STRING protein interaction network
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 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
protein homology
Your Input:
Gene Fusion
PNG1Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase; Conserved peptide N-glycanase; deglycosylating enzyme that cleaves N-glycans that are attached to misfolded ERAD substrate glycoproteins prior to proteasome-dependent degradation; localizes to the cytoplasm and nucleus; activity is enhanced by interaction with Rad23p; human ortholog NGLY1 is associated with a syndrome characterized by developmental delays, epilepsy, absence of tears and liver disease (363 aa)    
Predicted Functional Partners:
UV excision repair protein RAD23; Protein with ubiquitin-like N terminus; subunit of Nuclear Excision Repair Factor 2 (NEF2) with Rad4p that binds damaged DNA; enhances protein deglycosylation activity of Png1p; also involved, with Rad4p, in ubiquitylated protein turnover; Rad4p-Rad23p heterodimer binds to promoters of DNA damage response genes to repress their transcription in the absence of DNA damage
Transitional endoplasmic reticulum atpase; Cell division control protein 48; AAA ATPase; subunit of polyUb-selective segregase complex involved in ERAD, INM-associated degradation (INMAD), mitotic spindle disassembly, macroautophagy, PMN, ribosome-associated degradation, ribophagy, homotypic ER membrane fusion, SCF complex disassembly, cell wall integrity during heat stress, and telomerase regulation; mobilizes membrane-anchored transcription factors by regulated Ub/proteasome-dependent processing (RUP); human ortholog VCP complements a cdc48 mutant
Alpha-mannosidase; Vacuolar alpha mannosidase; involved in free oligosaccharide (fOS) degradation; delivered to the vacuole in a novel pathway separate from the secretory pathway
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
Cathepsin a (carboxypeptidase c); Vacuolar carboxypeptidase Y (proteinase C, CPY); broad-specificity C-terminal exopeptidase involved in non-specific protein degradation in the vacuole; member of the serine carboxypeptidase family
Xeroderma pigmentosum group c-complementing protein; Protein that recognizes and binds damaged DNA (with Rad23p) during NER; subunit of Nuclear Excision Repair Factor 2 (NEF2); also involved, with Rad23p, in turnover of ubiquitylated proteins; Rad4p-Rad23p heterodimer binds to promoters of DNA damage response genes to repress their transcription in the absence of DNA damage; NER stands for nucleotide excision repair; Belongs to the XPC family
Protein OS-9 homolog; ER quality-control lectin; integral subunit of the HRD ligase; participates in efficient ER retention of misfolded proteins by recognizing them and delivering them to Hrd1p; binds to glycans with terminal alpha-1,6 linked mannose on misfolded N-glycosylated proteins and participates in targeting proteins to ERAD; member of the OS-9 protein family
Nuclear-enriched ubiquitin-like polyubiquitin-binding protein; required for spindle pole body (SPB) duplication and for transit through the G2/M phase of the cell cycle; involved in proteolysis; interacts with the proteasome; protein abundance increases in response to DNA replication stress
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
DNA damage-inducible v-SNARE binding protein; role in suppression of protein secretion; may play a role in S-phase checkpoint control; has ubiquitin-associated (UBA), ubiquitin-like (UBL), and retroviral-like proteinase (RVP) domains
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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