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P49327

- FAS_HUMAN

UniProt

P49327 - FAS_HUMAN

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Protein

Fatty acid synthase

Gene
FASN, FAS
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].
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 activity By similarity
Active sitei581 – 5811For malonyltransferase activity By similarity
Active sitei878 – 8781For beta-hydroxyacyl dehydratase activity By similarity
Active sitei2308 – 23081For thioesterase activity1 Publication
Active sitei2481 – 24811For thioesterase activity By similarity

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. protein binding Source: UniProtKB
  17. 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. Melanosome
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. glycogen granule Source: Ensembl
  5. Golgi apparatus Source: HPA
  6. melanosome Source: UniProtKB-SubCell
  7. membrane Source: UniProt
  8. mitochondrion Source: Ensembl
  9. 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-acetyllysine By similarity
Modified residuei1704 – 17041N6-(pyridoxal phosphate)lysine; alternate By 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)serine
Modified residuei2198 – 21981Phosphoserine2 Publications
Modified residuei2204 – 22041Phosphothreonine3 Publications
Modified residuei2236 – 22361Phosphoserine1 Publication
Modified residuei2391 – 23911N6-acetyllysine By 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.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108488. 51 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 – 1310
Beta strandi16 – 183
Helixi19 – 279
Beta strandi36 – 405
Helixi44 – 463
Turni62 – 665
Helixi69 – 735
Helixi77 – 9216
Helixi97 – 1004
Beta strandi106 – 1105
Helixi115 – 1206
Turni124 – 1263
Helixi130 – 1356
Helixi139 – 14810
Beta strandi154 – 1585
Helixi160 – 1623
Helixi163 – 17614
Beta strandi181 – 1899
Helixi194 – 2029
Beta strandi227 – 2359
Helixi236 – 2383
Beta strandi243 – 25311
Helixi266 – 27914
Helixi284 – 2863
Beta strandi287 – 2915
Helixi300 – 31213
Beta strandi320 – 3234
Helixi326 – 3294
Helixi333 – 3353
Helixi336 – 35015
Helixi367 – 3704
Beta strandi373 – 3764
Beta strandi387 – 3937
Beta strandi397 – 40610
Helixi416 – 4194
Beta strandi422 – 4309
Helixi431 – 44313
Turni444 – 4463
Helixi448 – 45710
Turni462 – 4643
Beta strandi467 – 47711
Beta strandi481 – 4844
Beta strandi492 – 4965
Turni504 – 5096
Helixi510 – 5123
Helixi514 – 52714
Helixi528 – 5303
Helixi534 – 5396
Helixi545 – 5473
Helixi549 – 56921
Beta strandi575 – 5795
Helixi583 – 5908
Helixi596 – 61116
Beta strandi618 – 6258
Helixi627 – 6337
Beta strandi639 – 6457
Beta strandi648 – 6547
Helixi655 – 66713
Beta strandi672 – 6754
Beta strandi677 – 6793
Helixi685 – 6906
Helixi691 – 70111
Beta strandi702 – 7043
Beta strandi715 – 7173
Helixi719 – 7213
Helixi725 – 7284
Helixi732 – 7409
Helixi745 – 7495
Beta strandi757 – 7648
Helixi768 – 7747
Beta strandi780 – 7834
Helixi792 – 80514
Helixi812 – 8154
Helixi831 – 8333
Helixi847 – 8493
Helixi2127 – 21348
Turni2149 – 21535
Helixi2156 – 217015
Helixi2176 – 21805
Helixi2184 – 21929
Helixi2219 – 22224
Beta strandi2230 – 22334
Beta strandi2239 – 22413
Beta strandi2244 – 22474
Helixi2255 – 22573
Helixi2258 – 22636
Beta strandi2268 – 22714
Helixi2282 – 229312
Turni2294 – 22963
Beta strandi2303 – 23075
Helixi2309 – 232517
Beta strandi2333 – 23386
Helixi2343 – 235210
Helixi2360 – 237516
Helixi2380 – 23878
Beta strandi2390 – 23923
Helixi2393 – 240715
Helixi2413 – 243220
Beta strandi2443 – 24475
Turni2459 – 24635
Helixi2464 – 24663
Beta strandi2472 – 24765
Helixi2483 – 24853
Helixi2487 – 249913

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[»]
ProteinModelPortaliP49327.
SMRiP49327. Positions 2-853, 1220-2114, 2124-2194, 2218-2491.

Miscellaneous databases

EvolutionaryTraceiP49327.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2123 – 217957Acyl carrierAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 414414Beta-ketoacyl synthase By similarityAdd
BLAST
Regioni429 – 817389Acyl and malonyl transferases By similarityAdd
BLAST
Regioni1635 – 1863229Enoyl reductase By similarityAdd
BLAST
Regioni1864 – 2118255Beta-ketoacyl reductase By similarityAdd
BLAST
Regioni2207 – 2511305Thioesterase By similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3319.
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

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MEEVVIAGMS GKLPESENLQ EFWDNLIGGV DMVTDDDRRW KAGLYGLPRR     50
SGKLKDLSRF DASFFGVHPK QAHTMDPQLR LLLEVTYEAI VDGGINPDSL 100
RGTHTGVWVG VSGSETSEAL SRDPETLVGY SMVGCQRAMM ANRLSFFFDF 150
RGPSIALDTA CSSSLMALQN AYQAIHSGQC PAAIVGGINV LLKPNTSVQF 200
LRLGMLSPEG TCKAFDTAGN GYCRSEGVVA VLLTKKSLAR RVYATILNAG 250
TNTDGFKEQG VTFPSGDIQE QLIRSLYQSA GVAPESFEYI EAHGTGTKVG 300
DPQELNGITR ALCATRQEPL LIGSTKSNMG HPEPASGLAA LAKVLLSLEH 350
GLWAPNLHFH SPNPEIPALL DGRLQVVDQP LPVRGGNVGI NSFGFGGSNV 400
HIILRPNTQP PPAPAPHATL PRLLRASGRT PEAVQKLLEQ GLRHSQDLAF 450
LSMLNDIAAV PATAMPFRGY AVLGGERGGP EVQQVPAGER PLWFICSGMG 500
TQWRGMGLSL MRLDRFRDSI LRSDEAVKPF GLKVSQLLLS TDESTFDDIV 550
HSFVSLTAIQ IGLIDLLSCM GLRPDGIVGH SLGEVACGYA DGCLSQEEAV 600
LAAYWRGQCI KEAHLPPGAM AAVGLSWEEC KQRCPPGVVP ACHNSKDTVT 650
ISGPQAPVFE FVEQLRKEGV FAKEVRTGGM AFHSYFMEAI APPLLQELKK 700
VIREPKPRSA RWLSTSIPEA QWHSSLARTS SAEYNVNNLV SPVLFQEALW 750
HVPEHAVVLE IAPHALLQAV LKRGLKPSCT IIPLMKKDHR DNLEFFLAGI 800
GRLHLSGIDA NPNALFPPVE FPAPRGTPLI SPLIKWDHSL AWDVPAAEDF 850
PNGSGSPSAA IYNIDTSSES PDHYLVDHTL DGRVLFPATG YLSIVWKTLA 900
RALGLGVEQL PVVFEDVVLH QATILPKTGT VSLEVRLLEA SRAFEVSENG 950
NLVVSGKVYQ WDDPDPRLFD HPESPTPNPT EPLFLAQAEV YKELRLRGYD 1000
YGPHFQGILE ASLEGDSGRL LWKDNWVSFM DTMLQMSILG SAKHGLYLPT 1050
RVTAIHIDPA THRQKLYTLQ DKAQVADVVV SRWLRVTVAG GVHISGLHTE 1100
SAPRRQQEQQ VPILEKFCFT PHTEEGCLSE RAALQEELQL CKGLVQALQT 1150
KVTQQGLKMV VPGLDGAQIP RDPSQQELPR LLSAACRLQL NGNLQLELAQ 1200
VLAQERPKLP EDPLLSGLLD SPALKACLDT AVENMPSLKM KVVEVLAGHG 1250
HLYSRIPGLL SPHPLLQLSY TATDRHPQAL EAAQAELQQH DVAQGQWDPA 1300
DPAPSALGSA DLLVCNCAVA ALGDPASALS NMVAALREGG FLLLHTLLRG 1350
HPLGDIVAFL TSTEPQYGQG ILSQDAWESL FSRVSLRLVG LKKSFYGSTL 1400
FLCRRPTPQD SPIFLPVDDT SFRWVESLKG ILADEDSSRP VWLKAINCAT 1450
SGVVGLVNCL RREPGGNRLR CVLLSNLSST SHVPEVDPGS AELQKVLQGD 1500
LVMNVYRDGA WGAFRHFLLE EDKPEEPTAH AFVSTLTRGD LSSIRWVCSS 1550
LRHAQPTCPG AQLCTVYYAS LNFRDIMLAT GKLSPDAIPG KWTSQDSLLG 1600
MEFSGRDASG KRVMGLVPAK GLATSVLLSP DFLWDVPSNW TLEEAASVPV 1650
VYSTAYYALV VRGRVRPGET LLIHSGSGGV GQAAIAIALS LGCRVFTTVG 1700
SAEKRAYLQA RFPQLDSTSF ANSRDTSFEQ HVLWHTGGKG VDLVLNSLAE 1750
EKLQASVRCL ATHGRFLEIG KFDLSQNHPL GMAIFLKNVT FHGVLLDAFF 1800
NESSADWREV WALVQAGIRD GVVRPLKCTV FHGAQVEDAF RYMAQGKHIG 1850
KVVVQVLAEE PEAVLKGAKP KLMSAISKTF CPAHKSYIIA GGLGGFGLEL 1900
AQWLIQRGVQ KLVLTSRSGI RTGYQAKQVR RWRRQGVQVQ VSTSNISSLE 1950
GARGLIAEAA QLGPVGGVFN LAVVLRDGLL ENQTPEFFQD VCKPKYSGTL 2000
NLDRVTREAC PELDYFVVFS SVSCGRGNAG QSNYGFANSA MERICEKRRH 2050
EGLPGLAVQW GAIGDVGILV ETMSTNDTIV SGTLPQRMAS CLEVLDLFLN 2100
QPHMVLSSFV LAEKAAAYRD RDSQRDLVEA VAHILGIRDL AAVNLDSSLA 2150
DLGLDSLMSV EVRQTLEREL NLVLSVREVR QLTLRKLQEL SSKADEASEL 2200
ACPTPKEDGL AQQQTQLNLR SLLVNPEGPT LMRLNSVQSS ERPLFLVHPI 2250
EGSTTVFHSL ASRLSIPTYG LQCTRAAPLD SIHSLAAYYI DCIRQVQPEG 2300
PYRVAGYSYG ACVAFEMCSQ LQAQQSPAPT HNSLFLFDGS PTYVLAYTQS 2350
YRAKLTPGCE AEAETEAICF FVQQFTDMEH NRVLEALLPL KGLEERVAAA 2400
VDLIIKSHQG LDRQELSFAA RSFYYKLRAA EQYTPKAKYH GNVMLLRAKT 2450
GGAYGEDLGA DYNLSQVCDG KVSVHVIEGD HRTLLEGSGL ESIISIIHSS 2500
LAEPRVSVRE G 2511
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.

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 conflict

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

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 [» ]
ProteinModelPortali P49327.
SMRi P49327. Positions 2-853, 1220-2114, 2124-2194, 2218-2491.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108488. 51 interactions.
DIPi DIP-33681N.
IntActi P49327. 27 interactions.
MINTi MINT-1146154.

Chemistry

ChEMBLi CHEMBL4158.
DrugBanki DB01034. Cerulenin.
DB01083. Orlistat.
DB00339. Pyrazinamide.

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.
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: September 3, 2014
This is version 164 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

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