STRINGSTRING
STRING protein interaction network
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:
a 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 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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
EMC10Putative protein of unknown function; subunit of evolutionarily conserved EMC (Endoplasmic Reticulum Membrane Complex) implicated in ERAD (ER-associated degradation) and proper assembly of multi-pass transmembrane (TM) proteins; EMC acts in yeast as an ER-mitochondria tether that interacts with outer membrane protein Tom5p of TOM (Translocase of the Mitochondrial Outer Membrane) complex; YDR056C is not an essential protein. (205 aa)    
Predicted Functional Partners:
SOP4
ER-membrane protein; subunit of evolutionarily conserved EMC (Endoplasmic Reticulum Membrane Complex) implicated in ERAD (ER-associated degradation) and proper assembly of multi-pass transmembrane (TM) proteins; EMC acts in yeast as an ER-mitochondria tether that interacts with outer membrane protein Tom5 of TOM (Translocase of the Mitochondrial Outer Membrane) complex; suppressor of pma1-7, deletion of SOP4 slows down export of wild-type Pma1p and Pma1-7 from the ER.
   
 
 0.996
EMC1
Member of conserved endoplasmic reticulum membrane complex; involved in efficient folding of proteins in the ER; null mutant displays induction of the unfolded protein response; interacts with Gal80p; homologous to worm H17B01.4/EMC-1, fly CG2943, and human KIAA0090; Belongs to the EMC1 family.
   
 
 0.994
EMC4
Member of conserved ER transmembrane complex; required for efficient folding of proteins in the ER; null mutant displays induction of the unfolded protein response; homologous to worm ZK616.6/EMC-4 and fly CG11137; mutation is functionally complemented by human EMC4.
   
 
 0.992
EMC3
Member of conserved ER transmembrane complex; required for efficient folding of proteins in the ER; required for respiratory growth; null mutant displays induction of the unfolded protein response; homologous to worm Y62E10A.10/EMC-3, fly CG6750, human TMEM111.
   
 
 0.992
EMC6
Member of conserved ER transmembrane complex; required for efficient folding of proteins in the ER; null mutant displays induction of the unfolded protein response; homologous to worm F33D4.7/EMC-6, fly CG11781, human TMEM93.
   
 
 0.992
EMC2
Member of conserved ER transmembrane complex; required for efficient folding of proteins in the ER; null mutant displays induction of the unfolded protein response; homologous to worm Y57G7A.10/EMC-2, fly CG17556, human TTC35.
   
 
 0.989
EMC5
Member of conserved ER transmembrane complex; required for efficient folding of proteins in the ER; null mutant displays induction of the unfolded protein response, and also shows K1 killer toxin resistance; homologous to worm B0334.15/EMC-5, fly CG15168, human MMGT.
   
 
 0.987
ARP10
Actin-like protein ARP10; Component of the dynactin complex; localized to the pointed end of the Arp1p filament; may regulate membrane association of the complex; Belongs to the actin family. ARP10 subfamily.
   
 
 0.980
JNM1
Nuclear migration protein JNM1; Component of the yeast dynactin complex; consisting of Nip100p, Jnm1p, and Arp1p; required for proper nuclear migration and spindle partitioning during mitotic anaphase B.
   
 
 0.980
CAP2
Beta subunit of the capping protein heterodimer (Cap1p and Cap2p); capping protein (CP) binds to the barbed ends of actin filaments preventing further polymerization; localized predominantly to cortical actin patches; protein increases in abundance and relocalizes from bud neck to plasma membrane upon DNA replication stress.
   
 
 0.961
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
Server load: low (36%) [HD]