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P49327

- FAS_HUMAN

UniProt

P49327 - FAS_HUMAN

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Protein

Fatty acid synthase

Gene

FASN

Organism
Homo sapiens (Human)
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+.1 Publication
Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].1 Publication
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].1 Publication
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].1 Publication
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.1 Publication
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.1 Publication
An acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH.1 Publication
Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei161 – 1611For beta-ketoacyl synthase activityPROSITE-ProRule annotation
Active sitei581 – 5811For malonyltransferase activityPROSITE-ProRule annotation
Active sitei878 – 8781For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation
Active sitei2308 – 23081For thioesterase activity1 PublicationPROSITE-ProRule annotation
Active sitei2481 – 24811For thioesterase activityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1671 – 168818NADP (ER)By similarityAdd
BLAST
Nucleotide bindingi1886 – 190116NADP (KR)By similarityAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. acetyl-CoA metabolic process Source: Ensembl
  2. cellular lipid metabolic process Source: Reactome
  3. cellular response to interleukin-4 Source: Ensembl
  4. energy reserve metabolic process Source: Reactome
  5. fatty acid biosynthetic process Source: UniProtKB-KW
  6. fatty acid metabolic process Source: ProtInc
  7. long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
  8. osteoblast differentiation Source: UniProt
  9. pantothenate metabolic process Source: Reactome
  10. positive regulation of cellular metabolic process Source: Reactome
  11. small molecule metabolic process Source: Reactome
  12. triglyceride biosynthetic process Source: Reactome
  13. vitamin metabolic process Source: Reactome
  14. water-soluble vitamin metabolic process Source: Reactome
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

BioCyciMetaCyc:HS09992-MONOMER.
ReactomeiREACT_11172. Vitamin B5 (pantothenate) metabolism.
REACT_1319. Fatty Acyl-CoA Biosynthesis.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_2122. ChREBP activates metabolic gene expression.
SABIO-RKP49327.

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
Synonyms:FAS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:3594. FASN.

Subcellular locationi

Cytoplasm 1 Publication. Melanosome 1 Publication
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. glycogen granule Source: Ensembl
  5. Golgi apparatus Source: HPA
  6. membrane Source: UniProtKB
  7. mitochondrion Source: Ensembl
  8. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28006.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25112511Fatty acid synthasePRO_0000180276Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei70 – 701N6-acetyllysine1 Publication
Modified residuei207 – 2071Phosphoserine1 Publication
Modified residuei298 – 2981N6-acetyllysine1 Publication
Modified residuei436 – 4361N6-acetyllysine1 Publication
Modified residuei528 – 5281N6-acetyllysine1 Publication
Modified residuei673 – 6731N6-acetyllysine1 Publication
Modified residuei992 – 9921N6-acetyllysineBy similarity
Modified residuei1704 – 17041N6-(pyridoxal phosphate)lysine; alternateBy similarity
Modified residuei1704 – 17041N6-acetyllysine; alternate1 Publication
Modified residuei1771 – 17711N6-acetyllysine1 Publication
Modified residuei1847 – 18471N6-acetyllysine1 Publication
Modified residuei1995 – 19951N6-acetyllysine1 Publication
Modified residuei2156 – 21561O-(pantetheine 4'-phosphoryl)serine1 PublicationPROSITE-ProRule annotation
Modified residuei2198 – 21981Phosphoserine2 Publications
Modified residuei2204 – 22041Phosphothreonine3 Publications
Modified residuei2236 – 22361Phosphoserine1 Publication
Modified residuei2391 – 23911N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphopantetheine, Phosphoprotein

Proteomic databases

MaxQBiP49327.
PaxDbiP49327.
PRIDEiP49327.

PTM databases

PhosphoSiteiP49327.

Expressioni

Tissue specificityi

Ubiquitous. Prominent expression in brain, lung, and liver.2 Publications

Gene expression databases

BgeeiP49327.
CleanExiHS_FAS.
HS_FASN.
GenevestigatoriP49327.

Organism-specific databases

HPAiCAB005192.
CAB015417.
HPA006461.

Interactioni

Subunit structurei

Homodimer which is arranged in a head to tail fashion.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q99IB86EBI-356658,EBI-6927928From a different organism.

Protein-protein interaction databases

BioGridi108488. 57 interactions.
DIPiDIP-33681N.
IntActiP49327. 27 interactions.
MINTiMINT-1146154.

Structurei

Secondary structure

1
2511
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1310Combined sources
Beta strandi16 – 183Combined sources
Helixi19 – 279Combined sources
Beta strandi36 – 405Combined sources
Helixi44 – 463Combined sources
Turni62 – 665Combined sources
Helixi69 – 735Combined sources
Helixi77 – 9216Combined sources
Helixi97 – 1004Combined sources
Beta strandi106 – 1105Combined sources
Helixi115 – 1206Combined sources
Turni124 – 1263Combined sources
Helixi130 – 1356Combined sources
Helixi139 – 14810Combined sources
Beta strandi154 – 1585Combined sources
Helixi160 – 1623Combined sources
Helixi163 – 17614Combined sources
Beta strandi181 – 1899Combined sources
Helixi194 – 2029Combined sources
Beta strandi227 – 2359Combined sources
Helixi236 – 2383Combined sources
Beta strandi243 – 25311Combined sources
Helixi266 – 27914Combined sources
Helixi284 – 2863Combined sources
Beta strandi287 – 2915Combined sources
Helixi300 – 31213Combined sources
Beta strandi320 – 3234Combined sources
Helixi326 – 3294Combined sources
Helixi333 – 3353Combined sources
Helixi336 – 35015Combined sources
Helixi367 – 3704Combined sources
Beta strandi373 – 3764Combined sources
Beta strandi387 – 3937Combined sources
Beta strandi397 – 40610Combined sources
Helixi416 – 4194Combined sources
Beta strandi422 – 4309Combined sources
Helixi431 – 44313Combined sources
Turni444 – 4463Combined sources
Helixi448 – 45710Combined sources
Turni462 – 4643Combined sources
Beta strandi467 – 47711Combined sources
Beta strandi481 – 4844Combined sources
Beta strandi492 – 4965Combined sources
Turni504 – 5096Combined sources
Helixi510 – 5123Combined sources
Helixi514 – 52714Combined sources
Helixi528 – 5303Combined sources
Helixi534 – 5396Combined sources
Helixi545 – 5473Combined sources
Helixi549 – 56921Combined sources
Beta strandi575 – 5795Combined sources
Helixi583 – 5908Combined sources
Helixi596 – 61116Combined sources
Beta strandi618 – 6258Combined sources
Helixi627 – 6337Combined sources
Beta strandi639 – 6457Combined sources
Beta strandi648 – 6547Combined sources
Helixi655 – 66713Combined sources
Beta strandi672 – 6754Combined sources
Beta strandi677 – 6793Combined sources
Helixi685 – 6906Combined sources
Helixi691 – 70111Combined sources
Beta strandi702 – 7043Combined sources
Beta strandi715 – 7173Combined sources
Helixi719 – 7213Combined sources
Helixi725 – 7284Combined sources
Helixi732 – 7409Combined sources
Helixi745 – 7495Combined sources
Beta strandi757 – 7648Combined sources
Helixi768 – 7747Combined sources
Beta strandi780 – 7834Combined sources
Helixi792 – 80514Combined sources
Helixi812 – 8154Combined sources
Helixi831 – 8333Combined sources
Helixi847 – 8493Combined sources
Helixi2127 – 21348Combined sources
Turni2149 – 21535Combined sources
Helixi2156 – 217015Combined sources
Helixi2176 – 21805Combined sources
Helixi2184 – 21929Combined sources
Helixi2219 – 22224Combined sources
Beta strandi2230 – 22334Combined sources
Beta strandi2239 – 22413Combined sources
Beta strandi2244 – 22474Combined sources
Helixi2255 – 22573Combined sources
Helixi2258 – 22636Combined sources
Beta strandi2268 – 22714Combined sources
Helixi2282 – 229312Combined sources
Turni2294 – 22963Combined sources
Beta strandi2303 – 23075Combined sources
Helixi2309 – 232517Combined sources
Beta strandi2333 – 23386Combined sources
Helixi2343 – 235210Combined sources
Helixi2360 – 237516Combined sources
Helixi2380 – 23878Combined sources
Beta strandi2390 – 23923Combined sources
Helixi2393 – 240715Combined sources
Helixi2413 – 243220Combined sources
Beta strandi2443 – 24475Combined sources
Turni2459 – 24635Combined sources
Helixi2464 – 24663Combined sources
Beta strandi2472 – 24765Combined sources
Helixi2483 – 24853Combined sources
Helixi2487 – 249913Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4PIVX-ray2.30A/B1110-2114[»]
ProteinModelPortaliP49327.
SMRiP49327. Positions 2-853, 1220-2114, 2124-2194, 2218-2491.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49327.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2123 – 217957Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 414414Beta-ketoacyl synthaseBy similarityAdd
BLAST
Regioni429 – 817389Acyl and malonyl transferasesBy similarityAdd
BLAST
Regioni1635 – 1863229Enoyl reductaseBy similarityAdd
BLAST
Regioni1864 – 2118255Beta-ketoacyl reductaseBy similarityAdd
BLAST
Regioni2207 – 2511305ThioesteraseBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3319.
GeneTreeiENSGT00530000063309.
HOVERGENiHBG005640.
InParanoidiP49327.
KOiK00665.
OMAiGPGPHWD.
OrthoDBiEOG71K623.
PhylomeDBiP49327.
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.
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.
IPR029063. SAM-dependent_MTases-like.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF00698. 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]
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.

P49327-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEEVVIAGMS GKLPESENLQ EFWDNLIGGV DMVTDDDRRW KAGLYGLPRR
60 70 80 90 100
SGKLKDLSRF DASFFGVHPK QAHTMDPQLR LLLEVTYEAI VDGGINPDSL
110 120 130 140 150
RGTHTGVWVG VSGSETSEAL SRDPETLVGY SMVGCQRAMM ANRLSFFFDF
160 170 180 190 200
RGPSIALDTA CSSSLMALQN AYQAIHSGQC PAAIVGGINV LLKPNTSVQF
210 220 230 240 250
LRLGMLSPEG TCKAFDTAGN GYCRSEGVVA VLLTKKSLAR RVYATILNAG
260 270 280 290 300
TNTDGFKEQG VTFPSGDIQE QLIRSLYQSA GVAPESFEYI EAHGTGTKVG
310 320 330 340 350
DPQELNGITR ALCATRQEPL LIGSTKSNMG HPEPASGLAA LAKVLLSLEH
360 370 380 390 400
GLWAPNLHFH SPNPEIPALL DGRLQVVDQP LPVRGGNVGI NSFGFGGSNV
410 420 430 440 450
HIILRPNTQP PPAPAPHATL PRLLRASGRT PEAVQKLLEQ GLRHSQDLAF
460 470 480 490 500
LSMLNDIAAV PATAMPFRGY AVLGGERGGP EVQQVPAGER PLWFICSGMG
510 520 530 540 550
TQWRGMGLSL MRLDRFRDSI LRSDEAVKPF GLKVSQLLLS TDESTFDDIV
560 570 580 590 600
HSFVSLTAIQ IGLIDLLSCM GLRPDGIVGH SLGEVACGYA DGCLSQEEAV
610 620 630 640 650
LAAYWRGQCI KEAHLPPGAM AAVGLSWEEC KQRCPPGVVP ACHNSKDTVT
660 670 680 690 700
ISGPQAPVFE FVEQLRKEGV FAKEVRTGGM AFHSYFMEAI APPLLQELKK
710 720 730 740 750
VIREPKPRSA RWLSTSIPEA QWHSSLARTS SAEYNVNNLV SPVLFQEALW
760 770 780 790 800
HVPEHAVVLE IAPHALLQAV LKRGLKPSCT IIPLMKKDHR DNLEFFLAGI
810 820 830 840 850
GRLHLSGIDA NPNALFPPVE FPAPRGTPLI SPLIKWDHSL AWDVPAAEDF
860 870 880 890 900
PNGSGSPSAA IYNIDTSSES PDHYLVDHTL DGRVLFPATG YLSIVWKTLA
910 920 930 940 950
RALGLGVEQL PVVFEDVVLH QATILPKTGT VSLEVRLLEA SRAFEVSENG
960 970 980 990 1000
NLVVSGKVYQ WDDPDPRLFD HPESPTPNPT EPLFLAQAEV YKELRLRGYD
1010 1020 1030 1040 1050
YGPHFQGILE ASLEGDSGRL LWKDNWVSFM DTMLQMSILG SAKHGLYLPT
1060 1070 1080 1090 1100
RVTAIHIDPA THRQKLYTLQ DKAQVADVVV SRWLRVTVAG GVHISGLHTE
1110 1120 1130 1140 1150
SAPRRQQEQQ VPILEKFCFT PHTEEGCLSE RAALQEELQL CKGLVQALQT
1160 1170 1180 1190 1200
KVTQQGLKMV VPGLDGAQIP RDPSQQELPR LLSAACRLQL NGNLQLELAQ
1210 1220 1230 1240 1250
VLAQERPKLP EDPLLSGLLD SPALKACLDT AVENMPSLKM KVVEVLAGHG
1260 1270 1280 1290 1300
HLYSRIPGLL SPHPLLQLSY TATDRHPQAL EAAQAELQQH DVAQGQWDPA
1310 1320 1330 1340 1350
DPAPSALGSA DLLVCNCAVA ALGDPASALS NMVAALREGG FLLLHTLLRG
1360 1370 1380 1390 1400
HPLGDIVAFL TSTEPQYGQG ILSQDAWESL FSRVSLRLVG LKKSFYGSTL
1410 1420 1430 1440 1450
FLCRRPTPQD SPIFLPVDDT SFRWVESLKG ILADEDSSRP VWLKAINCAT
1460 1470 1480 1490 1500
SGVVGLVNCL RREPGGNRLR CVLLSNLSST SHVPEVDPGS AELQKVLQGD
1510 1520 1530 1540 1550
LVMNVYRDGA WGAFRHFLLE EDKPEEPTAH AFVSTLTRGD LSSIRWVCSS
1560 1570 1580 1590 1600
LRHAQPTCPG AQLCTVYYAS LNFRDIMLAT GKLSPDAIPG KWTSQDSLLG
1610 1620 1630 1640 1650
MEFSGRDASG KRVMGLVPAK GLATSVLLSP DFLWDVPSNW TLEEAASVPV
1660 1670 1680 1690 1700
VYSTAYYALV VRGRVRPGET LLIHSGSGGV GQAAIAIALS LGCRVFTTVG
1710 1720 1730 1740 1750
SAEKRAYLQA RFPQLDSTSF ANSRDTSFEQ HVLWHTGGKG VDLVLNSLAE
1760 1770 1780 1790 1800
EKLQASVRCL ATHGRFLEIG KFDLSQNHPL GMAIFLKNVT FHGVLLDAFF
1810 1820 1830 1840 1850
NESSADWREV WALVQAGIRD GVVRPLKCTV FHGAQVEDAF RYMAQGKHIG
1860 1870 1880 1890 1900
KVVVQVLAEE PEAVLKGAKP KLMSAISKTF CPAHKSYIIA GGLGGFGLEL
1910 1920 1930 1940 1950
AQWLIQRGVQ KLVLTSRSGI RTGYQAKQVR RWRRQGVQVQ VSTSNISSLE
1960 1970 1980 1990 2000
GARGLIAEAA QLGPVGGVFN LAVVLRDGLL ENQTPEFFQD VCKPKYSGTL
2010 2020 2030 2040 2050
NLDRVTREAC PELDYFVVFS SVSCGRGNAG QSNYGFANSA MERICEKRRH
2060 2070 2080 2090 2100
EGLPGLAVQW GAIGDVGILV ETMSTNDTIV SGTLPQRMAS CLEVLDLFLN
2110 2120 2130 2140 2150
QPHMVLSSFV LAEKAAAYRD RDSQRDLVEA VAHILGIRDL AAVNLDSSLA
2160 2170 2180 2190 2200
DLGLDSLMSV EVRQTLEREL NLVLSVREVR QLTLRKLQEL SSKADEASEL
2210 2220 2230 2240 2250
ACPTPKEDGL AQQQTQLNLR SLLVNPEGPT LMRLNSVQSS ERPLFLVHPI
2260 2270 2280 2290 2300
EGSTTVFHSL ASRLSIPTYG LQCTRAAPLD SIHSLAAYYI DCIRQVQPEG
2310 2320 2330 2340 2350
PYRVAGYSYG ACVAFEMCSQ LQAQQSPAPT HNSLFLFDGS PTYVLAYTQS
2360 2370 2380 2390 2400
YRAKLTPGCE AEAETEAICF FVQQFTDMEH NRVLEALLPL KGLEERVAAA
2410 2420 2430 2440 2450
VDLIIKSHQG LDRQELSFAA RSFYYKLRAA EQYTPKAKYH GNVMLLRAKT
2460 2470 2480 2490 2500
GGAYGEDLGA DYNLSQVCDG KVSVHVIEGD HRTLLEGSGL ESIISIIHSS
2510
LAEPRVSVRE G
Length:2,511
Mass (Da):273,427
Last modified:November 24, 2009 - v3
Checksum:i7A07171FEFA3287B
GO

Sequence cautioni

The sequence AAC50259.1 differs from that shown. Reason: Several sequencing errors.
The sequence AAB35516.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAE06070.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti459 – 4624AVPA → LSPT in AAA73576. 1 PublicationCurated
Sequence conflicti528 – 5292KP → NR in AAA73576. 1 PublicationCurated
Sequence conflicti637 – 6371G → A in AAA73576. 1 PublicationCurated
Sequence conflicti801 – 8011G → R in AAA73576. 1 PublicationCurated
Sequence conflicti902 – 9021A → P in AAA73576. 1 PublicationCurated
Sequence conflicti958 – 9581V → M in AAS09886. 1 PublicationCurated
Sequence conflicti1121 – 11211P → S in AAA73576. 1 PublicationCurated
Sequence conflicti1121 – 11211P → S in AAS09886. 1 PublicationCurated
Sequence conflicti1151 – 11511K → T in AAH63242. (PubMed:15489334)Curated
Sequence conflicti1353 – 13564LGDI → SGH in AAA73576. 1 PublicationCurated
Sequence conflicti1386 – 13861L → V in AAA73576. 1 PublicationCurated
Sequence conflicti1467 – 14682NR → T in AAA73576. 1 PublicationCurated
Sequence conflicti1827 – 18271K → E in AAS09886. 1 PublicationCurated
Sequence conflicti1934 – 19341R → A in AAA73576. 1 PublicationCurated
Sequence conflicti2065 – 20651D → H in AAB35516. (PubMed:7595075)Curated
Sequence conflicti2087 – 20871R → A in AAA73576. 1 PublicationCurated
Sequence conflicti2363 – 23631A → P in AAB35516. (PubMed:7595075)Curated
Sequence conflicti2428 – 24281R → G in AAA73576. 1 PublicationCurated
Sequence conflicti2453 – 24531A → T in AAB35516. (PubMed:7595075)Curated
Sequence conflicti2456 – 24561E → Q in AAB35516. (PubMed:7595075)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1483 – 14831V → I.
Corresponds to variant rs2228305 [ dbSNP | Ensembl ].
VAR_055479
Natural varianti1694 – 16941R → H.
Corresponds to variant rs2229424 [ dbSNP | Ensembl ].
VAR_055480
Natural varianti1888 – 18881I → V.
Corresponds to variant rs2228307 [ dbSNP | Ensembl ].
VAR_055481

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11801.1.
PIRiA57788.
G01880.
RefSeqiNP_004095.4. NM_004104.4.
UniGeneiHs.83190.

Genome annotation databases

EnsembliENST00000306749; ENSP00000304592; ENSG00000169710.
GeneIDi2194.
KEGGihsa:2194.
UCSCiuc002kdu.3. human.

Polymorphism databases

DMDMi269849686.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS11801.1.
PIRi A57788.
G01880.
RefSeqi NP_004095.4. NM_004104.4.
UniGenei Hs.83190.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
3HHD X-ray 2.15 A/B/C/D 2-963 [» ]
3TJM X-ray 1.48 A 2218-2500 [» ]
4PIV X-ray 2.30 A/B 1110-2114 [» ]
ProteinModelPortali P49327.
SMRi P49327. Positions 2-853, 1220-2114, 2124-2194, 2218-2491.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108488. 57 interactions.
DIPi DIP-33681N.
IntActi P49327. 27 interactions.
MINTi MINT-1146154.

Chemistry

ChEMBLi CHEMBL4158.
DrugBanki DB01034. Cerulenin.
DB01083. Orlistat.

PTM databases

PhosphoSitei P49327.

Polymorphism databases

DMDMi 269849686.

Proteomic databases

MaxQBi P49327.
PaxDbi P49327.
PRIDEi P49327.

Protocols and materials databases

DNASUi 2194.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000306749 ; ENSP00000304592 ; ENSG00000169710 .
GeneIDi 2194.
KEGGi hsa:2194.
UCSCi uc002kdu.3. human.

Organism-specific databases

CTDi 2194.
GeneCardsi GC17M080037.
H-InvDB HIX0014269.
HGNCi HGNC:3594. FASN.
HPAi CAB005192.
CAB015417.
HPA006461.
MIMi 600212. gene.
neXtProti NX_P49327.
PharmGKBi PA28006.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3319.
GeneTreei ENSGT00530000063309.
HOVERGENi HBG005640.
InParanoidi P49327.
KOi K00665.
OMAi GPGPHWD.
OrthoDBi EOG71K623.
PhylomeDBi P49327.
TreeFami TF300549.

Enzyme and pathway databases

BioCyci MetaCyc:HS09992-MONOMER.
Reactomei REACT_11172. Vitamin B5 (pantothenate) metabolism.
REACT_1319. Fatty Acyl-CoA Biosynthesis.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_2122. ChREBP activates metabolic gene expression.
SABIO-RK P49327.

Miscellaneous databases

ChiTaRSi FASN. human.
EvolutionaryTracei P49327.
GeneWikii Fatty_acid_synthase.
GenomeRNAii 2194.
NextBioi 8869.
PROi P49327.
SOURCEi Search...

Gene expression databases

Bgeei P49327.
CleanExi HS_FAS.
HS_FASN.
Genevestigatori P49327.

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.
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.
IPR029063. SAM-dependent_MTases-like.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF00698. 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 ]
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. 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.
    , 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. 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. 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. 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. 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.

Entry informationi

Entry nameiFAS_HUMAN
AccessioniPrimary (citable) accession number: P49327
Secondary accession number(s): Q13479
, Q16702, Q4LE83, Q6P4U5, Q6SS02, Q969R1, Q96C68, Q96IT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 24, 2009
Last modified: October 29, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3