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: 14q23.3
Cellular Component:  CatSper complex; cell surface; cytoplasm; cytosol; male germ cell nucleus; meiotic spindle; nucleus; plasma membrane; synaptonemal complex
Molecular Function:  ATP binding; ATP hydrolysis activity; ATP-dependent protein folding chaperone; disordered domain specific binding; enzyme binding; glycolipid binding; heat shock protein binding; protein binding; protein folding chaperone; protein-folding chaperone binding; tau protein binding; unfolded protein binding
Biological Process:  chaperone cofactor-dependent protein refolding; male meiosis I; male meiotic nuclear division; negative regulation of inclusion body assembly; positive regulation of ATPase-coupled calcium transmembrane transporter activity; positive regulation of G2/M transition of mitotic cell cycle; positive regulation of protein phosphorylation; protein refolding; response to cold; response to heat; response to unfolded protein; spermatid development; spermatogenesis; synaptonemal complex disassembly
Reference #:  P54652 (UniProtKB)
Alt. Names/Synonyms: epididymis secretory sperm binding protein; Heat shock 70 kDa protein 2; heat shock 70kD protein 2; heat shock 70kDa protein 2; heat shock protein family A (Hsp70) member 2; Heat shock-related 70 kDa protein 2; HSP70-2; HSP70-3; HSP72; HSPA2
Gene Symbols: HSPA2
Molecular weight: 70,021 Da
Basal Isoelectric point: 5.56  Predict pI for various phosphorylation states
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HSPA2

Protein Structure Not Found.


Cross-references to other databases:  AlphaFold  |  STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB  |  Ensembl Protein