241 human active and 13 inactive phosphatases in total;
194 phosphatases have substrate data;
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336 protein substrates;
83 non-protein substrates;
1215 dephosphorylation interactions;
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299 KEGG pathways;
876 Reactome pathways;
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last scientific update: 11 Mar, 2019
last maintenance update: 01 Sep, 2023
Cytoplasm Nucleus Note=Translocates to thenucleus during heat shock and resides in sub-nuclear structuresknown as SC35 speckles or nuclear splicing speckles
Function (UniProt annotation)
Contributes to the transparency and refractive index ofthe lens Has chaperone-like activity, preventing aggregation ofvarious proteins under a wide range of stress conditions
The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis.
The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis.
Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, cosedimentation in solution, dynamic light scattering, molecular sieving, transmission electron microscopy, two hybrid, two hybrid array, two hybrid prey pooling approach
direct interaction, physical, physical association
Affinity Capture-Western, FRET, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, beta lactamase complementation, coimmunoprecipitation, cosedimentation in solution, dynamic light scattering, experimental interaction detection, mass spectrometry studies of complexes, molecular sieving, nuclear magnetic resonance, transmission electron microscopy, two hybrid, two hybrid array, two hybrid bait and prey pooling approach, two hybrid prey pooling approach, validated two hybrid
association, direct interaction, physical, physical association
Affinity Capture-Western, FRET, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, beta lactamase complementation, coimmunoprecipitation, cosedimentation in solution, dynamic light scattering, experimental interaction detection, mass spectrometry studies of complexes, molecular sieving, nuclear magnetic resonance, transmission electron microscopy, two hybrid, two hybrid array, two hybrid bait and prey pooling approach, two hybrid prey pooling approach, validated two hybrid
association, direct interaction, physical, physical association
Affinity Capture-Western, FRET, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, beta lactamase complementation, coimmunoprecipitation, cosedimentation in solution, dynamic light scattering, experimental interaction detection, mass spectrometry studies of complexes, molecular sieving, nuclear magnetic resonance, transmission electron microscopy, two hybrid, two hybrid array, two hybrid bait and prey pooling approach, two hybrid prey pooling approach, validated two hybrid
association, direct interaction, physical, physical association
Affinity Capture-Western, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, cosedimentation in solution, dynamic light scattering, molecular sieving, transmission electron microscopy, two hybrid, two hybrid array, two hybrid prey pooling approach
direct interaction, physical, physical association
Affinity Capture-Western, FRET, Reconstituted Complex, Two-hybrid, anti bait coimmunoprecipitation, beta lactamase complementation, coimmunoprecipitation, cosedimentation in solution, dynamic light scattering, experimental interaction detection, mass spectrometry studies of complexes, molecular sieving, nuclear magnetic resonance, transmission electron microscopy, two hybrid, two hybrid array, two hybrid bait and prey pooling approach, two hybrid prey pooling approach, validated two hybrid
association, direct interaction, physical, physical association
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