DNAJB11 Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Endoplasmic reticulum; RNA processing; Secreted; Secreted, signal peptide
Chromosomal Location of Human Ortholog: 16|16 B1
Cellular Component:  cytoplasm; endoplasmic reticulum; endoplasmic reticulum chaperone complex; extracellular space; nucleus
Molecular Function:  protein binding; signaling receptor binding; unfolded protein binding
Biological Process:  mRNA modification; negative regulation of neurogenesis; positive regulation of ATPase activity; protein folding; protein maturation
Reference #:  Q99KV1 (UniProtKB)
Alt. Names/Synonyms: 1810031F23Rik; ABBP-2; AL024055; APOBEC1-binding protein 2; Dj9; DJB11; DnaJ (Hsp40) homolog, subfamily B, member 11; DnaJ homolog subfamily B member 11; Dnajb11; ER-associated DNAJ; ER-associated dnaJ protein 3; ER-associated Hsp40 co-chaperone; ERdj3; ERj3p; OTTMUSP00000031609
Gene Symbols: Dnajb11
Molecular weight: 40,555 Da
Basal Isoelectric point: 5.92  Predict pI for various phosphorylation states
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Protein Structure Not Found.

Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene