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P12276

- FAS_CHICK

UniProt

P12276 - FAS_CHICK

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Protein

Fatty acid synthase

Gene

FASN

Organism
Gallus gallus (Chicken)
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+.
Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].
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].
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.
An acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH.
Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei161 – 1611For beta-ketoacyl synthase activityPROSITE-ProRule annotation
Active sitei580 – 5801For acyl/malonyl transferase activityPROSITE-ProRule annotation
Active sitei878 – 8781For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation
Active sitei2309 – 23091For thioesterase activityPROSITE-ProRule annotation
Active sitei2482 – 24821For thioesterase activityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1675 – 169218NADP (ER)Add
BLAST
Nucleotide bindingi1889 – 190416NADP (KR)Add
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. enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity Source: UniProtKB-EC
  8. enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Source: InterPro
  9. myristoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  10. oleoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  11. palmitoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  12. zinc ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
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

SABIO-RKP12276.

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
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 25122511Fatty acid synthasePRO_0000180273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglutamate
Modified residuei1708 – 17081N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei2158 – 21581O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Acetylation, Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiP12276.
PRIDEiP12276.

Interactioni

Subunit structurei

Homodimer which is arranged in a head to tail fashion.

Protein-protein interaction databases

STRINGi9031.ENSGALP00000038133.

Structurei

3D structure databases

ProteinModelPortaliP12276.
SMRiP12276. Positions 421-821, 2122-2202, 2222-2508.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2125 – 218157Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – ?412411Beta-ketoacyl synthaseAdd
BLAST
Regioni427 – 815389Acyl and malonyl transferasesAdd
BLAST
Regioni1638 – 1866229Enoyl reductaseAdd
BLAST
Regioni1867 – 2119253Beta-ketoacyl reductaseAdd
BLAST
Regioni2209 – 2511303ThioesteraseAdd
BLAST

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3319.
HOGENOMiHOG000019642.
HOVERGENiHBG005640.
InParanoidiP12276.
PhylomeDBiP12276.

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.
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.
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: P12276-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEDVVIAGIA GKLPESENLQ EFWENLLNGV DMVTEDDRRW KPGIYGLPKR
60 70 80 90 100
NGKLKDIKKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI LDGGINPTAL
110 120 130 140 150
RGTDTGVWVG ASGSEALEAL SQDPEELLGY SMTGCQRAML ANRISYFYDF
160 170 180 190 200
TGPSLTIDTA CSSSLMALEN AYKAIRHGQC SAALVGGVNI LLKPNTSVQF
210 220 230 240 250
MKLGMLSPDG ACKAFDVSGN GYCRSEAVVV VLLTKKSMAK RVYATIVNAG
260 270 280 290 300
SNTDGFKEQG VTFPSGEMQQ QLVGSLYREC GIKPGDVEYV EAHGTGTKVG
310 320 330 340 350
DPQEVNGIVN VFCQCEREPL LIGSTKSNMG HPEPASGLAA LAKVILSLEH
360 370 380 390 400
GLWAPNLHFN DPNPDIPALH DGSLKVVCKP TPVKGGLVSI NSFGFGGSNA
410 420 430 440 450
HVILRPNEKK CQPQETCNLP RLVQVCGRTQ EAVEILIEES RKHGGCSPFL
460 470 480 490 500
SLLSDISAVP VSSMPYRGYT LVGTESDITE IQQVQASGRP LWYICSGMGT
510 520 530 540 550
QWKGMGLSLM KLDLFRQSIL RSDEALKSTG LKVSDLLLNA DENTFDDTVH
560 570 580 590 600
AFVGLAAIQI AQIDVLKAAG LQPDGILGHS VGELACGYAD NSLSHEEAVL
610 620 630 640 650
AAYWRGRCVK EAKLPPGGMA AVGLTWEECK QRCPPNVVPA CHNSEDTVTV
660 670 680 690 700
SGPLDSVSEF VTKLKKDGVF AKEVRRAGVA FHSYYMASIA PALLSALKKV
710 720 730 740 750
IPHPKPRSAR WISTSIPESQ WQSDLARNSS AEYHVNNLVN PVLFHEGLKH
760 770 780 790 800
IPENAVVVEI APHALLQAIL RRTLKPTCTI LPLMKKDHKN NLEFFLTQTG
810 820 830 840 850
KIHLTGINVL GNNLFPPVEY PVPVGTPLIS PYIKWDHSQD WDVPKAEDFP
860 870 880 890 900
SGSKGSASAS VYNIDVSPDS PDHYLVGHCI DGRVLYPATG YLVLAWRTLA
910 920 930 940 950
RSLGMVMEQT AVMFEEVTIH QATILPKKGS TQLEVRIMPA SHSFEVSGNG
960 970 980 990 1000
NLAVSGKISL LENDALKNFH NQLADFQSQA NVTAKSGLLM EDVYQELHLR
1010 1020 1030 1040 1050
GYNYGPTFQG VLECNSEGSA GKILWNGNWV TFLDTLLHLI VLAETGRSLR
1060 1070 1080 1090 1100
LPTRIRSVYI DPVLHQEQVY QYQDNVEAFD VVVDRCLDSL KAGGVQINGL
1110 1120 1130 1140 1150
HASVAPRRQQ ERISPTLEKF SFVPYIESDC LSSSTQLHAY LEHCKGLIQK
1160 1170 1180 1190 1200
LQAKMALHGV KLVIHGLETK GAAAGSPPAQ KGLQHILTEI CRLELNGNPH
1210 1220 1230 1240 1250
SELEQIVTQE KMHLQDDPLL NGLLDSSELK TCLDVAKENT TSHRMKIVEA
1260 1270 1280 1290 1300
LAGSGRLFSR VQSILNTQPL LQLDYIATDC TPETLSDNET ELHDAGISFS
1310 1320 1330 1340 1350
QWDPSSLPSG NLTNADLAVC NCSTSVLGNT AEIISNLAAA VKEGGFVLLH
1360 1370 1380 1390 1400
TLLKEETLGE IVSFLTSPDL QQKHSFLSQA QWEELFSKAS LNLVAMKRSF
1410 1420 1430 1440 1450
FGSVIFLCRR QSPAKAPILL PVDDTHYKWV DSLKEILADS SEQPLWLTAT
1460 1470 1480 1490 1500
NCGNSGILGM VNCLRLEAEG HRIRCVFVSN LSPSSTVPAT SLSSLEMQKI
1510 1520 1530 1540 1550
IERDLVMNVY RDGKWGSFRH LPLQQAQPQE LTECAYVNVL TRGDLSSLRW
1560 1570 1580 1590 1600
IVSPLRHFQT TNPNVQLCKV YYASLNFWDI MLATGKLSPD AIPGNWTLQQ
1610 1620 1630 1640 1650
CMLGMEFSGR DLAGRRVMGL LPAKGLATVV DCDKRFLWEV PENWTLEEAA
1660 1670 1680 1690 1700
SVPVVYATAY YALVVRGGMK KGESVLIHSG SGGVGQAAIA IALSMGCRVF
1710 1720 1730 1740 1750
ATVGSAEKRE YLQARFPQLD ANSFASSRNT TFQQHILRVT NGKGVSLVLN
1760 1770 1780 1790 1800
SLAEEKLQAS LRCLAQHGRF LEIGKFDLSN NSQLGMALFL KNVAFHGILL
1810 1820 1830 1840 1850
DSIFEEGNQE WEVVSELLTK GIKDGVVKPL RTTVFGKEEV EAAFRFMAQG
1860 1870 1880 1890 1900
KHIGKVMIKI QEEEKQYPLR SEPVKLSAIS RTSCPPTKSY IITGGLGGFG
1910 1920 1930 1940 1950
LELAQWLIER GAQKLVLTSR SGIRTGYQAK CVREWKALGI QVLVSTSDVG
1960 1970 1980 1990 2000
TLEGTQLLIE EALKLGPVGG IFNLAVVLKD AMIENQTPEL FWEVNKPKYS
2010 2020 2030 2040 2050
GTLHLDWVTR KKCPDLDYFV VFSSVSCGRG NAGQSNYGFA NSAMERICEQ
2060 2070 2080 2090 2100
RHHDGLPGLA VQWGAIGDVG ILKAMGNREV VIGGTVLQQI SSCLEVLDMF
2110 2120 2130 2140 2150
LNQPHPVMSS FVLAEKVSVK SEGGSQRDLV EAVAHILGVR DVSSLNAESS
2160 2170 2180 2190 2200
LADLGLDSLM GVEVRQTLER DYDIVMTMRE IRLLTINKLR ELSSKTGTAE
2210 2220 2230 2240 2250
ELKPSQVLKT GPGEPPKLDL NNLLVNPEGP TITRLNEVQS TERPLFLVHP
2260 2270 2280 2290 2300
IEGSIAVFYT LASKLHMPCY GLQCTKAAPL DSIQSLASYY IDCMKQIQPE
2310 2320 2330 2340 2350
GPYRIAGYSF GACVAFEMCS QLQAQQNASH ALNSLFLFDG SHSFVAAYTQ
2360 2370 2380 2390 2400
SYRAKLTQGN EAALETEALC AFVQQFTGIE YNKLLEILLP LEDLEARVNA
2410 2420 2430 2440 2450
AADLITQIHK NINREALSFA AASFYHKLKA ADKYIPESKY HGNVTLMRAK
2460 2470 2480 2490 2500
THNEYEEGLG GDYRLSEVCD GKVSVHIIEG DHRTLLEGDG VESIIGIIHG
2510
SLAEPRVSVR EG
Length:2,512
Mass (Da):274,782
Last modified:January 23, 2007 - v5
Checksum:i66FDE22F5CCF603C
GO
Isoform 1 (identifier: P12276-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2349-2349: T → TQCFSFSLF

Show »
Length:2,520
Mass (Da):275,742
Checksum:iCA1DA253E4BD0956
GO

Sequence cautioni

The sequence AAA82106.1 differs from that shown. Reason: Frameshift at position 2352. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 792QL → PV in AAA48767. (PubMed:2734291)Curated
Sequence conflicti117 – 1171L → A in AAA48767. (PubMed:2734291)Curated
Sequence conflicti676 – 6761R → S in AAA48767. (PubMed:2734291)Curated
Sequence conflicti1170 – 11701K → N in AAA48767. (PubMed:2734291)Curated
Sequence conflicti1179 – 11791A → T in AAA48767. (PubMed:2734291)Curated
Sequence conflicti1192 – 11921R → H in AAA48767. (PubMed:2734291)Curated
Sequence conflicti1199 – 11991P → L in AAA48767. (PubMed:2734291)Curated
Sequence conflicti1287 – 12882DN → ND in AAA48767. (PubMed:2734291)Curated
Sequence conflicti1373 – 13731K → E in AAA48767. (PubMed:2734291)Curated
Sequence conflicti1534 – 15341C → Y in AAA48767. (PubMed:2734291)Curated
Sequence conflicti1578 – 15781W → R in AAA48767. (PubMed:2734291)Curated
Sequence conflicti1686 – 169712QAAIA…LSMGC → ASSHCHRLEHGLA in AAA48767. (PubMed:2734291)CuratedAdd
BLAST
Sequence conflicti1733 – 17331Q → E in AAA48767. (PubMed:2734291)Curated
Sequence conflicti1746 – 17461S → N in AAA48767. (PubMed:2734291)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2349 – 23491T → TQCFSFSLF in isoform 1. CuratedVSP_000149

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03860 mRNA. Translation: AAA48767.1.
J04485 mRNA. Translation: AAB46389.1.
J02839 Genomic DNA. Translation: AAA82106.1. Frameshift.
PIRiS57248. XYCHFA.
UniGeneiGga.8951.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03860 mRNA. Translation: AAA48767.1 .
J04485 mRNA. Translation: AAB46389.1 .
J02839 Genomic DNA. Translation: AAA82106.1 . Frameshift.
PIRi S57248. XYCHFA.
UniGenei Gga.8951.

3D structure databases

ProteinModelPortali P12276.
SMRi P12276. Positions 421-821, 2122-2202, 2222-2508.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9031.ENSGALP00000038133.

Chemistry

BindingDBi P12276.
ChEMBLi CHEMBL1795136.

Proteomic databases

PaxDbi P12276.
PRIDEi P12276.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG3319.
HOGENOMi HOG000019642.
HOVERGENi HBG005640.
InParanoidi P12276.
PhylomeDBi P12276.

Enzyme and pathway databases

SABIO-RK P12276.

Miscellaneous databases

NextBioi 20816121.
PROi P12276.

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.
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.
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

  1. "Amino-terminal blocking group and sequence of the animal fatty acid synthase."
    Huang W.-Y., Chirala S.S., Wakil S.J.
    Arch. Biochem. Biophys. 314:45-49(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-12.
    Strain: White leghorn.
    Tissue: Liver.
  2. "Molecular cloning and sequencing of chicken liver fatty acid synthase cDNA."
    Holzer K.P., Liu W., Hammes G.G.
    Proc. Natl. Acad. Sci. U.S.A. 86:4387-4391(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 75-1775.
    Tissue: Liver.
  3. "A novel cDNA extension procedure. Isolation of chicken fatty acid synthase cDNA clones."
    Chirala S.S., Kasturi R., Pazirandeh M., Stolow D.T., Huang W.-Y., Wakil S.J.
    J. Biol. Chem. 264:3750-3757(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1568-2512, PARTIAL PROTEIN SEQUENCE.
  4. "Molecular cloning and sequencing of DNA complementary to chicken liver fatty acid synthase mRNA."
    Yuan Z., Liu W., Hammes G.G.
    Proc. Natl. Acad. Sci. U.S.A. 85:6328-6331(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1752-2512.
  5. "Characterization of a genomic and cDNA clone coding for the thioesterase domain and 3' noncoding region of the chicken liver fatty acid synthase gene."
    Kasturi R., Chirala S.S., Pazirandeh M., Wakil S.J.
    Biochemistry 27:7778-7785(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 2202-2512.
  6. "Complete amino acid sequence of chicken liver acyl carrier protein derived from the fatty acid synthase."
    Huang W.-Y., Stoops J.K., Wakil S.J.
    Arch. Biochem. Biophys. 270:92-98(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2122-2210.
  7. "Complete amino acid sequence of the thioesterase domain of chicken liver fatty acid synthase."
    Yang C.-Y., Huang W.-Y., Chirala S.S., Wakil S.J.
    Biochemistry 27:7773-7777(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2210-2509.
    Strain: White leghorn.
  8. "Amino acid sequences of pyridoxal 5'-phosphate binding sites and fluorescence resonance energy transfer in chicken liver fatty acid synthase."
    Chang S.I., Hammes G.G.
    Biochemistry 28:3781-3788(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 668-675 AND 1699-1710.

Entry informationi

Entry nameiFAS_CHICK
AccessioniPrimary (citable) accession number: P12276
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 145 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3