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Protein

Fatty acid synthase

Gene

FASN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei161For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei581For malonyltransferase activityPROSITE-ProRule annotation1
Active sitei878For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation1
Active sitei2308For thioesterase activityPROSITE-ProRule annotation1 Publication1
Active sitei2481For thioesterase activityPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1671 – 1688NADP (ER)By similarityAdd BLAST18
Nucleotide bindingi1886 – 1901NADP (KR)By similarityAdd BLAST16

GO - Molecular functioni

GO - Biological processi

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.
ZFISH:HS09992-MONOMER.
BRENDAi2.3.1.85. 2681.
ReactomeiR-HSA-163765. ChREBP activates metabolic gene expression.
R-HSA-199220. Vitamin B5 (pantothenate) metabolism.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-75105. Fatty Acyl-CoA Biosynthesis.
SABIO-RKP49327.
SIGNORiP49327.

Protein family/group databases

ESTHERihuman-FASN. Thioesterase.

Chemistry databases

SwissLipidsiSLP:000000765.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:3594. FASN.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • glycogen granule Source: Ensembl
  • Golgi apparatus Source: HPA
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • mitochondrion Source: Ensembl
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi2194.
OpenTargetsiENSG00000169710.
PharmGKBiPA28006.

Chemistry databases

ChEMBLiCHEMBL4158.
DrugBankiDB01034. Cerulenin.
DB01083. Orlistat.
GuidetoPHARMACOLOGYi2608.

Polymorphism and mutation databases

BioMutaiFASN.
DMDMi269849686.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001802761 – 2511Fatty acid synthaseAdd BLAST2511

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei63PhosphoserineCombined sources1
Modified residuei70N6-acetyllysineCombined sources1
Modified residuei207PhosphoserineCombined sources1
Modified residuei298N6-acetyllysineCombined sources1
Modified residuei436N6-acetyllysineCombined sources1
Modified residuei528N6-acetyllysineCombined sources1
Modified residuei673N6-acetyllysineCombined sources1
Modified residuei725PhosphoserineBy similarity1
Modified residuei992N6-acetyllysineBy similarity1
Modified residuei1174PhosphoserineCombined sources1
Modified residuei1411PhosphoserineCombined sources1
Modified residuei1584PhosphoserineCombined sources1
Modified residuei1594PhosphoserineBy similarity1
Modified residuei1704N6-(pyridoxal phosphate)lysine; alternateBy similarity1
Modified residuei1704N6-acetyllysine; alternateCombined sources1
Modified residuei1771N6-acetyllysineCombined sources1
Modified residuei1847N6-acetyllysineCombined sources1
Modified residuei1995N6-acetyllysineCombined sources1
Modified residuei2156O-(pantetheine 4'-phosphoryl)serine; alternatePROSITE-ProRule annotation1 Publication1
Modified residuei2156Phosphoserine; alternateBy similarity1
Modified residuei2198PhosphoserineCombined sources1
Modified residuei2204PhosphothreonineCombined sources1
Modified residuei2215PhosphothreonineCombined sources1
Modified residuei2236PhosphoserineCombined sources1
Modified residuei2391N6-acetyllysineBy similarity1
Cross-linki2449Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphopantetheine, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP49327.
MaxQBiP49327.
PaxDbiP49327.
PeptideAtlasiP49327.
PRIDEiP49327.

PTM databases

iPTMnetiP49327.
PhosphoSitePlusiP49327.
SwissPalmiP49327.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000169710.
CleanExiHS_FAS.
HS_FASN.
ExpressionAtlasiP49327. baseline and differential.
GenevisibleiP49327. HS.

Organism-specific databases

HPAiCAB005192.
CAB015417.
HPA006461.
HPA056108.

Interactioni

Subunit structurei

Homodimer which is arranged in a head to tail fashion (PubMed:17618296, PubMed:18022563, Ref. 27). Interacts with CEACAM1; this interaction is insulin and phosphorylation-dependent; reduces fatty-acid synthase activity (By similarity).By similarity3 Publications

Binary interactionsi

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

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi108488. 92 interactors.
DIPiDIP-33681N.
IntActiP49327. 47 interactors.
MINTiMINT-1146154.
STRINGi9606.ENSP00000304592.

Chemistry databases

BindingDBiP49327.

Structurei

Secondary structure

12511
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 13Combined sources10
Beta strandi16 – 18Combined sources3
Helixi19 – 27Combined sources9
Beta strandi36 – 40Combined sources5
Helixi44 – 46Combined sources3
Turni62 – 66Combined sources5
Helixi69 – 73Combined sources5
Helixi77 – 92Combined sources16
Helixi97 – 100Combined sources4
Beta strandi106 – 110Combined sources5
Helixi115 – 120Combined sources6
Turni124 – 126Combined sources3
Helixi130 – 135Combined sources6
Helixi139 – 148Combined sources10
Beta strandi154 – 158Combined sources5
Helixi160 – 162Combined sources3
Helixi163 – 176Combined sources14
Beta strandi181 – 189Combined sources9
Helixi194 – 202Combined sources9
Beta strandi227 – 235Combined sources9
Helixi236 – 238Combined sources3
Beta strandi243 – 253Combined sources11
Helixi266 – 279Combined sources14
Helixi284 – 286Combined sources3
Beta strandi287 – 291Combined sources5
Helixi300 – 312Combined sources13
Beta strandi320 – 323Combined sources4
Helixi326 – 329Combined sources4
Helixi333 – 335Combined sources3
Helixi336 – 350Combined sources15
Helixi367 – 370Combined sources4
Beta strandi373 – 376Combined sources4
Beta strandi387 – 393Combined sources7
Beta strandi397 – 406Combined sources10
Helixi416 – 419Combined sources4
Beta strandi422 – 430Combined sources9
Helixi431 – 443Combined sources13
Turni444 – 446Combined sources3
Helixi448 – 457Combined sources10
Turni462 – 464Combined sources3
Beta strandi467 – 477Combined sources11
Beta strandi481 – 484Combined sources4
Beta strandi492 – 496Combined sources5
Turni504 – 509Combined sources6
Helixi510 – 512Combined sources3
Helixi514 – 527Combined sources14
Helixi528 – 530Combined sources3
Helixi534 – 539Combined sources6
Helixi545 – 547Combined sources3
Helixi549 – 569Combined sources21
Beta strandi575 – 579Combined sources5
Helixi583 – 590Combined sources8
Helixi596 – 611Combined sources16
Beta strandi618 – 625Combined sources8
Helixi627 – 633Combined sources7
Beta strandi639 – 645Combined sources7
Beta strandi648 – 654Combined sources7
Helixi655 – 667Combined sources13
Beta strandi672 – 675Combined sources4
Beta strandi677 – 679Combined sources3
Helixi685 – 690Combined sources6
Helixi691 – 701Combined sources11
Beta strandi702 – 704Combined sources3
Beta strandi715 – 717Combined sources3
Helixi719 – 721Combined sources3
Helixi725 – 728Combined sources4
Helixi732 – 740Combined sources9
Helixi745 – 749Combined sources5
Beta strandi757 – 764Combined sources8
Helixi768 – 774Combined sources7
Beta strandi780 – 783Combined sources4
Helixi792 – 805Combined sources14
Helixi812 – 815Combined sources4
Helixi831 – 833Combined sources3
Helixi847 – 849Combined sources3
Beta strandi1113 – 1127Combined sources15
Turni1128 – 1130Combined sources3
Helixi1132 – 1149Combined sources18
Helixi1173 – 1175Combined sources3
Helixi1177 – 1187Combined sources11
Helixi1200 – 1205Combined sources6
Helixi1206 – 1211Combined sources6
Turni1213 – 1220Combined sources8
Helixi1222 – 1233Combined sources12
Beta strandi1236 – 1245Combined sources10
Helixi1247 – 1250Combined sources4
Helixi1252 – 1254Combined sources3
Helixi1256 – 1260Combined sources5
Beta strandi1263 – 1265Combined sources3
Beta strandi1267 – 1275Combined sources9
Helixi1277 – 1283Combined sources7
Helixi1284 – 1289Combined sources6
Beta strandi1293 – 1296Combined sources4
Helixi1305 – 1307Combined sources3
Beta strandi1309 – 1316Combined sources8
Turni1317 – 1319Combined sources3
Helixi1325 – 1335Combined sources11
Beta strandi1336 – 1349Combined sources14
Helixi1352 – 1360Combined sources9
Helixi1374 – 1383Combined sources10
Beta strandi1387 – 1394Combined sources8
Beta strandi1397 – 1404Combined sources8
Beta strandi1413 – 1416Combined sources4
Helixi1424 – 1433Combined sources10
Beta strandi1441 – 1445Combined sources5
Helixi1453 – 1460Combined sources8
Helixi1466 – 1468Combined sources3
Beta strandi1469 – 1474Combined sources6
Helixi1491 – 1499Combined sources9
Beta strandi1502 – 1507Combined sources6
Beta strandi1510 – 1518Combined sources9
Beta strandi1531 – 1537Combined sources7
Helixi1541 – 1543Combined sources3
Beta strandi1544 – 1548Combined sources5
Beta strandi1562 – 1570Combined sources9
Helixi1573 – 1579Combined sources7
Helixi1585 – 1587Combined sources3
Helixi1589 – 1592Combined sources4
Beta strandi1602 – 1606Combined sources5
Beta strandi1612 – 1616Combined sources5
Beta strandi1622 – 1628Combined sources7
Helixi1630 – 1632Combined sources3
Beta strandi1633 – 1635Combined sources3
Helixi1642 – 1645Combined sources4
Helixi1649 – 1659Combined sources11
Turni1660 – 1663Combined sources4
Beta strandi1670 – 1675Combined sources6
Helixi1679 – 1690Combined sources12
Beta strandi1694 – 1701Combined sources8
Helixi1702 – 1711Combined sources10
Helixi1717 – 1719Combined sources3
Beta strandi1720 – 1722Combined sources3
Beta strandi1723 – 1726Combined sources4
Helixi1728 – 1735Combined sources8
Turni1736 – 1738Combined sources3
Beta strandi1741 – 1746Combined sources6
Turni1747 – 1751Combined sources5
Helixi1753 – 1757Combined sources5
Beta strandi1760 – 1769Combined sources10
Turni1784 – 1788Combined sources5
Beta strandi1790 – 1794Combined sources5
Helixi1796 – 1799Combined sources4
Turni1801 – 1803Combined sources3
Helixi1805 – 1819Combined sources15
Beta strandi1828 – 1832Combined sources5
Helixi1833 – 1835Combined sources3
Helixi1836 – 1845Combined sources10
Beta strandi1849 – 1857Combined sources9
Beta strandi1885 – 1890Combined sources6
Turni1891 – 1893Combined sources3
Helixi1895 – 1906Combined sources12
Beta strandi1911 – 1915Combined sources5
Helixi1923 – 1934Combined sources12
Beta strandi1938 – 1942Combined sources5
Helixi1949 – 1962Combined sources14
Beta strandi1965 – 1970Combined sources6
Helixi1980 – 1982Combined sources3
Helixi1985 – 2009Combined sources25
Beta strandi2015 – 2021Combined sources7
Helixi2022 – 2025Combined sources4
Helixi2032 – 2050Combined sources19
Beta strandi2056 – 2060Combined sources5
Beta strandi2065 – 2067Combined sources3
Turni2068 – 2070Combined sources3
Beta strandi2075 – 2077Combined sources3
Helixi2088 – 2099Combined sources12
Beta strandi2104 – 2111Combined sources8
Helixi2127 – 2134Combined sources8
Turni2149 – 2153Combined sources5
Helixi2156 – 2170Combined sources15
Helixi2176 – 2180Combined sources5
Helixi2184 – 2192Combined sources9
Helixi2219 – 2222Combined sources4
Beta strandi2230 – 2233Combined sources4
Beta strandi2239 – 2241Combined sources3
Beta strandi2244 – 2247Combined sources4
Helixi2255 – 2257Combined sources3
Helixi2258 – 2263Combined sources6
Beta strandi2268 – 2271Combined sources4
Helixi2282 – 2293Combined sources12
Turni2294 – 2296Combined sources3
Beta strandi2303 – 2307Combined sources5
Helixi2309 – 2325Combined sources17
Beta strandi2333 – 2338Combined sources6
Helixi2343 – 2352Combined sources10
Helixi2360 – 2375Combined sources16
Helixi2380 – 2387Combined sources8
Beta strandi2390 – 2392Combined sources3
Helixi2393 – 2407Combined sources15
Helixi2413 – 2432Combined sources20
Beta strandi2443 – 2447Combined sources5
Beta strandi2453 – 2458Combined sources6
Turni2459 – 2463Combined sources5
Helixi2464 – 2466Combined sources3
Beta strandi2472 – 2476Combined sources5
Helixi2483 – 2485Combined sources3
Helixi2487 – 2499Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4W82X-ray1.70A/B1529-1867[»]
4W9NX-ray1.84A/B/C/D1529-1867[»]
4Z49X-ray1.70A/B2221-2502[»]
5C37X-ray2.30A/C1108-1523[»]
A/C1877-2122[»]
ProteinModelPortaliP49327.
SMRiP49327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49327.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2123 – 2179Acyl carrierPROSITE-ProRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 414Beta-ketoacyl synthaseBy similarityAdd BLAST414
Regioni429 – 817Acyl and malonyl transferasesBy similarityAdd BLAST389
Regioni1635 – 1863Enoyl reductaseBy similarityAdd BLAST229
Regioni1864 – 2118Beta-ketoacyl reductaseBy similarityAdd BLAST255
Regioni2207 – 2511ThioesteraseBy similarityAdd BLAST305

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1202. Eukaryota.
COG3321. LUCA.
GeneTreeiENSGT00530000063309.
HOVERGENiHBG005640.
InParanoidiP49327.
KOiK00665.
OMAiVYYALHH.
OrthoDBiEOG091G003K.
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.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR023102. Fatty_acid_synthase_dom_2.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
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.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR029063. SAM-dependent_MTases.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF16197. KAsynt_C_assoc. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF08242. Methyltransf_12. 1 hit.
PF00550. PP-binding. 1 hit.
PF14765. PS-DH. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00826. PKS_DH. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 2 hits.
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 AAB35516 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAC50259 differs from that shown. Several sequencing errors.Curated
The sequence BAE06070 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti459 – 462AVPA → LSPT in AAA73576 (Ref. 2) Curated4
Sequence conflicti528 – 529KP → NR in AAA73576 (Ref. 2) Curated2
Sequence conflicti637G → A in AAA73576 (Ref. 2) Curated1
Sequence conflicti801G → R in AAA73576 (Ref. 2) Curated1
Sequence conflicti902A → P in AAA73576 (Ref. 2) Curated1
Sequence conflicti958V → M in AAS09886 (Ref. 3) Curated1
Sequence conflicti1121P → S in AAA73576 (Ref. 2) Curated1
Sequence conflicti1121P → S in AAS09886 (Ref. 3) Curated1
Sequence conflicti1151K → T in AAH63242 (PubMed:15489334).Curated1
Sequence conflicti1353 – 1356LGDI → SGH in AAA73576 (Ref. 2) Curated4
Sequence conflicti1386L → V in AAA73576 (Ref. 2) Curated1
Sequence conflicti1467 – 1468NR → T in AAA73576 (Ref. 2) Curated2
Sequence conflicti1827K → E in AAS09886 (Ref. 3) Curated1
Sequence conflicti1934R → A in AAA73576 (Ref. 2) Curated1
Sequence conflicti2065D → H in AAB35516 (PubMed:7595075).Curated1
Sequence conflicti2087R → A in AAA73576 (Ref. 2) Curated1
Sequence conflicti2363A → P in AAB35516 (PubMed:7595075).Curated1
Sequence conflicti2428R → G in AAA73576 (Ref. 2) Curated1
Sequence conflicti2453A → T in AAB35516 (PubMed:7595075).Curated1
Sequence conflicti2456E → Q in AAB35516 (PubMed:7595075).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0554791483V → I.Corresponds to variant rs2228305dbSNPEnsembl.1
Natural variantiVAR_0554801694R → H.Corresponds to variant rs561903908dbSNPEnsembl.1
Natural variantiVAR_0554811888I → V.Corresponds to variant rs2228307dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_011521840.1. XM_011523538.2.
UniGeneiHs.83190.

Genome annotation databases

EnsembliENST00000306749; ENSP00000304592; ENSG00000169710.
GeneIDi2194.
KEGGihsa:2194.
UCSCiuc002kdu.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_011521840.1. XM_011523538.2.
UniGeneiHs.83190.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4W82X-ray1.70A/B1529-1867[»]
4W9NX-ray1.84A/B/C/D1529-1867[»]
4Z49X-ray1.70A/B2221-2502[»]
5C37X-ray2.30A/C1108-1523[»]
A/C1877-2122[»]
ProteinModelPortaliP49327.
SMRiP49327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108488. 92 interactors.
DIPiDIP-33681N.
IntActiP49327. 47 interactors.
MINTiMINT-1146154.
STRINGi9606.ENSP00000304592.

Chemistry databases

BindingDBiP49327.
ChEMBLiCHEMBL4158.
DrugBankiDB01034. Cerulenin.
DB01083. Orlistat.
GuidetoPHARMACOLOGYi2608.
SwissLipidsiSLP:000000765.

Protein family/group databases

ESTHERihuman-FASN. Thioesterase.

PTM databases

iPTMnetiP49327.
PhosphoSitePlusiP49327.
SwissPalmiP49327.

Polymorphism and mutation databases

BioMutaiFASN.
DMDMi269849686.

Proteomic databases

EPDiP49327.
MaxQBiP49327.
PaxDbiP49327.
PeptideAtlasiP49327.
PRIDEiP49327.

Protocols and materials databases

DNASUi2194.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306749; ENSP00000304592; ENSG00000169710.
GeneIDi2194.
KEGGihsa:2194.
UCSCiuc002kdu.4. human.

Organism-specific databases

CTDi2194.
DisGeNETi2194.
GeneCardsiFASN.
H-InvDBHIX0014269.
HGNCiHGNC:3594. FASN.
HPAiCAB005192.
CAB015417.
HPA006461.
HPA056108.
MIMi600212. gene.
neXtProtiNX_P49327.
OpenTargetsiENSG00000169710.
PharmGKBiPA28006.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1202. Eukaryota.
COG3321. LUCA.
GeneTreeiENSGT00530000063309.
HOVERGENiHBG005640.
InParanoidiP49327.
KOiK00665.
OMAiVYYALHH.
OrthoDBiEOG091G003K.
PhylomeDBiP49327.
TreeFamiTF300549.

Enzyme and pathway databases

BioCyciMetaCyc:HS09992-MONOMER.
ZFISH:HS09992-MONOMER.
BRENDAi2.3.1.85. 2681.
ReactomeiR-HSA-163765. ChREBP activates metabolic gene expression.
R-HSA-199220. Vitamin B5 (pantothenate) metabolism.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
R-HSA-75105. Fatty Acyl-CoA Biosynthesis.
SABIO-RKP49327.
SIGNORiP49327.

Miscellaneous databases

ChiTaRSiFASN. human.
EvolutionaryTraceiP49327.
GeneWikiiFatty_acid_synthase.
GenomeRNAii2194.
PROiP49327.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000169710.
CleanExiHS_FAS.
HS_FASN.
ExpressionAtlasiP49327. baseline and differential.
GenevisibleiP49327. HS.

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.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013149. ADH_C.
IPR023102. Fatty_acid_synthase_dom_2.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
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.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR029063. SAM-dependent_MTases.
IPR001031. Thioesterase.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
PF16197. KAsynt_C_assoc. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF08242. Methyltransf_12. 1 hit.
PF00550. PP-binding. 1 hit.
PF14765. PS-DH. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00826. PKS_DH. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00825. PKS_KS. 1 hit.
SM00823. PKS_PP. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 2 hits.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 190 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.