Q13085 (ACACA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetyl-CoA carboxylase 1
Short name=ACC1
EC=6.4.1.2

Alternative name(s):
ACC-alpha

Including the following 1 domains:

1. Biotin carboxylase
   EC=6.3.4.14

Gene names

Name:	ACACA
Synonyms:	ACAC, ACC1, ACCA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2346 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Ref.19
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. Ref.19 ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein]. Ref.19
Cofactor	Biotin. Binds 2 manganese ions per subunit.
Enzyme regulation	By phosphorylation By similarity. Activity is increased by oligomerization. Citrate and MID1IP1 promote oligomerization. Ref.19
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subunit structure	Monomer, homodimer, and homotetramer. Can form filamentous polymers. Interacts in its inactive phosphorylated form with the BRCT domains of BRCA1 which prevents ACACA dephosphorylation and inhibits lipid synthesis. Interacts with MID1IP1; interaction with MID1IP1 promotes oligomerization and increases its activity. Ref.8 Ref.10 Ref.19
Subcellular location	Cytoplasm.
Tissue specificity	Expressed in brain, placental, skeletal muscle, renal, pancreatic and adipose tissues; expressed at low level in pulmonary tissue; not detected in the liver.
Post-translational modification	Phosphorylation on Ser-1263 is required for interaction with BRCA1.
Involvement in disease	Acetyl-CoA carboxylase 1 deficiency (ACACAD) [MIM:613933]: An inborn error of de novo fatty acid synthesis associated with severe brain damage, persistent myopathy and poor growth. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain. Contains 1 carboxyltransferase domain.
Sequence caution	The sequence AAP94120.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Alternative promoter usage Polymorphism
Ligand	ATP-binding Biotin Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA metabolic process Inferred from sequence or structural similarity. Source: UniProtKB energy reserve metabolic process Traceable author statement. Source: Reactome fatty acid biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB lipid homeostasis Inferred from electronic annotation. Source: Compara long-chain fatty-acyl-CoA biosynthetic process Traceable author statement. Source: Reactome malonyl-CoA biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway multicellular organismal protein metabolic process Inferred from electronic annotation. Source: Compara positive regulation of cellular metabolic process Traceable author statement. Source: Reactome protein homotetramerization Inferred from sequence or structural similarity Ref.19. Source: UniProtKB tissue homeostasis Inferred from electronic annotation. Source: Compara triglyceride biosynthetic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from sequence or structural similarity Ref.19. Source: UniProtKB biotin carboxylase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AKR1B10	O60218	4	EBI-717681,EBI-1572139
BRCA1	P38398	2	EBI-717681,EBI-349905
SIRT1	Q96EB6	3	EBI-717681,EBI-1802965

Alternative products

This entry describes 4 isoforms produced by alternative promoter usage. [Align] [Select]

Isoform 1 (identifier: Q13085-1)

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 2 (identifier: Q13085-2)

Also known as: E5A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: MDEPSPLAQP...SLQDGLALHI → MEGSPEENKEMRYYMLQ

Isoform 3 (identifier: Q13085-3)

Also known as: E5B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.

Isoform 4 (identifier: Q13085-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MWWSTLMSILRARSFWKWISTQTVRIIRAVRAHFGGIM

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2346

2346

Acetyl-CoA carboxylase 1

PRO_0000146764

Regions

Domain

117 – 618

502

Biotin carboxylation

Domain

275 – 466

192

ATP-grasp

Domain

752 – 818

67

Biotinyl-binding

Domain

1698 – 2194

497

Carboxyltransferase

Nucleotide binding

315 – 320

6

ATP Potential

Sites

Active site

441

1

By similarity

Metal binding

424

1

Manganese 1 By similarity

Metal binding

437

1

Manganese 1 By similarity

Metal binding

437

1

Manganese 2 By similarity

Metal binding

439

1

Manganese 2 By similarity

Binding site

1823

1

Coenzyme A By similarity

Binding site

2127

1

Coenzyme A By similarity

Binding site

2129

1

Coenzyme A By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.7 Ref.16 Ref.20

Modified residue

5

1

Phosphoserine Ref.16 Ref.20

Modified residue

23

1

Phosphoserine Ref.15 Ref.17 Ref.20

Modified residue

25

1

Phosphoserine Ref.15 Ref.17

Modified residue

29

1

Phosphoserine Ref.9 Ref.14 Ref.15 Ref.16 Ref.17 Ref.20 Ref.22

Modified residue

48

1

Phosphoserine Ref.20

Modified residue

53

1

Phosphoserine Ref.9

Modified residue

78

1

Phosphoserine By similarity

Modified residue

80

1

Phosphoserine Ref.7 Ref.15 Ref.20 Ref.22

Modified residue

488

1

Phosphoserine Ref.13

Modified residue

786

1

N6-biotinyllysine By similarity

Modified residue

1201

1

Phosphoserine By similarity

Modified residue

1216

1

Phosphoserine By similarity

Modified residue

1263

1

Phosphoserine Ref.11

Modified residue

1334

1

N6-acetyllysine Ref.18

Natural variations

Alternative sequence

1 – 78

78

Missing in isoform 3.

VSP_026098

Alternative sequence

1 – 75

75

MDEPS…LALHI → MEGSPEENKEMRYYMLQ in isoform 2.

VSP_026099

Alternative sequence

1

1

M → MWWSTLMSILRARSFWKWIS TQTVRIIRAVRAHFGGIM in isoform 4.

VSP_026100

Natural variant

838

1

R → W.
Corresponds to variant rs2287351 [ dbSNP | Ensembl ].

VAR_042941

Natural variant

1687

1

R → Q in a colorectal cancer sample; somatic mutation. Ref.23

VAR_036514

Natural variant

2271

1

A → V Rare polymorphism; frequency <0.004; may play a role in breast cancer susceptibility. Ref.3

VAR_028929

Experimental info

Mutagenesis

78

1

S → A: No effect on interaction with BRCA1. Ref.11

Mutagenesis

344

1

S → A: No effect on interaction with BRCA1. Ref.11

Mutagenesis

432

1

S → A: No effect on interaction with BRCA1. Ref.11

Mutagenesis

1201

1

S → A: No effect on interaction with BRCA1. Ref.11

Mutagenesis

1263

1

S → A: Abolishes interaction with BRCA1. Ref.11

Mutagenesis

1585

1

S → A: No effect on interaction with BRCA1. Ref.11

Mutagenesis

1952

1

S → A: No effect on interaction with BRCA1. Ref.11

Mutagenesis

2211

1

S → A: No effect on interaction with BRCA1. Ref.11

Sequence conflict

66

1

S → A in AAC50139. Ref.1

Sequence conflict

79

1

M → W in AAC50139. Ref.1

Sequence conflict

89

1

R → G in AAC50139. Ref.1

Sequence conflict

182

1

P → A in AAC50139. Ref.1

Sequence conflict

234

1

S → N in AAC50139. Ref.1

Sequence conflict

299

1

Q → K in AAC50139. Ref.1

Sequence conflict

303

1

E → K in AAC50139. Ref.1

Sequence conflict

364

1

A → V in AAP94122. Ref.2

Sequence conflict

446

1

H → Q in AAC50139. Ref.1

Sequence conflict

494

1

D → N in AAC50139. Ref.1

Sequence conflict

554

1

D → G in AAC50139. Ref.1

Sequence conflict

622

1

Q → R in AAC50139. Ref.1

Sequence conflict

640

1

A → G in AAC50139. Ref.1

Sequence conflict

814

1

V → I in AAP94122. Ref.2

Sequence conflict

1061

1

N → S in AAC50139. Ref.1

Sequence conflict

1094 – 1095

2

EL → DV in AAC50139. Ref.1

Sequence conflict

1225

1

S → A in AAC50139. Ref.1

Sequence conflict

1257

1

S → C in AAC50139. Ref.1

Sequence conflict

1297

1

C → G in AAC50139. Ref.1

Sequence conflict

1320

1

V → A in AAC50139. Ref.1

Sequence conflict

1444

1

N → S in AAC50139. Ref.1

Sequence conflict

1474

1

F → L in AAC50139. Ref.1

Sequence conflict

1665 – 1666

2

TF → SL in AAC50139. Ref.1

Sequence conflict

1677

1

I → V in AAC50139. Ref.1

Sequence conflict

1741

1

P → S in AAC50139. Ref.1

Sequence conflict

1762

1

S → G in AAC50139. Ref.1

Sequence conflict

1822

1

C → S in AAC50139. Ref.1

Sequence conflict

1875

1

M → T in AAC50139. Ref.1

Sequence conflict

1888

1

D → G in AAC50139. Ref.1

Sequence conflict

1997

1

I → V in AAC50139. Ref.1

Sequence conflict

2013

1

Q → H in AAC50139. Ref.1

Sequence conflict

2058

1

D → H in AAC50139. Ref.1

Sequence conflict

2075

1

C → S in AAC50139. Ref.1

Sequence conflict

2098 – 2099

2

SS → PT in AAC50139. Ref.1

Sequence conflict

2158 – 2159

2

TA → PT in AAC50139. Ref.1

Sequence conflict

2166

1

N → S in AAC50139. Ref.1

Sequence conflict

2234

1

N → S in AAC50139. Ref.1

Sequence conflict

2321

1

H → R in AAP94122. Ref.2

Secondary structure

1

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2346

Helix Strand Turn

Details...

Helix

105 – 111

7

Beta strand

120 – 123

4

Helix

127 – 145

19

Beta strand

150 – 157

8

Helix

159 – 163

5

Helix

168 – 171

4

Beta strand

172 – 177

6

Helix

183 – 185

3

Turn

186 – 188

3

Helix

190 – 199

10

Beta strand

203 – 206

4

Turn

211 – 214

4

Helix

217 – 224

8

Beta strand

228 – 231

4

Helix

234 – 241

8

Helix

243 – 252

10

Turn

261 – 264

4

Helix

283 – 289

7

Helix

294 – 304

11

Beta strand

306 – 312

7

Beta strand

320 – 324

5

Turn

327 – 329

3

Helix

330 – 340

11

Beta strand

346 – 350

5

Beta strand

356 – 364

9

Beta strand

370 – 382

13

Beta strand

385 – 392

8

Helix

398 – 415

18

Beta strand

419 – 427

9

Beta strand

433 – 439

7

Turn

444 – 446

3

Helix

447 – 453

7

Helix

457 – 465

9

Helix

470 – 472

3

Helix

474 – 479

6

Turn

492 – 495

4

Beta strand

496 – 498

3

Beta strand

503 – 510

8

Beta strand

526 – 530

5

Beta strand

537 – 542

6

Beta strand

557 – 566

10

Helix

567 – 582

16

Helix

589 – 599

11

Helix

601 – 604

4

Helix

612 – 616

5

Helix

1582 – 1592

11

Helix

1598 – 1600

3

Helix

1601 – 1619

19

Helix

1628 – 1631

4

Beta strand

1632 – 1639

8

Beta strand

1645 – 1648

4

Beta strand

1656 – 1666

11

Beta strand

1675 – 1682

8

Helix

1687 – 1689

3

Helix

1693 – 1709

17

Beta strand

1713 – 1717

5

Helix

1728 – 1731

4

Beta strand

1735 – 1739

5

Helix

1744 – 1746

3

Beta strand

1748 – 1753

6

Helix

1755 – 1761

7

Helix

1762 – 1764

3

Beta strand

1767 – 1774

8

Beta strand

1777 – 1785

9

Helix

1795 – 1813

19

Beta strand

1816 – 1820

5

Beta strand

1822 – 1825

4

Helix

1827 – 1834

8

Beta strand

1837 – 1841

5

Beta strand

1845 – 1849

5

Helix

1851 – 1858

8

Helix

1866 – 1870

5

Helix

1872 – 1875

4

Turn

1876 – 1879

4

Beta strand

1882 – 1887

6

Helix

1888 – 1899

12

Beta strand

1914 – 1917

4

Helix

1934 – 1939

6

Beta strand

1944 – 1946

3

Beta strand

1961 – 1964

4

Beta strand

1971 – 1978

8

Beta strand

1981 – 1988

8

Beta strand

1993 – 1996

4

Beta strand

2010 – 2013

4

Helix

2020 – 2036

17

Beta strand

2040 – 2043

4

Helix

2053 – 2057

5

Helix

2060 – 2072

13

Beta strand

2078 – 2082

5

Beta strand

2087 – 2089

3

Helix

2090 – 2094

5

Helix

2098 – 2100

3

Turn

2102 – 2104

3

Beta strand

2105 – 2110

6

Beta strand

2114 – 2118

5

Helix

2120 – 2127

8

Helix

2130 – 2140

11

Helix

2142 – 2150

9

Helix

2158 – 2188

31

Helix

2193 – 2198

6

Beta strand

2201 – 2206

6

Helix

2208 – 2210

3

Helix

2211 – 2235

25

Helix

2241 – 2256

16

Helix

2258 – 2265

8

Helix

2267 – 2278

12

Helix

2289 – 2310

22

Helix

2312 – 2314

3

Helix

2315 – 2322

8

Helix

2323 – 2325

3

Helix

2328 – 2337

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: F1F0A518F8824FFC	FASTA	2,346	265,554
	10 20 30 40 50 60 MDEPSPLAQP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS PASVGSDTLS 70 80 90 100 110 120 DLGISSLQDG LALHIRSSMS GLHLVKQGRD RKKIDSQRDF TVASPAEFVT RFGGNKVIEK 130 140 150 160 170 180 VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG 190 200 210 220 230 240 GPNNNNYANV ELILDIAKRI PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL 250 260 270 280 290 300 GDKIASSIVA QTAGIPTLPW SGSGLRVDWQ ENDFSKRILN VPQELYEKGY VKDVDDGLQA 310 320 330 340 350 360 AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV 370 380 390 400 410 420 QILADQYGNA ISLFGRDCSV QRRHQKIIEE APATIATPAV FEHMEQCAVK LAKMVGYVSA 430 440 450 460 470 480 GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGIPL YRIKDIRMMY 490 500 510 520 530 540 GVSPWGDSPI DFEDSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY 550 560 570 580 590 600 FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET 610 620 630 640 650 660 ESFQMNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSVSN FLHSLERGQV 670 680 690 700 710 720 LPAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS CVEVDVHRLS DGGLLLSYDG 730 740 750 760 770 780 SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSVMRSPSAG KLIQYIVEDG GHVFAGQCYA 790 800 810 820 830 840 EIEVMKMVMT LTAVESGCIH YVKRPGAALD PGCVLAKMQL DNPSKVQQAE LHTGSLPRIQ 850 860 870 880 890 900 STALRGEKLH RVFHYVLDNL VNVMNGYCLP DPFFSSKVKD WVERLMKTLR DPSLPLLELQ 910 920 930 940 950 960 DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA TLNRKSEREV 970 980 990 1000 1010 1020 FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ FQNGHYDKCV FALREENKSD 1030 1040 1050 1060 1070 1080 MNTVLNYIFS HAQVTKKNLL VTMLIDQLCG RDPTLTDELL NILTELTQLS KTTNAKVALR 1090 1100 1110 1120 1130 1140 ARQVLIASHL PSYELRHNQV ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH 1150 1160 1170 1180 1190 1200 SNQVVRMAAL EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM 1210 1220 1230 1240 1250 1260 SFSSNLNHYG MTHVASVSDV LLDNSFTPPC QRMGGMVSFR TFEDFVRIFD EVMGCFSDSP 1270 1280 1290 1300 1310 1320 PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE DDRLAAMFRE FTQQNKATLV 1330 1340 1350 1360 1370 1380 DHGIRRLTFL VAQKDFRKQV NYEVDRRFHR EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ 1390 1400 1410 1420 1430 1440 LELNRMRNFD LTAIPCANHK MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE 1450 1460 1470 1480 1490 1500 YLQNEGERLL LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG 1510 1520 1530 1540 1550 1560 SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD SRTAQIMFQA 1570 1580 1590 1600 1610 1620 YGDKQGPLHG MLINTPYVTK DLLQSKRFQA QSLGTTYIYD IPEMFRQSLI KLWESMSTQA 1630 1640 1650 1660 1670 1680 FLPSPPLPSD MLTYTELVLD DQGQLVHMNR LPGGNEIGMV AWKMTFKSPE YPEGRDIIVI 1690 1700 1710 1720 1730 1740 GNDITYRIGS FGPQEDLLFL RASELARAEG IPRIYVSANS GARIGLAEEI RHMFHVAWVD 1750 1760 1770 1780 1790 1800 PEDPYKGYRY LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GIGPENLRGS 1810 1820 1830 1840 1850 1860 GMIAGESSLA YNEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG AGALNKVLGR 1870 1880 1890 1900 1910 1920 EVYTSNNQLG GIQIMHNNGV THCTVCDDFE GVFTVLHWLS YMPKSVHSSV PLLNSKDPID 1930 1940 1950 1960 1970 1980 RIIEFVPTKT PYDPRWMLAG RPHPTQKGQW LSGFFDYGSF SEIMQPWAQT VVVGRARLGG 1990 2000 2010 2020 2030 2040 IPVGVVAVET RTVELSIPAD PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL 2050 2060 2070 2080 2090 2100 MVFANWRGFS GGMKDMYDQV LKFGAYIVDG LRECCQPVLV YIPPQAELRG GSWVVIDSSI 2110 2120 2130 2140 2150 2160 NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER LGTPELSTAE 2170 2180 2190 2200 2210 2220 RKELENKLKE REEFLIPIYH QVAVQFADLH DTPGRMQEKG VISDILDWKT SRTFFYWRLR 2230 2240 2250 2260 2270 2280 RLLLEDLVKK KIHNANPELT DGQIQAMLRR WFVEVEGTVK AYVWDNNKDL AEWLEKQLTE 2290 2300 2310 2320 2330 2340 EDGVHSVIEE NIKCISRDYV LKQIRSLVQA NPEVAMDSII HMTQHISPTQ RAEVIRILST MDSPST
	Isoform 2 (E5A) [UniParc]. Checksum: 4E2C75958216CC8B	FASTA	2,288	259,686
	10 20 30 40 50 60 MEGSPEENKE MRYYMLQRSS MSGLHLVKQG RDRKKIDSQR DFTVASPAEF VTRFGGNKVI 70 80 90 100 110 120 EKVLIANNGI AAVKCMRSIR RWSYEMFRNE RAIRFVVMVT PEDLKANAEY IKMADHYVPV 130 140 150 160 170 180 PGGPNNNNYA NVELILDIAK RIPVQAVWAG WGHASENPKL PELLLKNGIA FMGPPSQAMW 190 200 210 220 230 240 ALGDKIASSI VAQTAGIPTL PWSGSGLRVD WQENDFSKRI LNVPQELYEK GYVKDVDDGL 250 260 270 280 290 300 QAAEEVGYPV MIKASEGGGG KGIRKVNNAD DFPNLFRQVQ AEVPGSPIFV MRLAKQSRHL 310 320 330 340 350 360 EVQILADQYG NAISLFGRDC SVQRRHQKII EEAPATIATP AVFEHMEQCA VKLAKMVGYV 370 380 390 400 410 420 SAGTVEYLYS QDGSFYFLEL NPRLQVEHPC TEMVADVNLP AAQLQIAMGI PLYRIKDIRM 430 440 450 460 470 480 MYGVSPWGDS PIDFEDSAHV PCPRGHVIAA RITSENPDEG FKPSSGTVQE LNFRSNKNVW 490 500 510 520 530 540 GYFSVAAAGG LHEFADSQFG HCFSWGENRE EAISNMVVAL KELSIRGDFR TTVEYLIKLL 550 560 570 580 590 600 ETESFQMNRI DTGWLDRLIA EKVQAERPDT MLGVVCGALH VADVSLRNSV SNFLHSLERG 610 620 630 640 650 660 QVLPAHTLLN TVDVELIYEG VKYVLKVTRQ SPNSYVVIMN GSCVEVDVHR LSDGGLLLSY 670 680 690 700 710 720 DGSSYTTYMK EEVDRYRITI GNKTCVFEKE NDPSVMRSPS AGKLIQYIVE DGGHVFAGQC 730 740 750 760 770 780 YAEIEVMKMV MTLTAVESGC IHYVKRPGAA LDPGCVLAKM QLDNPSKVQQ AELHTGSLPR 790 800 810 820 830 840 IQSTALRGEK LHRVFHYVLD NLVNVMNGYC LPDPFFSSKV KDWVERLMKT LRDPSLPLLE 850 860 870 880 890 900 LQDIMTSVSG RIPPNVEKSI KKEMAQYASN ITSVLCQFPS QQIANILDSH AATLNRKSER 910 920 930 940 950 960 EVFFMNTQSI VQLVQRYRSG IRGHMKAVVM DLLRQYLRVE TQFQNGHYDK CVFALREENK 970 980 990 1000 1010 1020 SDMNTVLNYI FSHAQVTKKN LLVTMLIDQL CGRDPTLTDE LLNILTELTQ LSKTTNAKVA 1030 1040 1050 1060 1070 1080 LRARQVLIAS HLPSYELRHN QVESIFLSAI DMYGHQFCIE NLQKLILSET SIFDVLPNFF 1090 1100 1110 1120 1130 1140 YHSNQVVRMA ALEVYVRRAY IAYELNSVQH RQLKDNTCVV EFQFMLPTSH PNRGNIPTLN 1150 1160 1170 1180 1190 1200 RMSFSSNLNH YGMTHVASVS DVLLDNSFTP PCQRMGGMVS FRTFEDFVRI FDEVMGCFSD 1210 1220 1230 1240 1250 1260 SPPQSPTFPE AGHTSLYDED KVPRDEPIHI LNVAIKTDCD IEDDRLAAMF REFTQQNKAT 1270 1280 1290 1300 1310 1320 LVDHGIRRLT FLVAQKDFRK QVNYEVDRRF HREFPKFFTF RARDKFEEDR IYRHLEPALA 1330 1340 1350 1360 1370 1380 FQLELNRMRN FDLTAIPCAN HKMHLYLGAA KVEVGTEVTD YRFFVRAIIR HSDLVTKEAS 1390 1400 1410 1420 1430 1440 FEYLQNEGER LLLEAMDELE VAFNNTNVRT DCNHIFLNFV PTVIMDPSKI EESVRSMVMR 1450 1460 1470 1480 1490 1500 YGSRLWKLRV LQAELKINIR LTPTGKAIPI RLFLTNESGY YLDISLYKEV TDSRTAQIMF 1510 1520 1530 1540 1550 1560 QAYGDKQGPL HGMLINTPYV TKDLLQSKRF QAQSLGTTYI YDIPEMFRQS LIKLWESMST 1570 1580 1590 1600 1610 1620 QAFLPSPPLP SDMLTYTELV LDDQGQLVHM NRLPGGNEIG MVAWKMTFKS PEYPEGRDII 1630 1640 1650 1660 1670 1680 VIGNDITYRI GSFGPQEDLL FLRASELARA EGIPRIYVSA NSGARIGLAE EIRHMFHVAW 1690 1700 1710 1720 1730 1740 VDPEDPYKGY RYLYLTPQDY KRVSALNSVH CEHVEDEGES RYKITDIIGK EEGIGPENLR 1750 1760 1770 1780 1790 1800 GSGMIAGESS LAYNEIITIS LVTCRAIGIG AYLVRLGQRT IQVENSHLIL TGAGALNKVL 1810 1820 1830 1840 1850 1860 GREVYTSNNQ LGGIQIMHNN GVTHCTVCDD FEGVFTVLHW LSYMPKSVHS SVPLLNSKDP 1870 1880 1890 1900 1910 1920 IDRIIEFVPT KTPYDPRWML AGRPHPTQKG QWLSGFFDYG SFSEIMQPWA QTVVVGRARL 1930 1940 1950 1960 1970 1980 GGIPVGVVAV ETRTVELSIP ADPANLDSEA KIIQQAGQVW FPDSAFKTYQ AIKDFNREGL 1990 2000 2010 2020 2030 2040 PLMVFANWRG FSGGMKDMYD QVLKFGAYIV DGLRECCQPV LVYIPPQAEL RGGSWVVIDS 2050 2060 2070 2080 2090 2100 SINPRHMEMY ADRESRGSVL EPEGTVEIKF RRKDLVKTMR RVDPVYIHLA ERLGTPELST 2110 2120 2130 2140 2150 2160 AERKELENKL KEREEFLIPI YHQVAVQFAD LHDTPGRMQE KGVISDILDW KTSRTFFYWR 2170 2180 2190 2200 2210 2220 LRRLLLEDLV KKKIHNANPE LTDGQIQAML RRWFVEVEGT VKAYVWDNNK DLAEWLEKQL 2230 2240 2250 2260 2270 2280 TEEDGVHSVI EENIKCISRD YVLKQIRSLV QANPEVAMDS IIHMTQHISP TQRAEVIRIL STMDSPST
	Isoform 3 (E5B) [UniParc]. Checksum: C78033F62C492D3E	FASTA	2,268	257,239
	10 20 30 40 50 60 MSGLHLVKQG RDRKKIDSQR DFTVASPAEF VTRFGGNKVI EKVLIANNGI AAVKCMRSIR 70 80 90 100 110 120 RWSYEMFRNE RAIRFVVMVT PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELILDIAK 130 140 150 160 170 180 RIPVQAVWAG WGHASENPKL PELLLKNGIA FMGPPSQAMW ALGDKIASSI VAQTAGIPTL 190 200 210 220 230 240 PWSGSGLRVD WQENDFSKRI LNVPQELYEK GYVKDVDDGL QAAEEVGYPV MIKASEGGGG 250 260 270 280 290 300 KGIRKVNNAD DFPNLFRQVQ AEVPGSPIFV MRLAKQSRHL EVQILADQYG NAISLFGRDC 310 320 330 340 350 360 SVQRRHQKII EEAPATIATP AVFEHMEQCA VKLAKMVGYV SAGTVEYLYS QDGSFYFLEL 370 380 390 400 410 420 NPRLQVEHPC TEMVADVNLP AAQLQIAMGI PLYRIKDIRM MYGVSPWGDS PIDFEDSAHV 430 440 450 460 470 480 PCPRGHVIAA RITSENPDEG FKPSSGTVQE LNFRSNKNVW GYFSVAAAGG LHEFADSQFG 490 500 510 520 530 540 HCFSWGENRE EAISNMVVAL KELSIRGDFR TTVEYLIKLL ETESFQMNRI DTGWLDRLIA 550 560 570 580 590 600 EKVQAERPDT MLGVVCGALH VADVSLRNSV SNFLHSLERG QVLPAHTLLN TVDVELIYEG 610 620 630 640 650 660 VKYVLKVTRQ SPNSYVVIMN GSCVEVDVHR LSDGGLLLSY DGSSYTTYMK EEVDRYRITI 670 680 690 700 710 720 GNKTCVFEKE NDPSVMRSPS AGKLIQYIVE DGGHVFAGQC YAEIEVMKMV MTLTAVESGC 730 740 750 760 770 780 IHYVKRPGAA LDPGCVLAKM QLDNPSKVQQ AELHTGSLPR IQSTALRGEK LHRVFHYVLD 790 800 810 820 830 840 NLVNVMNGYC LPDPFFSSKV KDWVERLMKT LRDPSLPLLE LQDIMTSVSG RIPPNVEKSI 850 860 870 880 890 900 KKEMAQYASN ITSVLCQFPS QQIANILDSH AATLNRKSER EVFFMNTQSI VQLVQRYRSG 910 920 930 940 950 960 IRGHMKAVVM DLLRQYLRVE TQFQNGHYDK CVFALREENK SDMNTVLNYI FSHAQVTKKN 970 980 990 1000 1010 1020 LLVTMLIDQL CGRDPTLTDE LLNILTELTQ LSKTTNAKVA LRARQVLIAS HLPSYELRHN 1030 1040 1050 1060 1070 1080 QVESIFLSAI DMYGHQFCIE NLQKLILSET SIFDVLPNFF YHSNQVVRMA ALEVYVRRAY 1090 1100 1110 1120 1130 1140 IAYELNSVQH RQLKDNTCVV EFQFMLPTSH PNRGNIPTLN RMSFSSNLNH YGMTHVASVS 1150 1160 1170 1180 1190 1200 DVLLDNSFTP PCQRMGGMVS FRTFEDFVRI FDEVMGCFSD SPPQSPTFPE AGHTSLYDED 1210 1220 1230 1240 1250 1260 KVPRDEPIHI LNVAIKTDCD IEDDRLAAMF REFTQQNKAT LVDHGIRRLT FLVAQKDFRK 1270 1280 1290 1300 1310 1320 QVNYEVDRRF HREFPKFFTF RARDKFEEDR IYRHLEPALA FQLELNRMRN FDLTAIPCAN 1330 1340 1350 1360 1370 1380 HKMHLYLGAA KVEVGTEVTD YRFFVRAIIR HSDLVTKEAS FEYLQNEGER LLLEAMDELE 1390 1400 1410 1420 1430 1440 VAFNNTNVRT DCNHIFLNFV PTVIMDPSKI EESVRSMVMR YGSRLWKLRV LQAELKINIR 1450 1460 1470 1480 1490 1500 LTPTGKAIPI RLFLTNESGY YLDISLYKEV TDSRTAQIMF QAYGDKQGPL HGMLINTPYV 1510 1520 1530 1540 1550 1560 TKDLLQSKRF QAQSLGTTYI YDIPEMFRQS LIKLWESMST QAFLPSPPLP SDMLTYTELV 1570 1580 1590 1600 1610 1620 LDDQGQLVHM NRLPGGNEIG MVAWKMTFKS PEYPEGRDII VIGNDITYRI GSFGPQEDLL 1630 1640 1650 1660 1670 1680 FLRASELARA EGIPRIYVSA NSGARIGLAE EIRHMFHVAW VDPEDPYKGY RYLYLTPQDY 1690 1700 1710 1720 1730 1740 KRVSALNSVH CEHVEDEGES RYKITDIIGK EEGIGPENLR GSGMIAGESS LAYNEIITIS 1750 1760 1770 1780 1790 1800 LVTCRAIGIG AYLVRLGQRT IQVENSHLIL TGAGALNKVL GREVYTSNNQ LGGIQIMHNN 1810 1820 1830 1840 1850 1860 GVTHCTVCDD FEGVFTVLHW LSYMPKSVHS SVPLLNSKDP IDRIIEFVPT KTPYDPRWML 1870 1880 1890 1900 1910 1920 AGRPHPTQKG QWLSGFFDYG SFSEIMQPWA QTVVVGRARL GGIPVGVVAV ETRTVELSIP 1930 1940 1950 1960 1970 1980 ADPANLDSEA KIIQQAGQVW FPDSAFKTYQ AIKDFNREGL PLMVFANWRG FSGGMKDMYD 1990 2000 2010 2020 2030 2040 QVLKFGAYIV DGLRECCQPV LVYIPPQAEL RGGSWVVIDS SINPRHMEMY ADRESRGSVL 2050 2060 2070 2080 2090 2100 EPEGTVEIKF RRKDLVKTMR RVDPVYIHLA ERLGTPELST AERKELENKL KEREEFLIPI 2110 2120 2130 2140 2150 2160 YHQVAVQFAD LHDTPGRMQE KGVISDILDW KTSRTFFYWR LRRLLLEDLV KKKIHNANPE 2170 2180 2190 2200 2210 2220 LTDGQIQAML RRWFVEVEGT VKAYVWDNNK DLAEWLEKQL TEEDGVHSVI EENIKCISRD 2230 2240 2250 2260 YVLKQIRSLV QANPEVAMDS IIHMTQHISP TQRAEVIRIL STMDSPST
	Isoform 4 [UniParc]. Checksum: 1F2B8F96208B9983	FASTA	2,383	269,999
	10 20 30 40 50 60 MWWSTLMSIL RARSFWKWIS TQTVRIIRAV RAHFGGIMDE PSPLAQPLEL NQHSRFIIGS 70 80 90 100 110 120 VSEDNSEDEI SNLVKLDLLE EKEGSLSPAS VGSDTLSDLG ISSLQDGLAL HIRSSMSGLH 130 140 150 160 170 180 LVKQGRDRKK IDSQRDFTVA SPAEFVTRFG GNKVIEKVLI ANNGIAAVKC MRSIRRWSYE 190 200 210 220 230 240 MFRNERAIRF VVMVTPEDLK ANAEYIKMAD HYVPVPGGPN NNNYANVELI LDIAKRIPVQ 250 260 270 280 290 300 AVWAGWGHAS ENPKLPELLL KNGIAFMGPP SQAMWALGDK IASSIVAQTA GIPTLPWSGS 310 320 330 340 350 360 GLRVDWQEND FSKRILNVPQ ELYEKGYVKD VDDGLQAAEE VGYPVMIKAS EGGGGKGIRK 370 380 390 400 410 420 VNNADDFPNL FRQVQAEVPG SPIFVMRLAK QSRHLEVQIL ADQYGNAISL FGRDCSVQRR 430 440 450 460 470 480 HQKIIEEAPA TIATPAVFEH MEQCAVKLAK MVGYVSAGTV EYLYSQDGSF YFLELNPRLQ 490 500 510 520 530 540 VEHPCTEMVA DVNLPAAQLQ IAMGIPLYRI KDIRMMYGVS PWGDSPIDFE DSAHVPCPRG 550 560 570 580 590 600 HVIAARITSE NPDEGFKPSS GTVQELNFRS NKNVWGYFSV AAAGGLHEFA DSQFGHCFSW 610 620 630 640 650 660 GENREEAISN MVVALKELSI RGDFRTTVEY LIKLLETESF QMNRIDTGWL DRLIAEKVQA 670 680 690 700 710 720 ERPDTMLGVV CGALHVADVS LRNSVSNFLH SLERGQVLPA HTLLNTVDVE LIYEGVKYVL 730 740 750 760 770 780 KVTRQSPNSY VVIMNGSCVE VDVHRLSDGG LLLSYDGSSY TTYMKEEVDR YRITIGNKTC 790 800 810 820 830 840 VFEKENDPSV MRSPSAGKLI QYIVEDGGHV FAGQCYAEIE VMKMVMTLTA VESGCIHYVK 850 860 870 880 890 900 RPGAALDPGC VLAKMQLDNP SKVQQAELHT GSLPRIQSTA LRGEKLHRVF HYVLDNLVNV 910 920 930 940 950 960 MNGYCLPDPF FSSKVKDWVE RLMKTLRDPS LPLLELQDIM TSVSGRIPPN VEKSIKKEMA 970 980 990 1000 1010 1020 QYASNITSVL CQFPSQQIAN ILDSHAATLN RKSEREVFFM NTQSIVQLVQ RYRSGIRGHM 1030 1040 1050 1060 1070 1080 KAVVMDLLRQ YLRVETQFQN GHYDKCVFAL REENKSDMNT VLNYIFSHAQ VTKKNLLVTM 1090 1100 1110 1120 1130 1140 LIDQLCGRDP TLTDELLNIL TELTQLSKTT NAKVALRARQ VLIASHLPSY ELRHNQVESI 1150 1160 1170 1180 1190 1200 FLSAIDMYGH QFCIENLQKL ILSETSIFDV LPNFFYHSNQ VVRMAALEVY VRRAYIAYEL 1210 1220 1230 1240 1250 1260 NSVQHRQLKD NTCVVEFQFM LPTSHPNRGN IPTLNRMSFS SNLNHYGMTH VASVSDVLLD 1270 1280 1290 1300 1310 1320 NSFTPPCQRM GGMVSFRTFE DFVRIFDEVM GCFSDSPPQS PTFPEAGHTS LYDEDKVPRD 1330 1340 1350 1360 1370 1380 EPIHILNVAI KTDCDIEDDR LAAMFREFTQ QNKATLVDHG IRRLTFLVAQ KDFRKQVNYE 1390 1400 1410 1420 1430 1440 VDRRFHREFP KFFTFRARDK FEEDRIYRHL EPALAFQLEL NRMRNFDLTA IPCANHKMHL 1450 1460 1470 1480 1490 1500 YLGAAKVEVG TEVTDYRFFV RAIIRHSDLV TKEASFEYLQ NEGERLLLEA MDELEVAFNN 1510 1520 1530 1540 1550 1560 TNVRTDCNHI FLNFVPTVIM DPSKIEESVR SMVMRYGSRL WKLRVLQAEL KINIRLTPTG 1570 1580 1590 1600 1610 1620 KAIPIRLFLT NESGYYLDIS LYKEVTDSRT AQIMFQAYGD KQGPLHGMLI NTPYVTKDLL 1630 1640 1650 1660 1670 1680 QSKRFQAQSL GTTYIYDIPE MFRQSLIKLW ESMSTQAFLP SPPLPSDMLT YTELVLDDQG 1690 1700 1710 1720 1730 1740 QLVHMNRLPG GNEIGMVAWK MTFKSPEYPE GRDIIVIGND ITYRIGSFGP QEDLLFLRAS 1750 1760 1770 1780 1790 1800 ELARAEGIPR IYVSANSGAR IGLAEEIRHM FHVAWVDPED PYKGYRYLYL TPQDYKRVSA 1810 1820 1830 1840 1850 1860 LNSVHCEHVE DEGESRYKIT DIIGKEEGIG PENLRGSGMI AGESSLAYNE IITISLVTCR 1870 1880 1890 1900 1910 1920 AIGIGAYLVR LGQRTIQVEN SHLILTGAGA LNKVLGREVY TSNNQLGGIQ IMHNNGVTHC 1930 1940 1950 1960 1970 1980 TVCDDFEGVF TVLHWLSYMP KSVHSSVPLL NSKDPIDRII EFVPTKTPYD PRWMLAGRPH 1990 2000 2010 2020 2030 2040 PTQKGQWLSG FFDYGSFSEI MQPWAQTVVV GRARLGGIPV GVVAVETRTV ELSIPADPAN 2050 2060 2070 2080 2090 2100 LDSEAKIIQQ AGQVWFPDSA FKTYQAIKDF NREGLPLMVF ANWRGFSGGM KDMYDQVLKF 2110 2120 2130 2140 2150 2160 GAYIVDGLRE CCQPVLVYIP PQAELRGGSW VVIDSSINPR HMEMYADRES RGSVLEPEGT 2170 2180 2190 2200 2210 2220 VEIKFRRKDL VKTMRRVDPV YIHLAERLGT PELSTAERKE LENKLKEREE FLIPIYHQVA 2230 2240 2250 2260 2270 2280 VQFADLHDTP GRMQEKGVIS DILDWKTSRT FFYWRLRRLL LEDLVKKKIH NANPELTDGQ 2290 2300 2310 2320 2330 2340 IQAMLRRWFV EVEGTVKAYV WDNNKDLAEW LEKQLTEEDG VHSVIEENIK CISRDYVLKQ 2350 2360 2370 2380 IRSLVQANPE VAMDSIIHMT QHISPTQRAE VIRILSTMDS PST

References

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[1]	"Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms." Abu-Elheiga L., Jayakumar A., Baldini A., Chirala S.S., Wakil S.J. Proc. Natl. Acad. Sci. U.S.A. 92:4011-4015(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[2]	"Human acetyl-CoA carboxylase 1 gene: presence of three promoters and heterogeneity at the 5'-untranslated mRNA region." Mao J., Chirala S.S., Wakil S.J. Proc. Natl. Acad. Sci. U.S.A. 100:7515-7520(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-366 (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-120 (ISOFORM 4). Tissue: Adipocyte.
[3]	"Acetyl-CoA carboxylase alpha gene and breast cancer susceptibility." Sinilnikova O.M., Ginolhac S.M., Magnard C., Leone M., Anczukow O., Hughes D., Moreau K., Thompson D., Coutanson C., Hall J., Romestaing P., Gerard J.-P., Bonadona V., Lasset C., Goldgar D.E., Joulin V., Venezia N.D., Lenoir G.M. Carcinogenesis 25:2417-2424(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-2271.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Brain.
[5]	"Characterisation of an N-terminal variant of acetyl-CoA carboxylase-alpha: expression in human tissues and evolutionary aspects." Travers M.T., Vallance A.J., Clegg R.A., Thomson R., Price N.T., Barber M.C. Biochim. Biophys. Acta 1634:97-106(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-113 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-93 (ISOFORM 3). Tissue: Mammary gland and Testis.
[6]	"Asymmetric expression of transcripts derived from the shared promoter between the divergently oriented ACACA and TADA2L genes." Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C., Joulin V. Genomics 85:71-84(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-47 (ISOFORM 1). Tissue: Testis.
[7]	Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-18; 39-45; 77-86; 99-111; 121-132; 153-170; 218-224; 267-276; 278-288; 323-335; 568-579; 589-615; 646-657; 748-755; 818-838; 985-992; 997-1008; 1083-1096; 1147-1169; 1192-1199; 1233-1247; 1283-1294; 1317-1325; 1327-1334; 1372-1385; 1401-1420; 1508-1514; 1553-1564; 1668-1687; 1714-1731; 1750-1759; 1782-1798; 1824-1833; 1838-1856; 1905-1916; 1922-1929; 1978-2009; 2063-2072; 2104-2111; 2115-2127; 2139-2161; 2200-2209; 2213-2218; 2221-2229 AND 2261-2293, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-80, MASS SPECTROMETRY. Tissue: Hepatoma.
[8]	"BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains." Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., Lenoir G.M., Venezia N.D. Oncogene 21:6729-6739(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BRCA1.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-53, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"BRCA1 affects lipid synthesis through its interaction with acetyl-CoA carboxylase." Moreau K., Dizin E., Ray H., Luquain C., Lefai E., Foufelle F., Billaud M., Lenoir G.M., Venezia N.D. J. Biol. Chem. 281:3172-3181(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BRCA1.
[11]	"ACCA phosphopeptide recognition by the BRCT repeats of BRCA1." Ray H., Moreau K., Dizin E., Callebaut I., Venezia N.D. J. Mol. Biol. 359:973-982(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-1263, MUTAGENESIS OF SER-78; SER-344; SER-432; SER-1201; SER-1263; SER-1585; SER-1952 AND SER-2211.
[12]	"Acetyl-CoA carboxylase deficiency: an inborn error of de novo fatty acid synthesis." Blom W., de Muinck Keizer S.M.P.F., Scholte H.R. N. Engl. J. Med. 305:465-466(1981) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN ACACAD.
[13]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29 AND SER-80, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-29, MASS SPECTROMETRY.
[17]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25 AND SER-29, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1334, MASS SPECTROMETRY.
[19]	"Crystal structure of Spot 14, a modulator of fatty acid synthesis." Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M., McKean W.B., Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J. Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, INTERACTION WITH MID1IP1.
[20]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-23; SER-29; SER-48 AND SER-80, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-80, MASS SPECTROMETRY.
[23]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-1687.
+	Additional computationally mapped references.

Web resources

Wikipedia

Acetyl-CoA carboxylase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U19822 mRNA. Translation: AAC50139.1.
AY315619 mRNA. Translation: AAP94114.1.
AY315620 mRNA. Translation: AAP94115.1.
AY315621 mRNA. Translation: AAP94116.1.
AY315623 mRNA. Translation: AAP94118.1.
AY315625 mRNA. Translation: AAP94120.1. Different initiation.
AY315627 mRNA. Translation: AAP94122.1.
AY237919 mRNA. Translation: AAP69841.1.
BC137287 mRNA. Translation: AAI37288.1.
AJ534888 mRNA. Translation: CAD59556.1.
AJ534889 mRNA. Translation: CAD59557.1.
AJ564444 mRNA. Translation: CAD92089.1.

IPI

IPI00011569.
IPI00396015.
IPI00396018.
IPI00847501.

PIR

I38928.

RefSeq

NP_942131.1. NM_198834.1.
NP_942133.1. NM_198836.1.
NP_942134.1. NM_198837.1.
NP_942135.1. NM_198838.1.
NP_942136.1. NM_198839.1.

UniGene

Hs.160556.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YL2	X-ray	2.30	A/B	78-617	[»]
3COJ	X-ray	3.21	H/I/J/K/L/M/N/O	1258-1270	[»]
4ASI	X-ray	2.80	A/B/C/D/E/F	1571-2338	[»]

ProteinModelPortal

Q13085.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36122N.

IntAct

Q13085. 26 interactions.

MINT

MINT-1415014.

PTM databases

PhosphoSite

Q13085.

Polymorphism databases

DMDM

118601083.

Proteomic databases

PaxDb

Q13085.

PRIDE

Q13085.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000335166; ENSP00000335323; ENSG00000132142.
ENST00000353139; ENSP00000344789; ENSG00000132142.
ENST00000360679; ENSP00000353898; ENSG00000132142.
ENST00000394406; ENSP00000377928; ENSG00000132142.
ENST00000451642; ENSP00000397282; ENSG00000132142.

GeneID

31.

KEGG

hsa:31.

UCSC

uc002hnk.3. human.
uc002hnl.3. human.
uc002hno.3. human.

Organism-specific databases

CTD

31.

GeneCards

GC17M035441.

HGNC

HGNC:84. ACACA.

HPA

CAB013715.

MIM

200350. gene.
613933. phenotype.

neXtProt

NX_Q13085.

PharmGKB

PA24421.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0511.

HOVERGEN

HBG005371.

InParanoid

Q13085.

KO

K11262.

OMA

ETESFQM.

OrthoDB

EOG4X0MRD.

Enzyme and pathway databases

BRENDA

6.4.1.2. 2681.

Reactome

REACT_111217. Metabolism.

SABIO-RK

Q13085.

UniPathway

UPA00655; UER00711.

Gene expression databases

ArrayExpress

Q13085.

Bgee

Q13085.

Genevestigator

Q13085.

GermOnline

ENSG00000132142. Homo sapiens.

Family and domain databases

Gene3D

3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.

InterPro

IPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
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.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]

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]

SMART

SM00878. Biotin_carb_C. 1 hit.
[Graphical view]

SUPFAM

SSF51230. Hybrid_motif. 1 hit.
SSF52440. PreATP-grasp-like. 1 hit.
SSF51246. Rudmnt_hyb_motif. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

BindingDB

Q13085.

ChEMBL

CHEMBL3351.

ChiTaRS

ACACA. human.

DrugBank

DB00121. Biotin.

EvolutionaryTrace

Q13085.

GenomeRNAi

31.

NextBio

111.

SOURCE

Search...

Entry information

Entry name

ACACA_HUMAN

Accession

Primary (citable) accession number: Q13085
Secondary accession number(s): B2RP68 , Q6KEV6, Q6XDA8, Q7Z2G8, Q7Z561, Q7Z563, Q7Z564, Q86WB2, Q86WB3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	October 31, 2006
Last modified:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.