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O00763

- ACACB_HUMAN

UniProt

O00763 - ACACB_HUMAN

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Protein
Acetyl-CoA carboxylase 2
Gene
ACACB, ACC2, ACCB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication
Binds 2 manganese ions per subunit By similarity.1 Publication

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-CoA
  3. KM=3.0 mM for NaHCO3

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi458 – 4636ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. acetyl-CoA carboxylase activity Source: UniProtKB
  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
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:6.4.1.2)
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
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24422.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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.

Miscellaneous databases

EvolutionaryTraceiO00763.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini259 – 761503Biotin carboxylation
Add
BLAST
Domaini414 – 609196ATP-grasp
Add
BLAST
Domaini895 – 96167Biotinyl-binding
Add
BLAST
Domaini1809 – 2305497Carboxyltransferase
Add
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.

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.

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.
VSP_000547Add
BLAST

Sequence conflict

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

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 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

« 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 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: September 3, 2014
This is version 145 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

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