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O00763 (ACACB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-CoA carboxylase 2

EC=6.4.1.2
Alternative name(s):
ACC-beta

Including the following 1 domains:

  1. Biotin carboxylase
    EC=6.3.4.14
Gene names
Name:ACACB
Synonyms:ACC2, ACCB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2458 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.

Catalytic activity

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. Ref.9

ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein]. Ref.9

Cofactor

Biotin By similarity. Ref.2

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

Enzyme regulation

Activity is increased by oligomerization. Activated by citrate. Citrate and MID1IP1 promote oligomerization. Inhibited by malonyl-CoA. Ref.2 Ref.9

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 with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity. Ref.9

Subcellular location

Endomembrane system. Note: May associate with membranes.

Tissue specificity

Predominantly expressed in the heart, skeletal muscles and liver. Ref.1

Post-translational modification

Phosphorylated by AMPK, leading to inactivate the enzyme. Ref.7

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Contains 1 carboxyltransferase domain.

Biophysicochemical properties

Kinetic parameters:

KM=120 µM for ATP Ref.2

KM=58 µM for Acetyl-CoA

KM=3.0 mM for NaHCO3

Sequence caution

The sequence AAB58382.1 differs from that shown. Reason: Many Frameshifts and conflicts.

The sequence CAE01470.2 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Biotin
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processacetyl-CoA metabolic process

Inferred from direct assay Ref.9. 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 electronic annotation. Source: UniProtKB-KW

malonyl-CoA biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

positive regulation of cellular metabolic process

Traceable author statement. Source: Reactome

protein homotetramerization

Inferred from direct assay Ref.9. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic 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

Traceable author statement. Source: Reactome

endomembrane system

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial outer membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

acetyl-CoA carboxylase activity

Inferred from direct assay Ref.9. Source: UniProtKB

biotin binding

Inferred from electronic annotation. Source: Ensembl

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

With

Entry

#Exp.

IntAct

Notes

HLCSP507474EBI-2211739,EBI-3915568

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: O00763-1)

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 Short (identifier: O00763-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1118-1187: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24582458Acetyl-CoA carboxylase 2
PRO_0000146767

Regions

Domain259 – 761503Biotin carboxylation
Domain414 – 609196ATP-grasp
Domain895 – 96167Biotinyl-binding
Domain1809 – 2305497Carboxyltransferase
Nucleotide binding458 – 4636ATP Potential

Sites

Active site5841 By similarity
Metal binding5671Manganese 1 By similarity
Metal binding5801Manganese 1 By similarity
Metal binding5801Manganese 2 By similarity
Metal binding5821Manganese 2 By similarity
Binding site19341Coenzyme A By similarity
Binding site22381Coenzyme A By similarity
Binding site22401Coenzyme A By similarity

Amino acid modifications

Modified residue2221Phosphoserine; by AMPK Ref.7
Modified residue9291N6-biotinyllysine By similarity

Natural variations

Alternative sequence1118 – 118770Missing in isoform Short.
VSP_000547
Natural variant1931R → L in a pancreatic ductal adenocarcinoma sample; somatic mutation. Ref.12
VAR_062667
Natural variant5521I → V.
Corresponds to variant rs16940029 [ dbSNP | Ensembl ].
VAR_031255
Natural variant6511A → T.
Corresponds to variant rs2300455 [ dbSNP | Ensembl ].
VAR_031256
Natural variant21411V → I. Ref.2 Ref.3
Corresponds to variant rs2075260 [ dbSNP | Ensembl ].
VAR_031257

Experimental info

Sequence conflict91C → R in ABF48723. Ref.2
Sequence conflict1201T → I in AAR37018. Ref.4
Sequence conflict4221I → T in AAR37018. Ref.4
Sequence conflict13401S → N in AAC50571. Ref.6
Sequence conflict13831D → G in AAC50571. Ref.6
Sequence conflict14251V → M in AAC50571. Ref.6
Sequence conflict1819 – 18213AEG → PEA in AAC50571. Ref.6
Sequence conflict1892 – 18932MI → IM in AAC50571. Ref.6

Secondary structure

.................................................................................................................................................................................................................................... 2458
Helix Strand Turn

Details...

Sequences

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

Last modified October 5, 2010. Version 3.
Checksum: ED12674A1A8A0706

FASTA2,458276,541
        10         20         30         40         50         60 
MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSKSEAN LIPSQEPFPA SDNSGETPQR 

        70         80         90        100        110        120 
NGEGHTLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP RNPLSSSDAA PSPELQANGT 

       130        140        150        160        170        180 
GTQGLEATDT NGLSSSARPQ GQQAGSPSKE DKKQANIKRQ LMTNFILGSF DDYSSDEDSV 

       190        200        210        220        230        240 
AGSSRESTRK GSRASLGALS LEAYLTTGEA ETRVPTMRPS MSGLHLVKRG REHKKLDLHR 

       250        260        270        280        290        300 
DFTVASPAEF VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT 

       310        320        330        340        350        360 
PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG WGHASENPKL 

       370        380        390        400        410        420 
PELLCKNGVA FLGPPSEAMW ALGDKIASTV VAQTLQVPTL PWSGSGLTVE WTEDDLQQGK 

       430        440        450        460        470        480 
RISVPEDVYD KGCVKDVDEG LEAAERIGFP LMIKASEGGG GKGIRKAESA EDFPILFRQV 

       490        500        510        520        530        540 
QSEIPGSPIF LMKLAQHARH LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP 

       550        560        570        580        590        600 
LAIFEFMEQC AIRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL 

       610        620        630        640        650        660 
PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA ARITSENPDE 

       670        680        690        700        710        720 
GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF GHCFSWGENR EEAISNMVVA 

       730        740        750        760        770        780 
LKELSIRGDF RTTVEYLINL LETESFQNND IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL 

       790        800        810        820        830        840 
NVADAMFRTC MTDFLHSLER GQVLPADSLL NLVDVELIYG GVKYILKVAR QSLTMFVLIM 

       850        860        870        880        890        900 
NGCHIEIDAH RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP 

       910        920        930        940        950        960 
SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQERG RVKYIKRPGA VLEAGCVVAR 

       970        980        990       1000       1010       1020 
LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL ENLTNVMSGF CLPEPVFSIK 

      1030       1040       1050       1060       1070       1080 
LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKS VRRVMAQYAS NITSVLCQFP 

      1090       1100       1110       1120       1130       1140 
SQQIATILDC HAATLQRKAD REVFFINTQS IVQLVQRYRS GIRGYMKTVV LDLLRRYLRV 

      1150       1160       1170       1180       1190       1200 
EHHFQQAHYD KCVINLREQF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD 

      1210       1220       1230       1240       1250       1260 
ELISILNELT QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP 

      1270       1280       1290       1300       1310       1320 
ENLKKLILSE TTIFDVLPTF FYHANKVVCM ASLEVYVRRG YIAYELNSLQ HRQLPDGTCV 

      1330       1340       1350       1360       1370       1380 
VEFQFMLPSS HPNRMTVPIS ITNPDLLRHS TELFMDSGFS PLCQRMGAMV AFRRFEDFTR 

      1390       1400       1410       1420       1430       1440 
NFDEVISCFA NVPKDTPLFS EARTSLYSED DCKSLREEPI HILNVSIQCA DHLEDEALVP 

      1450       1460       1470       1480       1490       1500 
ILRTFVQSKK NILVDYGLRR ITFLIAQEKE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL 

      1510       1520       1530       1540       1550       1560 
ELNRMRNFDL TAVPCANHKM HLYLGAAKVK EGVEVTDHRF FIRAIIRHSD LITKEASFEY 

      1570       1580       1590       1600       1610       1620 
LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPFKIEES VRYMVMRYGS 

      1630       1640       1650       1660       1670       1680 
RLWKLRVLQA EVKINIRQTT TGSAVPIRLF ITNESGYYLD ISLYKEVTDS RSGNIMFHSF 

      1690       1700       1710       1720       1730       1740 
GNKQGPQHGM LINTPYVTKD LLQAKRFQAQ TLGTTYIYDF PEMFRQALFK LWGSPDKYPK 

      1750       1760       1770       1780       1790       1800 
DILTYTELVL DSQGQLVEMN RLPGGNEVGM VAFKMRFKTQ EYPEGRDVIV IGNDITFRIG 

      1810       1820       1830       1840       1850       1860 
SFGPGEDLLY LRASEMARAE GIPKIYVAAN SGARIGMAEE IKHMFHVAWV DPEDPHKGFK 

      1870       1880       1890       1900       1910       1920 
YLYLTPQDYT RISSLNSVHC KHIEEGGESR YMITDIIGKD DGLGVENLRG SGMIAGESSL 

      1930       1940       1950       1960       1970       1980 
AYEEIVTISL VTCRAIGIGA YLVRLGQRVI QVENSHIILT GASALNKVLG REVYTSNNQL 

      1990       2000       2010       2020       2030       2040 
GGVQIMHYNG VSHITVPDDF EGVYTILEWL SYMPKDNHSP VPIITPTDPI DREIEFLPSR 

      2050       2060       2070       2080       2090       2100 
APYDPRWMLA GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE 

      2110       2120       2130       2140       2150       2160 
TRTVEVAVPA DPANLDSEAK IIQQAGQVWF PDSAYKTAQA VKDFNREKLP LMIFANWRGF 

      2170       2180       2190       2200       2210       2220 
SGGMKDMYDQ VLKFGAYIVD GLRQYKQPIL IYIPPYAELR GGSWVVIDAT INPLCIEMYA 

      2230       2240       2250       2260       2270       2280 
DKESRGGVLE PEGTVEIKFR KKDLIKSMRR IDPAYKKLME QLGEPDLSDK DRKDLEGRLK 

      2290       2300       2310       2320       2330       2340 
AREDLLLPIY HQVAVQFADF HDTPGRMLEK GVISDILEWK TARTFLYWRL RRLLLEDQVK 

      2350       2360       2370       2380       2390       2400 
QEILQASGEL SHVHIQSMLR RWFVETEGAV KAYLWDNNQV VVQWLEQHWQ AGDGPRSTIR 

      2410       2420       2430       2440       2450 
ENITYLKHDS VLKTIRGLVE ENPEVAVDCV IYLSQHISPA ERAQVVHLLS TMDSPAST 

« Hide

Isoform Short [UniParc].

Checksum: 10A218FFD1408B68
Show »

FASTA2,388268,166

References

« Hide 'large scale' references
[1]"Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two isoforms."
Abu-Elheiga L., Almarza-Ortega D.B., Baldini A., Wakil S.J.
J. Biol. Chem. 272:10669-10677(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), TISSUE SPECIFICITY.
Tissue: Liver.
[2]"Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes."
Cheng D., Chu C.-H., Chen L., Feder J.N., Mintier G.A., Wu Y., Cook J.W., Harpel M.R., Locke G.A., An Y., Tamura J.K.
Protein Expr. Purif. 51:11-21(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, VARIANT ILE-2141.
[3]"Corrected sequence for human acetyl-CoA carboxylase 2 obtained by alignment to human genomic DNA and PCR cloning from human skeletal muscle and heart cDNA."
Peng X.R., Lindgren K., Corneliussen B.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT ILE-2141.
Tissue: Heart.
[4]"Alternative splicing in the human acetyl-CoA carboxylase 2 (ACC2) gene."
Mao J., Wakil S.J.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: Heart.
[5]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Identification of a second human acetyl-CoA carboxylase gene."
Widmer J., Fassihi K.S., Schlichter S.C., Wheeler K.S., Crute B.E., King N., Nutile-Mcmenemy N., Noll W.W., Daniel S., Ha J., Kim K.-H., Witters L.A.
Biochem. J. 316:915-922(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1324-2109.
Tissue: Adipose tissue.
[7]"Regulation of 5'AMP-activated protein kinase activity and substrate utilization in exercising human skeletal muscle."
Wojtaszewski J.F., MacDonald C., Nielsen J.N., Hellsten Y., Hardie D.G., Kemp B.E., Kiens B., Richter E.A.
Am. J. Physiol. 284:E813-E822(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-222 BY AMPK.
[8]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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: CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, INTERACTION WITH MID1IP1.
[10]"Crystal structure of the biotin carboxylase domain of human acetyl-CoA carboxylase 2."
Cho Y.S., Lee J.I., Shin D., Kim H.T., Cheon Y.H., Seo C.I., Kim Y.E., Hyun Y.L., Lee Y.S., Sugiyama K., Park S.Y., Ro S., Cho J.M., Lee T.G., Heo Y.S.
Proteins 70:268-272(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 217-775.
[11]"Solution structure of RSGI RUH-053, an apo-biotin carboxy carrier protein from human transcarboxylase."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 885-971.
[12]"Core signaling pathways in human pancreatic cancers revealed by global genomic analyses."
Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P., Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., Nikolsky Y. expand/collapse author list , Hartigan J., Smith D.R., Hidalgo M., Leach S.D., Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C., Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N., Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.
Science 321:1801-1806(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-193.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U89344 mRNA. Translation: AAB58382.1. Sequence problems.
DQ493870 mRNA. Translation: ABF48723.1.
AJ575431 mRNA. Translation: CAE01470.2. Sequence problems.
AJ575592 mRNA. Translation: CAE01471.3.
AY382667 mRNA. Translation: AAR37018.1.
AC007637 Genomic DNA. No translation available.
U34591 mRNA. Translation: AAC50571.1.
PIRS71091.
RefSeqNP_001084.3. NM_001093.3.
XP_005253933.1. XM_005253876.2.
UniGeneHs.234898.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DN8NMR-A885-971[»]
2HJWX-ray2.50A217-775[»]
2KCCNMR-A891-965[»]
3FF6X-ray3.19A/B/C/D1693-2450[»]
3GIDX-ray2.30A/B238-760[»]
3GLKX-ray2.10A238-760[»]
3JRWX-ray2.60A217-775[»]
3JRXX-ray2.50A217-775[»]
3TDCX-ray2.41A1690-2445[»]
4HQ6X-ray2.70A217-776[»]
ProteinModelPortalO00763.
SMRO00763. Positions 237-758, 891-960, 1695-2449.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106550. 11 interactions.
DIPDIP-51617N.
IntActO00763. 5 interactions.
MINTMINT-6800190.
STRING9606.ENSP00000367079.

Chemistry

BindingDBO00763.
ChEMBLCHEMBL4829.
DrugBankDB00121. Biotin.
GuidetoPHARMACOLOGY1264.

PTM databases

PhosphoSiteO00763.

Proteomic databases

PaxDbO00763.
PRIDEO00763.

Protocols and materials databases

DNASU32.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338432; ENSP00000341044; ENSG00000076555. [O00763-1]
ENST00000377848; ENSP00000367079; ENSG00000076555. [O00763-1]
GeneID32.
KEGGhsa:32.
UCSCuc001tob.3. human. [O00763-1]

Organism-specific databases

CTD32.
GeneCardsGC12P109577.
H-InvDBHIX0036741.
HGNCHGNC:85. ACACB.
HPAHPA006554.
MIM601557. gene.
neXtProtNX_O00763.
PharmGKBPA24422.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0511.
HOVERGENHBG005371.
KOK11262.
OMAPPVGECI.
OrthoDBEOG7HXCPW.
PhylomeDBO00763.
TreeFamTF300061.

Enzyme and pathway databases

BRENDA6.4.1.2. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKO00763.
UniPathwayUPA00655; UER00711.

Gene expression databases

ArrayExpressO00763.
BgeeO00763.
CleanExHS_ACACB.
GenevestigatorO00763.

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.
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.
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

EvolutionaryTraceO00763.
GeneWikiACACB.
GenomeRNAi32.
NextBio123.
PROO00763.
SOURCESearch...

Entry information

Entry nameACACB_HUMAN
AccessionPrimary (citable) accession number: O00763
Secondary accession number(s): A6NK36 expand/collapse secondary AC list , Q16852, Q1HEC1, Q6KE87, Q6KE89, Q6TY48
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 141 of the entry and version 3 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 12

Human chromosome 12: entries, gene names and cross-references to MIM