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
MOD5Delta 2-isopentenyl pyrophosphate:tRNA isopentenyl transferase; required for biosynthesis of isopentenyladenosine in mitochondrial and cytoplasmic tRNAs; also has a role in tRNA gene-mediated silencing; gene encodes two isozymic forms; converts to a prion form, prion conversion contributes to azole antifungal resistance by upregulating ergosterol biosynthesis; homolog of human TRIT1, a mutation in which is associated with severe combined respiratory chain defects (428 aa)    
Predicted Functional Partners:
tRNA (guanine(26)-N(2))-dimethyltransferase, mitochondrial; tRNA methyltransferase; two forms of protein are made by alternative translation starts; localizes to both nucleus and mitochondrion to produce modified base N2,N2-dimethylguanosine in tRNAs in both compartments; nuclear Trm1p is evenly distributed around inner nuclear membrane in WT, but mislocalizes as puncta near ER-nucleus junctions in spindle pole body (SPB) mutants; both Trm1p inner nuclear membrane targeting and maintenance depend upon SPB
tRNA-dihydrouridine(20) synthase [NAD(P)+]; Dihydrouridine synthase; member of a family of dihydrouridine synthases including Dus1p, Smm1p, Dus3p, and Dus4p; modifies uridine residues at position 20 of cytoplasmic tRNAs
Methionyl-tRNA formyltransferase, mitochondrial; Methionyl-tRNA formyltransferase; catalyzes the formylation of initiator Met-tRNA in mitochondria; potential Cdc28p substrate
2'-O-ribose methyltransferase; methylates the 2'-O-ribose of tRNA-Phe, tRNA-Trp, and tRNA-Leu at positions C32 and N34 of tRNA anticodon loop; crucial biological role likely modification of tRNA-Phe; interacts with Trm732p and Rtt10p in 2'-O-methylation of C32 and N34 substrate tRNAs, respectively; yeast null mutant can be functionally complemented by human FTSJ1, mutations in which have been implicated in nonsyndromic X-linked intellectual disability (NSXLID); Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. TRM7 subfamily
tRNA(m(1)G37)methyltransferase; methylates a tRNA base adjacent to the anticodon that has a role in prevention of frameshifting; localized to both cytoplasm and mitochondria, and modifies both cytoplasmic and mitochondrial tRNAs; mutations in human ortholog TRMT5 are associated with skeletal muscle respiratory chain deficiencies, and trm5 mutations analogous to disease mutations decrease respiration; Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family
tRNA methyltransferase; methylates the N-1 position of guanine at position 9 in tRNAs; protein abundance increases in response to DNA replication stress; member of the SPOUT (SpoU-TrmD) methyltransferase family; human ortholog TRMT10A plays a role in the pathogenesis of microcephaly and early onset diabetes; an 18-mer originates from the TRM10 locus; genetic analysis shows the 18-mer is the translation regulator; Belongs to the class IV-like SAM-binding methyltransferase superfamily. TRM10 family
Pseudouridine synthase; catalyzes pseudouridylation at positions 35 and 56 in U2 snRNA, position 50 in 5S rRNA, position 13 in cytoplasmic tRNAs, and position 35 in pre-tRNA(Tyr); also pseudouridylates some mRNAs; relocates from nucleus to cytoplasm during heat shock and differentially modifies some mRNAs during heat shock; conserved in archaea, vertebrates, and some bacteria; Belongs to the pseudouridine synthase TruD family
Threonylcarbamoyl-AMP synthase; Protein involved in threonylcarbamoyl adenosine biosynthesis; Sua5p and Qri7p are necessary and sufficient for RNA t6A modification in vitro; null mutant lacks N6-threonylcarbamoyl adenosine (t6A) modification in the anticodon loop of ANN-decoding tRNA; member of conserved YrdC/Sua5 family; binds single-stranded telomeric DNA and null mutant has abnormal telomere length
Multisite-specific tRNA:(cytosine-C(5))-methyltransferase; S-adenosyl-L-methionine-dependent tRNA: m5C-methyltransferase; methylates cytosine to m5C at several positions in tRNAs and intron-containing pre-tRNAs; increases proportion of tRNALeu(CAA) with m5C at wobble position in response to hydrogen peroxide, causing selective translation of mRNA from genes enriched in TTG codon; loss of NCL1 confers hypersensitivity to oxidative stress; similar to Nop2p and human proliferation associated nucleolar protein p120
tRNA:pseudouridine synthase; introduces pseudouridines at position 38 or 39 in tRNA; also responsible for pseudouracil modification of some mRNAs; important for maintenance of translation efficiency and normal cell growth, localizes to both the nucleus and cytoplasm; non-essential for viability
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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