#ID(s) interactor A	ID(s) interactor B	Alt. ID(s) interactor A	Alt. ID(s) interactor B	Alias(es) interactor A	Alias(es) interactor B	Interaction detection method(s)	Publication 1st author(s)	Publication Identifier(s)	Taxid interactor A	Taxid interactor B	Interaction type(s)	Source database(s)	Interaction identifier(s)	Confidence value(s)	Expansion method(s)	Biological role(s) interactor A	Biological role(s) interactor B	Experimental role(s) interactor A	Experimental role(s) interactor B	Type(s) interactor A	Type(s) interactor B	Xref(s) interactor A	Xref(s) interactor B	Interaction Xref(s)	Annotation(s) interactor A	Annotation(s) interactor B	Interaction annotation(s)	Host organism(s)	Interaction parameter(s)	Creation date	Update date	Checksum(s) interactor A	Checksum(s) interactor B	Interaction Checksum(s)	Negative	Feature(s) interactor A	Feature(s) interactor B	Stoichiometry(s) interactor A	Stoichiometry(s) interactor B	Identification method participant A	Identification method participant B
uniprotkb:Q92686	intenz:3.4.22.52	intact:EBI-3908564|ensembl:ENSP00000284292|ensembl:ENSP00000399591	intact:EBI-21446733|chembl target:CHEMBL2111357	psi-mi:neug_human(display_long)|uniprotkb:NRGN(gene name)|psi-mi:NRGN(display_short)|uniprotkb:RC3(gene name synonym)	psi-mi:capns1-capn1_human(display_short)|psi-mi:3.4.22.52(display_long)|intact:mu-Calpain complex(complex recommended name)|intact:"CAPN1:CAPNS1"(complex systematic name)|intact:CAPN1/S1 complex(complex synonym)|intact:Conventional Calpain complex(complex synonym)|intact:CAPN1/CAPNS1 complex(complex synonym)|intact:Calpain-1 complex(complex synonym)	psi-mi:"MI:0435"(protease assay)	Becker et al. (2018)	pubmed:30157938|imex:IM-27592	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0570"(protein cleavage)	psi-mi:"MI:0486"(UniProt)	intact:EBI-21404824|imex:IM-27592-1	-	-	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:1302"(stable complex)	go:"GO:0070300"(phosphatidic acid binding)|go:"GO:0098978"(glutamatergic synapse)|go:"GO:0099170"(postsynaptic modulation of chemical synaptic transmission)|go:"GO:1900273"(positive regulation of long-term synaptic potentiation)|interpro:IPR000048(IQ calmodulin-binding region)|reactome:R-HSA-9620244|go:"GO:0021537"(telencephalon development)|go:"GO:0030424"(axon)|go:"GO:0031966"(mitochondrial membrane)|go:"GO:0043025"(neuronal cell body)|go:"GO:0044327"(dendritic spine head)|go:"GO:0045211"(postsynaptic membrane)|refseq:NP_001119653.1|refseq:NP_006167.1|ensembl:ENSG00000154146(gene)|ensembl:ENST00000284292(transcript)|ensembl:ENST00000412681(transcript)|go:"GO:0005516"(calmodulin binding)|go:"GO:0005547"(phosphatidylinositol-3,4,5-trisphosphate binding)|go:"GO:0005634"(nucleus)|go:"GO:0005829"(cytosol)|go:"GO:0007165"(signal transduction)|go:"GO:0007399"(nervous system development)|go:"GO:0008306"(associative learning)|go:"GO:0012510"(trans-Golgi network transport vesicle membrane)|go:"GO:0014069"(postsynaptic density)	pubmed:10639123(see-also)|pubmed:22711986(see-also)|pubmed:9271093(see-also)|pubmed:21849499(see-also)|complex portal:CPX-2674(inferred-from)|complex portal:CPX-4302(complex-primary)|efo:"EFO:0009019"(see-also)|pubmed:16411745(see-also)|evidence ontology:"ECO:0005546"|go:"GO:0110158"(calpain complex)|go:"GO:0005509"(calcium ion binding)|go:"GO:0004198"(calcium-dependent cysteine-type endopeptidase activity)|go:"GO:0006508"(proteolysis)|pubmed:21864727(see-also)|efo:"Orphanet:98473"(see-also)|efo:"EFO:0001059"(see-also)|efo:"EFO:0000249"(see-also)|efo:"EFO:0002508"(see-also)|efo:"EFO:0000685"(see-also)|efo:"EFO:0002687"(see-also)	-	-	complex-properties:"Calpain (CAPN1/muCL) and its small regulatory subunit (CAPNS1/30K) bind via their respective 5th (of 5) EF-hand motifs. The N-terminus of CAPNS1 contains hydrophobic Gly-clusters, the Gly-rich domain.     The catalytically-active cleft is rather deep and narrow which might explains calpain's preference for digesting inter-domain unstructured regions. It is formed by the two calpain protease core domains, PC1 and PC2, containing one Ca2+-binding sites per core. Calcium binding to several domains of both subunits releases the steric hindrance by allowing PC1 and PC2 to move closer to each other while the secondary structures remain essentially unchanged and may result in the dissociation of the small regulatory subunit from the catalytic subunits.     Most other members of the calpain family of proteins do not require a regulatory subunit and are activated directly by calcium binding."|antagonist:"Calpastatin (CAST, P20810)"|ligand:"Calcium ion (Ca2+, CHEBI:29108)"|disease:"Muscular dystrophy [Orphanet:98473]: Muscular dystrophy (MD) refers to a group of more than 30 genetic diseases characterized by progressive weakness and degeneration of the skeletal muscles that control movement."|disease:"Cataract [EFO:0001059]: Partial or complete opacity of the crystalline lens of one or both eyes that decreases visual acuity and eventually results in blindness. Some cataracts appear in infancy or in childhood, but most develop in older individuals."|disease:"Alzheimer's disease [EFO:0000249]: A progressive, neurodegenerative disease characterized by loss of function and death of nerve cells in several areas of the brain leading to loss of cognitive function such as memory and language."|disease:"Parkinson's disease [EFO:0002508]: A progressive degenerative disorder of the central nervous system characterized by loss of dopamine producing neurons in the substantia nigra and the presence of Lewy bodies in the substantia nigra and locus coeruleus. Signs and symptoms include tremor which is most pronounced during rest, muscle rigidity, slowing of the voluntary movements, a tendency to fall back, and a mask-like facial expression."|disease:"Rheumatoid arthritis [EFO:0000685]: A chronic, systemic autoimmune disorder characterized by inflammation in the synovial membranes and articular surfaces. It manifests primarily as a symmetric, erosive polyarthritis that spares the axial skeleton and is typically associated with the presence in the serum of rheumatoid factor."|disease:"Ischemia reperfusion injury [EFO:0002687]: Adverse functional, metabolic, or structural changes in ischemic tissues resulting from the restoration of blood flow to the tissue (reperfusion), including swelling; hemorrhage; necrosis; and damage from free radicals. The most common instance is myocardial reperfusion injury."|curated-complex:"A calcium-dependent protease complex that processes the substrate by limited proteolysis rather than degrading it. In some cases the proteolytic action activates the substrate, for example, it cleaves CDK5R1/p35 (Q15078) into its p25 form that is associated with Alzheimer's disease. Involved in cytoskeletal remodeling, signal transduction and implicated in cell cycle regulation and apoptosis. Finely-balanced calpain homeostasis is required as both over and under-activation causes disease. Calpain complexes recognise their substrates based on a short peptide sequence. Inhibited by the intrinsically-unstructured calpastatin (P20810) by its tight binding to the calpain catalytic subunit."|disease:"In general, under disease/damaged conditions, such as muscular dystrophy, cardiomyopathy, traumatic ischemia, or lissencephaly, the over-activation of conventional calpains (probably due to compromised intracellular Ca2+ homeostasis) has been identified as an exacerbating factor."|disease:"Autosomal recessive spastic paraplegia type 76 [EFO:0009019]: Spastic paraplegia-76 is an autosomal recessive neurologic disorder characterized by young-adult onset of slowly progressive spasticity of the lower limbs resulting in gait difficulties. Most affected individuals have upper limb involvement and additional features such as foot deformities and dysarthria. Cognition is unaffected."	figure legend:Fig. 3|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/01/17	2019/06/05	rogid:+wHR6g3nWBOZbKAfOZ7jg+pj9pQ9606	-	-	false	myc tag:?-?|flag tag:?-?	-	-	-	psi-mi:"MI:0113"(western blot)	psi-mi:"MI:0113"(western blot)
uniprotkb:Q92686	intenz:3.4.22.52	intact:EBI-3908564|ensembl:ENSP00000284292|ensembl:ENSP00000399591	intact:EBI-21446733|chembl target:CHEMBL2111357	psi-mi:neug_human(display_long)|uniprotkb:NRGN(gene name)|psi-mi:NRGN(display_short)|uniprotkb:RC3(gene name synonym)	psi-mi:capns1-capn1_human(display_short)|psi-mi:3.4.22.52(display_long)|intact:mu-Calpain complex(complex recommended name)|intact:"CAPN1:CAPNS1"(complex systematic name)|intact:CAPN1/S1 complex(complex synonym)|intact:Conventional Calpain complex(complex synonym)|intact:CAPN1/CAPNS1 complex(complex synonym)|intact:Calpain-1 complex(complex synonym)	psi-mi:"MI:0435"(protease assay)	Becker et al. (2018)	pubmed:30157938|imex:IM-27592	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0570"(protein cleavage)	psi-mi:"MI:0486"(UniProt)	intact:EBI-21404875|imex:IM-27592-7	-	-	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:1302"(stable complex)	go:"GO:0070300"(phosphatidic acid binding)|go:"GO:0098978"(glutamatergic synapse)|go:"GO:0099170"(postsynaptic modulation of chemical synaptic transmission)|go:"GO:1900273"(positive regulation of long-term synaptic potentiation)|interpro:IPR000048(IQ calmodulin-binding region)|reactome:R-HSA-9620244|go:"GO:0021537"(telencephalon development)|go:"GO:0030424"(axon)|go:"GO:0031966"(mitochondrial membrane)|go:"GO:0043025"(neuronal cell body)|go:"GO:0044327"(dendritic spine head)|go:"GO:0045211"(postsynaptic membrane)|refseq:NP_001119653.1|refseq:NP_006167.1|ensembl:ENSG00000154146(gene)|ensembl:ENST00000284292(transcript)|ensembl:ENST00000412681(transcript)|go:"GO:0005516"(calmodulin binding)|go:"GO:0005547"(phosphatidylinositol-3,4,5-trisphosphate binding)|go:"GO:0005634"(nucleus)|go:"GO:0005829"(cytosol)|go:"GO:0007165"(signal transduction)|go:"GO:0007399"(nervous system development)|go:"GO:0008306"(associative learning)|go:"GO:0012510"(trans-Golgi network transport vesicle membrane)|go:"GO:0014069"(postsynaptic density)	pubmed:10639123(see-also)|pubmed:22711986(see-also)|pubmed:9271093(see-also)|pubmed:21849499(see-also)|complex portal:CPX-2674(inferred-from)|complex portal:CPX-4302(complex-primary)|efo:"EFO:0009019"(see-also)|pubmed:16411745(see-also)|evidence ontology:"ECO:0005546"|go:"GO:0110158"(calpain complex)|go:"GO:0005509"(calcium ion binding)|go:"GO:0004198"(calcium-dependent cysteine-type endopeptidase activity)|go:"GO:0006508"(proteolysis)|pubmed:21864727(see-also)|efo:"Orphanet:98473"(see-also)|efo:"EFO:0001059"(see-also)|efo:"EFO:0000249"(see-also)|efo:"EFO:0002508"(see-also)|efo:"EFO:0000685"(see-also)|efo:"EFO:0002687"(see-also)	-	-	complex-properties:"Calpain (CAPN1/muCL) and its small regulatory subunit (CAPNS1/30K) bind via their respective 5th (of 5) EF-hand motifs. The N-terminus of CAPNS1 contains hydrophobic Gly-clusters, the Gly-rich domain.     The catalytically-active cleft is rather deep and narrow which might explains calpain's preference for digesting inter-domain unstructured regions. It is formed by the two calpain protease core domains, PC1 and PC2, containing one Ca2+-binding sites per core. Calcium binding to several domains of both subunits releases the steric hindrance by allowing PC1 and PC2 to move closer to each other while the secondary structures remain essentially unchanged and may result in the dissociation of the small regulatory subunit from the catalytic subunits.     Most other members of the calpain family of proteins do not require a regulatory subunit and are activated directly by calcium binding."|antagonist:"Calpastatin (CAST, P20810)"|ligand:"Calcium ion (Ca2+, CHEBI:29108)"|disease:"Muscular dystrophy [Orphanet:98473]: Muscular dystrophy (MD) refers to a group of more than 30 genetic diseases characterized by progressive weakness and degeneration of the skeletal muscles that control movement."|disease:"Cataract [EFO:0001059]: Partial or complete opacity of the crystalline lens of one or both eyes that decreases visual acuity and eventually results in blindness. Some cataracts appear in infancy or in childhood, but most develop in older individuals."|disease:"Alzheimer's disease [EFO:0000249]: A progressive, neurodegenerative disease characterized by loss of function and death of nerve cells in several areas of the brain leading to loss of cognitive function such as memory and language."|disease:"Parkinson's disease [EFO:0002508]: A progressive degenerative disorder of the central nervous system characterized by loss of dopamine producing neurons in the substantia nigra and the presence of Lewy bodies in the substantia nigra and locus coeruleus. Signs and symptoms include tremor which is most pronounced during rest, muscle rigidity, slowing of the voluntary movements, a tendency to fall back, and a mask-like facial expression."|disease:"Rheumatoid arthritis [EFO:0000685]: A chronic, systemic autoimmune disorder characterized by inflammation in the synovial membranes and articular surfaces. It manifests primarily as a symmetric, erosive polyarthritis that spares the axial skeleton and is typically associated with the presence in the serum of rheumatoid factor."|disease:"Ischemia reperfusion injury [EFO:0002687]: Adverse functional, metabolic, or structural changes in ischemic tissues resulting from the restoration of blood flow to the tissue (reperfusion), including swelling; hemorrhage; necrosis; and damage from free radicals. The most common instance is myocardial reperfusion injury."|curated-complex:"A calcium-dependent protease complex that processes the substrate by limited proteolysis rather than degrading it. In some cases the proteolytic action activates the substrate, for example, it cleaves CDK5R1/p35 (Q15078) into its p25 form that is associated with Alzheimer's disease. Involved in cytoskeletal remodeling, signal transduction and implicated in cell cycle regulation and apoptosis. Finely-balanced calpain homeostasis is required as both over and under-activation causes disease. Calpain complexes recognise their substrates based on a short peptide sequence. Inhibited by the intrinsically-unstructured calpastatin (P20810) by its tight binding to the calpain catalytic subunit."|disease:"In general, under disease/damaged conditions, such as muscular dystrophy, cardiomyopathy, traumatic ischemia, or lissencephaly, the over-activation of conventional calpains (probably due to compromised intracellular Ca2+ homeostasis) has been identified as an exacerbating factor."|disease:"Autosomal recessive spastic paraplegia type 76 [EFO:0009019]: Spastic paraplegia-76 is an autosomal recessive neurologic disorder characterized by young-adult onset of slowly progressive spasticity of the lower limbs resulting in gait difficulties. Most affected individuals have upper limb involvement and additional features such as foot deformities and dysarthria. Cognition is unaffected."	figure legend:Fig. 4|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/01/17	2019/06/05	rogid:+wHR6g3nWBOZbKAfOZ7jg+pj9pQ9606	-	-	false	-	-	-	-	psi-mi:"MI:0113"(western blot)	psi-mi:"MI:0113"(western blot)
uniprotkb:Q92686	intenz:3.4.22.52	intact:EBI-3908564|ensembl:ENSP00000284292|ensembl:ENSP00000399591	intact:EBI-21446733|chembl target:CHEMBL2111357	psi-mi:neug_human(display_long)|uniprotkb:NRGN(gene name)|psi-mi:NRGN(display_short)|uniprotkb:RC3(gene name synonym)	psi-mi:capns1-capn1_human(display_short)|psi-mi:3.4.22.52(display_long)|intact:mu-Calpain complex(complex recommended name)|intact:"CAPN1:CAPNS1"(complex systematic name)|intact:CAPN1/S1 complex(complex synonym)|intact:Conventional Calpain complex(complex synonym)|intact:CAPN1/CAPNS1 complex(complex synonym)|intact:Calpain-1 complex(complex synonym)	psi-mi:"MI:0435"(protease assay)	Becker et al. (2018)	pubmed:30157938|imex:IM-27592	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0570"(protein cleavage)	psi-mi:"MI:0486"(UniProt)	intact:EBI-21404842|imex:IM-27592-3	-	-	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:1302"(stable complex)	go:"GO:0070300"(phosphatidic acid binding)|go:"GO:0098978"(glutamatergic synapse)|go:"GO:0099170"(postsynaptic modulation of chemical synaptic transmission)|go:"GO:1900273"(positive regulation of long-term synaptic potentiation)|interpro:IPR000048(IQ calmodulin-binding region)|reactome:R-HSA-9620244|go:"GO:0021537"(telencephalon development)|go:"GO:0030424"(axon)|go:"GO:0031966"(mitochondrial membrane)|go:"GO:0043025"(neuronal cell body)|go:"GO:0044327"(dendritic spine head)|go:"GO:0045211"(postsynaptic membrane)|refseq:NP_001119653.1|refseq:NP_006167.1|ensembl:ENSG00000154146(gene)|ensembl:ENST00000284292(transcript)|ensembl:ENST00000412681(transcript)|go:"GO:0005516"(calmodulin binding)|go:"GO:0005547"(phosphatidylinositol-3,4,5-trisphosphate binding)|go:"GO:0005634"(nucleus)|go:"GO:0005829"(cytosol)|go:"GO:0007165"(signal transduction)|go:"GO:0007399"(nervous system development)|go:"GO:0008306"(associative learning)|go:"GO:0012510"(trans-Golgi network transport vesicle membrane)|go:"GO:0014069"(postsynaptic density)	pubmed:10639123(see-also)|pubmed:22711986(see-also)|pubmed:9271093(see-also)|pubmed:21849499(see-also)|complex portal:CPX-2674(inferred-from)|complex portal:CPX-4302(complex-primary)|efo:"EFO:0009019"(see-also)|pubmed:16411745(see-also)|evidence ontology:"ECO:0005546"|go:"GO:0110158"(calpain complex)|go:"GO:0005509"(calcium ion binding)|go:"GO:0004198"(calcium-dependent cysteine-type endopeptidase activity)|go:"GO:0006508"(proteolysis)|pubmed:21864727(see-also)|efo:"Orphanet:98473"(see-also)|efo:"EFO:0001059"(see-also)|efo:"EFO:0000249"(see-also)|efo:"EFO:0002508"(see-also)|efo:"EFO:0000685"(see-also)|efo:"EFO:0002687"(see-also)	-	-	complex-properties:"Calpain (CAPN1/muCL) and its small regulatory subunit (CAPNS1/30K) bind via their respective 5th (of 5) EF-hand motifs. The N-terminus of CAPNS1 contains hydrophobic Gly-clusters, the Gly-rich domain.     The catalytically-active cleft is rather deep and narrow which might explains calpain's preference for digesting inter-domain unstructured regions. It is formed by the two calpain protease core domains, PC1 and PC2, containing one Ca2+-binding sites per core. Calcium binding to several domains of both subunits releases the steric hindrance by allowing PC1 and PC2 to move closer to each other while the secondary structures remain essentially unchanged and may result in the dissociation of the small regulatory subunit from the catalytic subunits.     Most other members of the calpain family of proteins do not require a regulatory subunit and are activated directly by calcium binding."|antagonist:"Calpastatin (CAST, P20810)"|ligand:"Calcium ion (Ca2+, CHEBI:29108)"|disease:"Muscular dystrophy [Orphanet:98473]: Muscular dystrophy (MD) refers to a group of more than 30 genetic diseases characterized by progressive weakness and degeneration of the skeletal muscles that control movement."|disease:"Cataract [EFO:0001059]: Partial or complete opacity of the crystalline lens of one or both eyes that decreases visual acuity and eventually results in blindness. Some cataracts appear in infancy or in childhood, but most develop in older individuals."|disease:"Alzheimer's disease [EFO:0000249]: A progressive, neurodegenerative disease characterized by loss of function and death of nerve cells in several areas of the brain leading to loss of cognitive function such as memory and language."|disease:"Parkinson's disease [EFO:0002508]: A progressive degenerative disorder of the central nervous system characterized by loss of dopamine producing neurons in the substantia nigra and the presence of Lewy bodies in the substantia nigra and locus coeruleus. Signs and symptoms include tremor which is most pronounced during rest, muscle rigidity, slowing of the voluntary movements, a tendency to fall back, and a mask-like facial expression."|disease:"Rheumatoid arthritis [EFO:0000685]: A chronic, systemic autoimmune disorder characterized by inflammation in the synovial membranes and articular surfaces. It manifests primarily as a symmetric, erosive polyarthritis that spares the axial skeleton and is typically associated with the presence in the serum of rheumatoid factor."|disease:"Ischemia reperfusion injury [EFO:0002687]: Adverse functional, metabolic, or structural changes in ischemic tissues resulting from the restoration of blood flow to the tissue (reperfusion), including swelling; hemorrhage; necrosis; and damage from free radicals. The most common instance is myocardial reperfusion injury."|curated-complex:"A calcium-dependent protease complex that processes the substrate by limited proteolysis rather than degrading it. In some cases the proteolytic action activates the substrate, for example, it cleaves CDK5R1/p35 (Q15078) into its p25 form that is associated with Alzheimer's disease. Involved in cytoskeletal remodeling, signal transduction and implicated in cell cycle regulation and apoptosis. Finely-balanced calpain homeostasis is required as both over and under-activation causes disease. Calpain complexes recognise their substrates based on a short peptide sequence. Inhibited by the intrinsically-unstructured calpastatin (P20810) by its tight binding to the calpain catalytic subunit."|disease:"In general, under disease/damaged conditions, such as muscular dystrophy, cardiomyopathy, traumatic ischemia, or lissencephaly, the over-activation of conventional calpains (probably due to compromised intracellular Ca2+ homeostasis) has been identified as an exacerbating factor."|disease:"Autosomal recessive spastic paraplegia type 76 [EFO:0009019]: Spastic paraplegia-76 is an autosomal recessive neurologic disorder characterized by young-adult onset of slowly progressive spasticity of the lower limbs resulting in gait difficulties. Most affected individuals have upper limb involvement and additional features such as foot deformities and dysarthria. Cognition is unaffected."	figure legend:Fig. 2|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/01/17	2019/06/05	rogid:+wHR6g3nWBOZbKAfOZ7jg+pj9pQ9606	-	-	false	sufficient binding region:31-40|fluorescent dye label:n-n	-	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
uniprotkb:Q92686	intenz:3.4.22.52	intact:EBI-3908564|ensembl:ENSP00000284292|ensembl:ENSP00000399591	intact:EBI-21446733|chembl target:CHEMBL2111357	psi-mi:neug_human(display_long)|uniprotkb:NRGN(gene name)|psi-mi:NRGN(display_short)|uniprotkb:RC3(gene name synonym)	psi-mi:capns1-capn1_human(display_short)|psi-mi:3.4.22.52(display_long)|intact:mu-Calpain complex(complex recommended name)|intact:"CAPN1:CAPNS1"(complex systematic name)|intact:CAPN1/S1 complex(complex synonym)|intact:Conventional Calpain complex(complex synonym)|intact:CAPN1/CAPNS1 complex(complex synonym)|intact:Calpain-1 complex(complex synonym)	psi-mi:"MI:0435"(protease assay)	Becker et al. (2018)	pubmed:30157938|imex:IM-27592	taxid:9606(human)|taxid:9606(Homo sapiens)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0570"(protein cleavage)	psi-mi:"MI:0486"(UniProt)	intact:EBI-21404867|imex:IM-27592-5	-	-	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:1302"(stable complex)	go:"GO:0070300"(phosphatidic acid binding)|go:"GO:0098978"(glutamatergic synapse)|go:"GO:0099170"(postsynaptic modulation of chemical synaptic transmission)|go:"GO:1900273"(positive regulation of long-term synaptic potentiation)|interpro:IPR000048(IQ calmodulin-binding region)|reactome:R-HSA-9620244|go:"GO:0021537"(telencephalon development)|go:"GO:0030424"(axon)|go:"GO:0031966"(mitochondrial membrane)|go:"GO:0043025"(neuronal cell body)|go:"GO:0044327"(dendritic spine head)|go:"GO:0045211"(postsynaptic membrane)|refseq:NP_001119653.1|refseq:NP_006167.1|ensembl:ENSG00000154146(gene)|ensembl:ENST00000284292(transcript)|ensembl:ENST00000412681(transcript)|go:"GO:0005516"(calmodulin binding)|go:"GO:0005547"(phosphatidylinositol-3,4,5-trisphosphate binding)|go:"GO:0005634"(nucleus)|go:"GO:0005829"(cytosol)|go:"GO:0007165"(signal transduction)|go:"GO:0007399"(nervous system development)|go:"GO:0008306"(associative learning)|go:"GO:0012510"(trans-Golgi network transport vesicle membrane)|go:"GO:0014069"(postsynaptic density)	pubmed:10639123(see-also)|pubmed:22711986(see-also)|pubmed:9271093(see-also)|pubmed:21849499(see-also)|complex portal:CPX-2674(inferred-from)|complex portal:CPX-4302(complex-primary)|efo:"EFO:0009019"(see-also)|pubmed:16411745(see-also)|evidence ontology:"ECO:0005546"|go:"GO:0110158"(calpain complex)|go:"GO:0005509"(calcium ion binding)|go:"GO:0004198"(calcium-dependent cysteine-type endopeptidase activity)|go:"GO:0006508"(proteolysis)|pubmed:21864727(see-also)|efo:"Orphanet:98473"(see-also)|efo:"EFO:0001059"(see-also)|efo:"EFO:0000249"(see-also)|efo:"EFO:0002508"(see-also)|efo:"EFO:0000685"(see-also)|efo:"EFO:0002687"(see-also)	-	-	complex-properties:"Calpain (CAPN1/muCL) and its small regulatory subunit (CAPNS1/30K) bind via their respective 5th (of 5) EF-hand motifs. The N-terminus of CAPNS1 contains hydrophobic Gly-clusters, the Gly-rich domain.     The catalytically-active cleft is rather deep and narrow which might explains calpain's preference for digesting inter-domain unstructured regions. It is formed by the two calpain protease core domains, PC1 and PC2, containing one Ca2+-binding sites per core. Calcium binding to several domains of both subunits releases the steric hindrance by allowing PC1 and PC2 to move closer to each other while the secondary structures remain essentially unchanged and may result in the dissociation of the small regulatory subunit from the catalytic subunits.     Most other members of the calpain family of proteins do not require a regulatory subunit and are activated directly by calcium binding."|antagonist:"Calpastatin (CAST, P20810)"|ligand:"Calcium ion (Ca2+, CHEBI:29108)"|disease:"Muscular dystrophy [Orphanet:98473]: Muscular dystrophy (MD) refers to a group of more than 30 genetic diseases characterized by progressive weakness and degeneration of the skeletal muscles that control movement."|disease:"Cataract [EFO:0001059]: Partial or complete opacity of the crystalline lens of one or both eyes that decreases visual acuity and eventually results in blindness. Some cataracts appear in infancy or in childhood, but most develop in older individuals."|disease:"Alzheimer's disease [EFO:0000249]: A progressive, neurodegenerative disease characterized by loss of function and death of nerve cells in several areas of the brain leading to loss of cognitive function such as memory and language."|disease:"Parkinson's disease [EFO:0002508]: A progressive degenerative disorder of the central nervous system characterized by loss of dopamine producing neurons in the substantia nigra and the presence of Lewy bodies in the substantia nigra and locus coeruleus. Signs and symptoms include tremor which is most pronounced during rest, muscle rigidity, slowing of the voluntary movements, a tendency to fall back, and a mask-like facial expression."|disease:"Rheumatoid arthritis [EFO:0000685]: A chronic, systemic autoimmune disorder characterized by inflammation in the synovial membranes and articular surfaces. It manifests primarily as a symmetric, erosive polyarthritis that spares the axial skeleton and is typically associated with the presence in the serum of rheumatoid factor."|disease:"Ischemia reperfusion injury [EFO:0002687]: Adverse functional, metabolic, or structural changes in ischemic tissues resulting from the restoration of blood flow to the tissue (reperfusion), including swelling; hemorrhage; necrosis; and damage from free radicals. The most common instance is myocardial reperfusion injury."|curated-complex:"A calcium-dependent protease complex that processes the substrate by limited proteolysis rather than degrading it. In some cases the proteolytic action activates the substrate, for example, it cleaves CDK5R1/p35 (Q15078) into its p25 form that is associated with Alzheimer's disease. Involved in cytoskeletal remodeling, signal transduction and implicated in cell cycle regulation and apoptosis. Finely-balanced calpain homeostasis is required as both over and under-activation causes disease. Calpain complexes recognise their substrates based on a short peptide sequence. Inhibited by the intrinsically-unstructured calpastatin (P20810) by its tight binding to the calpain catalytic subunit."|disease:"In general, under disease/damaged conditions, such as muscular dystrophy, cardiomyopathy, traumatic ischemia, or lissencephaly, the over-activation of conventional calpains (probably due to compromised intracellular Ca2+ homeostasis) has been identified as an exacerbating factor."|disease:"Autosomal recessive spastic paraplegia type 76 [EFO:0009019]: Spastic paraplegia-76 is an autosomal recessive neurologic disorder characterized by young-adult onset of slowly progressive spasticity of the lower limbs resulting in gait difficulties. Most affected individuals have upper limb involvement and additional features such as foot deformities and dysarthria. Cognition is unaffected."	figure legend:Fig. 2|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/01/17	2019/06/05	rogid:+wHR6g3nWBOZbKAfOZ7jg+pj9pQ9606	-	-	false	fluorescent dye label:n-n|sufficient binding region:39-51	-	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
uniprotkb:Q9QUR6	uniprotkb:P60761	intact:EBI-8344942|intact:MINT-1854903|uniprotkb:Q80YS1|ensembl:ENSMUSP00000097444	intact:EBI-771601|uniprotkb:Q3TYH4|uniprotkb:B2RRN7|ensembl:ENSMUSP00000070113	psi-mi:ppce_mouse(display_long)|uniprotkb:Prep(gene name)|psi-mi:Prep(display_short)|uniprotkb:Pep(gene name synonym)|uniprotkb:Post-proline cleaving enzyme(gene name synonym)	psi-mi:neug_mouse(display_long)|uniprotkb:RC3(gene name synonym)|uniprotkb:Nrgn(gene name)|psi-mi:Nrgn(display_short)	psi-mi:"MI:0435"(protease assay)	Becker et al. (2018)	pubmed:30157938|imex:IM-27592	taxid:10090(mouse)|taxid:10090(Mus musculus)	taxid:10090(mouse)|taxid:10090(Mus musculus)	psi-mi:"MI:0570"(protein cleavage)	psi-mi:"MI:0486"(UniProt)	intact:EBI-21404983|imex:IM-27592-9	-	-	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_035286.1|ensembl:ENSMUSG00000019849(gene)|ensembl:ENSMUST00000099858(transcript)|go:"GO:0004175"(endopeptidase activity)|go:"GO:0004252"(serine-type endopeptidase activity)|go:"GO:0005634"(nucleus)|go:"GO:0005737"(cytoplasm)|go:"GO:0005829"(cytosol)|go:"GO:0006508"(proteolysis)|go:"GO:0019538"(protein metabolic process)|go:"GO:0042277"(peptide binding)|go:"GO:0070012"(oligopeptidase activity)|interpro:IPR001375(Peptidase S9, prolyl oligopeptidase active site region)|interpro:IPR002470(Peptidase S9A, prolyl oligopeptidase)|interpro:IPR002471(Peptidase S9, serine active site)|interpro:IPR023302|interpro:IPR029058|mint:Q9QUR6	refseq:NP_071312.1|go:"GO:0014069"(postsynaptic density)|go:"GO:0021537"(telencephalon development)|go:"GO:0030424"(axon)|go:"GO:0030425"(dendrite)|go:"GO:0031966"(mitochondrial membrane)|go:"GO:0035556"(intracellular signal transduction)|go:"GO:0043025"(neuronal cell body)|go:"GO:0044327"(dendritic spine head)|go:"GO:0045202"(synapse)|go:"GO:0045211"(postsynaptic membrane)|go:"GO:0070300"(phosphatidic acid binding)|go:"GO:0098794"(postsynapse)|go:"GO:0098978"(glutamatergic synapse)|go:"GO:0099170"(postsynaptic modulation of chemical synaptic transmission)|go:"GO:1900273"(positive regulation of long-term synaptic potentiation)|interpro:IPR000048(IQ calmodulin-binding region)|rcsb pdb:4E50|ensembl:ENSMUSG00000053310(gene)|ensembl:ENSMUST00000065668(transcript)|go:"GO:0005516"(calmodulin binding)|go:"GO:0005547"(phosphatidylinositol-3,4,5-trisphosphate binding)|go:"GO:0005634"(nucleus)|go:"GO:0005737"(cytoplasm)|go:"GO:0008306"(associative learning)|go:"GO:0012510"(trans-Golgi network transport vesicle membrane)	-	comment:mint|function:Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long	-	figure legend:Fig. 6|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/01/17	2019/05/20	rogid:LrkDBZS1o6Br0r14vkmXkGf5D4o10090	rogid:a++S4V0kObXutTb8DwokHhJfL3k10090	rigid:AhF9vqOiozYEFvVvgyXNyaFdZjM	false	-	sufficient binding region:70-78|fluorescent dye label:n-n	-	-	psi-mi:"MI:0867"(tag visualisation by fluorescence)	psi-mi:"MI:0867"(tag visualisation by fluorescence)
uniprotkb:Q9QUR6	uniprotkb:Q92686	intact:EBI-8344942|intact:MINT-1854903|uniprotkb:Q80YS1|ensembl:ENSMUSP00000097444	intact:EBI-3908564|ensembl:ENSP00000284292|ensembl:ENSP00000399591	psi-mi:ppce_mouse(display_long)|uniprotkb:Prep(gene name)|psi-mi:Prep(display_short)|uniprotkb:Pep(gene name synonym)|uniprotkb:Post-proline cleaving enzyme(gene name synonym)	psi-mi:neug_human(display_long)|uniprotkb:NRGN(gene name)|psi-mi:NRGN(display_short)|uniprotkb:RC3(gene name synonym)	psi-mi:"MI:0435"(protease assay)	Becker et al. (2018)	pubmed:30157938|imex:IM-27592	taxid:10090(mouse)|taxid:10090(Mus musculus)	taxid:9606(human)|taxid:9606(Homo sapiens)	psi-mi:"MI:0570"(protein cleavage)	psi-mi:"MI:0486"(UniProt)	intact:EBI-25435451|imex:IM-27592-10	-	-	psi-mi:"MI:0501"(enzyme)	psi-mi:"MI:0502"(enzyme target)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_035286.1|ensembl:ENSMUSG00000019849(gene)|ensembl:ENSMUST00000099858(transcript)|go:"GO:0004175"(endopeptidase activity)|go:"GO:0004252"(serine-type endopeptidase activity)|go:"GO:0005634"(nucleus)|go:"GO:0005737"(cytoplasm)|go:"GO:0005829"(cytosol)|go:"GO:0006508"(proteolysis)|go:"GO:0019538"(protein metabolic process)|go:"GO:0042277"(peptide binding)|go:"GO:0070012"(oligopeptidase activity)|interpro:IPR001375(Peptidase S9, prolyl oligopeptidase active site region)|interpro:IPR002470(Peptidase S9A, prolyl oligopeptidase)|interpro:IPR002471(Peptidase S9, serine active site)|interpro:IPR023302|interpro:IPR029058|mint:Q9QUR6	go:"GO:0070300"(phosphatidic acid binding)|go:"GO:0098978"(glutamatergic synapse)|go:"GO:0099170"(postsynaptic modulation of chemical synaptic transmission)|go:"GO:1900273"(positive regulation of long-term synaptic potentiation)|interpro:IPR000048(IQ calmodulin-binding region)|reactome:R-HSA-9620244|go:"GO:0021537"(telencephalon development)|go:"GO:0030424"(axon)|go:"GO:0031966"(mitochondrial membrane)|go:"GO:0043025"(neuronal cell body)|go:"GO:0044327"(dendritic spine head)|go:"GO:0045211"(postsynaptic membrane)|refseq:NP_001119653.1|refseq:NP_006167.1|ensembl:ENSG00000154146(gene)|ensembl:ENST00000284292(transcript)|ensembl:ENST00000412681(transcript)|go:"GO:0005516"(calmodulin binding)|go:"GO:0005547"(phosphatidylinositol-3,4,5-trisphosphate binding)|go:"GO:0005634"(nucleus)|go:"GO:0005829"(cytosol)|go:"GO:0007165"(signal transduction)|go:"GO:0007399"(nervous system development)|go:"GO:0008306"(associative learning)|go:"GO:0012510"(trans-Golgi network transport vesicle membrane)|go:"GO:0014069"(postsynaptic density)	-	comment:mint|function:Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long	-	figure legend:Fig. 9|full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:-1(in vitro)|taxid:-1(In vitro)	-	2019/01/17	2020/02/25	rogid:LrkDBZS1o6Br0r14vkmXkGf5D4o10090	rogid:+wHR6g3nWBOZbKAfOZ7jg+pj9pQ9606	rigid:TczcV43LM050a9Z/crAbIjNfHWY	false	-	sufficient binding region:50-78|fluorescent dye label:n-n|mutation:50-50	-	-	psi-mi:"MI:0427"(Identification by mass spectrometry)	psi-mi:"MI:0427"(Identification by mass spectrometry)