflict19341R → A in AAA73576. Ref.2
Sequence conflict20651D → H in AAB35516. Ref.9
Sequence conflict20871R → A in AAA73576. Ref.2
Sequence conflict23631A → P in AAB35516. Ref.9
Sequence conflict24281R → G in AAA73576. Ref.2
Sequence conflict24531A → T in AAB35516. Ref.9
Sequence conflict24561E → Q in AAB35516. Ref.9

Secondary structure

................................................................................................................................................................................................. 2511
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49327 [UniParc].

Last modified November 24, 2009. Version 3.
Checksum: 7A07171FEFA3287B

FASTA2,511273,427
        10         20         30         40         50         60 
MEEVVIAGMS GKLPESENLQ EFWDNLIGGV DMVTDDDRRW KAGLYGLPRR SGKLKDLSRF 

        70         80         90        100        110        120 
DASFFGVHPK QAHTMDPQLR LLLEVTYEAI VDGGINPDSL RGTHTGVWVG VSGSETSEAL 

       130        140        150        160        170        180 
SRDPETLVGY SMVGCQRAMM ANRLSFFFDF RGPSIALDTA CSSSLMALQN AYQAIHSGQC 

       190        200        210        220        230        240 
PAAIVGGINV LLKPNTSVQF LRLGMLSPEG TCKAFDTAGN GYCRSEGVVA VLLTKKSLAR 

       250        260        270        280        290        300 
RVYATILNAG TNTDGFKEQG VTFPSGDIQE QLIRSLYQSA GVAPESFEYI EAHGTGTKVG 

       310        320        330        340        350        360 
DPQELNGITR ALCATRQEPL LIGSTKSNMG HPEPASGLAA LAKVLLSLEH GLWAPNLHFH 

       370        380        390        400        410        420 
SPNPEIPALL DGRLQVVDQP LPVRGGNVGI NSFGFGGSNV HIILRPNTQP PPAPAPHATL 

       430        440        450        460        470        480 
PRLLRASGRT PEAVQKLLEQ GLRHSQDLAF LSMLNDIAAV PATAMPFRGY AVLGGERGGP 

       490        500        510        520        530        540 
EVQQVPAGER PLWFICSGMG TQWRGMGLSL MRLDRFRDSI LRSDEAVKPF GLKVSQLLLS 

       550        560        570        580        590        600 
TDESTFDDIV HSFVSLTAIQ IGLIDLLSCM GLRPDGIVGH SLGEVACGYA DGCLSQEEAV 

       610        620        630        640        650        660 
LAAYWRGQCI KEAHLPPGAM AAVGLSWEEC KQRCPPGVVP ACHNSKDTVT ISGPQAPVFE 

       670        680        690        700        710        720 
FVEQLRKEGV FAKEVRTGGM AFHSYFMEAI APPLLQELKK VIREPKPRSA RWLSTSIPEA 

       730        740        750        760        770        780 
QWHSSLARTS SAEYNVNNLV SPVLFQEALW HVPEHAVVLE IAPHALLQAV LKRGLKPSCT 

       790        800        810        820        830        840 
IIPLMKKDHR DNLEFFLAGI GRLHLSGIDA NPNALFPPVE FPAPRGTPLI SPLIKWDHSL 

       850        860        870        880        890        900 
AWDVPAAEDF PNGSGSPSAA IYNIDTSSES PDHYLVDHTL DGRVLFPATG YLSIVWKTLA 

       910        920        930        940        950        960 
RALGLGVEQL PVVFEDVVLH QATILPKTGT VSLEVRLLEA SRAFEVSENG NLVVSGKVYQ 

       970        980        990       1000       1010       1020 
WDDPDPRLFD HPESPTPNPT EPLFLAQAEV YKELRLRGYD YGPHFQGILE ASLEGDSGRL 

      1030       1040       1050       1060       1070       1080 
LWKDNWVSFM DTMLQMSILG SAKHGLYLPT RVTAIHIDPA THRQKLYTLQ DKAQVADVVV 

      1090       1100       1110       1120       1130       1140 
SRWLRVTVAG GVHISGLHTE SAPRRQQEQQ VPILEKFCFT PHTEEGCLSE RAALQEELQL 

      1150       1160       1170       1180       1190       1200 
CKGLVQALQT KVTQQGLKMV VPGLDGAQIP RDPSQQELPR LLSAACRLQL NGNLQLELAQ 

      1210       1220       1230       1240       1250       1260 
VLAQERPKLP EDPLLSGLLD SPALKACLDT AVENMPSLKM KVVEVLAGHG HLYSRIPGLL 

      1270       1280       1290       1300       1310       1320 
SPHPLLQLSY TATDRHPQAL EAAQAELQQH DVAQGQWDPA DPAPSALGSA DLLVCNCAVA 

      1330       1340       1350       1360       1370       1380 
ALGDPASALS NMVAALREGG FLLLHTLLRG HPLGDIVAFL TSTEPQYGQG ILSQDAWESL 

      1390       1400       1410       1420       1430       1440 
FSRVSLRLVG LKKSFYGSTL FLCRRPTPQD SPIFLPVDDT SFRWVESLKG ILADEDSSRP 

      1450       1460       1470       1480       1490       1500 
VWLKAINCAT SGVVGLVNCL RREPGGNRLR CVLLSNLSST SHVPEVDPGS AELQKVLQGD 

      1510       1520       1530       1540       1550       1560 
LVMNVYRDGA WGAFRHFLLE EDKPEEPTAH AFVSTLTRGD LSSIRWVCSS LRHAQPTCPG 

      1570       1580       1590       1600       1610       1620 
AQLCTVYYAS LNFRDIMLAT GKLSPDAIPG KWTSQDSLLG MEFSGRDASG KRVMGLVPAK 

      1630       1640       1650       1660       1670       1680 
GLATSVLLSP DFLWDVPSNW TLEEAASVPV VYSTAYYALV VRGRVRPGET LLIHSGSGGV 

      1690       1700       1710       1720       1730       1740 
GQAAIAIALS LGCRVFTTVG SAEKRAYLQA RFPQLDSTSF ANSRDTSFEQ HVLWHTGGKG 

      1750       1760       1770       1780       1790       1800 
VDLVLNSLAE EKLQASVRCL ATHGRFLEIG KFDLSQNHPL GMAIFLKNVT FHGVLLDAFF 

      1810       1820       1830       1840       1850       1860 
NESSADWREV WALVQAGIRD GVVRPLKCTV FHGAQVEDAF RYMAQGKHIG KVVVQVLAEE 

      1870       1880       1890       1900       1910       1920 
PEAVLKGAKP KLMSAISKTF CPAHKSYIIA GGLGGFGLEL AQWLIQRGVQ KLVLTSRSGI 

      1930       1940       1950       1960       1970       1980 
RTGYQAKQVR RWRRQGVQVQ VSTSNISSLE GARGLIAEAA QLGPVGGVFN LAVVLRDGLL 

      1990       2000       2010       2020       2030       2040 
ENQTPEFFQD VCKPKYSGTL NLDRVTREAC PELDYFVVFS SVSCGRGNAG QSNYGFANSA 

      2050       2060       2070       2080       2090       2100 
MERICEKRRH EGLPGLAVQW GAIGDVGILV ETMSTNDTIV SGTLPQRMAS CLEVLDLFLN 

      2110       2120       2130       2140       2150       2160 
QPHMVLSSFV LAEKAAAYRD RDSQRDLVEA VAHILGIRDL AAVNLDSSLA DLGLDSLMSV 

      2170       2180       2190       2200       2210       2220 
EVRQTLEREL NLVLSVREVR QLTLRKLQEL SSKADEASEL ACPTPKEDGL AQQQTQLNLR 

      2230       2240       2250       2260       2270       2280 
SLLVNPEGPT LMRLNSVQSS ERPLFLVHPI EGSTTVFHSL ASRLSIPTYG LQCTRAAPLD 

      2290       2300       2310       2320       2330       2340 
SIHSLAAYYI DCIRQVQPEG PYRVAGYSYG ACVAFEMCSQ LQAQQSPAPT HNSLFLFDGS 

      2350       2360       2370       2380       2390       2400 
PTYVLAYTQS YRAKLTPGCE AEAETEAICF FVQQFTDMEH NRVLEALLPL KGLEERVAAA 

      2410       2420       2430       2440       2450       2460 
VDLIIKSHQG LDRQELSFAA RSFYYKLRAA EQYTPKAKYH GNVMLLRAKT GGAYGEDLGA 

      2470       2480       2490       2500       2510 
DYNLSQVCDG KVSVHVIEGD HRTLLEGSGL ESIISIIHSS LAEPRVSVRE G 

« Hide

References

« Hide 'large scale' references
[1]"Human fatty acid synthase: properties and molecular cloning."
Jayakumar A., Tai M.-H., Huang W.-Y., Al-Feel W., Hsu M., Abu-Elheiga L., Chirala S.S., Wakil S.J.
Proc. Natl. Acad. Sci. U.S.A. 92:8695-8699(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, PHOSPHOPANTETHEINYLATION AT SER-2156, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"Molecular cloning of tumor-associated human fatty acid synthase."
Hennigar R.A., Jenner K.H., Heine H.S., Kayler A.E., Wood F.D., Kuhajda F.P., Pasternack G.R.
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Recharacterization of the human fatty acid synthase (FAS) gene."
Mao J., Wakil S.J.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Eye.
[7]Bienvenut W.V.
Submitted (JUL-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-12; 647-666; 791-802; 1242-1255; 1338-1349 AND 2126-2138, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[8]"Fatty acid synthesis: a potential selective target for antineoplastic therapy."
Kuhajda F.P., Jenner K., Wood F.D., Hennigar R.A., Jacobs L.B., Dick J.D., Pasternack G.R.
Proc. Natl. Acad. Sci. U.S.A. 91:6379-6383(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 753-758 AND 1285-1297.
[9]"Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation."
Semenkovich C.F., Coleman T., Fiedorek F.T. Jr.
J. Lipid Res. 36:1507-1521(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2047-2511, TISSUE SPECIFICITY.
[10]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[11]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2198 AND THR-2204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-2198; THR-2204 AND SER-2236, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-298; LYS-436; LYS-528; LYS-673; LYS-1704; LYS-1771; LYS-1847 AND LYS-1995, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Quaternary structure of human fatty acid synthase by electron cryomicroscopy."
Brink J., Ludtke S.J., Yang C.Y., Gu Z.-W., Wakil S.J., Chiu W.
Proc. Natl. Acad. Sci. U.S.A. 99:138-143(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING, STRUCTURE BY ELECTRON CRYOMICROSCOPY.
[20]"Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain."
Chakravarty B., Gu Z., Chirala S.S., Wakil S.J., Quiocho F.A.
Proc. Natl. Acad. Sci. U.S.A. 101:15567-15572(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 2218-2502.
[21]"Mechanism and substrate recognition of human holo ACP synthase."
Bunkoczi G., Pasta S., Joshi A., Wu X., Kavanagh K.L., Smith S., Oppermann U.
Chem. Biol. 14:1243-1253(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2119-2207 IN COMPLEX WITH AASDHPPT AND COENZYME A.
[22]"Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat."
Pemble C.W. IV, Johnson L.C., Kridel S.J., Lowther W.T.
Nat. Struct. Mol. Biol. 14:704-709(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2200-2511 IN COMPLEX WITH ORLISTAT, ACTIVE SITE FOR THIOESTERASE ACTIVITY.
[23]"Structure of the MAT domain of human FAS with malonyl-CoA."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 422-831 IN COMPLEX WITH MALONYL-COENZYME A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U26644 mRNA. Translation: AAC50259.1. Sequence problems.
U29344 mRNA. Translation: AAA73576.1.
AY451392 mRNA. Translation: AAS09886.1.
AB209988 mRNA. Translation: BAE06070.1. Different initiation.
AC135056 Genomic DNA. No translation available.
BC007267 mRNA. Translation: AAH07267.1.
BC007909 mRNA. Translation: AAH07909.1.
BC014634 mRNA. Translation: AAH14634.2.
BC063242 mRNA. Translation: AAH63242.1.
S80437 mRNA. Translation: AAB35516.1. Different initiation.
PIRA57788.
G01880.
RefSeqNP_004095.4. NM_004104.4.
UniGeneHs.83190.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XKTX-ray2.60A/B2218-2502[»]
2CG5X-ray2.70B2119-2207[»]
2JFDX-ray2.81A/B/C/D422-823[»]
2JFKX-ray2.40A/B/C/D422-831[»]
2PX6X-ray2.30A/B2200-2511[»]
3HHDX-ray2.15A/B/C/D2-963[»]
3TJMX-ray1.48A2218-2500[»]
ProteinModelPortalP49327.
SMRP49327. Positions 2-853, 1220-2114, 2124-2194, 2218-2491.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108488. 53 interactions.
DIPDIP-33681N.
IntActP49327. 27 interactions.
MINTMINT-1146154.

Chemistry

ChEMBLCHEMBL4158.
DrugBankDB01034. Cerulenin.
DB01083. Orlistat.
DB00339. Pyrazinamide.

PTM databases

PhosphoSiteP49327.

Polymorphism databases

DMDM269849686.

Proteomic databases

PaxDbP49327.
PRIDEP49327.

Protocols and materials databases

DNASU2194.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306749; ENSP00000304592; ENSG00000169710.
GeneID2194.
KEGGhsa:2194.
UCSCuc002kdu.3. human.

Organism-specific databases

CTD2194.
GeneCardsGC17M080037.
H-InvDBHIX0014269.
HGNCHGNC:3594. FASN.
HPACAB005192.
CAB015417.
HPA006461.
MIM600212. gene.
neXtProtNX_P49327.
PharmGKBPA28006.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3319.
HOVERGENHBG005640.
InParanoidP49327.
KOK00665.
OMAGLRTAQW.
OrthoDBEOG71K623.
PhylomeDBP49327.
TreeFamTF300549.

Enzyme and pathway databases

BioCycMetaCyc:HS09992-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP49327.

Gene expression databases

BgeeP49327.
CleanExHS_FAS.
HS_FASN.
GenevestigatorP49327.

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.
3.40.50.720. 2 hits.
InterProIPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR002198. DH_sc/Rdtase_SDR.
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.
IPR006162. PPantetheine_attach_site.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF00698. Acyl_transf_1. 1 hit.
PF00106. adh_short. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 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.
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

ChiTaRSFASN. human.
EvolutionaryTraceP49327.
GeneWikiFatty_acid_synthase.
GenomeRNAi2194.
NextBio8869.
PROP49327.
SOURCESearch...

Entry information

Entry nameFAS_HUMAN
AccessionPrimary (citable) accession number: P49327
Secondary accession number(s): Q13479 expand/collapse secondary AC list , Q16702, Q4LE83, Q6P4U5, Q6SS02, Q969R1, Q96C68, Q96IT0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 24, 2009
Last modified: April 16, 2014
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM