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2Y4U

Crystal structure of human P58(IPK) in space group P312

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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ASER274

222036

PDB entries from 2024-07-03

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