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Q5SWU9

- ACACA_MOUSE

UniProt

Q5SWU9 - ACACA_MOUSE

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Protein

Acetyl-CoA carboxylase 1

Gene
Acaca, Acac, Gm738
Organism
Mus musculus (Mouse)
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 By similarity.By similarity1 Publication

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.By similarity1 Publication
ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].1 Publication

Cofactori

Biotin By similarity.
Binds 2 manganese ions per subunit By similarity.

Enzyme regulationi

By phosphorylation By similarity. Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization.By similarity1 Publication

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 similarityBy similarity
Binding sitei2126 – 21261Coenzyme A By similarityBy similarity
Binding sitei2128 – 21281Coenzyme A By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi300 – 35758ATP Reviewed predictionAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. acetyl-CoA metabolic process Source: UniProtKB
  2. fatty acid biosynthetic process Source: UniProtKB
  3. lipid homeostasis Source: MGI
  4. lipid metabolic process Source: MGI
  5. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
  6. multicellular organismal protein metabolic process Source: MGI
  7. protein homotetramerization Source: UniProtKB
  8. tissue homeostasis Source: MGI
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

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 1 (EC:6.4.1.2)
Short name:
ACC1
Alternative name(s):
ACC-alpha
Acetyl-CoA carboxylase 265
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.14)
Gene namesi
Name:Acaca
Synonyms:Acac, Gm738
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:108451. Acaca.

Subcellular locationi

Cytoplasm 2 Publications

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23452345Acetyl-CoA carboxylase 1PRO_0000258040Add
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 – 251Phosphoserine1 Publication
Modified residuei29 – 291PhosphoserineBy similarity2 Publications
Modified residuei52 – 521Phosphoserine By similarity
Modified residuei77 – 771Phosphoserine By similarityBy similarity
Modified residuei79 – 791Phosphoserine; alternateBy similarity3 Publications
Modified residuei79 – 791Phosphoserine; by AMPK; alternate Inferred
Modified residuei785 – 7851N6-biotinyllysine By similarity
Modified residuei1200 – 12001Phosphoserine By similarityBy similarity
Modified residuei1215 – 12151Phosphoserine By similarity
Modified residuei1262 – 12621Phosphoserine By similarityBy similarity
Modified residuei1333 – 13331N6-acetyllysine By similarity

Post-translational modificationi

Phosphorylation on Ser-1262 is required for interaction with BRCA1 By similarity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ5SWU9.
PaxDbiQ5SWU9.
PRIDEiQ5SWU9.

PTM databases

PhosphoSiteiQ5SWU9.

Expressioni

Gene expression databases

ArrayExpressiQ5SWU9.
BgeeiQ5SWU9.
CleanExiMM_ACACA.
GenevestigatoriQ5SWU9.

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.2 Publications

Protein-protein interaction databases

BioGridi223322. 2 interactions.
DIPiDIP-32276N.
IntActiQ5SWU9. 8 interactions.
MINTiMINT-4091386.

Structurei

3D structure databases

ProteinModelPortaliQ5SWU9.
SMRiQ5SWU9. Positions 101-615, 747-816, 1580-2337.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini116 – 617502Biotin carboxylationAdd
BLAST
Domaini274 – 465192ATP-graspAdd
BLAST
Domaini751 – 81767Biotinyl-bindingAdd
BLAST
Domaini1697 – 2193497CarboxyltransferaseAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.

Phylogenomic databases

eggNOGiCOG0511.
GeneTreeiENSGT00550000074703.
HOVERGENiHBG005371.
InParanoidiQ5SWU9.
KOiK11262.
OMAiHVFSGQC.
OrthoDBiEOG7HXCPW.
PhylomeDBiQ5SWU9.
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.
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 promoter usage. Align

Isoform 1 (identifier: Q5SWU9-1) [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 LGISGLQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT 100
VASPAEFVTR FGGNKVIEKV LIANNGIAAV KCMRSIRRWS YEMFRNERAI 150
RFVVMVTPED LKANAEYIKM ADHYVPVPGG PNNNNYANVE 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 VSLRNSISNF 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 PFFSSRVKDW 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 SYELRHNQVE 1100
SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS NQVVRMAALE 1150
VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS 1200
FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE 1250
IMGCFCDSPP 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 PDGRDIIVIG NDITYRIGSF GPQEDLLFLR 1700
ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDP EDPYKGYKYL 1750
YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG 1800
MIAGESSLAY DEVITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA 1850
GALNKVLGRE VYTSNNQLGG IQIMHNNGVT HSTVCDDFEG VFTVLHWLSY 1900
MPKSVHSSVP LLNSKDPIDR IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL 1950
SGFFDYGSFS EIMQPWAQTV VVGRARLGGI PVGVVAVETR TVELSIPADP 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 IHNANPELTD GQIQAMLRRW 2250
FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE DGVRSVIEEN IKYISRDYVL 2300
KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM DSPST 2345
Length:2,345
Mass (Da):265,257
Last modified:December 21, 2004 - v1
Checksum:i6995C534B054FE02
GO
Isoform 2 (identifier: Q5SWU9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MMWWSTLMSLLRASSFWRRISAETIRIIRALRAYFERIM

Show »
Length:2,383
Mass (Da):269,958
Checksum:i57B7FB88C694692E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MMWWSTLMSLLRASSFWRRI SAETIRIIRALRAYFERIM in isoform 2. VSP_026101

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti623 – 6231E → G in AAS13685. 1 Publication
Sequence conflicti906 – 9061S → P in AAS13685. 1 Publication
Sequence conflicti933 – 9331C → Y in AAS13685. 1 Publication
Sequence conflicti1456 – 14561L → S in AAS13685. 1 Publication
Sequence conflicti1995 – 19951S → G in AAS13685. 1 Publication
Sequence conflicti2077 – 20771V → I in AAS13685. 1 Publication
Sequence conflicti2169 – 21691E → K in AAS13685. 1 Publication
Sequence conflicti2251 – 22511F → S in AAS13685. 1 Publication
Sequence conflicti2257 – 22571T → A in AAS13685. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY451393 mRNA. Translation: AAS13685.1.
AL596252, AL596447 Genomic DNA. Translation: CAI24019.1.
AL596447, AL596252 Genomic DNA. Translation: CAI25271.1.
AL596447 Genomic DNA. Translation: CAI25272.1.
AL596447 Genomic DNA. Translation: CAI25273.1.
AL596447 Genomic DNA. Translation: CAI25274.1.
AL596447 Genomic DNA. Translation: CAM21560.1.
AJ619664 mRNA. Translation: CAF02251.1.
AJ619665 Genomic DNA. Translation: CAF02252.1.
AF374167 mRNA. Translation: AAK57389.1.
AF374168 mRNA. Translation: AAK57390.1.
AF374169 mRNA. Translation: AAK57391.1.
AF374170 mRNA. Translation: AAK57392.1.
BC056500 mRNA. Translation: AAH56500.1.
CCDSiCCDS25185.1. [Q5SWU9-1]
RefSeqiNP_579938.2. NM_133360.2. [Q5SWU9-1]
XP_006532016.1. XM_006531953.1. [Q5SWU9-2]
XP_006532017.1. XM_006531954.1. [Q5SWU9-1]
XP_006532018.1. XM_006531955.1. [Q5SWU9-1]
XP_006532019.1. XM_006531956.1. [Q5SWU9-1]
XP_006532020.1. XM_006531957.1. [Q5SWU9-1]
UniGeneiMm.31374.

Genome annotation databases

EnsembliENSMUST00000020843; ENSMUSP00000020843; ENSMUSG00000020532. [Q5SWU9-1]
ENSMUST00000103201; ENSMUSP00000099490; ENSMUSG00000020532. [Q5SWU9-1]
ENSMUST00000133811; ENSMUSP00000116174; ENSMUSG00000020532.
GeneIDi107476.
KEGGimmu:107476.
UCSCiuc007kql.1. mouse. [Q5SWU9-1]

Keywords - Coding sequence diversityi

Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY451393 mRNA. Translation: AAS13685.1 .
AL596252 , AL596447 Genomic DNA. Translation: CAI24019.1 .
AL596447 , AL596252 Genomic DNA. Translation: CAI25271.1 .
AL596447 Genomic DNA. Translation: CAI25272.1 .
AL596447 Genomic DNA. Translation: CAI25273.1 .
AL596447 Genomic DNA. Translation: CAI25274.1 .
AL596447 Genomic DNA. Translation: CAM21560.1 .
AJ619664 mRNA. Translation: CAF02251.1 .
AJ619665 Genomic DNA. Translation: CAF02252.1 .
AF374167 mRNA. Translation: AAK57389.1 .
AF374168 mRNA. Translation: AAK57390.1 .
AF374169 mRNA. Translation: AAK57391.1 .
AF374170 mRNA. Translation: AAK57392.1 .
BC056500 mRNA. Translation: AAH56500.1 .
CCDSi CCDS25185.1. [Q5SWU9-1 ]
RefSeqi NP_579938.2. NM_133360.2. [Q5SWU9-1 ]
XP_006532016.1. XM_006531953.1. [Q5SWU9-2 ]
XP_006532017.1. XM_006531954.1. [Q5SWU9-1 ]
XP_006532018.1. XM_006531955.1. [Q5SWU9-1 ]
XP_006532019.1. XM_006531956.1. [Q5SWU9-1 ]
XP_006532020.1. XM_006531957.1. [Q5SWU9-1 ]
UniGenei Mm.31374.

3D structure databases

ProteinModelPortali Q5SWU9.
SMRi Q5SWU9. Positions 101-615, 747-816, 1580-2337.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 223322. 2 interactions.
DIPi DIP-32276N.
IntActi Q5SWU9. 8 interactions.
MINTi MINT-4091386.

Chemistry

ChEMBLi CHEMBL3086.

PTM databases

PhosphoSitei Q5SWU9.

Proteomic databases

MaxQBi Q5SWU9.
PaxDbi Q5SWU9.
PRIDEi Q5SWU9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020843 ; ENSMUSP00000020843 ; ENSMUSG00000020532 . [Q5SWU9-1 ]
ENSMUST00000103201 ; ENSMUSP00000099490 ; ENSMUSG00000020532 . [Q5SWU9-1 ]
ENSMUST00000133811 ; ENSMUSP00000116174 ; ENSMUSG00000020532 .
GeneIDi 107476.
KEGGi mmu:107476.
UCSCi uc007kql.1. mouse. [Q5SWU9-1 ]

Organism-specific databases

CTDi 31.
MGIi MGI:108451. Acaca.

Phylogenomic databases

eggNOGi COG0511.
GeneTreei ENSGT00550000074703.
HOVERGENi HBG005371.
InParanoidi Q5SWU9.
KOi K11262.
OMAi HVFSGQC.
OrthoDBi EOG7HXCPW.
PhylomeDBi Q5SWU9.
TreeFami TF300061.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .
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

NextBioi 358872.
PROi Q5SWU9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q5SWU9.
Bgeei Q5SWU9.
CleanExi MM_ACACA.
Genevestigatori Q5SWU9.

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. "Characterization of the mouse acetyl-CoA carboxylase 1 (ACC1) gene and identification of an intronless pseudogene."
    Mao J., Wakil S.J.
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Asymmetric expression of transcripts derived from the shared promoter between the divergently oriented ACACA and TADA2L genes."
    Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C., Joulin V.
    Genomics 85:71-84(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-119 (ISOFORM 2).
    Strain: Swiss.
    Tissue: Brain.
  4. "Acetyl-CoA carboxylase and SREBP expression during peripheral nervous system myelination."
    Salles J., Sargueil F., Knoll-Gellida A., Witters L.A., Cassagne C., Garbay B.
    Biochim. Biophys. Acta 1631:229-238(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-38; 1221-1348 AND 1681-1891.
    Strain: C57BL/6.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1501-2345.
    Strain: C57BL/6.
    Tissue: Brain.
  6. "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains."
    Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., Lenoir G.M., Venezia N.D.
    Oncogene 21:6729-6739(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 298-306 AND 2267-2275, INTERACTION WITH BRCA1, SUBCELLULAR LOCATION.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, INTERACTION WITH MID1IP1, PHOSPHORYLATION AT SER-79, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiACACA_MOUSE
AccessioniPrimary (citable) accession number: Q5SWU9
Secondary accession number(s): A2A6H4
, Q5SWU6, Q5SWU7, Q5SWU8, Q6JIZ1, Q6PHL9, Q705X8, Q705X9, Q91VC8, Q925C4, Q925C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: December 21, 2004
Last modified: September 3, 2014
This is version 105 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. 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

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