ACACB | ENSG00000076555 | NCBI 32

Details for: ACACB

Gene ID: 32

Symbol: ACACB

Ensembl ID: ENSG00000076555

Description: acetyl-CoA carboxylase beta

Associated with

Activation of gene expression by srebf (srebp)
(R-HSA-2426168)
Biotin transport and metabolism
(R-HSA-196780)
Carnitine metabolism
(R-HSA-200425)
Chrebp activates metabolic gene expression
(R-HSA-163765)
Fatty acid metabolism
(R-HSA-8978868)
Integration of energy metabolism
(R-HSA-163685)
Metabolism
(R-HSA-1430728)
Metabolism of lipids
(R-HSA-556833)
Metabolism of steroids
(R-HSA-8957322)
Metabolism of vitamins and cofactors
(R-HSA-196854)
Metabolism of water-soluble vitamins and cofactors
(R-HSA-196849)
Regulation of cholesterol biosynthesis by srebp (srebf)
(R-HSA-1655829)
Acetyl-coa carboxylase activity
(GO:0003989)
Acetyl-coa metabolic process
(GO:0006084)
Atp binding
(GO:0005524)
Biotin binding
(GO:0009374)
Cytosol
(GO:0005829)
Energy homeostasis
(GO:0097009)
Fatty acid biosynthetic process
(GO:0006633)
Fatty acid oxidation
(GO:0019395)
Glucose import
(GO:0046323)
Identical protein binding
(GO:0042802)
Intracellular aspartate homeostasis
(GO:0090459)
Intracellular glutamate homeostasis
(GO:0090461)
Lactic acid secretion
(GO:0046722)
Malonyl-coa biosynthetic process
(GO:2001295)
Metal ion binding
(GO:0046872)
Mitochondrial fatty acid beta-oxidation multienzyme complex
(GO:0016507)
Mitochondrial outer membrane
(GO:0005741)
Mitochondrion
(GO:0005739)
Negative regulation of fatty acid beta-oxidation
(GO:0031999)
Negative regulation of gene expression
(GO:0010629)
Nucleus
(GO:0005634)
Pentose-phosphate shunt
(GO:0006098)
Positive regulation of heart growth
(GO:0060421)
Positive regulation of lipid storage
(GO:0010884)
Protein binding
(GO:0005515)
Protein homotetramerization
(GO:0051289)
Regulation of cardiac muscle hypertrophy in response to stress
(GO:1903242)
Regulation of glucose metabolic process
(GO:0010906)
Response to nutrient
(GO:0007584)
Response to organic cyclic compound
(GO:0014070)
Response to xenobiotic stimulus
(GO:0009410)
Tricarboxylic acid metabolic process
(GO:0072350)

Other Information

Proteins

ACC-beta

Genular Protein ID: 3803571407

Symbol: ACACB_HUMAN

Name: ACC-beta

UniProtKB Accession Codes:

O00763 A6NK36 Q16852 Q1HEC1 Q6KE87 Q6KE89 Q6TY48

Database IDs:

Citations:

PubMed ID: 9099716

Title: Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two isoforms.

PubMed ID: 9099716

DOI: 10.1074/jbc.272.16.10669

PubMed ID: 16854592

Title: Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes.

PubMed ID: 16854592

DOI: 10.1016/j.pep.2006.06.005

PubMed ID: 16541075

Title: The finished DNA sequence of human chromosome 12.

PubMed ID: 16541075

DOI: 10.1038/nature04569

PubMed ID: 8670171

Title: Identification of a second human acetyl-CoA carboxylase gene.

PubMed ID: 8670171

DOI: 10.1042/bj3160915

PubMed ID: 10677481

Title: The subcellular localization of acetyl-CoA carboxylase 2.

PubMed ID: 10677481

DOI: 10.1073/pnas.97.4.1444

PubMed ID: 12488245

Title: Regulation of 5'AMP-activated protein kinase activity and substrate utilization in exercising human skeletal muscle.

PubMed ID: 12488245

DOI: 10.1152/ajpendo.00436.2002

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19236960

Title: Characterization of recombinant human acetyl-CoA carboxylase-2 steady-state kinetics.

PubMed ID: 19236960

DOI: 10.1016/j.bbapap.2009.02.004

PubMed ID: 19190759

Title: ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus.

PubMed ID: 19190759

DOI: 10.1371/journal.pone.0004369

PubMed ID: 20457939

Title: Induced polymerization of mammalian acetyl-CoA carboxylase by MIG12 provides a tertiary level of regulation of fatty acid synthesis.

PubMed ID: 20457939

DOI: 10.1073/pnas.1001292107

PubMed ID: 20952656

Title: Crystal structure of Spot 14, a modulator of fatty acid synthesis.

PubMed ID: 20952656

DOI: 10.1073/pnas.1012736107

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 17876819

Title: Crystal structure of the biotin carboxylase domain of human acetyl-CoA carboxylase 2.

PubMed ID: 17876819

DOI: 10.1002/prot.21611

PubMed ID: 18247344

Title: Biotinoyl domain of human acetyl-CoA carboxylase: Structural insights into the carboxyl transfer mechanism.

PubMed ID: 18247344

DOI: 10.1002/prot.21952

PubMed ID: 19390150

Title: The human ACC2 CT-domain C-terminus is required for full functionality and has a novel twist.

PubMed ID: 19390150

DOI: 10.1107/s0907444909008014

PubMed ID: 19900410

Title: Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK.

PubMed ID: 19900410

DOI: 10.1016/j.bbrc.2009.11.029

PubMed ID: 26976583

Title: Acetyl-CoA carboxylase inhibition by ND-630 reduces hepatic steatosis, improves insulin sensitivity, and modulates dyslipidemia in rats.

PubMed ID: 26976583

DOI: 10.1073/pnas.1520686113

PubMed ID: 18772397

Title: Core signaling pathways in human pancreatic cancers revealed by global genomic analyses.

PubMed ID: 18772397

DOI: 10.1126/science.1164368

Sequence Information:

Length: 2458
Mass: 276541
Checksum: ED12674A1A8A0706
Sequence:

MVLLLCLSCL IFSCLTFSWL KIWGKMTDSK PITKSKSEAN LIPSQEPFPA SDNSGETPQR 
NGEGHTLPKT PSQAEPASHK GPKDAGRRRN SLPPSHQKPP RNPLSSSDAA PSPELQANGT 
GTQGLEATDT NGLSSSARPQ GQQAGSPSKE DKKQANIKRQ LMTNFILGSF DDYSSDEDSV 
AGSSRESTRK GSRASLGALS LEAYLTTGEA ETRVPTMRPS MSGLHLVKRG REHKKLDLHR 
DFTVASPAEF VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT 
PEDLKANAEY IKMADHYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG WGHASENPKL 
PELLCKNGVA FLGPPSEAMW ALGDKIASTV VAQTLQVPTL PWSGSGLTVE WTEDDLQQGK 
RISVPEDVYD KGCVKDVDEG LEAAERIGFP LMIKASEGGG GKGIRKAESA EDFPILFRQV 
QSEIPGSPIF LMKLAQHARH LEVQILADQY GNAVSLFGRD CSIQRRHQKI VEEAPATIAP 
LAIFEFMEQC AIRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL 
PAAQLQIAMG VPLHRLKDIR LLYGESPWGV TPISFETPSN PPLARGHVIA ARITSENPDE 
GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF GHCFSWGENR EEAISNMVVA 
LKELSIRGDF RTTVEYLINL LETESFQNND IDTGWLDYLI AEKVQAEKPD IMLGVVCGAL 
NVADAMFRTC MTDFLHSLER GQVLPADSLL NLVDVELIYG GVKYILKVAR QSLTMFVLIM 
NGCHIEIDAH RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP 
SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQERG RVKYIKRPGA VLEAGCVVAR 
LELDDPSKVH PAEPFTGELP AQQTLPILGE KLHQVFHSVL ENLTNVMSGF CLPEPVFSIK 
LKEWVQKLMM TLRHPSLPLL ELQEIMTSVA GRIPAPVEKS VRRVMAQYAS NITSVLCQFP 
SQQIATILDC HAATLQRKAD REVFFINTQS IVQLVQRYRS GIRGYMKTVV LDLLRRYLRV 
EHHFQQAHYD KCVINLREQF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD 
ELISILNELT QLSKSEHCKV ALRARQILIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP 
ENLKKLILSE TTIFDVLPTF FYHANKVVCM ASLEVYVRRG YIAYELNSLQ HRQLPDGTCV 
VEFQFMLPSS HPNRMTVPIS ITNPDLLRHS TELFMDSGFS PLCQRMGAMV AFRRFEDFTR 
NFDEVISCFA NVPKDTPLFS EARTSLYSED DCKSLREEPI HILNVSIQCA DHLEDEALVP 
ILRTFVQSKK NILVDYGLRR ITFLIAQEKE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL 
ELNRMRNFDL TAVPCANHKM HLYLGAAKVK EGVEVTDHRF FIRAIIRHSD LITKEASFEY 
LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPFKIEES VRYMVMRYGS 
RLWKLRVLQA EVKINIRQTT TGSAVPIRLF ITNESGYYLD ISLYKEVTDS RSGNIMFHSF 
GNKQGPQHGM LINTPYVTKD LLQAKRFQAQ TLGTTYIYDF PEMFRQALFK LWGSPDKYPK 
DILTYTELVL DSQGQLVEMN RLPGGNEVGM VAFKMRFKTQ EYPEGRDVIV IGNDITFRIG 
SFGPGEDLLY LRASEMARAE GIPKIYVAAN SGARIGMAEE IKHMFHVAWV DPEDPHKGFK 
YLYLTPQDYT RISSLNSVHC KHIEEGGESR YMITDIIGKD DGLGVENLRG SGMIAGESSL 
AYEEIVTISL VTCRAIGIGA YLVRLGQRVI QVENSHIILT GASALNKVLG REVYTSNNQL 
GGVQIMHYNG VSHITVPDDF EGVYTILEWL SYMPKDNHSP VPIITPTDPI DREIEFLPSR 
APYDPRWMLA GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLG GIPVGVIAVE 
TRTVEVAVPA DPANLDSEAK IIQQAGQVWF PDSAYKTAQA VKDFNREKLP LMIFANWRGF 
SGGMKDMYDQ VLKFGAYIVD GLRQYKQPIL IYIPPYAELR GGSWVVIDAT INPLCIEMYA 
DKESRGGVLE PEGTVEIKFR KKDLIKSMRR IDPAYKKLME QLGEPDLSDK DRKDLEGRLK 
AREDLLLPIY HQVAVQFADF HDTPGRMLEK GVISDILEWK TARTFLYWRL RRLLLEDQVK 
QEILQASGEL SHVHIQSMLR RWFVETEGAV KAYLWDNNQV VVQWLEQHWQ AGDGPRSTIR 
ENITYLKHDS VLKTIRGLVE ENPEVAVDCV IYLSQHISPA ERAQVVHLLS TMDSPAST

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: ACACB

Associated with

Other Information

Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two isoforms. PubMed ID: 9099716

Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes. PubMed ID: 16854592

The finished DNA sequence of human chromosome 12. PubMed ID: 16541075

Identification of a second human acetyl-CoA carboxylase gene. PubMed ID: 8670171

The subcellular localization of acetyl-CoA carboxylase 2. PubMed ID: 10677481

Regulation of 5'AMP-activated protein kinase activity and substrate utilization in exercising human skeletal muscle. PubMed ID: 12488245

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Characterization of recombinant human acetyl-CoA carboxylase-2 steady-state kinetics. PubMed ID: 19236960

ACC2 is expressed at high levels in human white adipose and has an isoform with a novel N-terminus. PubMed ID: 19190759

Induced polymerization of mammalian acetyl-CoA carboxylase by MIG12 provides a tertiary level of regulation of fatty acid synthesis. PubMed ID: 20457939

Crystal structure of Spot 14, a modulator of fatty acid synthesis. PubMed ID: 20952656

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Crystal structure of the biotin carboxylase domain of human acetyl-CoA carboxylase 2. PubMed ID: 17876819

Biotinoyl domain of human acetyl-CoA carboxylase: Structural insights into the carboxyl transfer mechanism. PubMed ID: 18247344

The human ACC2 CT-domain C-terminus is required for full functionality and has a novel twist. PubMed ID: 19390150

Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK. PubMed ID: 19900410

Acetyl-CoA carboxylase inhibition by ND-630 reduces hepatic steatosis, improves insulin sensitivity, and modulates dyslipidemia in rats. PubMed ID: 26976583

Core signaling pathways in human pancreatic cancers revealed by global genomic analyses. PubMed ID: 18772397