MANF protein (Pongo abelii) - STRING interaction network

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second shell of interactors

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Known Interactions

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experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

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textmining

co-expression

protein homology

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[Homology]

Score

MANF

MANF isoform 1. (245 aa)

Predicted Functional Partners:

HSPA5

0.977

CRELD2

0.879

DNAJB11

0.861

SDF2L1

0.827

VSNL1

0.783

RTN1

0.738

ZFAND4

0.733

CALM1-2

0.689

ANKRD45

0.674

PPARGC1A

0.663

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
ANKRD45	DNAJB11	ENSPPYP00000000575	ENSPPYP00000016085	ANKRD45 isoform 1.	DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1.	0.615
ANKRD45	MANF	ENSPPYP00000000575	ENSPPYP00000015479	ANKRD45 isoform 1.	MANF isoform 1.	0.674
CALM1-2	MANF	ENSPPYP00000013880	ENSPPYP00000015479	Calmodulin 2.	MANF isoform 1.	0.689
CRELD2	DNAJB11	ENSPPYP00000013353	ENSPPYP00000016085	CRELD2 isoform 3.	DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1.	0.750
CRELD2	HSPA5	ENSPPYP00000013353	ENSPPYP00000021973	CRELD2 isoform 3.	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 [...]	0.628
CRELD2	MANF	ENSPPYP00000013353	ENSPPYP00000015479	CRELD2 isoform 3.	MANF isoform 1.	0.879
CRELD2	SDF2L1	ENSPPYP00000013353	ENSPPYP00000012946	CRELD2 isoform 3.	SDF2L1 isoform 1.	0.879
DNAJB11	ANKRD45	ENSPPYP00000016085	ENSPPYP00000000575	DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1.	ANKRD45 isoform 1.	0.615
DNAJB11	CRELD2	ENSPPYP00000016085	ENSPPYP00000013353	DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1.	CRELD2 isoform 3.	0.750
DNAJB11	HSPA5	ENSPPYP00000016085	ENSPPYP00000021973	DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1.	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 [...]	0.990
DNAJB11	MANF	ENSPPYP00000016085	ENSPPYP00000015479	DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1.	MANF isoform 1.	0.861
DNAJB11	SDF2L1	ENSPPYP00000016085	ENSPPYP00000012946	DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1.	SDF2L1 isoform 1.	0.882
HSPA5	CRELD2	ENSPPYP00000021973	ENSPPYP00000013353	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 [...]	CRELD2 isoform 3.	0.628
HSPA5	DNAJB11	ENSPPYP00000021973	ENSPPYP00000016085	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 [...]	DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1.	0.990
HSPA5	MANF	ENSPPYP00000021973	ENSPPYP00000015479	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 [...]	MANF isoform 1.	0.977
HSPA5	SDF2L1	ENSPPYP00000021973	ENSPPYP00000012946	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 [...]	SDF2L1 isoform 1.	0.649
MANF	ANKRD45	ENSPPYP00000015479	ENSPPYP00000000575	MANF isoform 1.	ANKRD45 isoform 1.	0.674
MANF	CALM1-2	ENSPPYP00000015479	ENSPPYP00000013880	MANF isoform 1.	Calmodulin 2.	0.689
MANF	CRELD2	ENSPPYP00000015479	ENSPPYP00000013353	MANF isoform 1.	CRELD2 isoform 3.	0.879
MANF	DNAJB11	ENSPPYP00000015479	ENSPPYP00000016085	MANF isoform 1.	DnaJ homolog subfamily B member 11; As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. It is necessary for maturation and correct trafficking of PKD1.	0.861