Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8

Summary

Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8 is a protein^[1].

Key Facts

• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's instance of is recorded as protein^[2].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's UniProt protein ID is recorded as P20163^[3].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's part of is recorded as Heat shock protein 70kD, peptide-binding domain superfamily^[4].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's part of is recorded as Heat shock protein 70kD, C-terminal domain superfamily^[5].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's part of is recorded as Heat shock protein 70 family^[6].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's part of is recorded as Heat shock protein 70, conserved site, protein family^[7].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's has part is recorded as Heat shock protein 70, conserved site^[8].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's RefSeq protein ID is recorded as NP_001293470^[9].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's RefSeq protein ID is recorded as NP_001370395^[10].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's molecular function is recorded as nucleotide binding^[11].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's molecular function is recorded as ATP binding^[12].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's molecular function is recorded as hydrolase activity^[13].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's molecular function is recorded as ATPase activity^[14].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's molecular function is recorded as heat shock protein binding^[15].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's molecular function is recorded as protein folding chaperone activity^[16].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's molecular function is recorded as unfolded protein binding^[17].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's molecular function is recorded as misfolded protein binding^[18].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's cell component is recorded as nucleus^[19].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's cell component is recorded as cytoplasm^[20].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's cell component is recorded as endoplasmic reticulum^[21].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's cell component is recorded as endoplasmic reticulum lumen^[22].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's cell component is recorded as rough endoplasmic reticulum^[23].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's cell component is recorded as membrane^[24].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's cell component is recorded as endoplasmic reticulum chaperone complex^[25].
• Endoplasmic reticulum chaperone BiP homolog;Heat shock 70 kDa protein D CELE_F43E2.8's biological process is recorded as response to unfolded protein^[26].