Reviewed, UniProtKB/Swiss-Prot O00763 (ACACB_HUMAN)

Names and origin

Protein names

Recommended name:
    Acetyl-CoA carboxylase 2
    EC=6.4.1.2
Alternative name(s):
    ACC-beta
Including the following 1 domains:
    1- Recommended name:
            Biotin carboxylase
              EC=6.3.4.14

Gene names

Name:	ACACB
Synonyms:	ACC2, ACCB

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2458 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. ATP + biotin-carboxyl-carrier protein + CO2 = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.
Cofactor	Biotin By similarity. Binds 2 manganese ions per subunit By similarity.
Enzyme regulation	Activated by citrate. Inhibited by malonyl-CoA. Ref.2
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subcellular location	Endomembrane system. Note: May associate with membranes.
Tissue specificity	Predominantly expressed in the heart, skeletal muscles and liver. Ref.1
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain. Contains 1 carboxyltransferase domain.
Biophysicochemical properties	Kinetic parameters: KM=120 µM for ATP KM=58 µM for Acetyl-CoA KM=3.0 mM for NaHCO3
Sequence caution	The sequence AAB58382.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Biotin Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of fatty acid oxidation Inferred from Experiment. Source: Reactome
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA cytosol Inferred from Experiment. Source: Reactome endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from electronic annotation. Source: EC biotin binding Inferred from electronic annotation. Source: InterPro biotin carboxylase activity Inferred from electronic annotation. Source: EC manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: O00763-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: O00763-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2458

2458

Acetyl-CoA carboxylase 2

PRO_0000146767

Regions

Domain

259 – 761

503

Biotin carboxylation

Domain

414 – 609

196

ATP-grasp

Domain

895 – 961

67

Biotinyl-binding

Domain

1809 – 2305

497

Carboxyltransferase

Nucleotide binding

458 – 463

6

ATP Potential

Sites

Active site

584

1

By similarity

Metal binding

567

1

Manganese 1 By similarity

Metal binding

580

1

Manganese 1 By similarity

Metal binding

580

1

Manganese 2 By similarity

Metal binding

582

1

Manganese 2 By similarity

Binding site

1934

1

Coenzyme A By similarity

Binding site

2238

1

Coenzyme A By similarity

Binding site

2240

1

Coenzyme A By similarity

Amino acid modifications

Modified residue

220

1

Phosphoserine By similarity

Modified residue

222

1

Phosphoserine By similarity

Modified residue

929

1

N6-biotinyllysine By similarity

Natural variations

Alternative sequence

1118 – 1187

70

Missing in isoform Short.

VSP_000547

Natural variant

552

1

I → V: dbSNP rs16940029.

VAR_031255

Natural variant

651

1

A → T: dbSNP rs2300455.

VAR_031256

Natural variant

2141

1

I → V: dbSNP rs2075260. Ref.4 Ref.5

VAR_031257

Experimental info

Sequence conflict

9

1

C → R in ABF48723. Ref.2

Sequence conflict

120

1

T → I in AAR37018. Ref.4

Sequence conflict

422

1

I → T in AAR37018. Ref.4

Sequence conflict

1340

1

S → N in AAC50571. Ref.6

Sequence conflict

1383

1

D → G in AAC50571. Ref.6

Sequence conflict

1425

1

V → M in AAC50571. Ref.6

Sequence conflict

1819 – 1821

3

AEG → PEA in AAC50571. Ref.6

Sequence conflict

1892 – 1893

2

MI → IM in AAC50571. Ref.6

Secondary structure

1

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2458

Helix Strand Turn

Details...

Helix

247 – 253

7

Beta strand

262 – 265

4

Helix

269 – 287

19

Beta strand

292 – 299

8

Helix

301 – 305

5

Helix

309 – 313

5

Beta strand

314 – 319

6

Helix

325 – 327

3

Turn

328 – 330

3

Helix

332 – 341

10

Beta strand

345 – 348

4

Turn

353 – 356

4

Helix

359 – 366

8

Beta strand

370 – 373

4

Helix

376 – 380

5

Helix

385 – 394

10

Turn

403 – 406

4

Helix

426 – 429

4

Helix

437 – 447

11

Beta strand

449 – 455

7

Beta strand

463 – 467

5

Turn

470 – 472

3

Helix

473 – 483

11

Beta strand

489 – 493

5

Beta strand

499 – 507

9

Beta strand

513 – 535

23

Helix

541 – 557

17

Beta strand

562 – 570

9

Beta strand

572 – 574

3

Beta strand

576 – 584

9

Turn

587 – 589

3

Helix

590 – 596

7

Helix

600 – 608

9

Helix

613 – 615

3

Helix

617 – 622

6

Beta strand

635 – 637

3

Beta strand

646 – 654

9

Beta strand

668 – 672

5

Beta strand

680 – 685

6

Beta strand

700 – 709

10

Helix

710 – 726

17

Helix

728 – 730

3

Turn

731 – 734

4

Helix

735 – 742

8

Helix

744 – 747

4

Helix

754 – 756

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified March 20, 2007. Version 2. Checksum: E9E072A910B490A5	FASTA	2,458	276,555
	10 20 30 40 50 60 MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSKSEAN LIPSQEPFPA SDNSGETPQR 70 80 90 100 110 120 NGEGHTLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP RNPLSSSDAA PSPELQANGT 130 140 150 160 170 180 GTQGLEATDT NGLSSSARPQ GQQAGSPSKE DKKQANIKRQ LMTNFILGSF DDYSSDEDSV 190 200 210 220 230 240 AGSSRESTRK GSRASLGALS LEAYLTTGEA ETRVPTMRPS MSGLHLVKRG REHKKLDLHR 250 260 270 280 290 300 DFTVASPAEF VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT 310 320 330 340 350 360 PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG WGHASENPKL 370 380 390 400 410 420 PELLCKNGVA FLGPPSEAMW ALGDKIASTV VAQTLQVPTL PWSGSGLTVE WTEDDLQQGK 430 440 450 460 470 480 RISVPEDVYD KGCVKDVDEG LEAAERIGFP LMIKASEGGG GKGIRKAESA EDFPILFRQV 490 500 510 520 530 540 QSEIPGSPIF LMKLAQHARH LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP 550 560 570 580 590 600 LAIFEFMEQC AIRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL 610 620 630 640 650 660 PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA ARITSENPDE 670 680 690 700 710 720 GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF GHCFSWGENR EEAISNMVVA 730 740 750 760 770 780 LKELSIRGDF RTTVEYLINL LETESFQNND IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL 790 800 810 820 830 840 NVADAMFRTC MTDFLHSLER GQVLPADSLL NLVDVELIYG GVKYILKVAR QSLTMFVLIM 850 860 870 880 890 900 NGCHIEIDAH RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP 910 920 930 940 950 960 SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQERG RVKYIKRPGA VLEAGCVVAR 970 980 990 1000 1010 1020 LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL ENLTNVMSGF CLPEPVFSIK 1030 1040 1050 1060 1070 1080 LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKS VRRVMAQYAS NITSVLCQFP 1090 1100 1110 1120 1130 1140 SQQIATILDC HAATLQRKAD REVFFINTQS IVQLVQRYRS GIRGYMKTVV LDLLRRYLRV 1150 1160 1170 1180 1190 1200 EHHFQQAHYD KCVINLREQF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD 1210 1220 1230 1240 1250 1260 ELISILNELT QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP 1270 1280 1290 1300 1310 1320 ENLKKLILSE TTIFDVLPTF FYHANKVVCM ASLEVYVRRG YIAYELNSLQ HRQLPDGTCV 1330 1340 1350 1360 1370 1380 VEFQFMLPSS HPNRMTVPIS ITNPDLLRHS TELFMDSGFS PLCQRMGAMV AFRRFEDFTR 1390 1400 1410 1420 1430 1440 NFDEVISCFA NVPKDTPLFS EARTSLYSED DCKSLREEPI HILNVSIQCA DHLEDEALVP 1450 1460 1470 1480 1490 1500 ILRTFVQSKK NILVDYGLRR ITFLIAQEKE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL 1510 1520 1530 1540 1550 1560 ELNRMRNFDL TAVPCANHKM HLYLGAAKVK EGVEVTDHRF FIRAIIRHSD LITKEASFEY 1570 1580 1590 1600 1610 1620 LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPFKIEES VRYMVMRYGS 1630 1640 1650 1660 1670 1680 RLWKLRVLQA EVKINIRQTT TGSAVPIRLF ITNESGYYLD ISLYKEVTDS RSGNIMFHSF 1690 1700 1710 1720 1730 1740 GNKQGPQHGM LINTPYVTKD LLQAKRFQAQ TLGTTYIYDF PEMFRQALFK LWGSPDKYPK 1750 1760 1770 1780 1790 1800 DILTYTELVL DSQGQLVEMN RLPGGNEVGM VAFKMRFKTQ EYPEGRDVIV IGNDITFRIG 1810 1820 1830 1840 1850 1860 SFGPGEDLLY LRASEMARAE GIPKIYVAAN SGARIGMAEE IKHMFHVAWV DPEDPHKGFK 1870 1880 1890 1900 1910 1920 YLYLTPQDYT RISSLNSVHC KHIEEGGESR YMITDIIGKD DGLGVENLRG SGMIAGESSL 1930 1940 1950 1960 1970 1980 AYEEIVTISL VTCRAIGIGA YLVRLGQRVI QVENSHIILT GASALNKVLG REVYTSNNQL 1990 2000 2010 2020 2030 2040 GGVQIMHYNG VSHITVPDDF EGVYTILEWL SYMPKDNHSP VPIITPTDPI DREIEFLPSR 2050 2060 2070 2080 2090 2100 APYDPRWMLA GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE 2110 2120 2130 2140 2150 2160 TRTVEVAVPA DPANLDSEAK IIQQAGQVWF PDSAYKTAQA IKDFNREKLP LMIFANWRGF 2170 2180 2190 2200 2210 2220 SGGMKDMYDQ VLKFGAYIVD GLRQYKQPIL IYIPPYAELR GGSWVVIDAT INPLCIEMYA 2230 2240 2250 2260 2270 2280 DKESRGGVLE PEGTVEIKFR KKDLIKSMRR IDPAYKKLME QLGEPDLSDK DRKDLEGRLK 2290 2300 2310 2320 2330 2340 AREDLLLPIY HQVAVQFADF HDTPGRMLEK GVISDILEWK TARTFLYWRL RRLLLEDQVK 2350 2360 2370 2380 2390 2400 QEILQASGEL SHVHIQSMLR RWFVETEGAV KAYLWDNNQV VVQWLEQHWQ AGDGPRSTIR 2410 2420 2430 2440 2450 ENITYLKHDS VLKTIRGLVE ENPEVAVDCV IYLSQHISPA ERAQVVHLLS TMDSPAST
	Isoform Short. Checksum: 14500D1CDB7E1CCB	FASTA	2,388	268,180
	10 20 30 40 50 60 MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSKSEAN LIPSQEPFPA SDNSGETPQR 70 80 90 100 110 120 NGEGHTLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP RNPLSSSDAA PSPELQANGT 130 140 150 160 170 180 GTQGLEATDT NGLSSSARPQ GQQAGSPSKE DKKQANIKRQ LMTNFILGSF DDYSSDEDSV 190 200 210 220 230 240 AGSSRESTRK GSRASLGALS LEAYLTTGEA ETRVPTMRPS MSGLHLVKRG REHKKLDLHR 250 260 270 280 290 300 DFTVASPAEF VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT 310 320 330 340 350 360 PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG WGHASENPKL 370 380 390 400 410 420 PELLCKNGVA FLGPPSEAMW ALGDKIASTV VAQTLQVPTL PWSGSGLTVE WTEDDLQQGK 430 440 450 460 470 480 RISVPEDVYD KGCVKDVDEG LEAAERIGFP LMIKASEGGG GKGIRKAESA EDFPILFRQV 490 500 510 520 530 540 QSEIPGSPIF LMKLAQHARH LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP 550 560 570 580 590 600 LAIFEFMEQC AIRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL 610 620 630 640 650 660 PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA ARITSENPDE 670 680 690 700 710 720 GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF GHCFSWGENR EEAISNMVVA 730 740 750 760 770 780 LKELSIRGDF RTTVEYLINL LETESFQNND IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL 790 800 810 820 830 840 NVADAMFRTC MTDFLHSLER GQVLPADSLL NLVDVELIYG GVKYILKVAR QSLTMFVLIM 850 860 870 880 890 900 NGCHIEIDAH RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP 910 920 930 940 950 960 SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQERG RVKYIKRPGA VLEAGCVVAR 970 980 990 1000 1010 1020 LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL ENLTNVMSGF CLPEPVFSIK 1030 1040 1050 1060 1070 1080 LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKS VRRVMAQYAS NITSVLCQFP 1090 1100 1110 1120 1130 1140 SQQIATILDC HAATLQRKAD REVFFINTQS IVQLVQRIDE LCGPDPSLSD ELISILNELT 1150 1160 1170 1180 1190 1200 QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP ENLKKLILSE 1210 1220 1230 1240 1250 1260 TTIFDVLPTF FYHANKVVCM ASLEVYVRRG YIAYELNSLQ HRQLPDGTCV VEFQFMLPSS 1270 1280 1290 1300 1310 1320 HPNRMTVPIS ITNPDLLRHS TELFMDSGFS PLCQRMGAMV AFRRFEDFTR NFDEVISCFA 1330 1340 1350 1360 1370 1380 NVPKDTPLFS EARTSLYSED DCKSLREEPI HILNVSIQCA DHLEDEALVP ILRTFVQSKK 1390 1400 1410 1420 1430 1440 NILVDYGLRR ITFLIAQEKE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL ELNRMRNFDL 1450 1460 1470 1480 1490 1500 TAVPCANHKM HLYLGAAKVK EGVEVTDHRF FIRAIIRHSD LITKEASFEY LQNEGERLLL 1510 1520 1530 1540 1550 1560 EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPFKIEES VRYMVMRYGS RLWKLRVLQA 1570 1580 1590 1600 1610 1620 EVKINIRQTT TGSAVPIRLF ITNESGYYLD ISLYKEVTDS RSGNIMFHSF GNKQGPQHGM 1630 1640 1650 1660 1670 1680 LINTPYVTKD LLQAKRFQAQ TLGTTYIYDF PEMFRQALFK LWGSPDKYPK DILTYTELVL 1690 1700 1710 1720 1730 1740 DSQGQLVEMN RLPGGNEVGM VAFKMRFKTQ EYPEGRDVIV IGNDITFRIG SFGPGEDLLY 1750 1760 1770 1780 1790 1800 LRASEMARAE GIPKIYVAAN SGARIGMAEE IKHMFHVAWV DPEDPHKGFK YLYLTPQDYT 1810 1820 1830 1840 1850 1860 RISSLNSVHC KHIEEGGESR YMITDIIGKD DGLGVENLRG SGMIAGESSL AYEEIVTISL 1870 1880 1890 1900 1910 1920 VTCRAIGIGA YLVRLGQRVI QVENSHIILT GASALNKVLG REVYTSNNQL GGVQIMHYNG 1930 1940 1950 1960 1970 1980 VSHITVPDDF EGVYTILEWL SYMPKDNHSP VPIITPTDPI DREIEFLPSR APYDPRWMLA 1990 2000 2010 2020 2030 2040 GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE TRTVEVAVPA 2050 2060 2070 2080 2090 2100 DPANLDSEAK IIQQAGQVWF PDSAYKTAQA IKDFNREKLP LMIFANWRGF SGGMKDMYDQ 2110 2120 2130 2140 2150 2160 VLKFGAYIVD GLRQYKQPIL IYIPPYAELR GGSWVVIDAT INPLCIEMYA DKESRGGVLE 2170 2180 2190 2200 2210 2220 PEGTVEIKFR KKDLIKSMRR IDPAYKKLME QLGEPDLSDK DRKDLEGRLK AREDLLLPIY 2230 2240 2250 2260 2270 2280 HQVAVQFADF HDTPGRMLEK GVISDILEWK TARTFLYWRL RRLLLEDQVK QEILQASGEL 2290 2300 2310 2320 2330 2340 SHVHIQSMLR RWFVETEGAV KAYLWDNNQV VVQWLEQHWQ AGDGPRSTIR ENITYLKHDS 2350 2360 2370 2380 VLKTIRGLVE ENPEVAVDCV IYLSQHISPA ERAQVVHLLS TMDSPAST

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two isoforms." Abu-Elheiga L., Almarza-Ortega D.B., Baldini A., Wakil S.J. J. Biol. Chem. 272:10669-10677(1997) [PubMed: 9099716] [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: 16854592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[3]	"Corrected sequence for human Acetyl-CoA carboxylase 2 obtained by alignement 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). 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), VARIANT VAL-2141. 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: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-2141.
[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: 8670171] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1324-2109. Tissue: Adipose tissue.
[7]	"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(2007) [PubMed: 17876819] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 217-775.
[8]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U89344 mRNA. Translation: AAB58382.1. Sequence problems.
DQ493870 mRNA. Translation: ABF48723.1.
AJ575431 mRNA. Translation: CAE01470.2. Different termination.
AJ575592 mRNA. Translation: CAE01471.3.
AY382667 mRNA. Translation: AAR37018.1.
U34591 mRNA. Translation: AAC50571.1.

IPI

IPI00013003.
IPI00157056.

PIR

S71091.

RefSeq

NP_001084.3.

UniGene

Hs.234898

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

O00763.

Proteomic databases

PRIDE

O00763.

Genome annotation databases

Ensembl

ENST00000338432; ENSP00000341044; ENSG00000076555; Homo sapiens. [Genome view]
ENST00000377848; ENSP00000367079; ENSG00000076555; Homo sapiens. [Genome view]
ENST00000377854; ENSP00000367085; ENSG00000076555; Homo sapiens. [Genome view]
ENST00000390027; ENSP00000374677; ENSG00000076555; Homo sapiens. [Genome view]

GeneID

32.

KEGG

hsa:32.

UCSC

uc001tob.1. human.

Organism-specific databases

CTD

32.

GeneCards

GC12P108017.

HGNC

HGNC:85. ACACB.

HPA

HPA006554.

MIM

601557. gene.

PharmGKB

PA24422.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O00763.

HOVERGEN

O00763.

Enzyme and pathway databases

BRENDA

6.3.4.14. 247.
6.4.1.2. 247.

Reactome

REACT_1505. Integration of energy metabolism.
REACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

O00763.

Bgee

O00763.

CleanEx

HS_ACACB.

Genevestigator

O00763.

GermOnline

ENSG00000076555. Homo sapiens.

Family and domain databases

InterPro

IPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR011764. BC.
IPR001882. Biotin_BS.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005479. CarbamoylP_synth_lsu_ATP-bd.
IPR005481. CarbamoylP_synth_lsu_N.
IPR000022. Carboxyl_trans.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR013817. Pre-ATP_grasp.
[Graphical view]

Gene3D

G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.

Pfam

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]

PROSITE

PS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. False negative.
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]

ProtoNet

Search...

Other Resources

DrugBank

DB00121. Biotin.

NextBio

123.

SOURCE

Search...

Entry information

Entry name

ACACB_HUMAN

Accession

Primary (citable) accession number: O00763
Secondary accession number(s): A6NK36 , Q16852, Q1HEC1, Q6KE87, Q6KE89, Q6TY48

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 20, 2007
Last modified:	October 13, 2009
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.