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
HMF1Protein HMF1; Member of the p14.5 protein family; functionally complements Mmf1p function when targeted to mitochondria; heat shock inducible; high-dosage growth inhibitor; forms a homotrimer in vitro; HMF1 has a paralog, MMF1, that arose from the whole genome duplication; Belongs to the RutC family (129 aa)    
Predicted Functional Partners:
Diphthine--ammonia ligase; Diphthamide synthetase; catalyzes the last amidation step of diphthamide biosynthesis using ammonium and ATP; evolutionarily conserved in eukaryotes; dph6 mutants exhibit diphthine accumulation and resistance to sordarin, which is indicative of defects in diphthamide formation on EF2; green fluorescent protein (GFP)-tagged protein localizes to the cytoplasm; DPH6/YLR143W is not an essential gene; In the C-terminal section; belongs to the RutC family
Diphthine methyl ester synthase; Methyltransferase required for synthesis of diphthamide; diphthamide is a modified histidine residue of translation elongation factor 2 (Eft1p or Eft2p); not essential for viability; GFP-Dph5p fusion protein localizes to the cytoplasm; Belongs to the diphthine synthase family
Diphthine methyltransferase; Methylesterase performing penultimate step of diphthamide biosynthesis; hydrolyzes methylated diphthine to produce diphthine and allows Dph6-catalyzed amidation reaction to occur; deletion leads to resistance to sordarin and accumulation of methylatediphthine; WD40 domain-containing protein; involved in endosomal recycling; forms complex with Rtt10p that functions in retromer-mediated pathway for recycling internalized cell-surface proteins
2-(3-amino-3-carboxypropyl)histidine synthase subunit 1; Protein required for synthesis of diphthamide; required along with Dph2p, Kti11p, Jjj3p, and Dph5p; diphthamide is a modified histidine residue of translation elongation factor 2 (Eft1p or Eft2p); may act in a complex with Dph2p and Kti11p
Diphthamide biosynthesis protein 3; Zn-ribbon protein that co-purifies with Dph1 and Dph2; in a complex required for synthesis of diphthamide on translation factor eEF2 and with Elongator subunits Iki3p, Elp2p, and Elp3p; involved in modification of wobble nucleosides in tRNAs; forms a stable heterodimer with Ats1p; Belongs to the DPH3 family
ATP-dependent clpX-like chaperone, mitochondrial; Non-proteolytic ATPase of the AAA family; stimulates incorporation of the pyridoxal phosphate cofactor into Hem1p (5-aminolevulinic acid synthase); localized to the mitochondrial matrix; ortholog of vertebrate CLPX, which promotes erythropoiesis
2-(3-amino-3-carboxypropyl)histidine synthase subunit 2; Protein required for synthesis of diphthamide; required along with Dph1p, Kti11p, Jjj3p, and Dph5p; diphthamide is a modified histidine residue of translation elongation factor 2 (Eft1p or Eft2p); may act in a complex with Dph1p and Kti11p
Putative mitochondrial ribosomal protein of the large subunit; similar to E. coli L34 ribosomal protein; required for respiratory growth, as are most mitochondrial ribosomal proteins; protein increases in abundance and relocalizes to the plasma membrane upon DNA replication stress
MIOREX complex component 3; Protein that associates with mitochondrial ribosome; likely functions in cristae junction formation; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies
Mitochondrial ribosomal protein of the large subunit; appears as two protein spots (YmL34 and YmL38) on two-dimensional SDS gels; protein abundance increases in response to DNA replication stress
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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