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P12276

- FAS_CHICK

UniProt

P12276 - FAS_CHICK

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Protein

Fatty acid synthase

Gene
FASN, FAS
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 activity By similarity
Active sitei580 – 5801For acyl/malonyl transferase activity By similarity
Active sitei878 – 8781For beta-hydroxyacyl dehydratase activity By similarity
Active sitei2309 – 23091For thioesterase activity By similarity
Active sitei2482 – 24821For thioesterase activity By similarity

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 groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
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)lysine By similarity
Modified residuei2158 – 21581O-(pantetheine 4'-phosphoryl)serine By similarity

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2125 – 218157Acyl carrierAdd
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

Phylogenomic databases

eggNOGiCOG3319.
HOGENOMiHOG000019642.
HOVERGENiHBG005640.
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

MEDVVIAGIA GKLPESENLQ EFWENLLNGV DMVTEDDRRW KPGIYGLPKR     50
NGKLKDIKKF DASFFGVHPK QAHTMDPQLR LLLEVSYEAI LDGGINPTAL 100
RGTDTGVWVG ASGSEALEAL SQDPEELLGY SMTGCQRAML ANRISYFYDF 150
TGPSLTIDTA CSSSLMALEN AYKAIRHGQC SAALVGGVNI LLKPNTSVQF 200
MKLGMLSPDG ACKAFDVSGN GYCRSEAVVV VLLTKKSMAK RVYATIVNAG 250
SNTDGFKEQG VTFPSGEMQQ QLVGSLYREC GIKPGDVEYV EAHGTGTKVG 300
DPQEVNGIVN VFCQCEREPL LIGSTKSNMG HPEPASGLAA LAKVILSLEH 350
GLWAPNLHFN DPNPDIPALH DGSLKVVCKP TPVKGGLVSI NSFGFGGSNA 400
HVILRPNEKK CQPQETCNLP RLVQVCGRTQ EAVEILIEES RKHGGCSPFL 450
SLLSDISAVP VSSMPYRGYT LVGTESDITE IQQVQASGRP LWYICSGMGT 500
QWKGMGLSLM KLDLFRQSIL RSDEALKSTG LKVSDLLLNA DENTFDDTVH 550
AFVGLAAIQI AQIDVLKAAG LQPDGILGHS VGELACGYAD NSLSHEEAVL 600
AAYWRGRCVK EAKLPPGGMA AVGLTWEECK QRCPPNVVPA CHNSEDTVTV 650
SGPLDSVSEF VTKLKKDGVF AKEVRRAGVA FHSYYMASIA PALLSALKKV 700
IPHPKPRSAR WISTSIPESQ WQSDLARNSS AEYHVNNLVN PVLFHEGLKH 750
IPENAVVVEI APHALLQAIL RRTLKPTCTI LPLMKKDHKN NLEFFLTQTG 800
KIHLTGINVL GNNLFPPVEY PVPVGTPLIS PYIKWDHSQD WDVPKAEDFP 850
SGSKGSASAS VYNIDVSPDS PDHYLVGHCI DGRVLYPATG YLVLAWRTLA 900
RSLGMVMEQT AVMFEEVTIH QATILPKKGS TQLEVRIMPA SHSFEVSGNG 950
NLAVSGKISL LENDALKNFH NQLADFQSQA NVTAKSGLLM EDVYQELHLR 1000
GYNYGPTFQG VLECNSEGSA GKILWNGNWV TFLDTLLHLI VLAETGRSLR 1050
LPTRIRSVYI DPVLHQEQVY QYQDNVEAFD VVVDRCLDSL KAGGVQINGL 1100
HASVAPRRQQ ERISPTLEKF SFVPYIESDC LSSSTQLHAY LEHCKGLIQK 1150
LQAKMALHGV KLVIHGLETK GAAAGSPPAQ KGLQHILTEI CRLELNGNPH 1200
SELEQIVTQE KMHLQDDPLL NGLLDSSELK TCLDVAKENT TSHRMKIVEA 1250
LAGSGRLFSR VQSILNTQPL LQLDYIATDC TPETLSDNET ELHDAGISFS 1300
QWDPSSLPSG NLTNADLAVC NCSTSVLGNT AEIISNLAAA VKEGGFVLLH 1350
TLLKEETLGE IVSFLTSPDL QQKHSFLSQA QWEELFSKAS LNLVAMKRSF 1400
FGSVIFLCRR QSPAKAPILL PVDDTHYKWV DSLKEILADS SEQPLWLTAT 1450
NCGNSGILGM VNCLRLEAEG HRIRCVFVSN LSPSSTVPAT SLSSLEMQKI 1500
IERDLVMNVY RDGKWGSFRH LPLQQAQPQE LTECAYVNVL TRGDLSSLRW 1550
IVSPLRHFQT TNPNVQLCKV YYASLNFWDI MLATGKLSPD AIPGNWTLQQ 1600
CMLGMEFSGR DLAGRRVMGL LPAKGLATVV DCDKRFLWEV PENWTLEEAA 1650
SVPVVYATAY YALVVRGGMK KGESVLIHSG SGGVGQAAIA IALSMGCRVF 1700
ATVGSAEKRE YLQARFPQLD ANSFASSRNT TFQQHILRVT NGKGVSLVLN 1750
SLAEEKLQAS LRCLAQHGRF LEIGKFDLSN NSQLGMALFL KNVAFHGILL 1800
DSIFEEGNQE WEVVSELLTK GIKDGVVKPL RTTVFGKEEV EAAFRFMAQG 1850
KHIGKVMIKI QEEEKQYPLR SEPVKLSAIS RTSCPPTKSY IITGGLGGFG 1900
LELAQWLIER GAQKLVLTSR SGIRTGYQAK CVREWKALGI QVLVSTSDVG 1950
TLEGTQLLIE EALKLGPVGG IFNLAVVLKD AMIENQTPEL FWEVNKPKYS 2000
GTLHLDWVTR KKCPDLDYFV VFSSVSCGRG NAGQSNYGFA NSAMERICEQ 2050
RHHDGLPGLA VQWGAIGDVG ILKAMGNREV VIGGTVLQQI SSCLEVLDMF 2100
LNQPHPVMSS FVLAEKVSVK SEGGSQRDLV EAVAHILGVR DVSSLNAESS 2150
LADLGLDSLM GVEVRQTLER DYDIVMTMRE IRLLTINKLR ELSSKTGTAE 2200
ELKPSQVLKT GPGEPPKLDL NNLLVNPEGP TITRLNEVQS TERPLFLVHP 2250
IEGSIAVFYT LASKLHMPCY GLQCTKAAPL DSIQSLASYY IDCMKQIQPE 2300
GPYRIAGYSF GACVAFEMCS QLQAQQNASH ALNSLFLFDG SHSFVAAYTQ 2350
SYRAKLTQGN EAALETEALC AFVQQFTGIE YNKLLEILLP LEDLEARVNA 2400
AADLITQIHK NINREALSFA AASFYHKLKA ADKYIPESKY HGNVTLMRAK 2450
THNEYEEGLG GDYRLSEVCD GKVSVHIIEG DHRTLLEGDG VESIIGIIHG 2500
SLAEPRVSVR EG 2512
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2349 – 23491T → TQCFSFSLF in isoform 1. VSP_000149

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 792QL → PV in AAA48767. 1 Publication
Sequence conflicti117 – 1171L → A in AAA48767. 1 Publication
Sequence conflicti676 – 6761R → S in AAA48767. 1 Publication
Sequence conflicti1170 – 11701K → N in AAA48767. 1 Publication
Sequence conflicti1179 – 11791A → T in AAA48767. 1 Publication
Sequence conflicti1192 – 11921R → H in AAA48767. 1 Publication
Sequence conflicti1199 – 11991P → L in AAA48767. 1 Publication
Sequence conflicti1287 – 12882DN → ND in AAA48767. 1 Publication
Sequence conflicti1373 – 13731K → E in AAA48767. 1 Publication
Sequence conflicti1534 – 15341C → Y in AAA48767. 1 Publication
Sequence conflicti1578 – 15781W → R in AAA48767. 1 Publication
Sequence conflicti1686 – 169712QAAIA…LSMGC → ASSHCHRLEHGLA in AAA48767. 1 PublicationAdd
BLAST
Sequence conflicti1733 – 17331Q → E in AAA48767. 1 Publication
Sequence conflicti1746 – 17461S → N in AAA48767. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
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: September 3, 2014
This is version 142 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

Similar proteinsi