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E9Q4Z2

- ACACB_MOUSE

UniProt

E9Q4Z2 - ACACB_MOUSE

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Protein

Acetyl-CoA carboxylase 2

Gene

Acacb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA By similarity. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase By similarity. Involved in inhibition of fatty acid and glucose oxidation and enhancement of fat storage (PubMed:11283375, PubMed:12920182, PubMed:15677334, PubMed:18487439, PubMed:22362781). May play a role in regulation of mitochondrial fatty acid oxidation through malonyl-CoA-dependent inhibition of carnitine palmitoyltransferase 1 (PubMed:10677481).By similarity5 Publications1 Publication

Catalytic activityi

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

Cofactori

Biotin.SAAS annotation
Binds 2 manganese ions per subunit.PROSITE-ProRule annotation

Enzyme regulationi

Activity is increased by oligomerization. Activated by citrate. Citrate and MID1IP1 promote oligomerization. Inhibited by malonyl-CoA.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi557 – 5571Manganese 1 By similarityPROSITE-ProRule annotation
Metal bindingi570 – 5701Manganese 1 By similarityPROSITE-ProRule annotation
Metal bindingi570 – 5701Manganese 2 By similarityPROSITE-ProRule annotation
Metal bindingi572 – 5721Manganese 2 By similarityPROSITE-ProRule annotation
Active sitei574 – 5741By similarity
Binding sitei1924 – 19241Coenzyme A By similarityBy similarity
Binding sitei2228 – 22281Coenzyme A By similarityBy similarity
Binding sitei2230 – 22301Coenzyme A By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi434 – 49158ATPPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. acetyl-CoA carboxylase activity Source: MGI
  2. ATP binding Source: UniProtKB-KW
  3. biotin binding Source: Ensembl
  4. biotin carboxylase activity Source: InterPro
  5. metal ion binding Source: InterPro

GO - Biological processi

  1. acetyl-CoA metabolic process Source: Ensembl
  2. fatty acid biosynthetic process Source: MGI
  3. malonyl-CoA biosynthetic process Source: UniProtKB
  4. negative regulation of fatty acid oxidation Source: UniProtKB
  5. positive regulation of heart growth Source: UniProtKB
  6. positive regulation of lipid storage Source: UniProtKB
  7. protein homotetramerization Source: Ensembl
  8. response to drug Source: Ensembl
  9. response to organic cyclic compound Source: Ensembl
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. 244.
ReactomeiREACT_189100. Defective HLCS causes multiple carboxylase deficiency.
REACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_206176. Biotin transport and metabolism.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA carboxylase 2By similarity (EC:6.4.1.2By similarity)
Alternative name(s):
ACC-betaBy similarity
Including the following 1 domains:
Biotin carboxylaseBy similarity (EC:6.3.4.14By similarity)
Gene namesi
Name:AcacbImported
Synonyms:Acc21 Publication, AccbImported
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:2140940. Acacb.

Subcellular locationi

Mitochondrion 1 Publication. Nucleus By similarity. Endomembrane system By similarity
Note: May associate with membranes.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Disruption phenotypei

Normal morphology, fertility, growth rate and lifespan but higher than normal food consumption and fatty acid oxidation rate and decreased fat content in adipose tissue and liver (PubMed:11283375). A high-fat/high-carbohydrate diet results in maintenance of normal insulin and glucose levels with less weight gain and less fat accumulation than wild-type mice (PubMed:12920182). Elevated levels of Ucp2 in adipose tissue and heart but not in skeletal muscle or liver, and elevated levels of Ucp3 in skeletal muscle but not in heart or brown adipose tissue (PubMed:12920182). Significant decrease in body weight, weight of epidydimal fat pads and levels of hepatic triglycerides under a range of dietary conditions including normal chow diet, fasting and refeeding a fat-free high-carbohydrate diet, and a high-fat/high-carbohydrate diet (PubMed:22362781). Up-regulation of lipogenic enzymes under de novo lipogenic conditions but reduced fat accumulation in liver (PubMed:22362781). Primary cultured adipocytes show increased fatty acid and glucose oxidation rates and increased lipolysis (PubMed:15677334). Reduced heart size, reduced Mlycd and malonyl-CoA levels in mutant hearts, reduced myocardial triglyceride levels, higher myocardial oleate and glucose oxidation rates, reduced levels of Ppara and reduced activation of Mtor (PubMed:18487439, PubMed:22730442). However, it has also been reported that mutants show no differences in body weight, food intake, body composition or glucose homeostasis as compared with controls fed on chow or a high-fat diet (PubMed:20368432).7 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi212 – 2121S → A: No phosphorylation by AMPK, reduced fatty acid oxidation in skeletal muscle, increased lipid deposition in skeletal muscle, and development of insulin resistance. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 2448Acetyl-CoA carboxylase 21 PublicationPRO_0000430774
Transit peptidei1 – ?Mitochondrion1 Publication

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei212 – 2121Phosphoserine; by AMPK1 Publication
Modified residuei919 – 9191N6-biotinyllysine By similarityBy similarity

Post-translational modificationi

Phosphorylated by AMPK, leading to inactivation of the enzyme. Required for the maintenance of skeletal muscle lipid and glucose homeostasis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiE9Q4Z2.
PRIDEiQ6JIZ0.

PTM databases

PhosphoSiteiQ6JIZ0.

Expressioni

Gene expression databases

ExpressionAtlasiE9Q4Z2. baseline and differential.

Interactioni

Subunit structurei

Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity.By similarity

Protein-protein interaction databases

MINTiMINT-1859452.

Structurei

3D structure databases

ProteinModelPortaliE9Q4Z2.
SMRiE9Q4Z2. Positions 227-748, 881-950, 1687-2435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini249 – 751503Biotin carboxylationSequence AnalysisAdd
BLAST
Domaini408 – 599192ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini885 – 95167Biotinyl-bindingSequence AnalysisAdd
BLAST
Domaini1799 – 2295497CarboxyltransferaseSequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.SAAS annotation
Contains 1 biotinyl-binding domain.SAAS annotation
Contains 1 carboxyltransferase domain.Sequence Analysis

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00550000074703.
HOGENOMiHOG000214115.
HOVERGENiHBG005371.
InParanoidiE9Q4Z2.
KOiK11262.
OMAiWRLRVAQ.
TreeFamiTF300061.

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.
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.
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]

Sequencei

Sequence statusi: Complete.

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

E9Q4Z2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVLLLFLTCL VFSCLTFSWL KIWGKMTDSK PLTNSKVEAN LLSSEESLSA
60 70 80 90 100
SELSGEQLQE HGDHSCLSYR GPRDASQQRN SLPSSCQRPP RNPLSSNDTW
110 120 130 140 150
PSPELQTNWT AAPGPEVPDA NGLSFPARPP SQRTVSPSRE DRKQAHIKRQ
160 170 180 190 200
LMTSFILGSL DDNSSDEDPS AGSFQNSSRK SSRASLGTLS QEAALNTSDP
210 220 230 240 250
ESHAPTMRPS MSGLHLVKRG REHKKLDLHR DFTVASPAEF VTRFGGNRVI
260 270 280 290 300
EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT PEDLKANAEY
310 320 330 340 350
IKMADQYVPV PGGPNNNNYA NVELIIDIAK RIPVQAVWAG WGHASENPKL
360 370 380 390 400
PELLCKHEIA FLGPPSEAMW ALGDKIASTI VAQTLQIPTL PWSGSGLTVE
410 420 430 440 450
WTEDSRHQGK CISVPEDVYE QGCVKDVDEG LQAAEKIGFP LMIKASEGGG
460 470 480 490 500
GKGIRKAESA EDFPMLFRQV QSEIPGSPIF LMKLAQNARH LEVQVLADQY
510 520 530 540 550
GNAVSLFGRD CSIQRRHQKI IEEAPATIAA PAVFEFMEQC AVLLAKMVGY
560 570 580 590 600
VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL PAAQLQIAMG
610 620 630 640 650
VPLHRLKDIR LLYGESPWGV TPIPFETPLS PPIARGHVIA ARITSENPDE
660 670 680 690 700
GFKPSSGTVQ ELNFRSNKNV WGYFSVAAAG GLHEFADSQF GHCFSWGENR
710 720 730 740 750
EEAISNMVVA LKELSIRGDF RTTVEYLVNL LETESFQNND IDTGWLDHLI
760 770 780 790 800
AQRVQAEKPD IMLGVVCGAL NVADAMFRTC MTEFLHSLER GQVLPADSLL
810 820 830 840 850
NIVDVELIYG GIKYALKVAR QSLTMFVLIM NGCHIEIDAH RLNDGGLLLS
860 870 880 890 900
YNGSSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP SAGKLMQYTV
910 920 930 940 950
EDGDHVEAGS SYAEMEVMKM IMTLNVQESG RVKYIKRPGV ILEAGCVVAR
960 970 980 990 1000
LELDDPSKVH AAQPFTGELP AQQTLPILGE KLHQVFHGVL ENLTNVMSGY
1010 1020 1030 1040 1050
CLPEPFFSMK LKDWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKA
1060 1070 1080 1090 1100
VRRVMAQYAS NITSVLCQFP SQQIATILDC HAATLQRKAD REVFFMNTQS
1110 1120 1130 1140 1150
IVQLVQRYRS GTRGYMKAVV LDLLRKYLNV EHHFQQAHYD KCVINLREQF
1160 1170 1180 1190 1200
KPDMTQVLDC IFSHSQVAKK NQLVTMLIDE LCGPDPTLSD ELTSILCELT
1210 1220 1230 1240 1250
QLSRSEHCKV ALRARQVLIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP
1260 1270 1280 1290 1300
ENLKKLILSE TTIFDVLPTF FYHENKVVCM ASLEVYVRRG YIAYELNSLQ
1310 1320 1330 1340 1350
HRELPDGTCV VEFQFMLPSS HPNRMAVPIS VSNPDLLRHS TELFMDSGFS
1360 1370 1380 1390 1400
PLCQRMGAMV AFRRFEEFTR NFDEVISCFA NVQTDTLLFS KACTSLYSEE
1410 1420 1430 1440 1450
DSKSLREEPI HILNVAIQCA DHMEDEALVP VFRAFVQSKK HILVDYGLRR
1460 1470 1480 1490 1500
ITFLVAQERE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL ELSRMRNFDL
1510 1520 1530 1540 1550
TAVPCANHKM HLYLGAAKVK EGLEVTDHRF FIRAIIRHSD LITKEASFEY
1560 1570 1580 1590 1600
LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPLKIEES
1610 1620 1630 1640 1650
VRDMVMRYGS RLWKLRVLQA EVKINIRQTT SDSAIPIRLF ITNESGYYLD
1660 1670 1680 1690 1700
ISLYREVTDS RSGNIMFHSF GNKQGSLHGM LINTPYVTKD LLQAKRFQAQ
1710 1720 1730 1740 1750
SLGTTYVYDF PEMFRQALFK LWGSPEKYPK DILTYTELVL DSQGQLVEMN
1760 1770 1780 1790 1800
RLPGCNEVGM VAFKMRFKTP EYPEGRDAVV IGNDITFQIG SFGIGEDFLY
1810 1820 1830 1840 1850
LRASEMARTE GIPQIYLAAN SGARMGLAEE IKQIFQVAWV DPEDPHKGFR
1860 1870 1880 1890 1900
YLYLTPQDYT QISSQNSVHC KHIEDEGESR YVIVDVIGKD ANLGVENLRG
1910 1920 1930 1940 1950
SGMIAGEASL AYEKTVTISM VTCRALGIGA YLVRLGQRVI QVENSHIILT
1960 1970 1980 1990 2000
GAGALNKVLG REVYTSNNQL GGVQIMHTNG VSHVTVPDDF EGVCTILEWL
2010 2020 2030 2040 2050
SFIPKDNRSP VPITTPSDPI DREIEFTPTK APYDPRWMLA GRPHPTLKGT
2060 2070 2080 2090 2100
WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE TRTVEVAVPA
2110 2120 2130 2140 2150
DPANLDSEAK IIQQAGQVWF PDSAYKTAQV IRDFNKERLP LMIFANWRGF
2160 2170 2180 2190 2200
SGGMKDMYEQ MLKFGAYIVD GLRLYEQPIL IYIPPCAELR GGSWVVLDST
2210 2220 2230 2240 2250
INPLCIEMYA DKESRGGVLE PEGTVEIKFR KKDLVKTIRR IDPVCKKLVG
2260 2270 2280 2290 2300
QLGKAQLPDK DRKELEGQLK AREELLLPIY HQVAVQFADL HDTPGHMLEK
2310 2320 2330 2340 2350
GIISDVLEWK TARTFFYWRL RRLLLEAQVK QEILRASPEL NHEHTQSMLR
2360 2370 2380 2390 2400
RWFVETEGAV KAYLWDSNQV VVQWLEQHWS AKDGLRSTIR ENINYLKRDS
2410 2420 2430 2440
VLKTIQSLVQ EHPEVIMDCV AYLSQHLTPA ERIQVAQLLS TTESPASS
Length:2,448
Mass (Da):275,750
Last modified:April 5, 2011 - v1
Checksum:i6CD686C7AF012A5E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241S → P in AAS13686. 1 PublicationCurated
Sequence conflicti534 – 5341F → S in AAS13686. 1 PublicationCurated
Sequence conflicti562 – 5621Q → R in AAS13686. 1 PublicationCurated
Sequence conflicti1315 – 13151F → S in AAS13686. 1 PublicationCurated
Sequence conflicti1402 – 14021S → N in AAS13686. 1 PublicationCurated
Sequence conflicti2341 – 23411N → S in AAS13686. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY451394 mRNA. Translation: AAS13686.1.
AC122282 Genomic DNA. No translation available.
RefSeqiNP_598665.2. NM_133904.2.
XP_006530176.1. XM_006530113.1.
UniGeneiMm.81793.

Genome annotation databases

EnsembliENSMUST00000031583; ENSMUSP00000031583; ENSMUSG00000042010.
ENSMUST00000102582; ENSMUSP00000099642; ENSMUSG00000042010.
GeneIDi100705.
KEGGimmu:100705.
UCSCiuc008yzi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY451394 mRNA. Translation: AAS13686.1 .
AC122282 Genomic DNA. No translation available.
RefSeqi NP_598665.2. NM_133904.2.
XP_006530176.1. XM_006530113.1.
UniGenei Mm.81793.

3D structure databases

ProteinModelPortali E9Q4Z2.
SMRi E9Q4Z2. Positions 227-748, 881-950, 1687-2435.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1859452.

PTM databases

PhosphoSitei Q6JIZ0.

Proteomic databases

MaxQBi E9Q4Z2.
PRIDEi Q6JIZ0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031583 ; ENSMUSP00000031583 ; ENSMUSG00000042010 .
ENSMUST00000102582 ; ENSMUSP00000099642 ; ENSMUSG00000042010 .
GeneIDi 100705.
KEGGi mmu:100705.
UCSCi uc008yzi.2. mouse.

Organism-specific databases

CTDi 32.
MGIi MGI:2140940. Acacb.

Phylogenomic databases

GeneTreei ENSGT00550000074703.
HOGENOMi HOG000214115.
HOVERGENi HBG005371.
InParanoidi E9Q4Z2.
KOi K11262.
OMAi WRLRVAQ.
TreeFami TF300061.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .
BRENDAi 6.4.1.2. 244.
Reactomei REACT_189100. Defective HLCS causes multiple carboxylase deficiency.
REACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_206176. Biotin transport and metabolism.

Miscellaneous databases

ChiTaRSi ACACB. mouse.
NextBioi 354598.
PROi E9Q4Z2.
SOURCEi Search...

Gene expression databases

ExpressionAtlasi E9Q4Z2. baseline and differential.

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.
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.
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. "Alternative splicing in the mouse acetyl-CoA carboxylase 2 (ACC2) gene."
    Mao J., Wakil S.J.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6JImported.
    Tissue: HeartImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6JImported.
  3. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  4. "Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2."
    Abu-Elheiga L., Matzuk M.M., Abo-Hashema K.A., Wakil S.J.
    Science 291:2613-2616(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. "Acetyl-CoA carboxylase 2 mutant mice are protected against obesity and diabetes induced by high-fat/high-carbohydrate diets."
    Abu-Elheiga L., Oh W., Kordari P., Wakil S.J.
    Proc. Natl. Acad. Sci. U.S.A. 100:10207-10212(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Glucose and fat metabolism in adipose tissue of acetyl-CoA carboxylase 2 knockout mice."
    Oh W., Abu-Elheiga L., Kordari P., Gu Z., Shaikenov T., Chirala S.S., Wakil S.J.
    Proc. Natl. Acad. Sci. U.S.A. 102:1384-1389(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. "Gene knockout of Acc2 has little effect on body weight, fat mass, or food intake."
    Olson D.P., Pulinilkunnil T., Cline G.W., Shulman G.I., Lowell B.B.
    Proc. Natl. Acad. Sci. U.S.A. 107:7598-7603(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. "Cardiac-specific deletion of acetyl CoA carboxylase 2 prevents metabolic remodeling during pressure-overload hypertrophy."
    Kolwicz S.C. Jr., Olson D.P., Marney L.C., Garcia-Menendez L., Synovec R.E., Tian R.
    Circ. Res. 111:728-738(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  11. "Acetyl-CoA carboxylase 2-/- mutant mice are protected against fatty liver under high-fat, high-carbohydrate dietary and de novo lipogenic conditions."
    Abu-Elheiga L., Wu H., Gu Z., Bressler R., Wakil S.J.
    J. Biol. Chem. 287:12578-12588(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  12. Cited for: PHOSPHORYLATION AT SER-212, MUTAGENESIS OF SER-212.

Entry informationi

Entry nameiACACB_MOUSE
AccessioniPrimary (citable) accession number: E9Q4Z2
Secondary accession number(s): Q6JIZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: April 5, 2011
Last modified: October 29, 2014
This is version 33 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, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3