PAPPA2 protein (Homo sapiens) - STRING network view

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PAPPA2

pappalysin 2; Metalloproteinase which specifically cleaves IGFBP-5. Shows limited proteolysis toward IGFBP-3 (1791 aa)

Predicted Functional Partners:

IGFBP5

0.977

IGFBP4

0.939

IGF1

0.917

IGF2

0.910

IGFALS

0.900

IGFBP3

0.664

ERO1L

0.490

ZDHHC21

0.468

ERO1LB

0.418

SIGLEC6

0.407

Your Current Organism:

Homo sapiens

NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
ERO1L	PAPPA2	ENSP00000379042	ENSP00000356634	ERO1-like (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of g [...]	pappalysin 2; Metalloproteinase which specifically cleaves IGFBP-5. Shows limited proteolysis toward IGFBP-3	0.490
ERO1LB	PAPPA2	ENSP00000346635	ENSP00000356634	ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...]	pappalysin 2; Metalloproteinase which specifically cleaves IGFBP-5. Shows limited proteolysis toward IGFBP-3	0.418
IGF1	IGF2	ENSP00000302665	ENSP00000391826	insulin-like growth factor 1 (somatomedin C); The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake	insulin-like growth factor 2 (somatomedin A)	0.919
IGF1	IGFALS	ENSP00000302665	ENSP00000416683	insulin-like growth factor 1 (somatomedin C); The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake	insulin-like growth factor binding protein, acid labile subunit; Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion	0.990
IGF1	IGFBP3	ENSP00000302665	ENSP00000370473	insulin-like growth factor 1 (somatomedin C); The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake	insulin-like growth factor binding protein 3; IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R	0.999
IGF1	IGFBP4	ENSP00000302665	ENSP00000269593	insulin-like growth factor 1 (somatomedin C); The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake	insulin-like growth factor binding protein 4; IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors	0.999
IGF1	IGFBP5	ENSP00000302665	ENSP00000233813	insulin-like growth factor 1 (somatomedin C); The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake	insulin-like growth factor binding protein 5; IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors	0.999
IGF1	PAPPA2	ENSP00000302665	ENSP00000356634	insulin-like growth factor 1 (somatomedin C); The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake	pappalysin 2; Metalloproteinase which specifically cleaves IGFBP-5. Shows limited proteolysis toward IGFBP-3	0.917
IGF2	IGF1	ENSP00000391826	ENSP00000302665	insulin-like growth factor 2 (somatomedin A)	insulin-like growth factor 1 (somatomedin C); The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake	0.919
IGF2	IGFALS	ENSP00000391826	ENSP00000416683	insulin-like growth factor 2 (somatomedin A)	insulin-like growth factor binding protein, acid labile subunit; Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion	0.925
IGF2	IGFBP3	ENSP00000391826	ENSP00000370473	insulin-like growth factor 2 (somatomedin A)	insulin-like growth factor binding protein 3; IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R	0.999
IGF2	IGFBP4	ENSP00000391826	ENSP00000269593	insulin-like growth factor 2 (somatomedin A)	insulin-like growth factor binding protein 4; IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors	0.987
IGF2	IGFBP5	ENSP00000391826	ENSP00000233813	insulin-like growth factor 2 (somatomedin A)	insulin-like growth factor binding protein 5; IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors	0.997
IGF2	PAPPA2	ENSP00000391826	ENSP00000356634	insulin-like growth factor 2 (somatomedin A)	pappalysin 2; Metalloproteinase which specifically cleaves IGFBP-5. Shows limited proteolysis toward IGFBP-3	0.910
IGFALS	IGF1	ENSP00000416683	ENSP00000302665	insulin-like growth factor binding protein, acid labile subunit; Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion	insulin-like growth factor 1 (somatomedin C); The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake	0.990
IGFALS	IGF2	ENSP00000416683	ENSP00000391826	insulin-like growth factor binding protein, acid labile subunit; Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion	insulin-like growth factor 2 (somatomedin A)	0.925
IGFALS	IGFBP3	ENSP00000416683	ENSP00000370473	insulin-like growth factor binding protein, acid labile subunit; Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion	insulin-like growth factor binding protein 3; IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R	0.998
IGFALS	IGFBP4	ENSP00000416683	ENSP00000269593	insulin-like growth factor binding protein, acid labile subunit; Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion	insulin-like growth factor binding protein 4; IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors	0.563
IGFALS	IGFBP5	ENSP00000416683	ENSP00000233813	insulin-like growth factor binding protein, acid labile subunit; Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion	insulin-like growth factor binding protein 5; IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors	0.989
IGFALS	PAPPA2	ENSP00000416683	ENSP00000356634	insulin-like growth factor binding protein, acid labile subunit; Involved in protein-protein interactions that result in protein complexes, receptor-ligand binding or cell adhesion	pappalysin 2; Metalloproteinase which specifically cleaves IGFBP-5. Shows limited proteolysis toward IGFBP-3	0.900

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