Fatty acid synthase - Homo sapiens (Human)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P49327 (FAS_HUMAN)

Last modified February 9, 2010. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Fatty acid synthase
    EC=2.3.1.85
Including the following 7 domains:
    1- Recommended name:
            [Acyl-carrier-protein] S-acetyltransferase
              EC=2.3.1.38
    2- Recommended name:
            [Acyl-carrier-protein] S-malonyltransferase
              EC=2.3.1.39
    3- Recommended name:
            3-oxoacyl-[acyl-carrier-protein] synthase
              EC=2.3.1.41
    4- Recommended name:
            3-oxoacyl-[acyl-carrier-protein] reductase
              EC=1.1.1.100
    5- Recommended name:
            3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
              EC=4.2.1.61
    6- Recommended name:
            Enoyl-[acyl-carrier-protein] reductase
              EC=1.3.1.10
    7- Recommended name:
            Oleoyl-[acyl-carrier-protein] hydrolase
              EC=3.1.2.14

Gene names

Name:	FASN
Synonyms:	FAS

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	2511 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

Hide | Top

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 (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] = hexadec-2-enoyl-[acyl-carrier-protein] + H₂O. Ref.1 Acyl-[acyl-carrier-protein] + NADP⁺ = 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.12
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 AAC50259.1 differs from that shown. Reason: Miscellaneous discrepancy. Several sequencing errors.

Hide | Top

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	NAD NADP Phosphopantetheine Pyridoxal phosphate
Molecular function	Hydrolase Lyase Oxidoreductase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA cytosol Ref.1 Inferred from Experiment. Source: Reactome melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Inferred from electronic annotation. Source: EC 3-oxoacyl-[acyl-carrier-protein] reductase activity Ref.1 Inferred from Experiment. Source: Reactome 3-oxoacyl-[acyl-carrier-protein] synthase activity Ref.1 Inferred from Experiment. Source: Reactome [acyl-carrier-protein] S-acetyltransferase activity Ref.1 Inferred from Experiment. Source: Reactome [acyl-carrier-protein] S-malonyltransferase activity Ref.1 Inferred from Experiment. Source: Reactome acyl carrier activity Inferred from electronic annotation. Source: InterPro cofactor binding Inferred from electronic annotation. Source: InterPro enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Ref.1 Inferred from Experiment. Source: Reactome oleoyl-[acyl-carrier-protein] hydrolase activity Ref.1 Inferred from Experiment. Source: Reactome phosphopantetheine binding Inferred from electronic annotation. Source: InterPro protein binding Ref.21 Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NDRG1	Q92597	1	EBI-356658,EBI-716486

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2511

2511

Fatty acid synthase

PRO_0000180276

Regions

Domain

2123 – 2179

Acyl carrier

Nucleotide binding

1671 – 1688

NADP (ER) By similarity

Nucleotide binding

1886 – 1901

NADP (KR) By similarity

Region

1 – 414

414

Beta-ketoacyl synthase By similarity

Region

429 – 817

389

Acyl and malonyl transferases By similarity

Region

1635 – 1863

229

Enoyl reductase By similarity

Region

1864 – 2118

255

Beta-ketoacyl reductase By similarity

Region

2207 – 2511

305

Thioesterase By similarity

Sites

Active site

161

For beta-ketoacyl synthase activity By similarity

Active site

581

For malonyltransferase activity By similarity

Active site

878

For beta-hydroxyacyl dehydratase activity By similarity

Active site

2308

For thioesterase activity Ref.22

Active site

2481

For thioesterase activity By similarity

Amino acid modifications

Modified residue

N-acetylmethionine Ref.7 Ref.16

Modified residue

N6-acetyllysine Ref.18

Modified residue

207

Phosphoserine Ref.16 Ref.14

Modified residue

298

N6-acetyllysine Ref.18

Modified residue

436

N6-acetyllysine Ref.18

Modified residue

528

N6-acetyllysine Ref.18

Modified residue

673

N6-acetyllysine Ref.18

Modified residue

1704

N6-(pyridoxal phosphate)lysine By similarity

Modified residue

1704

N6-acetyllysine Ref.18

Modified residue

1752

N6-acetyllysine Ref.18

Modified residue

1771

N6-acetyllysine Ref.18

Modified residue

1847

N6-acetyllysine Ref.18

Modified residue

1995

N6-acetyllysine Ref.18

Modified residue

2156

O-(pantetheine 4'-phosphoryl)serine By similarity

Modified residue

2198

Phosphoserine Ref.14

Modified residue

2204

Phosphothreonine Ref.16 Ref.14 Ref.10 Ref.11 Ref.13

Modified residue

2236

Phosphoserine Ref.14

Natural variations

Natural variant

1483

V → I: dbSNP rs2228305.

VAR_055479

Natural variant

1694

R → H: dbSNP rs2229424.

VAR_055480

Natural variant

1888

I → V: dbSNP rs2228307.

VAR_055481

Experimental info

Sequence conflict

459 – 462

AVPA → LSPT in AAA73576. Ref.2

Sequence conflict

528 – 529

KP → NR in AAA73576. Ref.2

Sequence conflict

637

G → A in AAA73576. Ref.2

Sequence conflict

801

G → R in AAA73576. Ref.2

Sequence conflict

902

A → P in AAA73576. Ref.2

Sequence conflict

958

V → M in AAS09886. Ref.3

Sequence conflict

1121

P → S in AAA73576. Ref.2

Sequence conflict

1121

P → S in AAS09886. Ref.3

Sequence conflict

1151

K → T in AAH63242. Ref.6

Sequence conflict

1353 – 1356

LGDI → SGH in AAA73576. Ref.2

Sequence conflict

1386

L → V in AAA73576. Ref.2

Sequence conflict

1467 – 1468

NR → T in AAA73576. Ref.2

Sequence conflict

1827

K → E in AAS09886. Ref.3

Sequence conflict

1934

R → A in AAA73576. Ref.2

Sequence conflict

2065

D → H in AAB35516. Ref.9

Sequence conflict

2087

R → A in AAA73576. Ref.2

Sequence conflict

2363

A → P in AAB35516. Ref.9

Sequence conflict

2428

R → G in AAA73576. Ref.2

Sequence conflict

2453

A → T in AAB35516. Ref.9

Sequence conflict

2456

E → Q in AAB35516. Ref.9

Secondary structure

2511

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P49327-1 [UniParc].

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

FASTA

2,511

273,427

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 7567999] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, PHOSPHOPANTETHEINE CONTENT, 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. Nusbaum C. Nature 440:1045-1049(2006) [PubMed: 16625196] [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: 15489334] [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, 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: 8022791] [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: 7595075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2047-2511, TISSUE SPECIFICITY.
[10]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2204, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2204, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"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: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2204, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-2198; THR-2204 AND SER-2236, MASS SPECTROMETRY.
[15]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND THR-2204, MASS SPECTROMETRY.
[17]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2204, MASS SPECTROMETRY.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-298; LYS-436; LYS-528; LYS-673; LYS-1704; LYS-1752; LYS-1771; LYS-1847 AND LYS-1995, MASS SPECTROMETRY.
[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: 11756679] [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: 15507492] [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: 18022563] [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: 17618296] [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.

Hide | Top

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.

IPI

IPI00026781.

PIR

A57788.
G01880.

RefSeq

NP_004095.4.

UniGene

Hs.83190

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XKT	X-ray	2.60	A/B	2218-2502	[»]
2CG5	X-ray	2.70	B	2119-2207	[»]
2JFD	X-ray	2.81	A/B/C/D	422-823	[»]
2JFK	X-ray	2.40	A/B/C/D	422-831	[»]
2PX6	X-ray	2.30	A/B	2200-2511	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33681N.

IntAct

P49327. 11 interactions.

STRING

P49327.

PTM databases

PhosphoSite

P49327.

Proteomic databases

PRIDE

P49327.

Genome annotation databases

Ensembl

ENST00000306749; ENSP00000304592; ENSG00000169710; Homo sapiens. [Genome view]

GeneID

2194.

KEGG

hsa:2194.

Organism-specific databases

CTD

2194.

GeneCards

GC17M077629.

H-InvDB

HIX0014269.

HGNC

HGNC:3594. FASN.

HPA

CAB005192.
HPA006461.

MIM

600212. gene.

PharmGKB

PA28006.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15444.

HOVERGEN

P49327.

InParanoid

P49327.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000169710-MONOMER.

BRENDA

1.1.1.100. 247.
1.3.1.10. 247.
2.3.1.38. 247.
2.3.1.39. 247.
2.3.1.41. 247.
2.3.1.85. 247.
3.1.2.14. 247.
4.2.1.61. 247.

Reactome

REACT_11193. Metabolism of vitamins and cofactors.
REACT_1505. Integration of energy metabolism.
REACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P49327.

Bgee

P49327.

CleanEx

HS_FAS.
HS_FASN.

Genevestigator

P49327.

GermOnline

ENSG00000169710. Homo sapiens.

Family and domain databases

InterPro

IPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPlipase.
IPR013149. ADH_Zn-bd.
IPR000794. Beta-ketoacyl_synthase.
IPR011032. GroES-like.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR006163. Phsphopanteth_bd.
IPR020842. PKS/FAS_KR.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR006162. PPantetheine_attach_site.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]

Gene3D

G3DSA:3.40.366.10. Ac_transferase_reg. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.

PANTHER

PTHR11712. Ketoacyl_synth. 1 hit.

Pfam

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.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]

SMART

SM00829. PKS_ER. 1 hit.
SM00822. PKS_KR. 1 hit.
[Graphical view]

PROSITE

PS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB01034. Cerulenin.
DB01083. Orlistat.
DB00339. Pyrazinamide.

NextBio

8869.

SOURCE

Search...

Hide | Top

Entry information

Entry name

FAS_HUMAN

Accession

Primary (citable) accession number: P49327
Secondary accession number(s): Q13479

Q96IT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	November 24, 2009
Last modified:	February 9, 2010
This is version 116 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.

Hide | Top

Relevant documents

Human chromosome 17

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents