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Protein

Acetyl-CoA carboxylase 2

Gene

ACACB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in inhibition of fatty acid and glucose oxidation and enhancement of fat storage (By similarity). May play a role in regulation of mitochondrial fatty acid oxidation through malonyl-CoA-dependent inhibition of carnitine palmitoyltransferase 1 (By similarity).By similarity1 Publication

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.2 Publications
ATP + biotin-[carboxyl-carrier-protein] + HCO3- = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].By similarity

Cofactori

Protein has several cofactor binding sites:

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=110 µM for ATP (isoform 2)1 Publication
  3. KM=58 µM for acetyl-CoA1 Publication
  4. KM=94 µM for acetyl-CoA (isoform 3)1 Publication
  5. KM=6.5 mM for NaHCO3 (isoform 3)1 Publication
  6. KM=3.0 mM for NaHCO31 Publication

    Pathwayi: malonyl-CoA biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
    Proteins known to be involved in this subpathway in this organism are:
    1. Acetyl-CoA carboxylase 1 (ACACA), Acetyl-CoA carboxylase 2 (ACACB)
    This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi567Manganese 1By similarity1
    Metal bindingi580Manganese 1By similarity1
    Metal bindingi580Manganese 2By similarity1
    Metal bindingi582Manganese 2By similarity1
    Active sitei584By similarity1
    Binding sitei1934Coenzyme ABy similarity1
    Binding sitei2238Coenzyme ABy similarity1
    Binding sitei2240Coenzyme ABy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi458 – 463ATPPROSITE-ProRule annotation6

    GO - Molecular functioni

    GO - Biological processi

    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

    BioCyciMetaCyc:HS01211-MONOMER.
    ZFISH:HS01211-MONOMER.
    BRENDAi6.3.4.14. 2681.
    6.4.1.2. 2681.
    ReactomeiR-HSA-163765. ChREBP activates metabolic gene expression.
    R-HSA-196780. Biotin transport and metabolism.
    R-HSA-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
    R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
    R-HSA-3371599. Defective HLCS causes multiple carboxylase deficiency.
    SABIO-RKO00763.
    SIGNORiO00763.
    UniPathwayiUPA00655; UER00711.

    Chemistry databases

    SwissLipidsiSLP:000000730.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA carboxylase 2 (EC:6.4.1.22 Publications)
    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
    Proteomesi
    • UP000005640 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:85. ACACB.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: Reactome
    • endomembrane system Source: UniProtKB-SubCell
    • mitochondrial outer membrane Source: Reactome
    • mitochondrion Source: UniProtKB
    • nucleus Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Nucleus

    Pathology & Biotechi

    Biotechnological usei

    Inhibition of ACACB may prevent lipid-induced insulin resistance and type 2 diabetes, making the enzyme a potential pharmaceutical target for treatment of obesity and type 2 diabetes.Curated

    Organism-specific databases

    DisGeNETi32.
    OpenTargetsiENSG00000076555.
    PharmGKBiPA24422.

    Chemistry databases

    ChEMBLiCHEMBL4829.
    DrugBankiDB00173. Adenine.
    DB00121. Biotin.
    GuidetoPHARMACOLOGYi1264.

    Polymorphism and mutation databases

    BioMutaiACACB.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_0000146767? – 2458Acetyl-CoA carboxylase 2Curated
    Transit peptidei1 – ?MitochondrionBy similarity

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei35PhosphoserineCombined sources1
    Modified residuei70PhosphothreonineCombined sources1
    Modified residuei91PhosphoserineCombined sources1
    Modified residuei95PhosphoserineCombined sources1
    Modified residuei200PhosphoserineCombined sources1
    Modified residuei207PhosphothreonineBy similarity1
    Modified residuei222Phosphoserine; by AMPK1 Publication1
    Modified residuei469PhosphoserineCombined sources1
    Modified residuei929N6-biotinyllysinePROSITE-ProRule annotationBy similarity1
    Modified residuei1340PhosphoserineBy similarity1
    Modified residuei1342PhosphothreonineCombined sources1
    Modified residuei1360PhosphoserineBy similarity1

    Post-translational modificationi

    Phosphorylated by AMPK, leading to inactivation of the enzyme. Required for the maintenance of skeletal muscle lipid and glucose homeostasis (By similarity).By similarity1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    EPDiO00763.
    MaxQBiO00763.
    PaxDbiO00763.
    PeptideAtlasiO00763.
    PRIDEiO00763.

    PTM databases

    iPTMnetiO00763.
    PhosphoSitePlusiO00763.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in heart, skeletal muscle, liver, adipose tissue, mammary gland, adrenal gland and colon (PubMed:9099716). Isoform 3 is expressed in skeletal muscle, adipose tissue and liver (at protein level) (PubMed:19190759). Isoform 3 is detected at high levels in adipose tissue with lower levels in heart, liver, skeletal muscle and testis (PubMed:19190759).2 Publications

    Gene expression databases

    BgeeiENSG00000076555.
    CleanExiHS_ACACB.
    ExpressionAtlasiO00763. baseline and differential.
    GenevisibleiO00763. HS.

    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. 13 interactors.
    DIPiDIP-51617N.
    IntActiO00763. 6 interactors.
    MINTiMINT-6800190.
    STRINGi9606.ENSP00000341044.

    Chemistry databases

    BindingDBiO00763.

    Structurei

    Secondary structure

    12458
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi247 – 253Combined sources7
    Beta strandi262 – 265Combined sources4
    Helixi269 – 287Combined sources19
    Beta strandi292 – 299Combined sources8
    Helixi301 – 305Combined sources5
    Helixi309 – 313Combined sources5
    Beta strandi314 – 319Combined sources6
    Helixi325 – 327Combined sources3
    Turni328 – 330Combined sources3
    Helixi332 – 341Combined sources10
    Beta strandi345 – 348Combined sources4
    Helixi353 – 356Combined sources4
    Helixi359 – 366Combined sources8
    Beta strandi370 – 373Combined sources4
    Helixi376 – 379Combined sources4
    Helixi385 – 394Combined sources10
    Turni403 – 406Combined sources4
    Helixi426 – 431Combined sources6
    Helixi437 – 447Combined sources11
    Beta strandi449 – 455Combined sources7
    Beta strandi464 – 467Combined sources4
    Turni470 – 472Combined sources3
    Helixi473 – 483Combined sources11
    Beta strandi489 – 493Combined sources5
    Beta strandi496 – 507Combined sources12
    Beta strandi509 – 511Combined sources3
    Beta strandi513 – 523Combined sources11
    Beta strandi524 – 527Combined sources4
    Beta strandi530 – 535Combined sources6
    Helixi541 – 558Combined sources18
    Beta strandi562 – 571Combined sources10
    Beta strandi572 – 574Combined sources3
    Beta strandi576 – 582Combined sources7
    Helixi589 – 596Combined sources8
    Helixi600 – 608Combined sources9
    Helixi613 – 615Combined sources3
    Helixi617 – 622Combined sources6
    Beta strandi635 – 637Combined sources3
    Beta strandi646 – 653Combined sources8
    Beta strandi669 – 671Combined sources3
    Beta strandi679 – 685Combined sources7
    Beta strandi700 – 709Combined sources10
    Helixi710 – 724Combined sources15
    Helixi728 – 730Combined sources3
    Helixi732 – 742Combined sources11
    Helixi744 – 748Combined sources5
    Helixi754 – 756Combined sources3
    Beta strandi896 – 898Combined sources3
    Beta strandi900 – 902Combined sources3
    Beta strandi903 – 910Combined sources8
    Beta strandi914 – 916Combined sources3
    Beta strandi921 – 927Combined sources7
    Beta strandi930 – 935Combined sources6
    Beta strandi937 – 944Combined sources8
    Beta strandi957 – 961Combined sources5
    Turni1698 – 1700Combined sources3
    Helixi1703 – 1711Combined sources9
    Helixi1717 – 1719Combined sources3
    Helixi1720 – 1732Combined sources13
    Beta strandi1742 – 1750Combined sources9
    Beta strandi1756 – 1759Combined sources4
    Beta strandi1767 – 1777Combined sources11
    Beta strandi1786 – 1793Combined sources8
    Helixi1798 – 1800Combined sources3
    Helixi1804 – 1820Combined sources17
    Beta strandi1824 – 1828Combined sources5
    Helixi1839 – 1842Combined sources4
    Beta strandi1846 – 1850Combined sources5
    Helixi1855 – 1857Combined sources3
    Beta strandi1859 – 1864Combined sources6
    Helixi1866 – 1872Combined sources7
    Turni1873 – 1876Combined sources4
    Beta strandi1878 – 1885Combined sources8
    Beta strandi1888 – 1896Combined sources9
    Beta strandi1899 – 1901Combined sources3
    Helixi1905 – 1924Combined sources20
    Beta strandi1927 – 1931Combined sources5
    Beta strandi1933 – 1936Combined sources4
    Helixi1938 – 1946Combined sources9
    Beta strandi1948 – 1952Combined sources5
    Beta strandi1956 – 1960Combined sources5
    Helixi1962 – 1969Combined sources8
    Helixi1977 – 1981Combined sources5
    Helixi1983 – 1986Combined sources4
    Turni1987 – 1990Combined sources4
    Beta strandi1993 – 1998Combined sources6
    Helixi1999 – 2010Combined sources12
    Helixi2045 – 2050Combined sources6
    Beta strandi2055 – 2057Combined sources3
    Beta strandi2072 – 2075Combined sources4
    Beta strandi2082 – 2089Combined sources8
    Beta strandi2092 – 2099Combined sources8
    Beta strandi2104 – 2108Combined sources5
    Beta strandi2120 – 2124Combined sources5
    Helixi2131 – 2147Combined sources17
    Beta strandi2151 – 2154Combined sources4
    Helixi2164 – 2168Combined sources5
    Helixi2171 – 2183Combined sources13
    Beta strandi2189 – 2193Combined sources5
    Beta strandi2198 – 2200Combined sources3
    Helixi2201 – 2205Combined sources5
    Helixi2209 – 2211Combined sources3
    Turni2213 – 2215Combined sources3
    Beta strandi2216 – 2221Combined sources6
    Beta strandi2225 – 2229Combined sources5
    Helixi2231 – 2238Combined sources8
    Helixi2241 – 2251Combined sources11
    Helixi2253 – 2261Combined sources9
    Helixi2269 – 2299Combined sources31
    Helixi2300 – 2302Combined sources3
    Helixi2304 – 2309Combined sources6
    Beta strandi2312 – 2317Combined sources6
    Helixi2319 – 2321Combined sources3
    Helixi2322 – 2344Combined sources23
    Helixi2345 – 2348Combined sources4
    Helixi2352 – 2365Combined sources14
    Helixi2369 – 2376Combined sources8
    Helixi2378 – 2388Combined sources11
    Helixi2404 – 2420Combined sources17
    Turni2423 – 2425Combined sources3
    Helixi2426 – 2435Combined sources10
    Helixi2439 – 2448Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5KKNX-ray2.60B/C238-760[»]
    ProteinModelPortaliO00763.
    SMRiO00763.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00763.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini259 – 761Biotin carboxylationAdd BLAST503
    Domaini414 – 609ATP-graspPROSITE-ProRule annotationAdd BLAST196
    Domaini888 – 962Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST75
    Domaini1695 – 2025CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST331
    Domaini2029 – 2345CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST317

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1695 – 2345CarboxyltransferasePROSITE-ProRule annotationAdd BLAST651

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
    Contains 1 biotin carboxylation domain.Curated
    Contains 1 biotinyl-binding domain.PROSITE-ProRule annotationCurated
    Contains 1 CoA carboxyltransferase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 CoA carboxyltransferase N-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG0368. Eukaryota.
    COG0439. LUCA.
    COG0511. LUCA.
    COG4799. LUCA.
    GeneTreeiENSGT00550000074703.
    HOVERGENiHBG005371.
    InParanoidiO00763.
    KOiK01946.
    OMAiMTDSKPI.
    OrthoDBiEOG091G02ND.
    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.
    IPR005481. BC-like_N.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    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.
    PF00289. Biotin_carb_N. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF01039. Carboxyl_trans. 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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: O00763-1) [UniParc]FASTAAdd to basket
    Also known as: Long

    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

            10         20         30         40         50
    MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSKSEAN LIPSQEPFPA
    60 70 80 90 100
    SDNSGETPQR NGEGHTLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP
    110 120 130 140 150
    RNPLSSSDAA PSPELQANGT GTQGLEATDT NGLSSSARPQ GQQAGSPSKE
    160 170 180 190 200
    DKKQANIKRQ LMTNFILGSF DDYSSDEDSV AGSSRESTRK GSRASLGALS
    210 220 230 240 250
    LEAYLTTGEA ETRVPTMRPS MSGLHLVKRG REHKKLDLHR DFTVASPAEF
    260 270 280 290 300
    VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT
    310 320 330 340 350
    PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG
    360 370 380 390 400
    WGHASENPKL PELLCKNGVA FLGPPSEAMW ALGDKIASTV VAQTLQVPTL
    410 420 430 440 450
    PWSGSGLTVE WTEDDLQQGK RISVPEDVYD KGCVKDVDEG LEAAERIGFP
    460 470 480 490 500
    LMIKASEGGG GKGIRKAESA EDFPILFRQV QSEIPGSPIF LMKLAQHARH
    510 520 530 540 550
    LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP LAIFEFMEQC
    560 570 580 590 600
    AIRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL
    610 620 630 640 650
    PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA
    660 670 680 690 700
    ARITSENPDE GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF
    710 720 730 740 750
    GHCFSWGENR EEAISNMVVA LKELSIRGDF RTTVEYLINL LETESFQNND
    760 770 780 790 800
    IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL NVADAMFRTC MTDFLHSLER
    810 820 830 840 850
    GQVLPADSLL NLVDVELIYG GVKYILKVAR QSLTMFVLIM NGCHIEIDAH
    860 870 880 890 900
    RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP
    910 920 930 940 950
    SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQERG RVKYIKRPGA
    960 970 980 990 1000
    VLEAGCVVAR LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL
    1010 1020 1030 1040 1050
    ENLTNVMSGF CLPEPVFSIK LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA
    1060 1070 1080 1090 1100
    GRIPAPVEKS VRRVMAQYAS NITSVLCQFP SQQIATILDC HAATLQRKAD
    1110 1120 1130 1140 1150
    REVFFINTQS IVQLVQRYRS GIRGYMKTVV LDLLRRYLRV EHHFQQAHYD
    1160 1170 1180 1190 1200
    KCVINLREQF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD
    1210 1220 1230 1240 1250
    ELISILNELT QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA
    1260 1270 1280 1290 1300
    IDMYGHQFCP ENLKKLILSE TTIFDVLPTF FYHANKVVCM ASLEVYVRRG
    1310 1320 1330 1340 1350
    YIAYELNSLQ HRQLPDGTCV VEFQFMLPSS HPNRMTVPIS ITNPDLLRHS
    1360 1370 1380 1390 1400
    TELFMDSGFS PLCQRMGAMV AFRRFEDFTR NFDEVISCFA NVPKDTPLFS
    1410 1420 1430 1440 1450
    EARTSLYSED DCKSLREEPI HILNVSIQCA DHLEDEALVP ILRTFVQSKK
    1460 1470 1480 1490 1500
    NILVDYGLRR ITFLIAQEKE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL
    1510 1520 1530 1540 1550
    ELNRMRNFDL TAVPCANHKM HLYLGAAKVK EGVEVTDHRF FIRAIIRHSD
    1560 1570 1580 1590 1600
    LITKEASFEY LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV
    1610 1620 1630 1640 1650
    IMDPFKIEES VRYMVMRYGS RLWKLRVLQA EVKINIRQTT TGSAVPIRLF
    1660 1670 1680 1690 1700
    ITNESGYYLD ISLYKEVTDS RSGNIMFHSF GNKQGPQHGM LINTPYVTKD
    1710 1720 1730 1740 1750
    LLQAKRFQAQ TLGTTYIYDF PEMFRQALFK LWGSPDKYPK DILTYTELVL
    1760 1770 1780 1790 1800
    DSQGQLVEMN RLPGGNEVGM VAFKMRFKTQ EYPEGRDVIV IGNDITFRIG
    1810 1820 1830 1840 1850
    SFGPGEDLLY LRASEMARAE GIPKIYVAAN SGARIGMAEE IKHMFHVAWV
    1860 1870 1880 1890 1900
    DPEDPHKGFK YLYLTPQDYT RISSLNSVHC KHIEEGGESR YMITDIIGKD
    1910 1920 1930 1940 1950
    DGLGVENLRG SGMIAGESSL AYEEIVTISL VTCRAIGIGA YLVRLGQRVI
    1960 1970 1980 1990 2000
    QVENSHIILT GASALNKVLG REVYTSNNQL GGVQIMHYNG VSHITVPDDF
    2010 2020 2030 2040 2050
    EGVYTILEWL SYMPKDNHSP VPIITPTDPI DREIEFLPSR APYDPRWMLA
    2060 2070 2080 2090 2100
    GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE
    2110 2120 2130 2140 2150
    TRTVEVAVPA DPANLDSEAK IIQQAGQVWF PDSAYKTAQA VKDFNREKLP
    2160 2170 2180 2190 2200
    LMIFANWRGF SGGMKDMYDQ VLKFGAYIVD GLRQYKQPIL IYIPPYAELR
    2210 2220 2230 2240 2250
    GGSWVVIDAT INPLCIEMYA DKESRGGVLE PEGTVEIKFR KKDLIKSMRR
    2260 2270 2280 2290 2300
    IDPAYKKLME QLGEPDLSDK DRKDLEGRLK AREDLLLPIY HQVAVQFADF
    2310 2320 2330 2340 2350
    HDTPGRMLEK GVISDILEWK TARTFLYWRL RRLLLEDQVK QEILQASGEL
    2360 2370 2380 2390 2400
    SHVHIQSMLR RWFVETEGAV KAYLWDNNQV VVQWLEQHWQ AGDGPRSTIR
    2410 2420 2430 2440 2450
    ENITYLKHDS VLKTIRGLVE ENPEVAVDCV IYLSQHISPA ERAQVVHLLS

    TMDSPAST
    Length:2,458
    Mass (Da):276,541
    Last modified:October 5, 2010 - v3
    Checksum:iED12674A1A8A0706
    GO
    Isoform 2 (identifier: O00763-2) [UniParc]FASTAAdd to basket
    Also known as: Short

    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
    Isoform 3Curated (identifier: O00763-3) [UniParc]FASTAAdd to basket
    Also known as: ACC2.v21 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         1-202: Missing.
         203-218: AYLTTGEAETRVPTMR → MSPAKCKICFPDREVK

    Show »
    Length:2,256
    Mass (Da):255,093
    Checksum:iA0736151D792EC18
    GO

    Sequence cautioni

    The sequence AAB58382 differs from that shown. Many Frameshifts and conflicts.Curated
    The sequence CAE01470 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti9C → R in ABF48723 (PubMed:16854592).Curated1
    Sequence conflicti120T → I in AAR37018 (Ref. 4) Curated1
    Sequence conflicti422I → T in AAR37018 (Ref. 4) Curated1
    Sequence conflicti1340S → N in AAC50571 (PubMed:8670171).Curated1
    Sequence conflicti1383D → G in AAC50571 (PubMed:8670171).Curated1
    Sequence conflicti1425V → M in AAC50571 (PubMed:8670171).Curated1
    Sequence conflicti1819 – 1821AEG → PEA in AAC50571 (PubMed:8670171).Curated3
    Sequence conflicti1892 – 1893MI → IM in AAC50571 (PubMed:8670171).Curated2

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_062667193R → L in a pancreatic ductal adenocarcinoma sample; somatic mutation. 1 Publication1
    Natural variantiVAR_031255552I → V.Corresponds to variant rs16940029dbSNPEnsembl.1
    Natural variantiVAR_031256651A → T.Corresponds to variant rs2300455dbSNPEnsembl.1
    Natural variantiVAR_0312572141V → I.2 PublicationsCorresponds to variant rs2075260dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0570811 – 202Missing in isoform 3. 1 PublicationAdd BLAST202
    Alternative sequenceiVSP_057082203 – 218AYLTT…VPTMR → MSPAKCKICFPDREVK in isoform 3. 1 PublicationAdd BLAST16
    Alternative sequenceiVSP_0005471118 – 1187Missing in isoform 2. 1 PublicationAdd BLAST70

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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_005253876.4. [O00763-1]
    XP_006719430.1. XM_006719367.3. [O00763-3]
    XP_011536561.1. XM_011538259.2. [O00763-1]
    UniGeneiHs.234898.
    Hs.676621.

    Genome annotation databases

    EnsembliENST00000338432; ENSP00000341044; ENSG00000076555. [O00763-1]
    ENST00000377848; ENSP00000367079; ENSG00000076555. [O00763-1]
    GeneIDi32.
    KEGGihsa:32.
    UCSCiuc001tob.4. human. [O00763-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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_005253876.4. [O00763-1]
    XP_006719430.1. XM_006719367.3. [O00763-3]
    XP_011536561.1. XM_011538259.2. [O00763-1]
    UniGeneiHs.234898.
    Hs.676621.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5KKNX-ray2.60B/C238-760[»]
    ProteinModelPortaliO00763.
    SMRiO00763.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi106550. 13 interactors.
    DIPiDIP-51617N.
    IntActiO00763. 6 interactors.
    MINTiMINT-6800190.
    STRINGi9606.ENSP00000341044.

    Chemistry databases

    BindingDBiO00763.
    ChEMBLiCHEMBL4829.
    DrugBankiDB00173. Adenine.
    DB00121. Biotin.
    GuidetoPHARMACOLOGYi1264.
    SwissLipidsiSLP:000000730.

    PTM databases

    iPTMnetiO00763.
    PhosphoSitePlusiO00763.

    Polymorphism and mutation databases

    BioMutaiACACB.

    Proteomic databases

    EPDiO00763.
    MaxQBiO00763.
    PaxDbiO00763.
    PeptideAtlasiO00763.
    PRIDEiO00763.

    Protocols and materials databases

    DNASUi32.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000338432; ENSP00000341044; ENSG00000076555. [O00763-1]
    ENST00000377848; ENSP00000367079; ENSG00000076555. [O00763-1]
    GeneIDi32.
    KEGGihsa:32.
    UCSCiuc001tob.4. human. [O00763-1]

    Organism-specific databases

    CTDi32.
    DisGeNETi32.
    GeneCardsiACACB.
    H-InvDBHIX0036741.
    HGNCiHGNC:85. ACACB.
    HPAiHPA006554.
    MIMi601557. gene.
    neXtProtiNX_O00763.
    OpenTargetsiENSG00000076555.
    PharmGKBiPA24422.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0368. Eukaryota.
    COG0439. LUCA.
    COG0511. LUCA.
    COG4799. LUCA.
    GeneTreeiENSGT00550000074703.
    HOVERGENiHBG005371.
    InParanoidiO00763.
    KOiK01946.
    OMAiMTDSKPI.
    OrthoDBiEOG091G02ND.
    PhylomeDBiO00763.
    TreeFamiTF300061.

    Enzyme and pathway databases

    UniPathwayiUPA00655; UER00711.
    BioCyciMetaCyc:HS01211-MONOMER.
    ZFISH:HS01211-MONOMER.
    BRENDAi6.3.4.14. 2681.
    6.4.1.2. 2681.
    ReactomeiR-HSA-163765. ChREBP activates metabolic gene expression.
    R-HSA-196780. Biotin transport and metabolism.
    R-HSA-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
    R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
    R-HSA-3371599. Defective HLCS causes multiple carboxylase deficiency.
    SABIO-RKO00763.
    SIGNORiO00763.

    Miscellaneous databases

    ChiTaRSiACACB. human.
    EvolutionaryTraceiO00763.
    GeneWikiiACACB.
    GenomeRNAii32.
    PROiO00763.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000076555.
    CleanExiHS_ACACB.
    ExpressionAtlasiO00763. baseline and differential.
    GenevisibleiO00763. HS.

    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.
    IPR005481. BC-like_N.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    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.
    PF00289. Biotin_carb_N. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF01039. Carboxyl_trans. 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]
    ProtoNetiSearch...

    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: November 2, 2016
    This is version 169 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.