endoplasmin; heat shock protein 90 kD beta member 1; 94 kD glucose-regulated protein; GRP94; gp96 homolog; tumor rejection antigen 1 (HSP90B1, TRA1)

Function: - molecular chaperone - functions in the processing & transport of secreted proteins - has ATPase activity - phosphorylated (putative) Structure: - homodimer; disulfide-linked - component of an EIF2 complex at least composed of CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 & HSPA5 (putative) - part of a large chaperone multiprotein complex consisting of: CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, UGT1A1 & very small amounts of ERP29, but not, or at very low levels, CALR nor CANX - belongs to the heat shock protein 90 family Compartment: - endoplasmic reticulum lumen. melanosome - identified by mass spectrometry in melanosome fractions from stage 1 to stage 4 Comparative biology: - alias hsp108 (in chicken); 94 kD glucose-regulated protein (GRP94) (in hamster)

General

chaperonin; chaperone heat shock protein [hsp]-90 family

Properties

SIZE: entity length = 803 aa MW = 92 kD COMPARTMENT: endoplasmic reticulum MOTIF: signal sequence {1-21} N-glycosylation site {N62} ATP-binding site NAME: ATP-binding site SITE: 107-107 MOTIF: N-glycosylation site {N107} cysteine residue {C138} MODIFICATION: cysteine residue {C-INTERCHAIN} ATP-binding site NAME: ATP-binding site SITE: 149-149 ATP-binding site NAME: ATP-binding site SITE: 162-162 ATP-binding site NAME: ATP-binding site SITE: 199-199 N-glycosylation site {N217} Ser phosphorylation site {S306} N-glycosylation site {N445} N-glycosylation site {N481} N-glycosylation site {N502} Tyr phosphorylation site {Y677} peptide motif {800-803}

Database Correlations

OMIM 191175 UniProt P14625 PFAM correlations Entrez Gene 7184 Kegg hsa:7184

References

UniProt :accession P14625