STRING protein interaction network
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 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 to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
HFA1Acetyl-CoA carboxylase, mitochondrial; Mitochondrial acetyl-coenzyme A carboxylase; catalyzes production of malonyl-CoA in mitochondrial fatty acid biosynthesis; relocalizes from mitochondrion to cytoplasm upon DNA replication stress; genetic and comparative analysis suggests that translation begins at a non-canonical (Ile) start codon at -372 relative to the annotated start codon (2123 aa)    
Predicted Functional Partners:
Beta subunit of fatty acid synthetase; complex catalyzes the synthesis of long-chain saturated fatty acids; contains acetyltransacylase, dehydratase, enoyl reductase, malonyl transacylase, and palmitoyl transacylase activities
Alpha subunit of fatty acid synthetase; complex catalyzes the synthesis of long-chain saturated fatty acids; contains the acyl-carrier protein domain and beta-ketoacyl reductase, beta-ketoacyl synthase and self-pantetheinylation activities
Acetyl-coA synthetase isoform; along with Acs1p, acetyl-coA synthetase isoform is the nuclear source of acetyl-coA for histone acetylation; mutants affect global transcription; required for growth on glucose; expressed under anaerobic conditions; Belongs to the ATP-dependent AMP-binding enzyme family
Malonyl CoA-acyl carrier protein transacylase, mitochondrial; Predicted malonyl-CoA:ACP transferase; putative component of a type-II mitochondrial fatty acid synthase that produces intermediates for phospholipid remodeling
Biotin:apoprotein ligase; covalently modifies proteins with the addition of biotin, required for acetyl-CoA carboxylase (Acc1p) holoenzyme formation; comparative analysis suggests that a mitochondrially targeted form may result from translation starting at a non-canonical codon upstream of the annotated start codon; human homolog HLCS can complement yeast BPL1 mutant
Acetyl-coA synthetase isoform; along with Acs2p, acetyl-coA synthetase isoform is the nuclear source of acetyl-coA for histone acetylation; expressed during growth on nonfermentable carbon sources and under aerobic conditions; Belongs to the ATP-dependent AMP-binding enzyme family
Acetyl-CoA carboxylase, biotin containing enzyme; catalyzes carboxylation of cytosolic acetyl-CoA to form malonyl-CoA and regulates histone acetylation by regulating the availablity of acetyl-CoA; required for de novo biosynthesis of long-chain fatty acids; ACC1 has a paralog, HFA1, that arose from the whole genome duplication
Acetyl-CoA hydrolase; Protein with CoA transferase activity; particularly for CoASH transfer from succinyl-CoA to acetate; has minor acetyl-CoA-hydrolase activity; phosphorylated; required for acetate utilization and for diploid pseudohyphal growth; Belongs to the acetyl-CoA hydrolase/transferase family
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; human ACAT1 functionally complements the growth defect caused by repression of ERG10 expression
Pyruvate dehydrogenase e2 component (dihydrolipoamide acetyltransferase); Dihydrolipoamide acetyltransferase component (E2) of the PDC; the pyruvate dehydrogenase complex (PDC) catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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