CHORDC1 protein (Pongo abelii) - STRING interaction network

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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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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Assay-based Predictions

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co-expression

Genomic Predictions

gene neighborhood

gene co-occurrence

gene fusions

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
AHSA1	CHORDC1	ENSPPYP00000006854	ENSPPYP00000004308	AHSA1 isoform 1.	Cysteine and histidine-rich domain-containing protein 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity).	0.781
AHSA1	ENSPPYP00000015333	ENSPPYP00000006854	ENSPPYP00000015333	AHSA1 isoform 1.	annotation not available	0.896
AHSA1	ENSPPYP00000016659	ENSPPYP00000006854	ENSPPYP00000016659	AHSA1 isoform 1.	annotation not available	0.896
AHSA1	HSP90AB1	ENSPPYP00000006854	ENSPPYP00000018631	AHSA1 isoform 1.	Heat shock protein HSP 90-beta; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interact [...]	0.982
AHSA1	HSPH1	ENSPPYP00000006854	ENSPPYP00000005987	AHSA1 isoform 1.	Heat shock protein 105 kDa; Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering substrate release. Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities.	0.541
AHSA1	SUGT1	ENSPPYP00000006854	ENSPPYP00000006144	AHSA1 isoform 1.	SGT1 homolog, MIS12 kinetochore complex assembly cochaperone.	0.410
AHSA1	TTC4	ENSPPYP00000006854	ENSPPYP00000001529	AHSA1 isoform 1.	Tetratricopeptide repeat domain 4.	0.592
AHSA2P	CHORDC1	ENSPPYP00000013812	ENSPPYP00000004308	AHSA2 isoform 5.	Cysteine and histidine-rich domain-containing protein 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity).	0.709
AHSA2P	ENSPPYP00000015333	ENSPPYP00000013812	ENSPPYP00000015333	AHSA2 isoform 5.	annotation not available	0.612
AHSA2P	ENSPPYP00000016659	ENSPPYP00000013812	ENSPPYP00000016659	AHSA2 isoform 5.	annotation not available	0.612
AHSA2P	HSP90AB1	ENSPPYP00000013812	ENSPPYP00000018631	AHSA2 isoform 5.	Heat shock protein HSP 90-beta; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interact [...]	0.612
AHSA2P	HSPH1	ENSPPYP00000013812	ENSPPYP00000005987	AHSA2 isoform 5.	Heat shock protein 105 kDa; Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering substrate release. Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities.	0.541
AHSA2P	SUGT1	ENSPPYP00000013812	ENSPPYP00000006144	AHSA2 isoform 5.	SGT1 homolog, MIS12 kinetochore complex assembly cochaperone.	0.410
AHSA2P	TTC4	ENSPPYP00000013812	ENSPPYP00000001529	AHSA2 isoform 5.	Tetratricopeptide repeat domain 4.	0.462
CHORDC1	AHSA1	ENSPPYP00000004308	ENSPPYP00000006854	Cysteine and histidine-rich domain-containing protein 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity).	AHSA1 isoform 1.	0.781
CHORDC1	AHSA2P	ENSPPYP00000004308	ENSPPYP00000013812	Cysteine and histidine-rich domain-containing protein 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity).	AHSA2 isoform 5.	0.709
CHORDC1	EDRF1	ENSPPYP00000004308	ENSPPYP00000003210	Cysteine and histidine-rich domain-containing protein 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity).	Erythroid differentiation-related factor 1; Transcription factor involved in erythroid differentiation. Involved in transcriptional activation of the globin gene (By similarity).	0.713
CHORDC1	ENSPPYP00000015333	ENSPPYP00000004308	ENSPPYP00000015333	Cysteine and histidine-rich domain-containing protein 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity).	annotation not available	0.746
CHORDC1	ENSPPYP00000016659	ENSPPYP00000004308	ENSPPYP00000016659	Cysteine and histidine-rich domain-containing protein 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity).	annotation not available	0.746
CHORDC1	HSP90AB1	ENSPPYP00000004308	ENSPPYP00000018631	Cysteine and histidine-rich domain-containing protein 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis (By similarity).	Heat shock protein HSP 90-beta; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interact [...]	0.821