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P11497

- ACACA_RAT

UniProt

P11497 - ACACA_RAT

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Protein

Acetyl-CoA carboxylase 1

Gene

Acaca

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

Protein has several cofactor binding sites:
  • biotinNote: Biotin.
  • Mn2+By similarityNote: 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.By similarity

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi314 – 3196ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. acetyl-CoA carboxylase activity Source: RGD
  2. ATP binding 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 1PRO_0000146765Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei5 – 51PhosphoserineBy similarity
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei25 – 251PhosphoserineBy similarity
Modified residuei29 – 291PhosphoserineBy similarity
Modified residuei52 – 521PhosphoserineBy similarity
Modified residuei77 – 771Phosphoserine1 Publication
Modified residuei79 – 791Phosphoserine; by AMPK2 Publications
Modified residuei785 – 7851N6-biotinyllysine1 PublicationPROSITE-ProRule annotation
Modified residuei1200 – 12001Phosphoserine; by AMPK; in vitro3 Publications
Modified residuei1215 – 12151Phosphoserine; by AMPK; in vitro1 Publication
Modified residuei1262 – 12621PhosphoserineBy similarity
Modified residuei1333 – 13331N6-acetyllysineBy 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).By similarity

Protein-protein interaction databases

BioGridi248868. 1 interaction.
STRINGi10116.ENSRNOP00000050703.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini116 – 617502Biotin carboxylationAdd
BLAST
Domaini274 – 465192ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini744 – 81875Biotinyl-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1697 – 2193497CarboxyltransferaseAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.Curated
Contains 1 biotinyl-binding domain.CuratedPROSITE-ProRule annotation
Contains 1 carboxyltransferase domain.Curated

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

        10         20         30         40         50
MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP
60 70 80 90 100
ASVSSDTLSD LGISALQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT
110 120 130 140 150
VASPAEFVTR FGGNKVIEKV LIANNGIAAV KCMRSIRRWS YEMFRNERAI
160 170 180 190 200
RFVVMVTPED LKANAEYIKM ADHYVPVPGG ANNNNYANVE LILDIAKRIP
210 220 230 240 250
VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG DKIASSIVAQ
260 270 280 290 300
TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA
310 320 330 340 350
EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL
360 370 380 390 400
AKQSRHLEVQ ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF
410 420 430 440 450
EHMEQCAVKL AKMVGYVSAG TVEYLYSQDG SFYFLELNPR LQVEHPCTEM
460 470 480 490 500
VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG VSPWGDAPID FENSAHVPCP
510 520 530 540 550
RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF SVAAAGGLHE
560 570 580 590 600
FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE
610 620 630 640 650
SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VNLRNSISNF
660 670 680 690 700
LHSLERGQVL PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC
710 720 730 740 750
VEVDVHRLSD GGLLLSYDGS SYTTYMKEEV DRYRITIGNK TCVFEKENDP
760 770 780 790 800
SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE IEVMKMVMTL TAVESGCIHY
810 820 830 840 850
VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS TALRGEKLHR
860 870 880 890 900
VFHYVLDNLV NVMNGYCLPD PFFSSKVKDW VERLMKTLRD PSLPLLELQD
910 920 930 940 950
IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT
960 970 980 990 1000
LNRKSEREVF FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF
1010 1020 1030 1040 1050
QNGHYDKCVF ALREENKSDM NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR
1060 1070 1080 1090 1100
DPTLTDELLN ILTELTQLSK TTNAKVALRA RQVLIASHLP SYDVRHNQVE
1110 1120 1130 1140 1150
SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS NQVVRMAALE
1160 1170 1180 1190 1200
VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS
1210 1220 1230 1240 1250
FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE
1260 1270 1280 1290 1300
VMGCFCDSPP QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED
1310 1320 1330 1340 1350
DRLAAMFREF TQQNKATLVE HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE
1360 1370 1380 1390 1400
FPKFFTFRAR DKFEEDRIYR HLEPALAFQL ELNRMRNFDL TAIPCANHKM
1410 1420 1430 1440 1450
HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY LQNEGERLLL
1460 1470 1480 1490 1500
EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS
1510 1520 1530 1540 1550
RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS
1560 1570 1580 1590 1600
RTAQIMFQAY GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI
1610 1620 1630 1640 1650
PEMFRQSLIK LWESMSTQAF LPSPPLPSDI LTYTELVLDD QGQLVHMNRL
1660 1670 1680 1690 1700
PGGNEIGMVA WKMSLKSPEY PDGRDVIVIG NDITYRIGSF GPQEDLLFLR
1710 1720 1730 1740 1750
ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDS EDPYKGYKYL
1760 1770 1780 1790 1800
YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG
1810 1820 1830 1840 1850
MIAGESSLAY DEIITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA
1860 1870 1880 1890 1900
GALNKVLGRE VYTSNNQLGG IQIMHNNGVT HCTVCDDFEG VFTVLHWLSY
1910 1920 1930 1940 1950
MPKNVHSSVP LLNSKDPIDR IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL
1960 1970 1980 1990 2000
SGFFDYGSFS EIMQPWAQTV VVGRARLGGI PVGVVAVETR TVELSVPADP
2010 2020 2030 2040 2050
ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM VFANWRGFSG
2060 2070 2080 2090 2100
GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN
2110 2120 2130 2140 2150
PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL
2160 2170 2180 2190 2200
GTPELSPTER KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV
2210 2220 2230 2240 2250
INDILDWKTS RTFFYWRLRR LLLEDLVKKK IHSANPELTD GQIQAMLRRW
2260 2270 2280 2290 2300
FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE DGVRSVIEEN IKYISRDYVL
2310 2320 2330 2340
KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM DSPST
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. 1 PublicationVSP_011753

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 147 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