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Q13085 (ACACA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-CoA carboxylase 1

Short name=ACC1
EC=6.4.1.2
Alternative name(s):
ACC-alpha

Including the following 1 domains:

  1. Biotin carboxylase
    EC=6.3.4.14
Gene names
Name:ACACA
Synonyms:ACAC, ACC1, ACCA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2346 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.20

Catalytic activity

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. Ref.20

ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein]. Ref.20

Cofactor

Biotin.

Binds 2 manganese ions per subunit.

Enzyme regulation

By phosphorylation By similarity. Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization. Ref.20

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.

Subunit structure

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. Ref.8 Ref.10 Ref.20

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in brain, placental, skeletal muscle, renal, pancreatic and adipose tissues; expressed at low level in pulmonary tissue; not detected in the liver.

Post-translational modification

Phosphorylation on Ser-1263 is required for interaction with BRCA1.

Involvement in disease

Acetyl-CoA carboxylase 1 deficiency (ACACAD) [MIM:613933]: An inborn error of de novo fatty acid synthesis associated with severe brain damage, persistent myopathy and poor growth.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Contains 1 carboxyltransferase domain.

Sequence caution

The sequence AAP94120.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative promoter usage
Polymorphism
   LigandATP-binding
Biotin
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processacetyl-CoA metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

biotin metabolic process

Traceable author statement. Source: Reactome

carnitine shuttle

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

energy reserve metabolic process

Traceable author statement. Source: Reactome

fatty acid biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

lipid homeostasis

Inferred from electronic annotation. Source: Ensembl

long-chain fatty-acyl-CoA biosynthetic process

Traceable author statement. Source: Reactome

malonyl-CoA biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

multicellular organismal protein metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cellular metabolic process

Traceable author statement. Source: Reactome

protein homotetramerization

Inferred from sequence or structural similarity Ref.20. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

tissue homeostasis

Inferred from electronic annotation. Source: Ensembl

triglyceride biosynthetic process

Traceable author statement. Source: Reactome

vitamin metabolic process

Traceable author statement. Source: Reactome

water-soluble vitamin metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetyl-CoA carboxylase activity

Inferred from sequence or structural similarity Ref.20. Source: UniProtKB

biotin carboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative promoter usage. [Align] [Select]
Isoform 1 (identifier: Q13085-1)

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.
Isoform 2 (identifier: Q13085-2)

Also known as: E5A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: MDEPSPLAQP...SLQDGLALHI → MEGSPEENKEMRYYMLQ
Isoform 3 (identifier: Q13085-3)

Also known as: E5B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.
Isoform 4 (identifier: Q13085-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23462346Acetyl-CoA carboxylase 1
PRO_0000146764

Regions

Domain117 – 618502Biotin carboxylation
Domain275 – 466192ATP-grasp
Domain752 – 81867Biotinyl-binding
Domain1698 – 2194497Carboxyltransferase
Nucleotide binding315 – 3206ATP Potential

Sites

Active site4411 By similarity
Metal binding4241Manganese 1 By similarity
Metal binding4371Manganese 1 By similarity
Metal binding4371Manganese 2 By similarity
Metal binding4391Manganese 2 By similarity
Binding site18231Coenzyme A By similarity
Binding site21271Coenzyme A By similarity
Binding site21291Coenzyme A By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.17 Ref.21
Modified residue51Phosphoserine Ref.17 Ref.21
Modified residue231Phosphoserine Ref.15 Ref.18 Ref.21
Modified residue251Phosphoserine Ref.15 Ref.18
Modified residue291Phosphoserine Ref.9 Ref.14 Ref.15 Ref.17 Ref.18 Ref.21 Ref.23
Modified residue531Phosphoserine Ref.9
Modified residue781Phosphoserine By similarity
Modified residue801Phosphoserine Ref.7 Ref.15 Ref.21 Ref.23
Modified residue4881Phosphoserine Ref.13
Modified residue7861N6-biotinyllysine By similarity
Modified residue12011Phosphoserine By similarity
Modified residue12161Phosphoserine By similarity
Modified residue12631Phosphoserine Ref.11
Modified residue13341N6-acetyllysine Ref.19

Natural variations

Alternative sequence1 – 7878Missing in isoform 3.
VSP_026098
Alternative sequence1 – 7575MDEPS…LALHI → MEGSPEENKEMRYYMLQ in isoform 2.
VSP_026099
Alternative sequence11M → MWWSTLMSILRARSFWKWIS TQTVRIIRAVRAHFGGIM in isoform 4.
VSP_026100
Natural variant8381R → W.
Corresponds to variant rs2287351 [ dbSNP | Ensembl ].
VAR_042941
Natural variant16871R → Q in a colorectal cancer sample; somatic mutation. Ref.24
VAR_036514
Natural variant22711A → V Rare polymorphism; frequency <0.004; may play a role in breast cancer susceptibility. Ref.3
VAR_028929

Experimental info

Mutagenesis781S → A: No effect on interaction with BRCA1. Ref.11
Mutagenesis3441S → A: No effect on interaction with BRCA1. Ref.11
Mutagenesis4321S → A: No effect on interaction with BRCA1. Ref.11
Mutagenesis12011S → A: No effect on interaction with BRCA1. Ref.11
Mutagenesis12631S → A: Abolishes interaction with BRCA1. Ref.11
Mutagenesis15851S → A: No effect on interaction with BRCA1. Ref.11
Mutagenesis19521S → A: No effect on interaction with BRCA1. Ref.11
Mutagenesis22111S → A: No effect on interaction with BRCA1. Ref.11
Sequence conflict661S → A in AAC50139. Ref.1
Sequence conflict791M → W in AAC50139. Ref.1
Sequence conflict891R → G in AAC50139. Ref.1
Sequence conflict1821P → A in AAC50139. Ref.1
Sequence conflict2341S → N in AAC50139. Ref.1
Sequence conflict2991Q → K in AAC50139. Ref.1
Sequence conflict3031E → K in AAC50139. Ref.1
Sequence conflict3641A → V in AAP94122. Ref.2
Sequence conflict4461H → Q in AAC50139. Ref.1
Sequence conflict4941D → N in AAC50139. Ref.1
Sequence conflict5541D → G in AAC50139. Ref.1
Sequence conflict6221Q → R in AAC50139. Ref.1
Sequence conflict6401A → G in AAC50139. Ref.1
Sequence conflict8141V → I in AAP94122. Ref.2
Sequence conflict10611N → S in AAC50139. Ref.1
Sequence conflict1094 – 10952EL → DV in AAC50139. Ref.1
Sequence conflict12251S → A in AAC50139. Ref.1
Sequence conflict12571S → C in AAC50139. Ref.1
Sequence conflict12971C → G in AAC50139. Ref.1
Sequence conflict13201V → A in AAC50139. Ref.1
Sequence conflict14441N → S in AAC50139. Ref.1
Sequence conflict14741F → L in AAC50139. Ref.1
Sequence conflict1665 – 16662TF → SL in AAC50139. Ref.1
Sequence conflict16771I → V in AAC50139. Ref.1
Sequence conflict17411P → S in AAC50139. Ref.1
Sequence conflict17621S → G in AAC50139. Ref.1
Sequence conflict18221C → S in AAC50139. Ref.1
Sequence conflict18751M → T in AAC50139. Ref.1
Sequence conflict18881D → G in AAC50139. Ref.1
Sequence conflict19971I → V in AAC50139. Ref.1
Sequence conflict20131Q → H in AAC50139. Ref.1
Sequence conflict20581D → H in AAC50139. Ref.1
Sequence conflict20751C → S in AAC50139. Ref.1
Sequence conflict2098 – 20992SS → PT in AAC50139. Ref.1
Sequence conflict2158 – 21592TA → PT in AAC50139. Ref.1
Sequence conflict21661N → S in AAC50139. Ref.1
Sequence conflict22341N → S in AAC50139. Ref.1
Sequence conflict23211H → R in AAP94122. Ref.2

Secondary structure

............................................................................................................................................................................................................... 2346
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: F1F0A518F8824FFC

FASTA2,346265,554
        10         20         30         40         50         60 
MDEPSPLAQP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS PASVGSDTLS 

        70         80         90        100        110        120 
DLGISSLQDG LALHIRSSMS GLHLVKQGRD RKKIDSQRDF TVASPAEFVT RFGGNKVIEK 

       130        140        150        160        170        180 
VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG 

       190        200        210        220        230        240 
GPNNNNYANV ELILDIAKRI PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL 

       250        260        270        280        290        300 
GDKIASSIVA QTAGIPTLPW SGSGLRVDWQ ENDFSKRILN VPQELYEKGY VKDVDDGLQA 

       310        320        330        340        350        360 
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV 

       370        380        390        400        410        420 
QILADQYGNA ISLFGRDCSV QRRHQKIIEE APATIATPAV FEHMEQCAVK LAKMVGYVSA 

       430        440        450        460        470        480 
GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGIPL YRIKDIRMMY 

       490        500        510        520        530        540 
GVSPWGDSPI DFEDSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY 

       550        560        570        580        590        600 
FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET 

       610        620        630        640        650        660 
ESFQMNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSVSN FLHSLERGQV 

       670        680        690        700        710        720 
LPAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS CVEVDVHRLS DGGLLLSYDG 

       730        740        750        760        770        780 
SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSVMRSPSAG KLIQYIVEDG GHVFAGQCYA 

       790        800        810        820        830        840 
EIEVMKMVMT LTAVESGCIH YVKRPGAALD PGCVLAKMQL DNPSKVQQAE LHTGSLPRIQ 

       850        860        870        880        890        900 
STALRGEKLH RVFHYVLDNL VNVMNGYCLP DPFFSSKVKD WVERLMKTLR DPSLPLLELQ 

       910        920        930        940        950        960 
DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA TLNRKSEREV 

       970        980        990       1000       1010       1020 
FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ FQNGHYDKCV FALREENKSD 

      1030       1040       1050       1060       1070       1080 
MNTVLNYIFS HAQVTKKNLL VTMLIDQLCG RDPTLTDELL NILTELTQLS KTTNAKVALR 

      1090       1100       1110       1120       1130       1140 
ARQVLIASHL PSYELRHNQV ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH 

      1150       1160       1170       1180       1190       1200 
SNQVVRMAAL EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM 

      1210       1220       1230       1240       1250       1260 
SFSSNLNHYG MTHVASVSDV LLDNSFTPPC QRMGGMVSFR TFEDFVRIFD EVMGCFSDSP 

      1270       1280       1290       1300       1310       1320 
PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE DDRLAAMFRE FTQQNKATLV 

      1330       1340       1350       1360       1370       1380 
DHGIRRLTFL VAQKDFRKQV NYEVDRRFHR EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ 

      1390       1400       1410       1420       1430       1440 
LELNRMRNFD LTAIPCANHK MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE 

      1450       1460       1470       1480       1490       1500 
YLQNEGERLL LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG 

      1510       1520       1530       1540       1550       1560 
SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD SRTAQIMFQA 

      1570       1580       1590       1600       1610       1620 
YGDKQGPLHG MLINTPYVTK DLLQSKRFQA QSLGTTYIYD IPEMFRQSLI KLWESMSTQA 

      1630       1640       1650       1660       1670       1680 
FLPSPPLPSD MLTYTELVLD DQGQLVHMNR LPGGNEIGMV AWKMTFKSPE YPEGRDIIVI 

      1690       1700       1710       1720       1730       1740 
GNDITYRIGS FGPQEDLLFL RASELARAEG IPRIYVSANS GARIGLAEEI RHMFHVAWVD 

      1750       1760       1770       1780       1790       1800 
PEDPYKGYRY LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GIGPENLRGS 

      1810       1820       1830       1840       1850       1860 
GMIAGESSLA YNEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG AGALNKVLGR 

      1870       1880       1890       1900       1910       1920 
EVYTSNNQLG GIQIMHNNGV THCTVCDDFE GVFTVLHWLS YMPKSVHSSV PLLNSKDPID 

      1930       1940       1950       1960       1970       1980 
RIIEFVPTKT PYDPRWMLAG RPHPTQKGQW LSGFFDYGSF SEIMQPWAQT VVVGRARLGG 

      1990       2000       2010       2020       2030       2040 
IPVGVVAVET RTVELSIPAD PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL 

      2050       2060       2070       2080       2090       2100 
MVFANWRGFS GGMKDMYDQV LKFGAYIVDG LRECCQPVLV YIPPQAELRG GSWVVIDSSI 

      2110       2120       2130       2140       2150       2160 
NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER LGTPELSTAE 

      2170       2180       2190       2200       2210       2220 
RKELENKLKE REEFLIPIYH QVAVQFADLH DTPGRMQEKG VISDILDWKT SRTFFYWRLR 

      2230       2240       2250       2260       2270       2280 
RLLLEDLVKK KIHNANPELT DGQIQAMLRR WFVEVEGTVK AYVWDNNKDL AEWLEKQLTE 

      2290       2300       2310       2320       2330       2340 
EDGVHSVIEE NIKCISRDYV LKQIRSLVQA NPEVAMDSII HMTQHISPTQ RAEVIRILST 


MDSPST 

« Hide

Isoform 2 (E5A) [UniParc].

Checksum: 4E2C75958216CC8B
Show »

FASTA2,288259,686
Isoform 3 (E5B) [UniParc].

Checksum: C78033F62C492D3E
Show »

FASTA2,268257,239
Isoform 4 [UniParc].

Checksum: 1F2B8F96208B9983
Show »

FASTA2,383269,999

References

« Hide 'large scale' references
[1]"Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms."
Abu-Elheiga L., Jayakumar A., Baldini A., Chirala S.S., Wakil S.J.
Proc. Natl. Acad. Sci. U.S.A. 92:4011-4015(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]"Human acetyl-CoA carboxylase 1 gene: presence of three promoters and heterogeneity at the 5'-untranslated mRNA region."
Mao J., Chirala S.S., Wakil S.J.
Proc. Natl. Acad. Sci. U.S.A. 100:7515-7520(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-366 (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-120 (ISOFORM 4).
Tissue: Adipocyte.
[3]"Acetyl-CoA carboxylase alpha gene and breast cancer susceptibility."
Sinilnikova O.M., Ginolhac S.M., Magnard C., Leone M., Anczukow O., Hughes D., Moreau K., Thompson D., Coutanson C., Hall J., Romestaing P., Gerard J.-P., Bonadona V., Lasset C., Goldgar D.E., Joulin V., Venezia N.D., Lenoir G.M.
Carcinogenesis 25:2417-2424(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-2271.
[4]"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] (ISOFORM 4).
Tissue: Brain.
[5]"Characterisation of an N-terminal variant of acetyl-CoA carboxylase-alpha: expression in human tissues and evolutionary aspects."
Travers M.T., Vallance A.J., Clegg R.A., Thomson R., Price N.T., Barber M.C.
Biochim. Biophys. Acta 1634:97-106(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-113 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-93 (ISOFORM 3).
Tissue: Mammary gland and Testis.
[6]"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 [MRNA] OF 1-47 (ISOFORM 1).
Tissue: Testis.
[7]Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-18; 39-45; 77-86; 99-111; 121-132; 153-170; 218-224; 267-276; 278-288; 323-335; 568-579; 589-615; 646-657; 748-755; 818-838; 985-992; 997-1008; 1083-1096; 1147-1169; 1192-1199; 1233-1247; 1283-1294; 1317-1325; 1327-1334; 1372-1385; 1401-1420; 1508-1514; 1553-1564; 1668-1687; 1714-1731; 1750-1759; 1782-1798; 1824-1833; 1838-1856; 1905-1916; 1922-1929; 1978-2009; 2063-2072; 2104-2111; 2115-2127; 2139-2161; 2200-2209; 2213-2218; 2221-2229 AND 2261-2293, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-80, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hepatoma.
[8]"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: INTERACTION WITH BRCA1.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"BRCA1 affects lipid synthesis through its interaction with acetyl-CoA carboxylase."
Moreau K., Dizin E., Ray H., Luquain C., Lefai E., Foufelle F., Billaud M., Lenoir G.M., Venezia N.D.
J. Biol. Chem. 281:3172-3181(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRCA1.
[11]"ACCA phosphopeptide recognition by the BRCT repeats of BRCA1."
Ray H., Moreau K., Dizin E., Callebaut I., Venezia N.D.
J. Mol. Biol. 359:973-982(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1263, MUTAGENESIS OF SER-78; SER-344; SER-432; SER-1201; SER-1263; SER-1585; SER-1952 AND SER-2211.
[12]"Acetyl-CoA carboxylase deficiency: an inborn error of de novo fatty acid synthesis."
Blom W., de Muinck Keizer S.M.P.F., Scholte H.R.
N. Engl. J. Med. 305:465-466(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ACACAD.
[13]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29 AND SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25 AND SER-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Crystal structure of Spot 14, a modulator of fatty acid synthesis."
Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M., McKean W.B., Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J.
Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, INTERACTION WITH MID1IP1.
[21]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-23; SER-29 AND SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-1687.
+Additional computationally mapped references.

Web resources

Wikipedia

Acetyl-CoA carboxylase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U19822 mRNA. Translation: AAC50139.1.
AY315619 mRNA. Translation: AAP94114.1.
AY315620 mRNA. Translation: AAP94115.1.
AY315621 mRNA. Translation: AAP94116.1.
AY315623 mRNA. Translation: AAP94118.1.
AY315625 mRNA. Translation: AAP94120.1. Different initiation.
AY315627 mRNA. Translation: AAP94122.1.
AY237919 mRNA. Translation: AAP69841.1.
BC137287 mRNA. Translation: AAI37288.1.
AJ534888 mRNA. Translation: CAD59556.1.
AJ534889 mRNA. Translation: CAD59557.1.
AJ564444 mRNA. Translation: CAD92089.1.
PIRI38928.
RefSeqNP_942131.1. NM_198834.1.
NP_942133.1. NM_198836.1.
NP_942134.1. NM_198837.1.
NP_942135.1. NM_198838.1.
NP_942136.1. NM_198839.1.
XP_005257323.1. XM_005257266.2.
XP_005257324.1. XM_005257267.2.
UniGeneHs.160556.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YL2X-ray2.30A/B78-617[»]
3COJX-ray3.21H/I/J/K/L/M/N/O1258-1270[»]
4ASIX-ray2.80A/B/C/D/E/F1571-2338[»]
ProteinModelPortalQ13085.
SMRQ13085. Positions 102-817, 1581-2338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106549. 62 interactions.
DIPDIP-36122N.
IntActQ13085. 26 interactions.
MINTMINT-1415014.

Chemistry

BindingDBQ13085.
ChEMBLCHEMBL3351.
DrugBankDB00121. Biotin.
GuidetoPHARMACOLOGY1263.

PTM databases

PhosphoSiteQ13085.

Polymorphism databases

DMDM118601083.

Proteomic databases

PaxDbQ13085.
PRIDEQ13085.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335166; ENSP00000335323; ENSG00000132142. [Q13085-3]
ENST00000353139; ENSP00000344789; ENSG00000132142. [Q13085-4]
ENST00000360679; ENSP00000353898; ENSG00000132142. [Q13085-2]
ENST00000394406; ENSP00000377928; ENSG00000132142. [Q13085-1]
ENST00000451642; ENSP00000397282; ENSG00000132142.
GeneID31.
KEGGhsa:31.
UCSCuc002hnk.3. human. [Q13085-1]
uc002hnl.3. human. [Q13085-2]
uc002hno.3. human. [Q13085-4]

Organism-specific databases

CTD31.
GeneCardsGC17M035441.
HGNCHGNC:84. ACACA.
HPACAB013715.
MIM200350. gene.
613933. phenotype.
neXtProtNX_Q13085.
PharmGKBPA24421.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0511.
HOVERGENHBG005371.
InParanoidQ13085.
KOK11262.
OMAETESFQM.
OrthoDBEOG7HXCPW.
PhylomeDBQ13085.
TreeFamTF300061.

Enzyme and pathway databases

BRENDA6.4.1.2. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ13085.
UniPathwayUPA00655; UER00711.

Gene expression databases

ArrayExpressQ13085.
BgeeQ13085.
GenevestigatorQ13085.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProIPR013537. 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.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF08326. 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]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEPS50975. 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]
ProtoNetSearch...

Other

ChiTaRSACACA. human.
EvolutionaryTraceQ13085.
GeneWikiACACA.
GenomeRNAi31.
NextBio111.
PROQ13085.
SOURCESearch...

Entry information

Entry nameACACA_HUMAN
AccessionPrimary (citable) accession number: Q13085
Secondary accession number(s): B2RP68 expand/collapse secondary AC list , Q6KEV6, Q6XDA8, Q7Z2G8, Q7Z561, Q7Z563, Q7Z564, Q86WB2, Q86WB3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 31, 2006
Last modified: April 16, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM