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STRINGSTRING
CNPY1 CNPY1 TMEM4 TMEM4 TOR3A TOR3A TOR1B TOR1B DNAJC3 DNAJC3 CNPY2 CNPY2 TOR1A TOR1A PDIA6 PDIA6 UGGT2 UGGT2 HYOU1 HYOU1 PRSS36 PRSS36 UBC UBC UGGT1 UGGT1 TOR4A TOR4A PDIA5 PDIA5 GZMM GZMM NAGLU NAGLU GUSB GUSB TOR2A TOR2A HGSNAT HGSNAT
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 Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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 each other.
Known Interactions
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
NAGLUN-acetylglucosaminidase, alpha; Involved in the degradation of heparan sulfate (743 aa)
UGGT1UDP-glucose glycoprotein glucosyltransferase 1; Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation (1555 aa)
TOR1Btorsin family 1, member B (torsin B); May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins (By similarity) (336 aa)
GZMMgranzyme M (lymphocyte met-ase 1); Cleaves peptide substrates after methionine, leucine, and norleucine. Physiological substrates include EZR, alpha- tubulins and the apoptosis inhibitor BIRC5/Survivin. Promotes caspase activation and subsequent apoptosis of target cells (257 aa)
PRSS36protease, serine, 36; Serine protease. Hydrolyzes the peptides N-t-Boc-Gln- Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC and, to a lesser extent, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Val-Leu-Lys-AMC. Has a preference for substrates with an Arg instead of a Lys residue in position P1 (855 aa)
PDIA6protein disulfide isomerase family A, member 6; May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (440 aa)
CNPY2canopy 2 homolog (zebrafish); Positive regulator of neurite outgrowth by stabilizing myosin regulatory light chain (MRLC). It prevents MIR-mediated MRLC ubiquitination and its subsequent proteasomal degradation (182 aa)
GUSBglucuronidase, beta; Plays an important role in the degradation of dermatan and keratan sulfates (651 aa)
CNPY1canopy 1 homolog (zebrafish) (92 aa)
PDIA5protein disulfide isomerase family A, member 5 (519 aa)
UBCubiquitin C (685 aa)
TOR1Atorsin family 1, member A (torsin A); May serve as a molecular chaperone assisting in the proper folding of secreted and/or membrane proteins. In the nucleus, displaces the nuclear membrane proteins SUN2, SYNE2 and SYNE3, leaving nuclear pores and SUN1 unchanged (332 aa)
TOR4Atorsin family 4, member A (423 aa)
TOR3Atorsin family 3, member A (397 aa)
TOR2Atorsin family 2, member A; Salusins -alpha and -beta may be endocrine and/or paracrine factors able to increase intracellular calcium concentrations and induce cell mitogenesis. Salusins may also be potent hypotensive peptides (321 aa)
UGGT2UDP-glucose glycoprotein glucosyltransferase 2; Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation (By similarity) (1516 aa)
DNAJC3DnaJ (Hsp40) homolog, subfamily C, member 3; Involved in the unfolded protein response (UPR) during ER stress. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity (504 aa)
HGSNATheparan-alpha-glucosaminide N-acetyltransferase; Lysosomal acetyltransferase that acetylates the non- reducing terminal alpha-glucosamine residue of intralysosomal heparin or heparan sulfate, converting it into a substrate for luminal alpha-N-acetyl glucosaminidase (635 aa)
HYOU1hypoxia up-regulated 1; Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding (999 aa)
TMEM4Uncharacterized protein (263 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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