STRINGSTRING
HPA3 protein (Saccharomyces cerevisiae) - STRING interaction network
"HPA3" - D-Amino acid N-acetyltransferase, catalyzes N-acetylation of D-amino acids through ordered bi-bi mechanism in which acetyl-CoA is first substrate bound and CoA is last product liberated in Saccharomyces cerevisiae
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
HPA3D-Amino acid N-acetyltransferase, catalyzes N-acetylation of D-amino acids through ordered bi-bi mechanism in which acetyl-CoA is first substrate bound and CoA is last product liberated; similar to Hpa2p, acetylates histones weakly in vitro; N-acetyltransferase that acetylates histone H4 at ’Lys- 8’. Also acetylates polyamines like putrescine, spermidine and spermine (PubMed-23775086). Acts on a wide range of D-amino acids. Catalyzes the N-acetylation through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated ( [...] (179 aa)    
Predicted Functional Partners:
HPA2
Tetrameric histone acetyltransferase with similarity to Gcn5p, Hat1p, Elp3p, and Hpa3p; acetylates histones H3 and H4 in vitro and exhibits autoacetylation activity; N-acetyltransferase that acetylates histone H3 at ’Lys- 14’ and histone H4 at ’Lys-5’ and ’Lys-12’. Also acetylates polyamines like putrescine, spermidine and spermine, and certain other small basic proteins like nuclear HMG proteins (156 aa)
   
   
0.805
IMD2
Inosine monophosphate dehydrogenase, catalyzes the rate-limiting step in GTP biosynthesis, expression is induced by mycophenolic acid resulting in resistance to the drug, expression is repressed by nutrient limitatio; Catalyzes the conversion of inosine 5’-phosphate (IMP) to xanthosine 5’-phosphate (XMP), the first committed and rate- limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. In contrast to the other IMPDH alleles IMD3 and IMD4, the enzymatic activity of IMD2 seems to be intrinsically drug resistant (523 aa)
         
  0.659
IMD1
Nonfunctional protein with homology to IMP dehydrogenase; probable pseudogene, located close to the telomere; is not expressed at detectable levels; YAR073W and YAR075W comprise a continuous reading frame in some strains of S. cerevisiae (403 aa)
         
  0.659
UGA1
Gamma-aminobutyrate (GABA) transaminase (4-aminobutyrate aminotransferase) involved in the 4-aminobutyrate and glutamate degradation pathways; required for normal oxidative stress tolerance and nitrogen utilization; Required for the degradation of gamma-aminobutyric acid (GABA), which is important for utilization of GABA as nitrogen source and for oxidative stress tolerance. Deaminates GABA to succinate semialdehyde, which in turn is converted to succinate by the succinate-semialdehyde dehydrogenase UGA2. Cannot transaminate beta-alanine (BAL) (471 aa)
       
  0.643
IMD3
Inosine monophosphate dehydrogenase, catalyzes the first step of GMP biosynthesis, member of a four-gene family in S. cerevisiae, constitutively expressed; Catalyzes the conversion of inosine 5’-phosphate (IMP) to xanthosine 5’-phosphate (XMP), the first committed and rate- limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth (523 aa)
         
  0.633
POX1
Fatty-acyl coenzyme A oxidase, involved in the fatty acid beta-oxidation pathway; localized to the peroxisomal matrix (748 aa)
         
  0.632
ERG10
Acetyl-CoA C-acetyltransferase (acetoacetyl-CoA thiolase), cytosolic enzyme that transfers an acetyl group from one acetyl-CoA molecule to another, forming acetoacetyl-CoA; involved in the first step in mevalonate biosynthesis; Catalyzes the formation of acetoacetyl-CoA in the biosynthesis of mevalonate, an intermediate required for the biosynthesis of sterols and nonsterol isoprenoids (398 aa)
         
  0.628
POT1
3-ketoacyl-CoA thiolase with broad chain length specificity, cleaves 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA during beta-oxidation of fatty acids (417 aa)
         
  0.628
ALD6
Cytosolic aldehyde dehydrogenase, activated by Mg2+ and utilizes NADP+ as the preferred coenzyme; required for conversion of acetaldehyde to acetate; constitutively expressed; locates to the mitochondrial outer surface upon oxidative stress; Cytosolic aldehyde dehydrogenase which utilizes NADP+ as the preferred coenzyme. Performs the conversion of acetaldehyde to acetate (500 aa)
   
 
  0.627
ALD4
Mitochondrial aldehyde dehydrogenase, required for growth on ethanol and conversion of acetaldehyde to acetate; phosphorylated; activity is K+ dependent; utilizes NADP+ or NAD+ equally as coenzymes; expression is glucose repressed; Potassium-activated aldehyde dehydrogenase involved in acetate formation during anaerobic growth on glucose (519 aa)
   
 
  0.627
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
Server load: low (7%) [HD]