HSPA2 Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells. Belongs to the heat shock protein 70 family. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Heat shock protein
Chromosomal Location of Human Ortholog: 12 C3|12 33.73 cM
Cellular Component:  CatSper complex; cell surface; cytoplasm; cytoskeleton; cytosol; male germ cell nucleus; meiotic spindle; nucleus; plasma membrane; synaptonemal complex
Molecular Function:  ATP binding; ATPase activity; ATPase activity, coupled; chaperone binding; disordered domain specific binding; enzyme binding; glycolipid binding; heat shock protein binding; misfolded protein binding; nucleotide binding; protein binding; protein binding involved in protein folding; tau protein binding; unfolded protein binding
Biological Process:  cell differentiation; cellular response to heat; cellular response to unfolded protein; chaperone cofactor-dependent protein refolding; male meiosis I; male meiotic nuclear division; negative regulation of inclusion body assembly; positive regulation of ATPase activity; positive regulation of calcium-transporting ATPase activity; positive regulation of G2/M transition of mitotic cell cycle; positive regulation of protein phosphorylation; protein refolding; response to unfolded protein; spermatid development; spermatogenesis; synaptonemal complex disassembly; vesicle-mediated transport
Reference #:  P17156 (UniProtKB)
Alt. Names/Synonyms: 70kD; 70kDa; Hcp70.2; heat shock 70kDa protein 2; heat shock protein 2; Heat shock protein 70.2; heat shock protein, 70 kDa 2; Heat shock-related 70 kDa protein 2; Hsp70; Hsp70-2; HSP70.2; HSP70A2; HSP72; Hspa2; MGC58299; MGC7795
Gene Symbols: Hspa2
Molecular weight: 69,642 Da
Basal Isoelectric point: 5.51  Predict pI for various phosphorylation states
Select Structure to View Below


Protein Structure Not Found.

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