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2Y4T

Crystal structure of the human co-chaperone P58(IPK)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004860molecular_functionprotein kinase inhibitor activity
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005790cellular_componentsmooth endoplasmic reticulum
A0005829cellular_componentcytosol
A0006417biological_processregulation of translation
A0006986biological_processresponse to unfolded protein
A0016020cellular_componentmembrane
A0019901molecular_functionprotein kinase binding
A0034975biological_processprotein folding in endoplasmic reticulum
A0034976biological_processresponse to endoplasmic reticulum stress
A0035578cellular_componentazurophil granule lumen
A0036494biological_processpositive regulation of translation initiation in response to endoplasmic reticulum stress
A0043066biological_processnegative regulation of apoptotic process
A0051087molecular_functionprotein-folding chaperone binding
A0051603biological_processproteolysis involved in protein catabolic process
A0051607biological_processdefense response to virus
A0051787molecular_functionmisfolded protein binding
A0070062cellular_componentextracellular exosome
A0070417biological_processcellular response to cold
A1903561cellular_componentextracellular vesicle
A1903912biological_processnegative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation
B0004860molecular_functionprotein kinase inhibitor activity
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005788cellular_componentendoplasmic reticulum lumen
B0005790cellular_componentsmooth endoplasmic reticulum
B0005829cellular_componentcytosol
B0006417biological_processregulation of translation
B0006986biological_processresponse to unfolded protein
B0016020cellular_componentmembrane
B0019901molecular_functionprotein kinase binding
B0034975biological_processprotein folding in endoplasmic reticulum
B0034976biological_processresponse to endoplasmic reticulum stress
B0035578cellular_componentazurophil granule lumen
B0036494biological_processpositive regulation of translation initiation in response to endoplasmic reticulum stress
B0043066biological_processnegative regulation of apoptotic process
B0051087molecular_functionprotein-folding chaperone binding
B0051603biological_processproteolysis involved in protein catabolic process
B0051607biological_processdefense response to virus
B0051787molecular_functionmisfolded protein binding
B0070062cellular_componentextracellular exosome
B0070417biological_processcellular response to cold
B1903561cellular_componentextracellular vesicle
B1903912biological_processnegative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation
C0004860molecular_functionprotein kinase inhibitor activity
C0005576cellular_componentextracellular region
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0005788cellular_componentendoplasmic reticulum lumen
C0005790cellular_componentsmooth endoplasmic reticulum
C0005829cellular_componentcytosol
C0006417biological_processregulation of translation
C0006986biological_processresponse to unfolded protein
C0016020cellular_componentmembrane
C0019901molecular_functionprotein kinase binding
C0034975biological_processprotein folding in endoplasmic reticulum
C0034976biological_processresponse to endoplasmic reticulum stress
C0035578cellular_componentazurophil granule lumen
C0036494biological_processpositive regulation of translation initiation in response to endoplasmic reticulum stress
C0043066biological_processnegative regulation of apoptotic process
C0051087molecular_functionprotein-folding chaperone binding
C0051603biological_processproteolysis involved in protein catabolic process
C0051607biological_processdefense response to virus
C0051787molecular_functionmisfolded protein binding
C0070062cellular_componentextracellular exosome
C0070417biological_processcellular response to cold
C1903561cellular_componentextracellular vesicle
C1903912biological_processnegative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ASER274
BSER274
CSER274

223166

PDB entries from 2024-07-31

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