Heat shock-related 70 kDa protein 2

Name	Heat shock-related 70 kDa protein 2
Synonyms	Heat shock 70 kDa protein 2
Gene Name	HSPA2
Organism	Human
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	None
Molecular Weight	70020.43
Theoretical pI	None
GO Classification	Functions ATP binding unfolded protein binding enzyme binding disordered domain specific binding Processes protein refolding spermatid development response to unfolded protein male meiotic nuclear division negative regulation of inclusion body assembly response to heat spermatogenesis response to cold Components membrane nucleus meiotic spindle CatSper complex cytosol extracellular exosome blood microparticle
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
Transmembrane Regions
GenBank Protein ID
UniProtKB ID	P54652
UniProtKB Entry Name
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
GenBank Gene ID
GeneCard ID	None
GenAtlas ID
HGNC ID
Chromosome Location	14
Locus	14q23.3
References	Bonnycastle LL, Yu CE, Hunt CR, Trask BJ, Clancy KP, Weber JL, Patterson D, Schellenberg GD: Cloning, sequencing, and mapping of the human chromosome 14 heat shock protein gene (HSPA2). Genomics. 1994 Sep 1;23(1):85-93. [7829106 ] Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [15489334 ] Roux AF, Nguyen VT, Squire JA, Cox DW: A heat shock gene at 14q22: mapping and expression. Hum Mol Genet. 1994 Oct;3(10):1819-22. [7849706 ] Jarczowski F, Fischer G, Edlich F: FKBP36 forms complexes with clathrin and Hsp72 in spermatocytes. Biochemistry. 2008 Jul 1;47(26):6946-52. doi: 10.1021/bi8001506. Epub 2008 Jun 5. [18529014 ] Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [21269460 ] Jakobsson ME, Moen A, Bousset L, Egge-Jacobsen W, Kernstock S, Melki R, Falnes PO: Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation. J Biol Chem. 2013 Sep 27;288(39):27752-63. doi: 10.1074/jbc.M113.483248. Epub 2013 Aug 6. [23921388 ] Radons J: The human HSP70 family of chaperones: where do we stand? Cell Stress Chaperones. 2016 May;21(3):379-404. doi: 10.1007/s12192-016-0676-6. Epub 2016 Feb 10. [26865365 ] Wisniewska M, Karlberg T, Lehtio L, Johansson I, Kotenyova T, Moche M, Schuler H: Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78. PLoS One. 2010 Jan 11;5(1):e8625. doi: 10.1371/journal.pone.0008625. [20072699 ]

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