P4HB protein (Pongo abelii) - STRING interaction network

Nodes:

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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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query proteins and first shell of interactors

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second shell of interactors

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proteins of unknown 3D structure

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a 3D structure is known or predicted

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co-expression

Genomic Predictions

gene neighborhood

gene co-occurrence

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Your Current Organism:

Pongo abelii

NCBI taxonomy Id: 9601
Other names: Orang-utan, Orangutan, P. abelii, Pongo pygmaeus abeli, Pongo pygmaeus abelii, Sumatran orangutan, orang utan

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
CALR	ENSPPYP00000001345	ENSPPYP00000010780	ENSPPYP00000001345	Calreticulin.	annotation not available	0.990
CALR	HSP90B1	ENSPPYP00000010780	ENSPPYP00000023483	Calreticulin.	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. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. Belongs to the heat shock protein 90 family.	0.996
CALR	HSPA5	ENSPPYP00000010780	ENSPPYP00000021973	Calreticulin.	Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...]	0.977
CALR	P4HB	ENSPPYP00000010780	ENSPPYP00000009818	Calreticulin.	Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...]	0.990
CALR	PDIA3	ENSPPYP00000010780	ENSPPYP00000007276	Calreticulin.	Protein disulfide-isomerase A3.	0.999
CALR	PDIA6	ENSPPYP00000010780	ENSPPYP00000014123	Calreticulin.	Protein disulfide-isomerase A6; May function as a chaperone that inhibits aggregation of misfolded proteins. Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling. May also regulate the UPR via the EIF2AK3 UPR sensor. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin. Belongs to the protein disulfide isomerase family.	0.949
ENSPPYP00000001345	CALR	ENSPPYP00000001345	ENSPPYP00000010780	annotation not available	Calreticulin.	0.990
ENSPPYP00000001345	HSPA5	ENSPPYP00000001345	ENSPPYP00000021973	annotation not available	Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...]	0.991
ENSPPYP00000001345	P4HB	ENSPPYP00000001345	ENSPPYP00000009818	annotation not available	Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...]	0.968
ENSPPYP00000001345	PDIA3	ENSPPYP00000001345	ENSPPYP00000007276	annotation not available	Protein disulfide-isomerase A3.	0.954
ENSPPYP00000001345	PDIA6	ENSPPYP00000001345	ENSPPYP00000014123	annotation not available	Protein disulfide-isomerase A6; May function as a chaperone that inhibits aggregation of misfolded proteins. Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling. May also regulate the UPR via the EIF2AK3 UPR sensor. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin. Belongs to the protein disulfide isomerase family.	0.932
ERO1A	ERO1B	ENSPPYP00000006611	ENSPPYP00000000089	ERO1A isoform 1.	ERO1B isoform 1.	0.736
ERO1A	HSPA5	ENSPPYP00000006611	ENSPPYP00000021973	ERO1A isoform 1.	Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...]	0.724
ERO1A	P4HB	ENSPPYP00000006611	ENSPPYP00000009818	ERO1A isoform 1.	Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...]	0.993
ERO1A	PDIA3	ENSPPYP00000006611	ENSPPYP00000007276	ERO1A isoform 1.	Protein disulfide-isomerase A3.	0.760
ERO1A	PDIA6	ENSPPYP00000006611	ENSPPYP00000014123	ERO1A isoform 1.	Protein disulfide-isomerase A6; May function as a chaperone that inhibits aggregation of misfolded proteins. Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling. May also regulate the UPR via the EIF2AK3 UPR sensor. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin. Belongs to the protein disulfide isomerase family.	0.952
ERO1B	ERO1A	ENSPPYP00000000089	ENSPPYP00000006611	ERO1B isoform 1.	ERO1A isoform 1.	0.736
ERO1B	HSPA5	ENSPPYP00000000089	ENSPPYP00000021973	ERO1B isoform 1.	Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...]	0.720
ERO1B	P4HB	ENSPPYP00000000089	ENSPPYP00000009818	ERO1B isoform 1.	Protein disulfide-isomerase; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chape [...]	0.963
ERO1B	PDIA3	ENSPPYP00000000089	ENSPPYP00000007276	ERO1B isoform 1.	Protein disulfide-isomerase A3.	0.739