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O00763

- ACACB_HUMAN

UniProt

O00763 - ACACB_HUMAN

Protein

Acetyl-CoA carboxylase 2

Gene

ACACB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    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 activityi

    ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.1 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

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

    Kineticsi

    1. KM=120 µM for ATP1 Publication
    2. KM=58 µM for Acetyl-CoA1 Publication
    3. KM=3.0 mM for NaHCO31 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi567 – 5671Manganese 1By similarity
    Metal bindingi580 – 5801Manganese 1By similarity
    Metal bindingi580 – 5801Manganese 2By similarity
    Metal bindingi582 – 5821Manganese 2By similarity
    Active sitei584 – 5841By similarity
    Binding sitei1934 – 19341Coenzyme ABy similarity
    Binding sitei2238 – 22381Coenzyme ABy similarity
    Binding sitei2240 – 22401Coenzyme ABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi458 – 4636ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. acetyl-CoA metabolic process Source: UniProtKB
    2. biotin metabolic process Source: Reactome
    3. carnitine shuttle Source: Reactome
    4. cellular lipid metabolic process Source: Reactome
    5. energy reserve metabolic process Source: Reactome
    6. fatty acid biosynthetic process Source: UniProtKB-KW
    7. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
    8. positive regulation of cellular metabolic process Source: Reactome
    9. protein homotetramerization Source: UniProtKB
    10. response to drug Source: Ensembl
    11. response to organic cyclic compound Source: Ensembl
    12. small molecule metabolic process Source: Reactome
    13. vitamin metabolic process Source: Reactome
    14. water-soluble vitamin metabolic process Source: Reactome

    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

    BioCyciMetaCyc:HS01211-MONOMER.
    BRENDAi6.4.1.2. 2681.
    ReactomeiREACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
    REACT_11153. Biotin transport and metabolism.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
    REACT_2122. ChREBP activates metabolic gene expression.
    SABIO-RKO00763.
    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA carboxylase 2 (EC:6.4.1.2)
    Alternative name(s):
    ACC-beta
    Including the following 1 domains:
    Biotin carboxylase (EC:6.3.4.14)
    Gene namesi
    Name:ACACB
    Synonyms:ACC2, ACCB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:85. ACACB.

    Subcellular locationi

    Endomembrane system
    Note: May associate with membranes.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endomembrane system Source: UniProtKB-SubCell
    3. mitochondrial outer membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24422.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24582458Acetyl-CoA carboxylase 2PRO_0000146767Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei222 – 2221Phosphoserine; by AMPK1 Publication
    Modified residuei929 – 9291N6-biotinyllysineBy similarity

    Post-translational modificationi

    Phosphorylated by AMPK, leading to inactivate the enzyme.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO00763.
    PaxDbiO00763.
    PRIDEiO00763.

    PTM databases

    PhosphoSiteiO00763.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiO00763.
    BgeeiO00763.
    CleanExiHS_ACACB.
    GenevestigatoriO00763.

    Organism-specific databases

    HPAiHPA006554.

    Interactioni

    Subunit structurei

    Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HLCSP507474EBI-2211739,EBI-3915568

    Protein-protein interaction databases

    BioGridi106550. 5 interactions.
    DIPiDIP-51617N.
    IntActiO00763. 5 interactions.
    MINTiMINT-6800190.
    STRINGi9606.ENSP00000367079.

    Structurei

    Secondary structure

    1
    2458
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi247 – 2537
    Beta strandi262 – 2654
    Helixi269 – 28719
    Beta strandi292 – 2998
    Helixi301 – 3055
    Helixi309 – 3135
    Beta strandi314 – 3196
    Helixi325 – 3273
    Turni328 – 3303
    Helixi332 – 34110
    Beta strandi345 – 3484
    Helixi353 – 3564
    Helixi359 – 3668
    Beta strandi370 – 3734
    Helixi376 – 3794
    Helixi385 – 39410
    Turni403 – 4064
    Helixi426 – 4316
    Helixi437 – 44711
    Beta strandi449 – 4557
    Beta strandi464 – 4674
    Turni470 – 4723
    Helixi473 – 48311
    Beta strandi489 – 4935
    Beta strandi496 – 50712
    Beta strandi509 – 5113
    Beta strandi513 – 52311
    Beta strandi524 – 5274
    Beta strandi530 – 5356
    Helixi541 – 55818
    Beta strandi562 – 57110
    Beta strandi572 – 5743
    Beta strandi576 – 5827
    Helixi589 – 5968
    Helixi600 – 6089
    Helixi613 – 6153
    Helixi617 – 6226
    Beta strandi635 – 6373
    Beta strandi646 – 6538
    Beta strandi669 – 6713
    Beta strandi679 – 6857
    Beta strandi700 – 70910
    Helixi710 – 72415
    Helixi728 – 7303
    Helixi732 – 74211
    Helixi744 – 7485
    Helixi754 – 7563
    Beta strandi896 – 8983
    Beta strandi900 – 9023
    Beta strandi903 – 9108
    Beta strandi914 – 9163
    Beta strandi921 – 9277
    Beta strandi930 – 9356
    Beta strandi937 – 9448
    Beta strandi957 – 9615
    Turni1698 – 17003
    Helixi1703 – 17119
    Helixi1717 – 17193
    Helixi1720 – 173213
    Beta strandi1742 – 17509
    Beta strandi1756 – 17594
    Beta strandi1767 – 177711
    Beta strandi1786 – 17938
    Helixi1798 – 18003
    Helixi1804 – 182017
    Beta strandi1824 – 18285
    Helixi1839 – 18424
    Beta strandi1846 – 18505
    Helixi1855 – 18573
    Beta strandi1859 – 18646
    Helixi1866 – 18727
    Turni1873 – 18764
    Beta strandi1878 – 18858
    Beta strandi1888 – 18969
    Beta strandi1899 – 19013
    Helixi1905 – 192420
    Beta strandi1927 – 19315
    Beta strandi1933 – 19364
    Helixi1938 – 19469
    Beta strandi1948 – 19525
    Beta strandi1956 – 19605
    Helixi1962 – 19698
    Helixi1977 – 19815
    Helixi1983 – 19864
    Turni1987 – 19904
    Beta strandi1993 – 19986
    Helixi1999 – 201012
    Helixi2045 – 20506
    Beta strandi2055 – 20573
    Beta strandi2072 – 20754
    Beta strandi2082 – 20898
    Beta strandi2092 – 20998
    Beta strandi2104 – 21085
    Beta strandi2120 – 21245
    Helixi2131 – 214717
    Beta strandi2151 – 21544
    Helixi2164 – 21685
    Helixi2171 – 218313
    Beta strandi2189 – 21935
    Beta strandi2198 – 22003
    Helixi2201 – 22055
    Helixi2209 – 22113
    Turni2213 – 22153
    Beta strandi2216 – 22216
    Beta strandi2225 – 22295
    Helixi2231 – 22388
    Helixi2241 – 225111
    Helixi2253 – 22619
    Helixi2269 – 229931
    Helixi2300 – 23023
    Helixi2304 – 23096
    Beta strandi2312 – 23176
    Helixi2319 – 23213
    Helixi2322 – 234423
    Helixi2345 – 23484
    Helixi2352 – 236514
    Helixi2369 – 23768
    Helixi2378 – 238811
    Helixi2404 – 242017
    Turni2423 – 24253
    Helixi2426 – 243510
    Helixi2439 – 244810

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliO00763.
    SMRiO00763. Positions 237-758, 891-960, 1695-2449.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00763.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini259 – 761503Biotin carboxylationAdd
    BLAST
    Domaini414 – 609196ATP-graspPROSITE-ProRule annotationAdd
    BLAST
    Domaini895 – 96167Biotinyl-bindingAdd
    BLAST
    Domaini1809 – 2305497CarboxyltransferaseAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0511.
    HOVERGENiHBG005371.
    KOiK11262.
    OMAiWRLRVAQ.
    OrthoDBiEOG7HXCPW.
    PhylomeDBiO00763.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: O00763-1) [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

    MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSKSEAN LIPSQEPFPA     50
    SDNSGETPQR NGEGHTLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP 100
    RNPLSSSDAA PSPELQANGT GTQGLEATDT NGLSSSARPQ GQQAGSPSKE 150
    DKKQANIKRQ LMTNFILGSF DDYSSDEDSV AGSSRESTRK GSRASLGALS 200
    LEAYLTTGEA ETRVPTMRPS MSGLHLVKRG REHKKLDLHR DFTVASPAEF 250
    VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT 300
    PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG 350
    WGHASENPKL PELLCKNGVA FLGPPSEAMW ALGDKIASTV VAQTLQVPTL 400
    PWSGSGLTVE WTEDDLQQGK RISVPEDVYD KGCVKDVDEG LEAAERIGFP 450
    LMIKASEGGG GKGIRKAESA EDFPILFRQV QSEIPGSPIF LMKLAQHARH 500
    LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP LAIFEFMEQC 550
    AIRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL 600
    PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA 650
    ARITSENPDE GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF 700
    GHCFSWGENR EEAISNMVVA LKELSIRGDF RTTVEYLINL LETESFQNND 750
    IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL NVADAMFRTC MTDFLHSLER 800
    GQVLPADSLL NLVDVELIYG GVKYILKVAR QSLTMFVLIM NGCHIEIDAH 850
    RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP 900
    SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQERG RVKYIKRPGA 950
    VLEAGCVVAR LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL 1000
    ENLTNVMSGF CLPEPVFSIK LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA 1050
    GRIPAPVEKS VRRVMAQYAS NITSVLCQFP SQQIATILDC HAATLQRKAD 1100
    REVFFINTQS IVQLVQRYRS GIRGYMKTVV LDLLRRYLRV EHHFQQAHYD 1150
    KCVINLREQF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD 1200
    ELISILNELT QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA 1250
    IDMYGHQFCP ENLKKLILSE TTIFDVLPTF FYHANKVVCM ASLEVYVRRG 1300
    YIAYELNSLQ HRQLPDGTCV VEFQFMLPSS HPNRMTVPIS ITNPDLLRHS 1350
    TELFMDSGFS PLCQRMGAMV AFRRFEDFTR NFDEVISCFA NVPKDTPLFS 1400
    EARTSLYSED DCKSLREEPI HILNVSIQCA DHLEDEALVP ILRTFVQSKK 1450
    NILVDYGLRR ITFLIAQEKE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL 1500
    ELNRMRNFDL TAVPCANHKM HLYLGAAKVK EGVEVTDHRF FIRAIIRHSD 1550
    LITKEASFEY LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV 1600
    IMDPFKIEES VRYMVMRYGS RLWKLRVLQA EVKINIRQTT TGSAVPIRLF 1650
    ITNESGYYLD ISLYKEVTDS RSGNIMFHSF GNKQGPQHGM LINTPYVTKD 1700
    LLQAKRFQAQ TLGTTYIYDF PEMFRQALFK LWGSPDKYPK DILTYTELVL 1750
    DSQGQLVEMN RLPGGNEVGM VAFKMRFKTQ EYPEGRDVIV IGNDITFRIG 1800
    SFGPGEDLLY LRASEMARAE GIPKIYVAAN SGARIGMAEE IKHMFHVAWV 1850
    DPEDPHKGFK YLYLTPQDYT RISSLNSVHC KHIEEGGESR YMITDIIGKD 1900
    DGLGVENLRG SGMIAGESSL AYEEIVTISL VTCRAIGIGA YLVRLGQRVI 1950
    QVENSHIILT GASALNKVLG REVYTSNNQL GGVQIMHYNG VSHITVPDDF 2000
    EGVYTILEWL SYMPKDNHSP VPIITPTDPI DREIEFLPSR APYDPRWMLA 2050
    GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE 2100
    TRTVEVAVPA DPANLDSEAK IIQQAGQVWF PDSAYKTAQA VKDFNREKLP 2150
    LMIFANWRGF SGGMKDMYDQ VLKFGAYIVD GLRQYKQPIL IYIPPYAELR 2200
    GGSWVVIDAT INPLCIEMYA DKESRGGVLE PEGTVEIKFR KKDLIKSMRR 2250
    IDPAYKKLME QLGEPDLSDK DRKDLEGRLK AREDLLLPIY HQVAVQFADF 2300
    HDTPGRMLEK GVISDILEWK TARTFLYWRL RRLLLEDQVK QEILQASGEL 2350
    SHVHIQSMLR RWFVETEGAV KAYLWDNNQV VVQWLEQHWQ AGDGPRSTIR 2400
    ENITYLKHDS VLKTIRGLVE ENPEVAVDCV IYLSQHISPA ERAQVVHLLS 2450
    TMDSPAST 2458
    Length:2,458
    Mass (Da):276,541
    Last modified:October 5, 2010 - v3
    Checksum:iED12674A1A8A0706
    GO
    Isoform Short (identifier: O00763-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:2,388
    Mass (Da):268,166
    Checksum:i10A218FFD1408B68
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91C → R in ABF48723. (PubMed:16854592)Curated
    Sequence conflicti120 – 1201T → I in AAR37018. 1 PublicationCurated
    Sequence conflicti422 – 4221I → T in AAR37018. 1 PublicationCurated
    Sequence conflicti1340 – 13401S → N in AAC50571. (PubMed:8670171)Curated
    Sequence conflicti1383 – 13831D → G in AAC50571. (PubMed:8670171)Curated
    Sequence conflicti1425 – 14251V → M in AAC50571. (PubMed:8670171)Curated
    Sequence conflicti1819 – 18213AEG → PEA in AAC50571. (PubMed:8670171)Curated
    Sequence conflicti1892 – 18932MI → IM in AAC50571. (PubMed:8670171)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti193 – 1931R → L in a pancreatic ductal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_062667
    Natural varianti552 – 5521I → V.
    Corresponds to variant rs16940029 [ dbSNP | Ensembl ].
    VAR_031255
    Natural varianti651 – 6511A → T.
    Corresponds to variant rs2300455 [ dbSNP | Ensembl ].
    VAR_031256
    Natural varianti2141 – 21411V → I.2 Publications
    Corresponds to variant rs2075260 [ dbSNP | Ensembl ].
    VAR_031257

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1118 – 118770Missing in isoform Short. 1 PublicationVSP_000547Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS31898.1. [O00763-1]
    PIRiS71091.
    RefSeqiNP_001084.3. NM_001093.3. [O00763-1]
    XP_005253933.1. XM_005253876.2. [O00763-1]
    XP_006719428.1. XM_006719365.1. [O00763-1]
    UniGeneiHs.234898.

    Genome annotation databases

    EnsembliENST00000338432; ENSP00000341044; ENSG00000076555. [O00763-1]
    ENST00000377848; ENSP00000367079; ENSG00000076555. [O00763-1]
    GeneIDi32.
    KEGGihsa:32.
    UCSCiuc001tob.3. human. [O00763-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS31898.1. [O00763-1 ]
    PIRi S71091.
    RefSeqi NP_001084.3. NM_001093.3. [O00763-1 ]
    XP_005253933.1. XM_005253876.2. [O00763-1 ]
    XP_006719428.1. XM_006719365.1. [O00763-1 ]
    UniGenei Hs.234898.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DN8 NMR - A 885-971 [» ]
    2HJW X-ray 2.50 A 217-775 [» ]
    2KCC NMR - A 891-965 [» ]
    3FF6 X-ray 3.19 A/B/C/D 1693-2450 [» ]
    3GID X-ray 2.30 A/B 238-760 [» ]
    3GLK X-ray 2.10 A 238-760 [» ]
    3JRW X-ray 2.60 A 217-775 [» ]
    3JRX X-ray 2.50 A 217-775 [» ]
    3TDC X-ray 2.41 A 1690-2445 [» ]
    4HQ6 X-ray 2.70 A 217-776 [» ]
    ProteinModelPortali O00763.
    SMRi O00763. Positions 237-758, 891-960, 1695-2449.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106550. 5 interactions.
    DIPi DIP-51617N.
    IntActi O00763. 5 interactions.
    MINTi MINT-6800190.
    STRINGi 9606.ENSP00000367079.

    Chemistry

    BindingDBi O00763.
    ChEMBLi CHEMBL4829.
    DrugBanki DB00173. Adenine.
    DB00121. Biotin.
    GuidetoPHARMACOLOGYi 1264.

    PTM databases

    PhosphoSitei O00763.

    Proteomic databases

    MaxQBi O00763.
    PaxDbi O00763.
    PRIDEi O00763.

    Protocols and materials databases

    DNASUi 32.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338432 ; ENSP00000341044 ; ENSG00000076555 . [O00763-1 ]
    ENST00000377848 ; ENSP00000367079 ; ENSG00000076555 . [O00763-1 ]
    GeneIDi 32.
    KEGGi hsa:32.
    UCSCi uc001tob.3. human. [O00763-1 ]

    Organism-specific databases

    CTDi 32.
    GeneCardsi GC12P109577.
    H-InvDB HIX0036741.
    HGNCi HGNC:85. ACACB.
    HPAi HPA006554.
    MIMi 601557. gene.
    neXtProti NX_O00763.
    PharmGKBi PA24422.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0511.
    HOVERGENi HBG005371.
    KOi K11262.
    OMAi WRLRVAQ.
    OrthoDBi EOG7HXCPW.
    PhylomeDBi O00763.
    TreeFami TF300061.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .
    BioCyci MetaCyc:HS01211-MONOMER.
    BRENDAi 6.4.1.2. 2681.
    Reactomei REACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
    REACT_11153. Biotin transport and metabolism.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
    REACT_2122. ChREBP activates metabolic gene expression.
    SABIO-RK O00763.

    Miscellaneous databases

    EvolutionaryTracei O00763.
    GeneWikii ACACB.
    GenomeRNAii 32.
    NextBioi 123.
    PROi O00763.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00763.
    Bgeei O00763.
    CleanExi HS_ACACB.
    Genevestigatori O00763.

    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

    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.
      , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-193.

    Entry informationi

    Entry nameiACACB_HUMAN
    AccessioniPrimary (citable) accession number: O00763
    Secondary accession number(s): A6NK36
    , Q16852, Q1HEC1, Q6KE87, Q6KE89, Q6TY48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 146 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3