node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ADAM2 | CALR3 | ENSP00000265708 | ENSP00000269881 | Disintegrin and metalloproteinase domain-containing protein 2; Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein; ADAM metallopeptidase domain containing | Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family | 0.693 |
ADAM2 | PDILT | ENSP00000265708 | ENSP00000305465 | Disintegrin and metalloproteinase domain-containing protein 2; Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein; ADAM metallopeptidase domain containing | Protein disulfide-isomerase-like protein of the testis; Probable redox-inactive chaperone involved in spermatogenesis; Belongs to the protein disulfide isomerase family | 0.593 |
ADAM2 | TPST2 | ENSP00000265708 | ENSP00000339813 | Disintegrin and metalloproteinase domain-containing protein 2; Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein; ADAM metallopeptidase domain containing | Protein-tyrosine sulfotransferase 2; Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3’-phosphoadenylyl sulfate (PAPS) as cosubstrate; Sulfotransferases, membrane bound | 0.568 |
CALR3 | ADAM2 | ENSP00000269881 | ENSP00000265708 | Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family | Disintegrin and metalloproteinase domain-containing protein 2; Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein; ADAM metallopeptidase domain containing | 0.693 |
CALR3 | DNAJC10 | ENSP00000269881 | ENSP00000264065 | Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family | DnaJ homolog subfamily C member 10; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, [...] | 0.693 |
CALR3 | ERP27 | ENSP00000269881 | ENSP00000266397 | Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family | Endoplasmic reticulum protein 27; Belongs to the protein disulfide isomerase family | 0.701 |
CALR3 | HSP90B1 | ENSP00000269881 | ENSP00000299767 | Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family | Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity; Belongs to the heat shock protein 90 family | 0.888 |
CALR3 | HSPA5 | ENSP00000269881 | ENSP00000324173 | Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family | 78 kDa glucose-regulated protein; Plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate (By similarity); Belongs to the heat shock protein 70 family | 0.607 |
CALR3 | HYOU1 | ENSP00000269881 | ENSP00000480150 | Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family | Hypoxia up-regulated protein 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; Belongs to the heat shock protein 70 family | 0.703 |
CALR3 | PDILT | ENSP00000269881 | ENSP00000305465 | Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family | Protein disulfide-isomerase-like protein of the testis; Probable redox-inactive chaperone involved in spermatogenesis; Belongs to the protein disulfide isomerase family | 0.814 |
CALR3 | RPN2 | ENSP00000269881 | ENSP00000237530 | Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains; Belongs to the SWP1 family | 0.623 |
CALR3 | SSR4 | ENSP00000269881 | ENSP00000317331 | Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family | Translocon-associated protein subunit delta; TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins; Belongs to the TRAP-delta family | 0.597 |
CALR3 | TPST2 | ENSP00000269881 | ENSP00000339813 | Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family | Protein-tyrosine sulfotransferase 2; Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3’-phosphoadenylyl sulfate (PAPS) as cosubstrate; Sulfotransferases, membrane bound | 0.731 |
DNAJC10 | CALR3 | ENSP00000264065 | ENSP00000269881 | DnaJ homolog subfamily C member 10; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, [...] | Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family | 0.693 |
DNAJC10 | ERP27 | ENSP00000264065 | ENSP00000266397 | DnaJ homolog subfamily C member 10; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, [...] | Endoplasmic reticulum protein 27; Belongs to the protein disulfide isomerase family | 0.558 |
DNAJC10 | HSP90B1 | ENSP00000264065 | ENSP00000299767 | DnaJ homolog subfamily C member 10; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, [...] | Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity; Belongs to the heat shock protein 90 family | 0.971 |
DNAJC10 | HSPA5 | ENSP00000264065 | ENSP00000324173 | DnaJ homolog subfamily C member 10; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, [...] | 78 kDa glucose-regulated protein; Plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate (By similarity); Belongs to the heat shock protein 70 family | 0.997 |
DNAJC10 | HYOU1 | ENSP00000264065 | ENSP00000480150 | DnaJ homolog subfamily C member 10; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, [...] | Hypoxia up-regulated protein 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; Belongs to the heat shock protein 70 family | 0.979 |
DNAJC10 | PDILT | ENSP00000264065 | ENSP00000305465 | DnaJ homolog subfamily C member 10; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, [...] | Protein disulfide-isomerase-like protein of the testis; Probable redox-inactive chaperone involved in spermatogenesis; Belongs to the protein disulfide isomerase family | 0.565 |
ERP27 | CALR3 | ENSP00000266397 | ENSP00000269881 | Endoplasmic reticulum protein 27; Belongs to the protein disulfide isomerase family | Calreticulin-3; During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium- binding may be absent or much lower than that of CALR; Belongs to the calreticulin family | 0.701 |