STRINGSTRING
rad-23 rad-23 rpn-10 rpn-10 xpc-1 xpc-1 png-1 png-1 ufd-2 ufd-2 rpn-13 rpn-13 atx-3 atx-3 rpt-2 rpt-2 ubql-1 ubql-1 rpt-5 rpt-5 ubq-2 ubq-2
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.
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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
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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
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[Homology]
Score
rad-23Uncharacterized protein. (323 aa)    
Predicted Functional Partners:
rpn-10
26S proteasome non-ATPase regulatory subunit 4; Binds and presumably selects ubiquitin-conjugates for destruction (By similarity). Required for protein degradation and ubiquitin-proteasome system (UBS) function and regulates proteasomal subunit expression. Involvement in UBS might be cell type specific. Regulator of the autophagy-lysosome pathway that may confer resistance to autophagy by regulating the expression of autophagy-related proteins such as lgg-1, and by regulating lysosome formation, possibly by modulating elt-2 activity. Required for fertility, sperm production, and sex de [...]
   
 
 0.999
xpc-1
XPC (Xeroderma Pigmentosum group C) DNA repair gene homolog.
   
 0.999
png-1
Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase; Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta- aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native protein [...]
   
 0.995
ufd-2
Ubiquitin conjugation factor E4 ufd-2; Acts as an E4 ubiquitin ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase. The elongation of preexisting ubiquitin chains preferentially targets ubiquitin 'Lys-29' and 'Lys-48' residues. Also functions as an E3 ligase in conjunction with specific E1 and E2 ligases. Probably by regulating protein ubiquitination at DNA damage repair sites, coordinates DNA double- strand-break repair and apoptosis in the germline. Required for germline apoptosis in response to DNA damage downstream of cep [...]
   
 
 0.995
rpn-13
Proteasomal ubiquitin receptor ADRM1 homolog; May function as a proteasomal ubiquitin receptor. May promote the deubiquitinating activity associated with the 26S proteasome. Belongs to the ADRM1 family.
   
 
 0.990
atx-3
Ataxin-3 homolog; Acts as chain editing deubiquitinating enzyme that binds and cleaves 'Lys-48'-linked polyubiquitin chains, with a preference for chains containing four or more ubiquitin molecules thereby modulating protein degradation by the ubiquitin-proteasome pathway. Probably by regulating the IGF-1-insulin-like pathway, regulates lifespan. Regulates germline DNA double-strand-break repair and apoptosis in response to DNA damage by recruiting E4 ubiquitin- protein ligase ufd-2 to DNA repair foci. Interacts with key regulators of transcription and represses transcription (By simil [...]
   
 0.989
rpt-2
Probable 26S proteasome regulatory subunit 4; The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). May play a role in the degradation of microtubule severing protein mei-1.
   
 0.989
ubql-1
Ubiquilin; May play a role in the ER-associated protein degradation pathway (ERAD) possibly via its interaction with ER-localized proteins ubxn-4 and cdc-48.1 and/or cdc48.2, providing a link between the polyubiquitinated ERAD substrates and the proteasome. Also plays an important role in the regulation of other protein degradation mechanisms and pathways including ubiquitin-proteasome system (UPS) and autophagy (By similarity). Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by intera [...]
   
 
 0.985
rpt-5
26S protease regulatory subunit 6A; Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required (By similarity). Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair (By similarity). Belongs to the heterohexameric ring of AAA [...]
   
 
 0.978
ubq-2
Ubiquitin-60S ribosomal protein L40; [Ubiquitin]: exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is invol [...]
   
 0.973
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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