Heat shock-related 70 kDa protein 2
Details
- Name
- Heat shock-related 70 kDa protein 2
- Synonyms
- Heat shock 70 kDa protein 2
- Gene Name
- HSPA2
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0049749|Heat shock-related 70 kDa protein 2 MSARGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQV AMNPTNTIFDAKRLIGRKFEDATVQSDMKHWPFRVVSEGGKPKVQVEYKGETKTFFPEEI SSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAA AIAYGLDKKGCAGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRM VSHLAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSI TRARFEELNADLFRGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGK ELNKSINPDEAVAYGAAVQAAILIGDKSENVQDLLLLDVTPLSLGIETAGGVMTPLIKRN TTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVT FDIDANGILNVTAADKSTGKENKITITNDKGRLSKDDIDRMVQEAERYKSEDEANRDRVA AKNALESYTYNIKQTVEDEKLRGKISEQDKNKILDKCQEVINWLDRNQMAEKDEYEHKQK ELERVCNPIISKLYQGGPGGGSGGGGSGASGGPTIEEVD
- Number of residues
- 639
- Molecular Weight
- 70020.43
- Theoretical pI
- Not Available
- GO Classification
- FunctionsATP binding / disordered domain specific binding / enzyme binding / unfolded protein bindingProcessesmale meiotic nuclear division / negative regulation of inclusion body assembly / protein refolding / response to cold / response to heat / response to unfolded protein / spermatid development / spermatogenesisComponentsblood microparticle / CatSper complex / cytosol / extracellular exosome / meiotic spindle / membrane / nucleus
- General Function
- 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 (PubMed:26865365). Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (By similarity).
- Specific Function
- Atp binding
- Pfam Domain Function
- HSP70 (PF00012)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0049750|Heat shock-related 70 kDa protein 2 (HSPA2) ATGTCTGCCCGTGGCCCGGCTATCGGCATCGACCTGGGCACCACCTATTCGTGCGTCGGG GTCTTCCAACATGGCAAGGTGGAGATCATCGCCAACGACCAGGGCAATCGCACCACCCCC AGCTACGTGGCCTTCACGGACACCGAGCGCCTCATCGGCGACGCCGCCAAGAACCAGGTG GCCATGAACCCCACCAACACCATCTTCGACGCCAAGAGGCTGATTGGACGGAAATTCGAG GATGCCACAGTGCAGTCGGATATGAAACACTGGCCGTTCCGGGTGGTGAGCGAGGGAGGC AAGCCCAAAGTGCAAGTAGAGTACAAGGGGGAGACCAAGACCTTCTTCCCAGAGGAGATA TCCTCCATGGTCCTCACGAAGATGAAGGAGATCGCGGAAGCCTACCTGGGGGGCAAGGTG CACAGCGCGGTCATAACGGTCCCGGCCTATTTCAACGACTCGCAGCGCCAGGCCACCAAG GACGCAGGCACCATCACGGGGCTCAATGTGCTGCGCATCATCAACGAGCCCACGGCGGCG GCCATCGCCTACGGCCTGGACAAGAAGGGCTGCGCGGGCGGCGAGAAGAACGTGCTCATC TTTGACCTGGGCGGTGGCACTTTCGACGTGTCCATCCTGACCATCGAGGATGGCATCTTC GAGGTGAAGTCCACGGCCGGCGACACCCACCTGGGCGGTGAGGACTTCGACAACCGCATG GTGAGCCACCTGGCGGAGGAGTTCAAGCGCAAGCACAAGAAGGACATTGGGCCCAACAAG CGCGCCGTGAGGCGGCTGCGCACCGCTTGCGAGCGCGCCAAGCGCACCCTGAGCTCGTCC ACGCAGGCGAGCATCGAGATCGACTCGCTCTACGAGGGCGTGGACTTCTATACGTCCATC ACGCGCGCCCGCTTCGAGGAGCTCAATGCCGACCTCTTTCGCGGGACCCTGGAGCCGGTG GAGAAGGCGCTGCGCGACGCCAAGCTGGACAAGGGCCAGATCCAGGAGATCGTGCTGGTG GGCGGCTCCACTCGTATCCCCAAGATCCAGAAGCTGCTGCAGGATTTCTTCAACGGCAAG GAGCTGAACAAGAGCATCAACCCCGACGAGGCGGTGGCCTATGGCGCCGCGGTGCAGGCG GCCATCCTCATCGGCGACAAATCAGAGAATGTGCAGGACCTGCTGCTACTCGACGTGACC CCGTTGTCGCTGGGCATCGAGACAGCTGGCGGTGTCATGACCCCACTCATCAAGAGGAAC ACCACGATCCCCACCAAGCAGACGCAGACCTTCACCACCTACTCGGACAACCAGAGCAGC GTACTGGTGCAGGTATACGAGGGCGAACGGGCCATGACCAAGGACAATAACCTGCTGGGC AAGTTCGACCTGACCGGGATTCCCCCTGCGCCTCGCGGGGTCCCCCAAATCGAGGTTACC TTCGACATTGACGCCAATGGCATCCTTAACGTTACCGCCGCCGACAAGAGCACCGGTAAG GAAAACAAAATCACCATCACCAATGACAAAGGTCGTCTGAGCAAGGACGACATTGACCGG ATGGTGCAGGAGGCGGAGCGGTACAAATCGGAAGATGAGGCGAATCGCGACCGAGTCGCG GCCAAAAACGCCCTGGAGTCCTATACCTACAACATCAAGCAGACGGTGGAAGACGAGAAA CTGAGGGGCAAGATTAGCGAGCAGGACAAAAACAAGATCCTCGACAAGTGTCAGGAGGTG ATCAACTGGCTCGACCGAAACCAGATGGCAGAGAAAGATGAGTATGAACACAAGCAGAAA GAGCTCGAAAGAGTTTGCAACCCCATCATCAGCAAACTTTACCAAGGTGGTCCTGGCGGC GGCAGCGGCGGCGGCGGTTCAGGAGCCTCCGGGGGACCCACCATCGAAGAAGTGGACTAA
- Chromosome Location
- 14
- Locus
- 14q23.3
- External Identifiers
Resource Link UniProtKB ID P54652 UniProtKB Entry Name HSP72_HUMAN HGNC ID HGNC:5235 - General References
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