STRINGSTRING
PP1S34_86V6.1 protein (Physcomitrella patens) - STRING interaction network
"PP1S34_86V6.1" - Annotation not available in Physcomitrella patens
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
PP1S34_86V6.1Annotation not available (492 aa)    
Predicted Functional Partners:
CTU1
Predicted protein; Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position (348 aa)
     
  0.997
PP1S41_307V6.1
Predicted protein (708 aa)
     
  0.962
PP1S18_114V6.1
Predicted protein (454 aa)
     
  0.962
PP1S14_349V6.1
Predicted protein (434 aa)
       
      0.909
PP1S99_92V6.1
Predicted protein; Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2- thiolation reaction by being thiocarboxylated (-COSH) at its C- terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces [...] (99 aa)
       
  0.878
CNX5
Predicted protein; 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 that is generated from the pers [...] (467 aa)
     
 
  0.700
PP1S42_262V6.1
Predicted protein; Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) (443 aa)
       
      0.643
PP1S3_478V6.1
Predicted protein; Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) (437 aa)
       
      0.643
PP1S385_31V6.1
Predicted protein (504 aa)
       
      0.643
PP1S29_183V6.1
Predicted protein (462 aa)
       
      0.643
Your Current Organism:
Physcomitrella patens
NCBI taxonomy Id: 3218
Other names: Bryophyta, Bryophytina, Bryopsida, Funariaceae, Funariales, Funariidae, Moss Superclass V, Musci, P. patens, Physcomitrella, Physcomitrella Bruch & Schimp, Physcomitrella patens, Physcomitrella patens (Hedw.) Bruch & Schimp., Physcomitrium patens, Physcomitrium patens (Hedw.) Mitt., bryophytes, mosses
Server load: low (10%) [HD]