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
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Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
HUL5Probable E3 ubiquitin-protein ligase HUL5; Multiubiquitin chain assembly factor (E4); proteasome processivity factor that elongates polyUb chains on substrates, opposing Ubp6p, a branched polyubiquitin protease; required for retrograde transport of misfolded proteins during ERAD; required for ubiquitination of a subset of cytosolic misfolded proteins upon heat shock. (910 aa)    
Predicted Functional Partners:
RKR1
RING domain E3 ubiquitin ligase; involved in ubiquitin-mediated degradation of non-stop proteins and translationally stalled ER membrane proteins; component of ribosome-bound RQC (ribosome quality control) complex; degrades products of mRNAs lacking a termination codon regardless of a poly(A) tail; functional connections to chromatin modification; homolog of mouse Listerin, mutations in which reported to cause neurodegeneration; Belongs to the LTN1 family.
   
 0.885
UBP6
Ubiquitin-specific protease; situated in the base subcomplex of the 26S proteasome, releases free ubiquitin from branched polyubiquitin chains en bloc, rather than from the distal tip of the chain; negatively regulates degradation of ubiquitinated proteins by the proteasome; works in opposition to Hul5p polyubiquitin elongation activity; mutant has aneuploidy tolerance; human homolog UBP14 complements yeast null mutant.
   
 
 0.855
SAN1
Ubiquitin-protein ligase; involved in proteasome-dependent degradation of aberrant nuclear proteins; targets substrates with regions of exposed hydrophobicity containing 5 or more contiguous hydrophobic residues; contains intrinsically disordered regions that contribute to substrate recognition; prefers a window of exposed hydrophobicity that causes a particular level of protein insolubility, suggesting that San1p evolved to target highly aggregation-prone proteins.
      
 0.837
YGL140C
Uncharacterized membrane protein YGL140C; Putative protein of unknown function; non-essential gene; contains multiple predicted transmembrane domains.
   
  
 0.836
RPN11
Ubiquitin carboxyl-terminal hydrolase RPN11; Metalloprotease subunit of 19S regulatory particle; part of 26S proteasome lid; couples the deubiquitination and degradation of proteasome substrates; involved, independent of catalytic activity, in fission of mitochondria and peroxisomes; protein abundance increases in response to DNA replication stress.
   
 
 0.830
UFD4
Ubiquitin-protein ligase (E3); interacts with Rpt4p and Rpt6p, two subunits of the 19S particle of the 26S proteasome; cytoplasmic E3 involved in the degradation of ubiquitin fusion proteins; relative distribution to the nucleus increases upon DNA replication stress.
   
 
0.822
UBR1
E3 ubiquitin ligase (N-recognin); heterodimerizes with Rad6p to recognize and ubiquitinate substrates of the N-end rule pathway; role in endoplasmic reticulum-associated protein degradation (ERAD) in the absence of canonical ER membrane ligases or after stress; major role in targeting misfolded cytosolic proteins for degradation; regulates peptide transport via Cup9p ubiquitination; mutation in human UBR1 causes Johansson-Blizzard Syndrome (JBS).
   
  
 0.778
UFD2
E4 ubiquitin-protein ligase UFD2; Ubiquitin chain assembly factor (E4); cooperates with a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin protein ligase (E3) to conjugate ubiquitin to substrates; also functions as an E3.
   
 
 0.775
SSM4
ERAD-associated E3 ubiquitin-protein ligase DOA10; Membrane-embedded ubiquitin-protein ligase; ER and inner nuclear membrane localized RING-CH domain E3 ligase involved in ER-associated protein degradation (ERAD); targets misfolded cytosolic/nucleoplasmic domains of soluble and membrane embedded proteins (ERAD-C) and a transmembrane domain containing substrate (ERAD-M), Sbh2p; C-terminal element (CTE), conserved in human ortholog MARCH10/TEB4, determines substrate selectivity.
   
  
 0.764
UBI4
Polyubiquitin; Ubiquitin; becomes conjugated to proteins, marking them for selective degradation via the ubiquitin-26S proteasome system; essential for the cellular stress response; encoded as a polyubiquitin precursor comprised of 5 head-to-tail repeats; protein abundance increases in response to DNA replication stress.
   
 
 0.729
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
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