2QC7

Crystal structure of the protein-disulfide isomerase related chaperone ERp29

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003756	molecular_function	protein disulfide isomerase activity
A	0005515	molecular_function	protein binding
A	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005790	cellular_component	smooth endoplasmic reticulum
A	0006457	biological_process	protein folding
A	0006886	biological_process	intracellular protein transport
A	0009306	biological_process	protein secretion
A	0009986	cellular_component	cell surface
A	0010628	biological_process	positive regulation of gene expression
A	0010629	biological_process	negative regulation of gene expression
A	0016020	cellular_component	membrane
A	0042470	cellular_component	melanosome
A	0042803	molecular_function	protein homodimerization activity
A	0043335	biological_process	protein unfolding
A	0043410	biological_process	positive regulation of MAPK cascade
A	0050709	biological_process	negative regulation of protein secretion
A	0051087	molecular_function	protein-folding chaperone binding
A	1902235	biological_process	regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway
B	0003756	molecular_function	protein disulfide isomerase activity
B	0005515	molecular_function	protein binding
B	0005783	cellular_component	endoplasmic reticulum
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0005790	cellular_component	smooth endoplasmic reticulum
B	0006457	biological_process	protein folding
B	0006886	biological_process	intracellular protein transport
B	0009306	biological_process	protein secretion
B	0009986	cellular_component	cell surface
B	0010628	biological_process	positive regulation of gene expression
B	0010629	biological_process	negative regulation of gene expression
B	0016020	cellular_component	membrane
B	0042470	cellular_component	melanosome
B	0042803	molecular_function	protein homodimerization activity
B	0043335	biological_process	protein unfolding
B	0043410	biological_process	positive regulation of MAPK cascade
B	0050709	biological_process	negative regulation of protein secretion
B	0051087	molecular_function	protein-folding chaperone binding
B	1902235	biological_process	regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine; by PKDCC","evidences":[{"source":"PubMed","id":"25171405","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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