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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Cooccurrence
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[Homology]
Score
SAN1Ubiquitin-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. (610 aa)    
Predicted Functional Partners:
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).
    
 
 0.984
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.
   
 
 0.935
SPT16
Subunit of the heterodimeric FACT complex (Spt16p-Pob3p); FACT associates with chromatin via interaction with Nhp6Ap and Nhp6Bp, and reorganizes nucleosomes to facilitate access to DNA by RNA and DNA polymerases; specifically required for diauxic shift-induced H2B deposition onto rDNA genes; mutations cause reduced nucleosome occupancy over highly transcribed regions; coregulates transcription with Mot1p through preinitiation complex assembly and nucleosome organization.
    
 
 0.890
SIR4
Regulatory protein SIR4; SIR protein involved in assembly of silent chromatin domains; silent information regulator (SIR) along with SIR2 and SIR3; involved in assembly of silent chromatin domains at telomeres and the silent mating-type loci; some alleles of SIR4 prolong lifespan; required for telomere hypercluster formation in quiescent yeast cells.
   
 
 0.881
CDC13
Cell division control protein 13; Single stranded DNA-binding protein found at TG1-3 telomere G-tails; key roles in regulation of telomerase, telomere end protection, conventional telomere replication; regulates telomere replication through recruitment of specific sub-complexes, essential function is telomere capping; forms homodimer via N-terminus; disruption of dimerization leads to short telomeres; autophagy and proteasome are involved in Cdc13p degradation; differentially phosphorylated through cell cycle.
   
 
 0.852
HUL5
Probable 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.
      
 0.837
HRD1
ERAD-associated E3 ubiquitin-protein ligase HRD1; Ubiquitin-protein ligase involved in ER-associated degradation (ERAD) of misfolded proteins; upon autoubiquitination triggers retrotranslocation of misfolded proteins to cytosol for degradation; genetically linked to the unfolded protein response (UPR); regulated through association with Hrd3p; contains an H2 ring finger; likely plays a general role in targeting proteins that persistently associate with and potentially obstruct the ER-localized translocon; Belongs to the HRD1 family.
    
 
 0.757
UBR2
Cytoplasmic ubiquitin-protein ligase (E3); component of the Mub1p-Ubr2p-Rad6p ubiquitin ligase complex required for the ubiquitination and degradation of Rpn4p; mediates formation of the ternary complex.
   
 
 0.721
UBC1
Ubiquitin-conjugating enzyme; key E2 partner with Ubc4p for the anaphase-promoting complex (APC); mediates selective degradation of short-lived and abnormal proteins; plays a role in vesicle biogenesis and ER-associated protein degradation (ERAD); component of the cellular stress response; protein abundance increases in response to DNA replication stress key E2 partner with Ubc4p for the anaphase-promoting complex (APC).
    
 
 0.712
SSA1
Heat shock protein SSA1; ATPase involved in protein folding and NLS-directed nuclear transport; member of HSP70 family; required for ubiquitin-dependent degradation of short-lived proteins; forms chaperone complex with Ydj1p; localized to nucleus, cytoplasm, cell wall; 98% identical to paralog Ssa2p with different functional specificity in propagation of yeast [URE3] prions, vacuolar-mediated degradations of gluconeogenesis enzymes; general targeting factor of Hsp104p to prion fibrils.
    
 
 0.709
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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