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ENSPREP00000025366 ENSPREP00000025366 LOC103464541 LOC103464541 LOC103467931 LOC103467931 mocs3 mocs3 atg7 atg7 uba6 uba6 uba2 uba2 nae1 nae1 sae1 sae1 LOC103465053 LOC103465053 UBA3 UBA3 uba5 uba5
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
Others
textmining
co-expression
protein homology
Your Input:
ENSPREP00000025366ThiF domain-containing protein. (53 aa)
LOC103464541Ubiquitin-like modifier activating enzyme 7; Belongs to the ubiquitin-activating E1 family. (1012 aa)
LOC103467931Ubiquitin-like modifier activating enzyme 1; Belongs to the ubiquitin-activating E1 family. (768 aa)
mocs3Adenylyltransferase and sulfurtransferase MOCS3; Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl- adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (- COSH) of their C-terminus. The reaction probably involves hydrogen sulfide [...] (459 aa)
atg7ATG7 autophagy related 7 homolog (S. cerevisiae). (720 aa)
uba6Ubiquitin like modifier activating enzyme 6. (1044 aa)
uba2SUMO-activating enzyme subunit 2; The heterodimer acts as an E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2. Belongs to the ubiquitin-activating E1 family. (599 aa)
nae1NEDD8-activating enzyme E1 regulatory subunit; Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Belongs to the ubiquitin-activating E1 family. ULA1 subfamily. (533 aa)
sae1SUMO1 activating enzyme subunit 1. (344 aa)
LOC103465053Ubiquitin-like modifier activating enzyme 3. (442 aa)
UBA3Ubiquitin like modifier activating enzyme 3. (462 aa)
uba5Ubiquitin-like modifier activating enzyme 5. (400 aa)
Your Current Organism:
Poecilia reticulata
NCBI taxonomy Id: 8081
Other names: Acanthophacelus reticulata, P. reticulata, Poecilia (Acanthophacelus) reticulata, Poecilia latipinna reticulata, guppy
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