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  • 11.0 [archived version]
STRINGSTRING
DAO DAO CRAT CRAT SCP2 SCP2 HSD17B4 HSD17B4 GNPAT GNPAT ECH1 ECH1 CPT2 CPT2 DECR2 DECR2 ACOX1 ACOX1 EHHADH EHHADH CAT CAT
"CRAT" - Carnitine O-acetyltransferase in Homo sapiens
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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CRATCarnitine O-acetyltransferase; Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria; Belongs to the carnitine/choline acetyltransferase family (626 aa)    
Predicted Functional Partners:
HSD17B4
Peroxisomal multifunctional enzyme type 2; Bifunctional enzyme acting on the peroxisomal beta- oxidation pathway for fatty acids. Catalyzes the formation of 3- ketoacyl-CoA intermediates from both straight-chain and 2-methyl- branched-chain fatty acids; Short chain dehydrogenase/reductase superfamily (761 aa)
     
 
  0.989
CAT
Catalase; Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells; Belongs to the catalase family (527 aa)
     
 
  0.966
ACOX1
Peroxisomal acyl-coenzyme A oxidase 1; Catalyzes the desaturation of acyl-CoAs to 2-trans- enoyl-CoAs. Isoform 1 shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Isoform 2 is twice as active as isoform 1 against 16-hydroxy- palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl- CoA (660 aa)
     
 
  0.962
CPT2
Carnitine O-palmitoyltransferase 2, mitochondrial; Carnitine palmitoyltransferase 2 (658 aa)
   
 
0.961
DAO
D-amino-acid oxidase; Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D- amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids; Belongs to the DAMOX/DASOX family (347 aa)
         
  0.955
ECH1
Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial; Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4- trans-dienoyl-CoA (328 aa)
     
 
  0.955
DECR2
Peroxisomal 2,4-dienoyl-CoA reductase; Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19- docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid; Belongs to the short-chain dehydrogenases/reducta [...] (292 aa)
     
 
  0.953
EHHADH
Peroxisomal bifunctional enzyme; enoyl-CoA hydratase and 3-hydroxyacyl CoA dehydrogenase; In the C-terminal section; belongs to the 3- hydroxyacyl-CoA dehydrogenase family (723 aa)
     
 
  0.952
GNPAT
Glyceronephosphate O-acyltransferase (680 aa)
     
 
  0.951
SCP2
Non-specific lipid-transfer protein; Mediates in vitro the transfer of all common phospholipids, cholesterol and gangliosides between membranes. May play a role in regulating steroidogenesis (547 aa)
     
 
  0.948
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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