CRAT | ENSG00000095321 | NCBI 1384

Details for: CRAT

Gene ID: 1384

Symbol: CRAT

Ensembl ID: ENSG00000095321

Description: carnitine O-acetyltransferase

Associated with

Beta-oxidation of pristanoyl-coa
(R-HSA-389887)
Fatty acid metabolism
(R-HSA-8978868)
Metabolism
(R-HSA-1430728)
Metabolism of lipids
(R-HSA-556833)
Peroxisomal lipid metabolism
(R-HSA-390918)
Peroxisomal protein import
(R-HSA-9033241)
Protein localization
(R-HSA-9609507)
Acyl-coa oxidase activity
(GO:0003997)
Carnitine metabolic process, coa-linked
(GO:0019254)
Carnitine o-acetyltransferase activity
(GO:0004092)
Carnitine o-octanoyltransferase activity
(GO:0008458)
Cytosol
(GO:0005829)
Endoplasmic reticulum
(GO:0005783)
Fatty acid beta-oxidation using acyl-coa oxidase
(GO:0033540)
Medium-chain fatty acid metabolic process
(GO:0051791)
Mitochondrial inner membrane
(GO:0005743)
Mitochondrion
(GO:0005739)
Peroxisomal matrix
(GO:0005782)
Peroxisome
(GO:0005777)
Short-chain fatty acid metabolic process
(GO:0046459)

Other Information

Proteins

Carnitine acetyltransferase

Genular Protein ID: 2676163847

Symbol: CACP_HUMAN

Name: Carnitine acetyltransferase

UniProtKB Accession Codes:

P43155 Q5T952 Q9BW16

Database IDs:

Citations:

PubMed ID: 15164053

Title: DNA sequence and analysis of human chromosome 9.

PubMed ID: 15164053

DOI: 10.1038/nature02465

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 7945262

Title: Divergent sequences in the 5' region of cDNA suggest alternative splicing as a mechanism for the generation of carnitine acetyltransferases with different subcellular localizations.

PubMed ID: 7945262

DOI: 10.1042/bj3030037

PubMed ID: 7829107

Title: Molecular cloning of cDNAs encoding human carnitine acetyltransferase and mapping of the corresponding gene to chromosome 9q34.1.

PubMed ID: 7829107

DOI: 10.1006/geno.1994.1463

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 23485643

Title: Substrate specificity of human carnitine acetyltransferase: Implications for fatty acid and branched-chain amino acid metabolism.

PubMed ID: 23485643

DOI: 10.1016/j.bbadis.2013.02.012

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: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 29395073

Title: Impaired Transferrin Receptor Palmitoylation and Recycling in Neurodegeneration with Brain Iron Accumulation.

PubMed ID: 29395073

DOI: 10.1016/j.ajhg.2018.01.003

PubMed ID: 12562770

Title: Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer.

PubMed ID: 12562770

DOI: 10.1074/jbc.m212356200

PubMed ID: 15099582

Title: Structural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase.

PubMed ID: 15099582

DOI: 10.1016/j.jsb.2004.01.011

Sequence Information:

Length: 626
Mass: 70858
Checksum: 51B65E7C94E458D7
Sequence:

MLAFAARTVV KPLGFLKPFS LMKASSRFKA HQDALPRLPV PPLQQSLDHY LKALQPIVSE 
EEWAHTKQLV DEFQASGGVG ERLQKGLERR ARKTENWLSE WWLKTAYLQY RQPVVIYSSP 
GVMLPKQDFV DLQGQLRFAA KLIEGVLDFK VMIDNETLPV EYLGGKPLCM NQYYQILSSC 
RVPGPKQDTV SNFSKTKKPP THITVVHNYQ FFELDVYHSD GTPLTADQIF VQLEKIWNSS 
LQTNKEPVGI LTSNHRNSWA KAYNTLIKDK VNRDSVRSIQ KSIFTVCLDA TMPRVSEDVY 
RSHVAGQMLH GGGSRLNSGN RWFDKTLQFI VAEDGSCGLV YEHAAAEGPP IVTLLDYVIE 
YTKKPELVRS PLVPLPMPKK LRFNITPEIK SDIEKAKQNL SIMIQDLDIT VMVFHHFGKD 
FPKSEKLSPD AFIQMALQLA YYRIYGQACA TYESASLRMF HLGRTDTIRS ASMDSLTFVK 
AMDDSSVTEH QKVELLRKAV QAHRGYTDRA IRGEAFDRHL LGLKLQAIED LVSMPDIFMD 
TSYAIAMHFH LSTSQVPAKT DCVMFFGPVV PDGYGVCYNP MEAHINFSLS AYNSCAETNA 
ARLAHYLEKA LLDMRALLQS HPRAKL

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: CRAT

Associated with

Other Information

DNA sequence and analysis of human chromosome 9. PubMed ID: 15164053

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Divergent sequences in the 5' region of cDNA suggest alternative splicing as a mechanism for the generation of carnitine acetyltransferases with different subcellular localizations. PubMed ID: 7945262

Molecular cloning of cDNAs encoding human carnitine acetyltransferase and mapping of the corresponding gene to chromosome 9q34.1. PubMed ID: 7829107

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Substrate specificity of human carnitine acetyltransferase: Implications for fatty acid and branched-chain amino acid metabolism. PubMed ID: 23485643

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

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

Impaired Transferrin Receptor Palmitoylation and Recycling in Neurodegeneration with Brain Iron Accumulation. PubMed ID: 29395073

Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer. PubMed ID: 12562770

Structural and mutational characterization of L-carnitine binding to human carnitine acetyltransferase. PubMed ID: 15099582