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O00763

- ACACB_HUMAN

UniProt

O00763 - ACACB_HUMAN

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Protein

Acetyl-CoA carboxylase 2

Gene

ACACB

Organism
Homo sapiens (Human)
Status
Reviewed - 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] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].By similarity

Cofactori

Protein has several cofactor binding sites:
  • biotinBy similarityNote: Biotin.By similarity
  • Mn2+By similarityNote: 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=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

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

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
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.
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:6.4.1.22 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
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:85. ACACB.

Subcellular locationi

Mitochondrion 1 Publication. Nucleus 1 Publication. Endomembrane system
Note: May associate with membranes.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrial outer membrane Source: Reactome
  3. mitochondrion Source: UniProtKB
  4. 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

PharmGKBiPA24422.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 2458Acetyl-CoA carboxylase 2CuratedPRO_0000146767
Transit peptidei1 – ?MitochondrionBy similarity

Amino acid modifications

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

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

MaxQBiO00763.
PaxDbiO00763.
PRIDEiO00763.

PTM databases

PhosphoSiteiO00763.

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

BgeeiO00763.
CleanExiHS_ACACB.
ExpressionAtlasiO00763. baseline and differential.
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 – 2537Combined sources
Beta strandi262 – 2654Combined sources
Helixi269 – 28719Combined sources
Beta strandi292 – 2998Combined sources
Helixi301 – 3055Combined sources
Helixi309 – 3135Combined sources
Beta strandi314 – 3196Combined sources
Helixi325 – 3273Combined sources
Turni328 – 3303Combined sources
Helixi332 – 34110Combined sources
Beta strandi345 – 3484Combined sources
Helixi353 – 3564Combined sources
Helixi359 – 3668Combined sources
Beta strandi370 – 3734Combined sources
Helixi376 – 3794Combined sources
Helixi385 – 39410Combined sources
Turni403 – 4064Combined sources
Helixi426 – 4316Combined sources
Helixi437 – 44711Combined sources
Beta strandi449 – 4557Combined sources
Beta strandi464 – 4674Combined sources
Turni470 – 4723Combined sources
Helixi473 – 48311Combined sources
Beta strandi489 – 4935Combined sources
Beta strandi496 – 50712Combined sources
Beta strandi509 – 5113Combined sources
Beta strandi513 – 52311Combined sources
Beta strandi524 – 5274Combined sources
Beta strandi530 – 5356Combined sources
Helixi541 – 55818Combined sources
Beta strandi562 – 57110Combined sources
Beta strandi572 – 5743Combined sources
Beta strandi576 – 5827Combined sources
Helixi589 – 5968Combined sources
Helixi600 – 6089Combined sources
Helixi613 – 6153Combined sources
Helixi617 – 6226Combined sources
Beta strandi635 – 6373Combined sources
Beta strandi646 – 6538Combined sources
Beta strandi669 – 6713Combined sources
Beta strandi679 – 6857Combined sources
Beta strandi700 – 70910Combined sources
Helixi710 – 72415Combined sources
Helixi728 – 7303Combined sources
Helixi732 – 74211Combined sources
Helixi744 – 7485Combined sources
Helixi754 – 7563Combined sources
Beta strandi896 – 8983Combined sources
Beta strandi900 – 9023Combined sources
Beta strandi903 – 9108Combined sources
Beta strandi914 – 9163Combined sources
Beta strandi921 – 9277Combined sources
Beta strandi930 – 9356Combined sources
Beta strandi937 – 9448Combined sources
Beta strandi957 – 9615Combined sources
Turni1698 – 17003Combined sources
Helixi1703 – 17119Combined sources
Helixi1717 – 17193Combined sources
Helixi1720 – 173213Combined sources
Beta strandi1742 – 17509Combined sources
Beta strandi1756 – 17594Combined sources
Beta strandi1767 – 177711Combined sources
Beta strandi1786 – 17938Combined sources
Helixi1798 – 18003Combined sources
Helixi1804 – 182017Combined sources
Beta strandi1824 – 18285Combined sources
Helixi1839 – 18424Combined sources
Beta strandi1846 – 18505Combined sources
Helixi1855 – 18573Combined sources
Beta strandi1859 – 18646Combined sources
Helixi1866 – 18727Combined sources
Turni1873 – 18764Combined sources
Beta strandi1878 – 18858Combined sources
Beta strandi1888 – 18969Combined sources
Beta strandi1899 – 19013Combined sources
Helixi1905 – 192420Combined sources
Beta strandi1927 – 19315Combined sources
Beta strandi1933 – 19364Combined sources
Helixi1938 – 19469Combined sources
Beta strandi1948 – 19525Combined sources
Beta strandi1956 – 19605Combined sources
Helixi1962 – 19698Combined sources
Helixi1977 – 19815Combined sources
Helixi1983 – 19864Combined sources
Turni1987 – 19904Combined sources
Beta strandi1993 – 19986Combined sources
Helixi1999 – 201012Combined sources
Helixi2045 – 20506Combined sources
Beta strandi2055 – 20573Combined sources
Beta strandi2072 – 20754Combined sources
Beta strandi2082 – 20898Combined sources
Beta strandi2092 – 20998Combined sources
Beta strandi2104 – 21085Combined sources
Beta strandi2120 – 21245Combined sources
Helixi2131 – 214717Combined sources
Beta strandi2151 – 21544Combined sources
Helixi2164 – 21685Combined sources
Helixi2171 – 218313Combined sources
Beta strandi2189 – 21935Combined sources
Beta strandi2198 – 22003Combined sources
Helixi2201 – 22055Combined sources
Helixi2209 – 22113Combined sources
Turni2213 – 22153Combined sources
Beta strandi2216 – 22216Combined sources
Beta strandi2225 – 22295Combined sources
Helixi2231 – 22388Combined sources
Helixi2241 – 225111Combined sources
Helixi2253 – 22619Combined sources
Helixi2269 – 229931Combined sources
Helixi2300 – 23023Combined sources
Helixi2304 – 23096Combined sources
Beta strandi2312 – 23176Combined sources
Helixi2319 – 23213Combined sources
Helixi2322 – 234423Combined sources
Helixi2345 – 23484Combined sources
Helixi2352 – 236514Combined sources
Helixi2369 – 23768Combined sources
Helixi2378 – 238811Combined sources
Helixi2404 – 242017Combined sources
Turni2423 – 24253Combined sources
Helixi2426 – 243510Combined sources
Helixi2439 – 244810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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
Domaini888 – 96275Biotinyl-bindingPROSITE-ProRule annotationAdd
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.CuratedPROSITE-ProRule annotation
Contains 1 carboxyltransferase domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0511.
GeneTreeiENSGT00550000074703.
HOVERGENiHBG005371.
InParanoidiO00763.
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 (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. Align

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

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 sequencei1 – 202202Missing in isoform 3. 1 PublicationVSP_057081Add
BLAST
Alternative sequencei203 – 21816AYLTT…VPTMR → MSPAKCKICFPDREVK in isoform 3. 1 PublicationVSP_057082Add
BLAST
Alternative sequencei1118 – 118770Missing in isoform 2. 1 PublicationVSP_000547Add
BLAST

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_005253876.2. [O00763-1]
XP_006719428.1. XM_006719365.1. [O00763-1]
XP_006719430.1. XM_006719367.1.
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:
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 .
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 ]
XP_006719430.1. XM_006719367.1.
UniGenei Hs.234898.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00550000074703.
HOVERGENi HBG005371.
InParanoidi O00763.
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

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

Gene expression databases

Bgeei O00763.
CleanExi HS_ACACB.
ExpressionAtlasi O00763. baseline and differential.
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

« Hide 'large scale' publications
  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 1 AND 2), 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 1), COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, 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 1), 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 1).
    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. Cited for: SUBCELLULAR LOCATION.
  8. "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.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus."
    Castle J.C., Hara Y., Raymond C.K., Garrett-Engele P., Ohwaki K., Kan Z., Kusunoki J., Johnson J.M.
    PLoS ONE 4:E4369-E4369(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ALTERNATIVE SPLICING (ISOFORM 3), TISSUE SPECIFICITY.
  11. Cited for: CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, INTERACTION WITH MID1IP1.
  12. "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.
  13. "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.
  14. 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: November 26, 2014
This is version 148 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