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P11497

- ACACA_RAT

UniProt

P11497 - ACACA_RAT

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Protein
Acetyl-CoA carboxylase 1
Gene
Acaca, Acac
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

Cofactori

Biotin.
Binds 2 manganese ions per subunit By similarity.

Enzyme regulationi

Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization By similarity. Activity is increased by phosphorylation.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi423 – 4231Manganese 1 By similarity
Metal bindingi436 – 4361Manganese 1 By similarity
Metal bindingi436 – 4361Manganese 2 By similarity
Metal bindingi438 – 4381Manganese 2 By similarity
Active sitei440 – 4401 By similarity
Binding sitei1822 – 18221Coenzyme A By similarity
Binding sitei2126 – 21261Coenzyme A By similarity
Binding sitei2128 – 21281Coenzyme A By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi314 – 3196ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: RGD
  2. acetyl-CoA carboxylase activity Source: RGD
  3. biotin binding Source: RGD
  4. biotin carboxylase activity Source: UniProtKB-EC
  5. kinase binding Source: RGD
  6. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. acetyl-CoA metabolic process Source: RGD
  2. fatty acid biosynthetic process Source: RGD
  3. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
  4. protein homotetramerization Source: UniProtKB
  5. response to drug Source: RGD
  6. response to organic cyclic compound Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.4.1.2. 5301.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA carboxylase 1 (EC:6.4.1.2)
Short name:
ACC1
Alternative name(s):
ACC-alpha
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.14)
Gene namesi
Name:Acaca
Synonyms:Acac
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621248. Acaca.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23452345Acetyl-CoA carboxylase 1
PRO_0000146765Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei5 – 51Phosphoserine By similarity
Modified residuei23 – 231Phosphoserine By similarity
Modified residuei25 – 251Phosphoserine By similarity
Modified residuei29 – 291Phosphoserine By similarity
Modified residuei52 – 521Phosphoserine By similarity
Modified residuei77 – 771Phosphoserine1 Publication
Modified residuei79 – 791Phosphoserine; by AMPK2 Publications
Modified residuei785 – 7851N6-biotinyllysine
Modified residuei1200 – 12001Phosphoserine; by AMPK; in vitro3 Publications
Modified residuei1215 – 12151Phosphoserine; by AMPK; in vitro1 Publication
Modified residuei1262 – 12621Phosphoserine By similarity
Modified residuei1333 – 13331N6-acetyllysine By similarity

Post-translational modificationi

The N-terminus is blocked.
Phosphorylation on Ser-1262 is required for interaction with BRCA1 By similarity.
Phosphorylation at Ser-79 by AMPK inactivates enzyme activity. Phosphorylated in vitro at Ser-1200 and Ser-1215 by AMPK; the relevance of phosphorylation of these sites in vivo is however unclear.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP11497.
PRIDEiP11497.

PTM databases

PhosphoSiteiP11497.

Expressioni

Gene expression databases

GenevestigatoriP11497.

Interactioni

Subunit structurei

Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts in its inactive phosphorylated form with the BRCT domains of BRCA1 which prevents ACACA dephosphorylation and inhibits lipid synthesis. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity By similarity.

Protein-protein interaction databases

BioGridi248868. 1 interaction.
STRINGi10116.ENSRNOP00000050703.

Structurei

3D structure databases

ProteinModelPortaliP11497.
SMRiP11497. Positions 96-615, 741-833, 1791-2118.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini116 – 617502Biotin carboxylation
Add
BLAST
Domaini274 – 465192ATP-grasp
Add
BLAST
Domaini751 – 81767Biotinyl-binding
Add
BLAST
Domaini1697 – 2193497Carboxyltransferase
Add
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.

Phylogenomic databases

eggNOGiCOG0511.
HOGENOMiHOG000214115.
HOVERGENiHBG005371.
InParanoidiP11497.
KOiK11262.
PhylomeDBiP11497.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
3.90.226.10. 3 hits.
InterProiIPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
IPR000022. Carboxyl_trans.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF08326. ACC_central. 1 hit.
PF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52096. SSF52096. 2 hits.
SSF52440. SSF52440. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P11497-1) [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

MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP     50
ASVSSDTLSD LGISALQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT 100
VASPAEFVTR FGGNKVIEKV LIANNGIAAV KCMRSIRRWS YEMFRNERAI 150
RFVVMVTPED LKANAEYIKM ADHYVPVPGG ANNNNYANVE LILDIAKRIP 200
VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG DKIASSIVAQ 250
TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA 300
EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL 350
AKQSRHLEVQ ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF 400
EHMEQCAVKL AKMVGYVSAG TVEYLYSQDG SFYFLELNPR LQVEHPCTEM 450
VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG VSPWGDAPID FENSAHVPCP 500
RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF SVAAAGGLHE 550
FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE 600
SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VNLRNSISNF 650
LHSLERGQVL PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC 700
VEVDVHRLSD GGLLLSYDGS SYTTYMKEEV DRYRITIGNK TCVFEKENDP 750
SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE IEVMKMVMTL TAVESGCIHY 800
VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS TALRGEKLHR 850
VFHYVLDNLV NVMNGYCLPD PFFSSKVKDW VERLMKTLRD PSLPLLELQD 900
IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT 950
LNRKSEREVF FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF 1000
QNGHYDKCVF ALREENKSDM NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR 1050
DPTLTDELLN ILTELTQLSK TTNAKVALRA RQVLIASHLP SYDVRHNQVE 1100
SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS NQVVRMAALE 1150
VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS 1200
FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE 1250
VMGCFCDSPP QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED 1300
DRLAAMFREF TQQNKATLVE HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE 1350
FPKFFTFRAR DKFEEDRIYR HLEPALAFQL ELNRMRNFDL TAIPCANHKM 1400
HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY LQNEGERLLL 1450
EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS 1500
RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS 1550
RTAQIMFQAY GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI 1600
PEMFRQSLIK LWESMSTQAF LPSPPLPSDI LTYTELVLDD QGQLVHMNRL 1650
PGGNEIGMVA WKMSLKSPEY PDGRDVIVIG NDITYRIGSF GPQEDLLFLR 1700
ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDS EDPYKGYKYL 1750
YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG 1800
MIAGESSLAY DEIITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA 1850
GALNKVLGRE VYTSNNQLGG IQIMHNNGVT HCTVCDDFEG VFTVLHWLSY 1900
MPKNVHSSVP LLNSKDPIDR IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL 1950
SGFFDYGSFS EIMQPWAQTV VVGRARLGGI PVGVVAVETR TVELSVPADP 2000
ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM VFANWRGFSG 2050
GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN 2100
PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL 2150
GTPELSPTER KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV 2200
INDILDWKTS RTFFYWRLRR LLLEDLVKKK IHSANPELTD GQIQAMLRRW 2250
FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE DGVRSVIEEN IKYISRDYVL 2300
KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM DSPST 2345
Length:2,345
Mass (Da):265,194
Last modified:October 1, 1989 - v1
Checksum:i78E9CF9ADE1E8771
GO
Isoform 2 (identifier: P11497-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1189-1196: Missing.

Show »
Length:2,337
Mass (Da):264,328
Checksum:i9590EEFFE39D73CD
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1189 – 11968Missing in isoform 2.
VSP_011753

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03808 mRNA. Translation: AAA40653.1.
M26731 Genomic DNA. Translation: AAA40652.1.
EF121986 mRNA. Translation: ABL63425.1.
EF121987 mRNA. Translation: ABL63426.1.
M26195 mRNA. Translation: AAA40654.1.
M26196 mRNA. Translation: AAA40655.1.
M26197 mRNA. Translation: AAA40656.1.
M55315 mRNA. No translation available.
PIRiA35578.
RefSeqiNP_071529.1. NM_022193.1. [P11497-1]
UniGeneiRn.163753.
Rn.217177.
Rn.44372.

Genome annotation databases

GeneIDi60581.
KEGGirno:60581.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03808 mRNA. Translation: AAA40653.1 .
M26731 Genomic DNA. Translation: AAA40652.1 .
EF121986 mRNA. Translation: ABL63425.1 .
EF121987 mRNA. Translation: ABL63426.1 .
M26195 mRNA. Translation: AAA40654.1 .
M26196 mRNA. Translation: AAA40655.1 .
M26197 mRNA. Translation: AAA40656.1 .
M55315 mRNA. No translation available.
PIRi A35578.
RefSeqi NP_071529.1. NM_022193.1. [P11497-1 ]
UniGenei Rn.163753.
Rn.217177.
Rn.44372.

3D structure databases

ProteinModelPortali P11497.
SMRi P11497. Positions 96-615, 741-833, 1791-2118.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248868. 1 interaction.
STRINGi 10116.ENSRNOP00000050703.

Chemistry

BindingDBi P11497.
ChEMBLi CHEMBL2397.

PTM databases

PhosphoSitei P11497.

Proteomic databases

PaxDbi P11497.
PRIDEi P11497.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 60581.
KEGGi rno:60581.

Organism-specific databases

CTDi 31.
RGDi 621248. Acaca.

Phylogenomic databases

eggNOGi COG0511.
HOGENOMi HOG000214115.
HOVERGENi HBG005371.
InParanoidi P11497.
KOi K11262.
PhylomeDBi P11497.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .
BRENDAi 6.4.1.2. 5301.

Miscellaneous databases

NextBioi 612298.
PROi P11497.

Gene expression databases

Genevestigatori P11497.

Family and domain databases

Gene3Di 3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
3.90.226.10. 3 hits.
InterProi IPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005481. CarbamoylP_synth_lsu_N.
IPR000022. Carboxyl_trans.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR029045. ClpP/crotonase-like_dom.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF08326. ACC_central. 1 hit.
PF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view ]
SMARTi SM00878. Biotin_carb_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52096. SSF52096. 2 hits.
SSF52440. SSF52440. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the coding sequence and primary amino acid sequence of acetyl-coenzyme A carboxylase."
    Lopez-Casillas F., Bai D.-H., Luo X., Kong I.-S., Hermodson M.A., Kim K.-H.
    Proc. Natl. Acad. Sci. U.S.A. 85:5784-5788(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Structural features of the acetyl-CoA carboxylase gene: mechanisms for the generation of mRNAs with 5' end heterogeneity."
    Luo X.N., Park K., Lopez-Casillas F., Kim K.-H.
    Proc. Natl. Acad. Sci. U.S.A. 86:4042-4046(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Fine-mapping and comprehensive transcript analysis reveals nonsynonymous variants within a novel 1.17 Mb blood pressure QTL region on rat chromosome 10."
    Saad Y., Garrett M.R., Manickavasagam E., Yerga-Woolwine S., Farms P., Radecki T., Joe B.
    Genomics 89:343-353(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: Dahl salt-sensitive and Lewis.
  4. "Heterogeneity at the 5' end of rat acetyl-coenzyme A carboxylase mRNA. Lipogenic conditions enhance synthesis of a unique mRNA in liver."
    Lopez-Casillas F., Kim K.-H.
    J. Biol. Chem. 264:7176-7184(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-33.
  5. "Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase."
    Munday M.R., Campbell D.G., Carling D., Hardie D.G.
    Eur. J. Biochem. 175:331-338(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 76-85 AND 1198-1201, PHOSPHORYLATION AT SER-77; SER-79 AND SER-1200.
  6. "Acetyl-CoA carboxylase mRNA species with or without inhibitory coding sequence for Ser-1200 phosphorylation."
    Kong I.-S., Lopez-Casillas F., Kim K.-H.
    J. Biol. Chem. 265:13695-13701(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1167-1200 (ISOFORMS 1 AND 2), PHOSPHORYLATION AT SER-1200.
  7. "Unique structural features and differential phosphorylation of the 280-kDa component (isozyme) of rat liver acetyl-CoA carboxylase."
    Winz R., Hess D., Aebersold R., Brownsey R.W.
    J. Biol. Chem. 269:14438-14445(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Wistar.
    Tissue: Liver.
  8. "Analysis of the biotin-binding site on acetyl-CoA carboxylase from rat."
    Bai D.-H., Moon T.-W., Lopez-Casillas F., Andrews P.C., Kim K.-H.
    Eur. J. Biochem. 182:239-245(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOTINYLATION AT LYS-785.
  9. "Diurnal rhythm of phosphorylation of rat liver acetyl-CoA carboxylase by the AMP-activated protein kinase, demonstrated using freeze-clamping. Effects of high fat diets."
    Davies S.P., Carling D., Munday M.R., Hardie D.G.
    Eur. J. Biochem. 203:615-623(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-79; SER-1200 AND SER-1215.
  10. "Phosphorylation of rat muscle acetyl-CoA carboxylase by AMP-activated protein kinase and protein kinase A."
    Winder W.W., Wilson H.A., Hardie D.G., Rasmussen B.B., Hutber C.A., Call G.B., Clayton R.D., Conley L.M., Yoon S., Zhou B.
    J. Appl. Physiol. 82:219-225(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY AMPK.
  11. "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."
    Moser K., White F.M.
    J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACACA_RAT
AccessioniPrimary (citable) accession number: P11497
Secondary accession number(s): A1EC79, P97902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: September 3, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi