HSPA2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005634 nucleus	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation of HSPA2 to nucleus based on phylogenetic inference from multiple HSP70 orthologs across species. HSP70 family members are well documented to localize to the nucleus, particularly under stress conditions and during specific cell cycle stages. For HSPA2 specifically, the mouse ortholog (Hsp70-2/P17156) has been shown to associate with synaptonemal complexes in the nucleus of meiotic spermatocytes (PMID:8622925). HSPA2 was also detected in the human sperm nucleus by proteomics (PMID:21630459). The IBA annotation is well supported by phylogenetic evidence and consistent with known biology. Reason: HSP70 family members are known to localize to the nucleus. HSPA2 in particular is associated with synaptonemal complexes within the nucleus of meiotic spermatocytes (PMID:8622925), and was detected in the sperm nucleus proteome (PMID:21630459). The IBA annotation from phylogenetic inference is well supported. Supporting Evidence: PMID:8622925 We previously found that HSP70-2 is associated with synaptonemal complexes in the nucleus of meiotic spermatocytes from mice and hamsters.
GO:0005737 cytoplasm	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation of HSPA2 to cytoplasm based on phylogenetic inference. HSP70 family members are predominantly cytoplasmic proteins. UniProt notes the subcellular location of HSPA2 as cytoplasm/cytoskeleton/spindle (UniProt P54652). Hageman et al. (PMID:21231916) expressed HSPA2 in cell culture and demonstrated cytoplasmic chaperone activities (luciferase refolding, polyQ aggregation suppression), confirming cytoplasmic localization. This is a well-supported core localization. Reason: HSPA2 is a cytoplasmic chaperone as demonstrated by functional assays in the cytoplasm (PMID:21231916) and consistent with the known biology of HSP70 family members. The IBA phylogenetic annotation is correct. Supporting Evidence: PMID:21231916 we assessed the effect of overexpression of each of these HSPs on refolding of heat-denatured luciferase and on the suppression of aggregation of a non-foldable polyQ (polyglutamine)-expanded Huntingtin fragment
GO:0005886 plasma membrane	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: IBA annotation of HSPA2 to plasma membrane based on phylogenetic inference. Several HSP70 family members have been shown to localize to the plasma membrane and cell surface, particularly under stress conditions. For HSPA2, the mouse ortholog (P17156) has been annotated to cell surface (GO_REF:0000107, Ensembl Compara). UniProt notes that HSPA2 is a component of the CatSper complex (by similarity), which is a sperm cell surface ion channel complex. The IBA annotation is plausible but plasma membrane localization is not a core feature of HSPA2 function. Reason: Plasma membrane localization of HSP70 family members is documented but is not the primary site of HSPA2 function. The main functional localizations are cytoplasm/cytosol and nucleus (synaptonemal complex). Plasma membrane association may relate to its role in the CatSper complex in sperm or stress-related surface presentation.
GO:0016887 ATP hydrolysis activity	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation of HSPA2 for ATP hydrolysis activity based on phylogenetic inference from HSP70 orthologs. ATP hydrolysis is the fundamental mechanistic step driving the HSP70 chaperone cycle. The N-terminal nucleotide-binding domain of HSPA2 (residues 2-389) binds and hydrolyzes ATP, and the crystal structure of the HSPA2 ATPase domain has been solved in complex with ADP and phosphate (PDB:3I33, PMID:20072699). UniProt describes the allosteric coupling between ATP hydrolysis and substrate binding (UniProt P54652). This is a core molecular function of HSPA2. Reason: ATP hydrolysis is the fundamental catalytic activity of all HSP70 family members, driving the chaperone cycle. The HSPA2 ATPase domain crystal structure confirms this activity (PDB:3I33, PMID:20072699). The IBA annotation is strongly supported by structural evidence on HSPA2 itself and conserved HSP70 mechanism.
GO:0031072 heat shock protein binding	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: IBA annotation of HSPA2 for heat shock protein binding based on phylogenetic inference from HSP70-family proteins including HSPA1A, HSPA1B, HSPA6, HSPA8, and HSPA1L. This annotation should be interpreted as conserved binding within the heat-shock/chaperone network, not as a catch-all for HSPBP1, BAG4, or HSF2 interactions because those partners are not themselves heat shock proteins. Falcon synthesis also lists HSPA1A, HSPA8, and HSP90AA1 among HSPA2-associated chaperone-network proteins, but direct paralog-specific biochemical support remains less central than HSPA2's ATPase/foldase activity. Reason: The PANTHER IBA annotation is plausible for conserved HSP70 chaperone-network binding, but HSPBP1, BAG4, and HSF2 should not be used to justify GO:0031072 because those proteins are co-chaperones or transcription factors rather than heat shock proteins. Retain the term as non-core; the core molecular functions are ATP hydrolysis and protein folding chaperone activity.
GO:0044183 protein folding chaperone	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation of HSPA2 as a protein folding chaperone based on phylogenetic inference from HSP70 orthologs including DnaK. This is the central molecular function of HSPA2. Hageman et al. (PMID:21231916) directly demonstrated that HSPA2 has chaperone activity by showing it supports refolding of heat-denatured luciferase and suppresses aggregation of polyQ-expanded Huntingtin. UniProt describes HSPA2 as a "molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides" (UniProt P54652). This is the core molecular function annotation for HSPA2. Reason: Protein folding chaperone activity is the core molecular function of HSPA2, directly demonstrated by in vitro assays (PMID:21231916) and consistent with the well-characterized HSP70 chaperone mechanism. The IBA annotation is strongly supported by both phylogenetic and experimental evidence. Supporting Evidence: PMID:21231916 we assessed the effect of overexpression of each of these HSPs on refolding of heat-denatured luciferase and on the suppression of aggregation of a non-foldable polyQ (polyglutamine)-expanded Huntingtin fragment file:human/HSPA2/HSPA2-deep-research-falcon.md Across recent primary studies, the most defensible primary function annotation is that HSPA2 is an ATP-dependent molecular chaperone supporting proteostasis (folding/refolding and quality control).
GO:0005829 cytosol	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation of HSPA2 to cytosol based on phylogenetic inference. HSPA2 is a cytosolic chaperone. This annotation is also supported by direct experimental evidence (IDA) from PMID:21231916, where HSPA2 was overexpressed and shown to function in the cytosol. The IBA annotation is consistent with the IDA evidence and with the known biology of HSP70 family members. Reason: Cytosol is the primary functional compartment for HSPA2 chaperone activity, supported by both phylogenetic inference and direct experimental evidence (PMID:21231916 IDA). The IBA annotation is correct.
GO:0042026 protein refolding	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation of HSPA2 for involvement in protein refolding based on phylogenetic inference from HSP70 orthologs. Protein refolding is a core biological process mediated by HSP70 chaperones. Hageman et al. (PMID:21231916) directly demonstrated HSPA2 supports refolding of heat-denatured luciferase, providing experimental confirmation. This IBA annotation is strongly supported. Reason: Protein refolding is a core function of HSP70 chaperones, directly demonstrated for HSPA2 by luciferase refolding assays (PMID:21231916). The IBA annotation is well supported by phylogenetic and experimental evidence. Supporting Evidence: PMID:21231916 we assessed the effect of overexpression of each of these HSPs on refolding of heat-denatured luciferase
GO:0000166 nucleotide binding	IEA GO_REF:0000043	ACCEPT	Summary: IEA annotation of HSPA2 for nucleotide binding based on UniProtKB/Swiss-Prot keyword mapping (KW-0547 Nucleotide-binding). HSPA2 has a well-characterized nucleotide-binding domain (residues 2-389) with multiple ATP binding sites confirmed by crystal structure (PDB:3I33). This is a correct but overly general annotation; GO:0005524 "ATP binding" is more specific and already annotated. Nonetheless, nucleotide binding is technically correct as a parent term. Reason: Nucleotide binding is correct for HSPA2, which has an N-terminal nucleotide-binding domain confirmed by crystal structure. While broader than the more specific ATP binding annotation (GO:0005524), it is not incorrect as an IEA annotation derived from keyword mapping.
GO:0005524 ATP binding	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation of HSPA2 for ATP binding based on combined automated annotation using InterPro (IPR013126 HSP70 family) and UniProtKB keyword (KW-0067 ATP-binding). The crystal structure of HSPA2 NBD in complex with ADP and phosphate (PDB:3I33, PMID:20072699) directly confirms ATP binding. UniProt annotates multiple ATP binding sites at residues 13-16, 72, 205-207, 271-278, and 342-345 (UniProt P54652). This is a well-supported core molecular function. Reason: ATP binding is fundamental to HSPA2 function and is confirmed by crystal structure (PDB:3I33) and multiple annotated binding sites in the NBD domain. The IEA annotation is correct.
GO:0005819 spindle	IEA GO_REF:0000044	ACCEPT	Summary: IEA annotation of HSPA2 to spindle based on UniProtKB/Swiss-Prot subcellular location vocabulary mapping. UniProt records HSPA2 subcellular location as "Cytoplasm, cytoskeleton, spindle" based on similarity to mouse Hsp70-2 (P17156). The mouse ortholog co-localizes with SHCBP1L at the spindle during meiosis. This is consistent with the meiotic spindle localization annotated elsewhere (GO:0072687). The more specific term GO:0072687 "meiotic spindle" is preferable, but spindle is not wrong as a broader term. Reason: HSPA2 localizes to the meiotic spindle based on similarity data from the mouse ortholog (UniProt P17156). The broader term "spindle" is acceptable as an IEA annotation, though GO:0072687 "meiotic spindle" is more specific and also annotated.
GO:0006986 response to unfolded protein	IEA GO_REF:0000117	ACCEPT	Summary: IEA annotation of HSPA2 for response to unfolded protein based on ARBA machine learning. As a member of the HSP70 chaperone family, HSPA2 is involved in the cellular response to unfolded proteins. UniProt describes HSPA2 as a molecular chaperone involved in "protection of the proteome from stress" and "the re-folding of misfolded proteins" (UniProt P54652). HSPA2 is constitutively expressed but its role in proteostasis is consistent with involvement in unfolded protein response. Reason: HSPA2 is a molecular chaperone that assists in refolding of misfolded proteins and suppresses protein aggregation (PMID:21231916), which are key components of the response to unfolded protein. The IEA annotation is correct.
GO:0007283 spermatogenesis	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation of HSPA2 for involvement in spermatogenesis based on combined automated annotation using orthology to mouse Hsp70-2 (P17156) and UniProtKB keyword (KW-0744 Spermatogenesis). The mouse knockout study (PMID:8622925) directly demonstrated that Hsp70-2 disruption causes failed meiosis, germ cell apoptosis, and male infertility. HSPA2 is the human ortholog and is constitutively expressed at very high levels in testis (PMID:7829106). This is a core specialized function of HSPA2. Reason: Spermatogenesis is a core specialized function of HSPA2, demonstrated by mouse knockout studies showing male infertility (PMID:8622925) and supported by high testicular expression (PMID:7829106). The IEA annotation is strongly supported. Supporting Evidence: PMID:8622925 Male mice homozygous for the mutant allele (Hsp70-2 -/-) did not synthesize HSP70-2, lacked postmeiotic spermatids and mature sperm, and were infertile. PMID:7829106 HSPA2 is constitutively expressed in most tissues, with very high levels in testis and skeletal muscle.
GO:0016887 ATP hydrolysis activity	IEA GO_REF:0000002	ACCEPT	Summary: IEA annotation of HSPA2 for ATP hydrolysis activity based on InterPro record (IPR013126 HSP70 family) to GO term mapping. This is a duplicate of the IBA annotation for the same term (GO:0016887). ATP hydrolysis is the core catalytic activity of the HSP70 ATPase domain. The crystal structure of the HSPA2 ATPase domain (PDB:3I33) confirms this activity. Duplicate annotations with different evidence codes are acceptable. Reason: ATP hydrolysis activity is the core catalytic function of HSPA2, confirmed by crystal structure of the ATPase domain (PDB:3I33). The IEA from InterPro is correct and consistent with the IBA annotation.
GO:0019899 enzyme binding	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: IEA annotation of HSPA2 for enzyme binding based on ARBA machine learning. HSPA2 interacts with METTL21A (HSPA-KMT), an enzyme that trimethylates Lys-564 of HSPA2 (PMID:23921388). This qualifies as enzyme binding. However, this is a somewhat uninformative term; the interaction with METTL21A is more accurately described as HSPA2 being a substrate of this methyltransferase rather than HSPA2 having "enzyme binding" as a core molecular function. As a chaperone, HSPA2 also interacts with numerous enzymes as clients. Reason: Enzyme binding is technically correct (HSPA2 interacts with METTL21A methyltransferase, PMID:23921388), but it is not an informative description of HSPA2 core function. As a chaperone, HSPA2 binds many proteins including enzymes as clients or regulatory partners.
GO:0030154 cell differentiation	IEA GO_REF:0000043	MARK AS OVER ANNOTATED	Summary: IEA annotation of HSPA2 for cell differentiation based on UniProtKB keyword mapping (KW-0221 Differentiation). This is a very broad term. The differentiation keyword in UniProt for HSPA2 presumably relates to its role in spermatogenesis, specifically spermatid differentiation and development. The more specific terms GO:0007283 "spermatogenesis" and GO:0007286 "spermatid development" are already annotated and are more informative. Cell differentiation is too generic to be useful for HSPA2. Reason: GO:0030154 "cell differentiation" is too broad and uninformative for HSPA2. The relevant differentiation context is spermatogenesis/spermatid development, which is already captured by more specific annotations (GO:0007283, GO:0007286). This general term adds no useful information.
GO:0042026 protein refolding	IEA GO_REF:0000117	ACCEPT	Summary: IEA annotation of HSPA2 for protein refolding based on ARBA machine learning. This is a duplicate of the IBA and IDA annotations for the same term. Protein refolding is a core function of HSPA2, directly demonstrated by luciferase refolding assays (PMID:21231916). The IEA annotation is correct and consistent with experimental evidence. Reason: Protein refolding is a core function of HSPA2, confirmed by experimental evidence (PMID:21231916 IDA) and phylogenetic inference (IBA). The IEA annotation is correct.
GO:0051082 unfolded protein binding	IEA GO_REF:0000117	MODIFY	Summary: GO:0051082 "unfolded protein binding" is now formally obsolete (go-ontology#30962) because the term describes binding rather than the actual molecular activity. HSPA2 is a bona fide ATP-dependent foldase chaperone, not merely a passive binder of unfolded proteins. The IEA annotation via ARBA machine learning correctly identifies the chaperone-related function but uses the wrong term. UniProt describes HSPA2 as a "molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides" (UniProt P54652). The correct replacement is GO:0044183 "protein folding chaperone", which already has an IBA annotation for this gene, further confirming the appropriateness of the replacement. Reason: GO:0051082 is now formally obsolete per go-ontology#30962 because it conflates passive binding with active chaperone function. For HSP70 family members like HSPA2, the correct term is GO:0044183 "protein folding chaperone" (foldase), as the protein actively assists protein folding through ATP-dependent cycles. This IEA annotation should be replaced with the correct MF term. Proposed replacements: protein folding chaperone
GO:0005515 protein binding	IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in...	MARK AS OVER ANNOTATED	Summary: IPI annotation of HSPA2 for protein binding based on interaction with HSPBP1 (Q9NZL4) detected in Rual et al. (PMID:16189514), a proteome-scale yeast two-hybrid study of human protein-protein interactions. HSPBP1 is a known HSP70 co-chaperone/nucleotide exchange factor. The interaction between HSPA2 and HSPBP1 is functionally relevant and has been confirmed in multiple independent studies. However, "protein binding" is uninformative and this co-chaperone/NEF interaction should not be replaced with heat shock protein binding because HSPBP1 is not an HSP. Reason: The interaction with HSPBP1 (a co-chaperone/NEF) is real and confirmed across multiple studies, but GO:0005515 "protein binding" is uninformative. GO:0031072 "heat shock protein binding" would be semantically incorrect here because HSPBP1 is not a heat shock protein. Mark as over-annotated rather than propose an incorrect replacement.
GO:0005515 protein binding	IPI PMID:16713569 A protein-protein interaction network for human inherited at...	MARK AS OVER ANNOTATED	Summary: IPI annotation of HSPA2 for protein binding based on interaction with HSPBP1 (Q9NZL4) detected in Lim et al. (PMID:16713569), a protein-protein interaction network study for inherited ataxias. This is another detection of the HSPA2-HSPBP1 co-chaperone interaction. As with the other HSPBP1 interaction entries, "protein binding" is uninformative but should not be replaced by heat shock protein binding because HSPBP1 is not an HSP. Reason: Same rationale as the PMID:16189514 entry. HSPA2-HSPBP1 interaction is a co-chaperone/NEF interaction. GO:0005515 is uninformative, and GO:0031072 would be incorrect for this non-HSP partner.
GO:0005515 protein binding	IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc...	MARK AS OVER ANNOTATED	Summary: IPI annotation of HSPA2 for protein binding based on interactions detected in Taipale et al. (PMID:25036637), a quantitative chaperone interaction network study. The GOA data shows interactions with BAG4 (O95429), HSF2 (Q03933), and Q96BE0. BAG4 is a BAG domain co-chaperone that acts as a nucleotide exchange factor for HSP70s. HSF2 is a heat shock transcription factor. These are functionally relevant interactions for a chaperone. However, "protein binding" remains uninformative; these interactions reflect chaperone-co-chaperone interactions or client binding. Reason: The interactions with BAG4 (co-chaperone) and HSF2 are real and functionally relevant from a chaperone network study, but "protein binding" is uninformative. GO:0031072 is not an appropriate replacement because BAG4 is a BAG-domain nucleotide exchange factor/co-chaperone and HSF2 is a transcription factor, not a heat shock protein.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	MARK AS OVER ANNOTATED	Summary: IPI annotation of HSPA2 for protein binding based on interactions with TRIM38 (O00635) and HSPBP1 (Q9NZL4) detected in Rolland et al. (PMID:25416956), a proteome-scale interactome mapping study. The HSPBP1 interaction is a well-validated co-chaperone interaction. TRIM38 is an E3 ubiquitin ligase; its interaction with HSPA2 could relate to chaperone- mediated targeting of substrates for ubiquitination. "Protein binding" is too generic for these functionally informative interactions. Reason: Contains validated co-chaperone interaction (HSPBP1) and ubiquitin ligase interaction (TRIM38). GO:0005515 "protein binding" is uninformative; the HSPBP1 interaction is not heat shock protein binding and the TRIM38 interaction lacks enough functional specificity for a better replacement.
GO:0005515 protein binding	IPI PMID:28514442 Architecture of the human interactome defines protein commun...	MARK AS OVER ANNOTATED	Summary: IPI annotation of HSPA2 for protein binding based on interaction with HSPBP1 (Q9NZL4) detected in Huttlin et al. (PMID:28514442), a study on the architecture of the human interactome. This is yet another independent confirmation of the HSPA2-HSPBP1 co-chaperone interaction. "Protein binding" is uninformative for this functionally well-characterized interaction. Reason: Another confirmation of HSPA2-HSPBP1 co-chaperone interaction. GO:0005515 is uninformative, but GO:0031072 would be incorrect because HSPBP1 is not a heat shock protein.
GO:0005515 protein binding	IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari...	MARK AS OVER ANNOTATED	Summary: IPI annotation of HSPA2 for protein binding based on interaction with TRIM38 (O00635) detected in Sahni et al. (PMID:31515488), a large-scale study on disruption of protein interactions by genetic variants. TRIM38 is an E3 ubiquitin ligase, not a heat shock protein, so the interaction cannot be captured by GO:0031072. Without functional characterization of the HSPA2-TRIM38 pair, "protein binding" is uninformative. Reason: Single binary interaction with TRIM38 (an E3 ubiquitin ligase) detected in a high-throughput screen does not justify a specific molecular function annotation. GO:0031072 "heat shock protein binding" is biologically incorrect because TRIM38 is not an HSP. Mark as over-annotated rather than propose a replacement.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	MARK AS OVER ANNOTATED	Summary: IPI annotation of HSPA2 for protein binding based on interaction with BAG4 (O95429) detected in Luck et al. (PMID:32296183), a reference map of the human binary protein interactome. BAG4 is a co-chaperone containing a BAG domain that functions as a nucleotide exchange factor for HSP70 proteins. This is a functionally relevant chaperone-co-chaperone interaction. "Protein binding" is uninformative. Reason: BAG4 is an HSP70 co-chaperone; this interaction is functionally relevant but is not heat shock protein binding because BAG4 is a BAG-domain nucleotide exchange factor/co-chaperone. Mark the generic GO:0005515 annotation as over-annotated.
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	MARK AS OVER ANNOTATED	Summary: IPI annotation of HSPA2 for protein binding based on a large number of interactions detected in Mair et al. (PMID:32814053), an interactome mapping study focused on neurodegenerative disease proteins. The GOA data lists interactions with many partners including HTT (P42858), SSB, SOCS6, multiple zinc finger proteins, and others — predominantly non-HSP partners. Some of these (HTT) are likely chaperone-client interactions relevant to aggregation suppression, consistent with the role of HSPA2 in suppressing polyQ aggregation (PMID:21231916). However, many interactions from large-scale screens are non-specific or transient chaperone-client contacts, and the diverse partner set cannot be summarized by GO:0031072 "heat shock protein binding" (most partners are not HSPs). Reason: The diverse, non-HSP-dominated set of partners in this large-scale interactome screen cannot be captured by GO:0031072. Functionally relevant chaperone-client and chaperone-co-chaperone interactions of HSPA2 are already represented by GO:0044183 (protein folding chaperone) and GO:0031072 (heat shock protein binding) annotations supported by better-characterised pairs. Mark this generic "protein binding" annotation as over-annotated.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	MARK AS OVER ANNOTATED	Summary: IPI annotation of HSPA2 for protein binding based on interactions with HSF2 (Q03933) and HSPBP1 (Q9NZL4) detected in Huttlin et al. (PMID:33961781), a dual proteome-scale network study. Both are functionally relevant interactions: HSPBP1 is a co-chaperone and HSF2 is a heat shock transcription factor that could be regulated by chaperone interactions. "Protein binding" is uninformative. Reason: Both interaction partners (HSPBP1 co-chaperone, HSF2 transcription factor) are functionally relevant, but neither supports heat shock protein binding. GO:0005515 is therefore too generic and should be marked as over-annotated rather than modified to GO:0031072.
GO:0005515 protein binding	IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce...	MARK AS OVER ANNOTATED	Summary: IPI annotation of HSPA2 for protein binding based on interaction with HSPBP1 (Q9NZL4) detected in Cho et al. (PMID:35271311), the OpenCell endogenous tagging study. This is another independent confirmation of the HSPA2-HSPBP1 co-chaperone interaction using endogenous tagging, a method less prone to overexpression artifacts. "Protein binding" is uninformative. Reason: Another independent confirmation of HSPA2-HSPBP1 interaction using endogenous tagging. GO:0005515 is uninformative, and GO:0031072 is not appropriate for the non-HSP co-chaperone HSPBP1.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	MARK AS OVER ANNOTATED	Summary: IPI annotation of HSPA2 for protein binding based on interactions with HSF2 (Q03933) and HSPBP1 (Q9NZL4) detected in Kim et al. (PMID:40205054), a multimodal cell mapping study. These are the same well-validated interaction partners seen across multiple studies. "Protein binding" is uninformative. Reason: Well-validated interactions with HSPBP1 and HSF2. GO:0005515 is uninformative, but these partners do not justify GO:0031072 because HSPBP1 is a co-chaperone/NEF and HSF2 is a transcription factor.
GO:0000795 synaptonemal complex	IEA GO_REF:0000107	ACCEPT	Summary: IEA annotation of HSPA2 to synaptonemal complex based on Ensembl Compara orthology transfer from mouse Hsp70-2 (P17156). The mouse knockout study (PMID:8622925) directly demonstrated that HSP70-2 is associated with synaptonemal complexes in meiotic spermatocytes: "We previously found that HSP70-2 is associated with synaptonemal complexes in the nucleus of meiotic spermatocytes from mice and hamsters. While synaptonemal complexes assembled in Hsp70-2 -/- spermatocytes, structural abnormalities became apparent in these cells by late prophase." This is a well-supported specialized localization for HSPA2 during male meiosis. Reason: Synaptonemal complex localization is directly demonstrated for the mouse ortholog Hsp70-2 in meiotic spermatocytes (PMID:8622925) and is a key aspect of the specialized meiotic function of HSPA2. The IEA transfer from mouse is well justified. Supporting Evidence: PMID:8622925 We previously found that HSP70-2 is associated with synaptonemal complexes in the nucleus of meiotic spermatocytes from mice and hamsters. While synaptonemal complexes assembled in Hsp70-2 -/- spermatocytes, structural abnormalities became apparent in these cells by late prophase
GO:0001673 male germ cell nucleus	IEA GO_REF:0000107	ACCEPT	Summary: IEA annotation of HSPA2 to male germ cell nucleus based on Ensembl Compara orthology transfer from mouse Hsp70-2 (P17156). The mouse ortholog has been demonstrated to localize within the nucleus of meiotic spermatocytes where it associates with synaptonemal complexes (PMID:8622925). HSPA2 was also detected in the human sperm nucleus proteome (PMID:21630459). This is a well-supported specialized localization. Reason: Male germ cell nucleus localization is strongly supported by the mouse knockout study showing association with synaptonemal complexes in spermatocyte nuclei (PMID:8622925) and by proteomics detection in human sperm nuclei (PMID:21630459). Supporting Evidence: PMID:8622925 HSP70-2 is associated with synaptonemal complexes in the nucleus of meiotic spermatocytes from mice and hamsters.
GO:0009986 cell surface	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA annotation of HSPA2 to cell surface based on Ensembl Compara orthology transfer from mouse Hsp70-2 (P17156). HSP70 family members have been reported at the cell surface in various contexts, particularly in sperm cells where HSPA2 may be surface-exposed as part of the CatSper complex or other surface structures. This is consistent with the CatSper complex annotation and the plasma membrane IBA annotation. However, cell surface localization is not a core feature of HSPA2 function. Reason: Cell surface localization is plausible for HSPA2, particularly in sperm cells, but is not a core functional localization. The primary functional compartments are cytosol and nucleus (synaptonemal complex).
GO:0036128 CatSper complex	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA annotation of HSPA2 as part of the CatSper complex based on Ensembl Compara orthology transfer from mouse Hsp70-2 (P17156). UniProt notes "Component of the CatSper complex" for HSPA2 (by similarity to mouse). CatSper is a sperm-specific calcium ion channel complex essential for sperm motility and male fertility. HSPA2 association with CatSper is consistent with its specialized role in spermatogenesis and sperm function. Reason: CatSper complex membership is supported by mouse ortholog data and UniProt annotation (by similarity). This is a specialized sperm function consistent with the spermatogenesis role, but is a secondary localization rather than a core molecular function annotation.
GO:0048156 tau protein binding	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: IEA annotation of HSPA2 for tau protein binding based on Ensembl Compara orthology transfer from rat Hspa2 (P14659). HSP70 family members, particularly HSPA8/Hsc70, have been shown to interact with tau and participate in its degradation through chaperone-mediated autophagy. However, this annotation is transferred from the rat ortholog and the tau binding evidence may be stronger for other HSP70 family members (particularly HSPA8). For HSPA2, tau binding would represent a general chaperone-client interaction rather than a specific function. Reason: Tau protein binding is likely a general chaperone-client interaction shared across HSP70 family members rather than a specific function of HSPA2. The annotation is transferred from rat and may be more relevant to HSPA8/Hsc70 which is the primary constitutive HSP70 in neurons. For HSPA2, which has a specialized testis/meiosis role, tau binding is not a core function.
GO:0051087 protein-folding chaperone binding	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA annotation of HSPA2 for protein-folding chaperone binding based on Ensembl Compara orthology transfer from rat Hspa2 (P14659). HSP70 family members interact with true protein-folding chaperones such as DNAJ/HSP40 proteins and other HSP-family chaperones. HSPA2 has IntAct/UniProt evidence for DNAJA3 interaction and Falcon synthesis lists HSPA1A, HSPA8, and HSP90AA1 among HSPA2-associated chaperone-network proteins. HSPBP1 and BAG4 interactions are co-chaperone/NEF interactions and should not be used as direct support for this term. Reason: Retain as a plausible non-core chaperone-network binding annotation when restricted to true chaperone partners such as DNAJA3 and HSP-family proteins. The annotation should not be justified by HSPBP1 or BAG4 alone, because those are not protein-folding chaperones in the sense required by GO:0051087.
GO:0051861 glycolipid binding	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: IEA annotation of HSPA2 for glycolipid binding based on Ensembl Compara orthology transfer from mouse Hsp70-2 (P17156). This annotation likely relates to the reported interaction of HSP70 family members with sulfogalactosylglycerolipid (SGG/seminolipid) on the sperm surface, which has been proposed to play a role in sperm-egg interaction. This is a specialized sperm biology function. However, glycolipid binding is not a well-established molecular function of HSPA2 based on direct evidence and may represent an over-annotation based on indirect or limited evidence. Reason: Glycolipid binding is a specialized annotation transferred from the mouse ortholog that is based on limited evidence about HSP70-seminolipid interactions on sperm surfaces. This is not a well-characterized core molecular function of HSPA2 and likely represents over-annotation.
GO:0072687 meiotic spindle	IEA GO_REF:0000107	ACCEPT	Summary: IEA annotation of HSPA2 to meiotic spindle based on Ensembl Compara orthology transfer from mouse Hsp70-2 (P17156). UniProt notes that HSPA2 co-localizes with SHCBP1L at the spindle during meiosis (by similarity). This is consistent with the specialized meiotic function of HSPA2 in male germ cells. The more specific meiotic spindle term is appropriate given HSPA2's established role in male meiosis (PMID:8622925). Reason: Meiotic spindle localization is supported by mouse ortholog data showing HSPA2 co-localizes with SHCBP1L at the spindle during meiosis (UniProt, by similarity to P17156). This is consistent with HSPA2's essential role in male meiosis (PMID:8622925).
GO:0007283 spermatogenesis	ISS GO_REF:0000024	ACCEPT	Summary: ISS annotation of HSPA2 for spermatogenesis based on manual transfer from mouse ortholog Hsp70-2 (P17156). The mouse knockout study (PMID:8622925) definitively demonstrated that Hsp70-2 is required for spermatogenesis: male knockout mice lacked postmeiotic spermatids and mature sperm and were infertile. HSPA2 is the human ortholog with 98.2% amino acid identity (PMID:7829106). This is a core specialized function. Reason: Spermatogenesis is a core specialized function, directly demonstrated by mouse knockout (PMID:8622925). The ISS transfer from mouse is strongly justified by high sequence conservation (98.2% identity, PMID:7829106). Supporting Evidence: PMID:8622925 Male mice homozygous for the mutant allele (Hsp70-2 -/-) did not synthesize HSP70-2, lacked postmeiotic spermatids and mature sperm, and were infertile.
GO:0072687 meiotic spindle	ISS GO_REF:0000024	ACCEPT	Summary: ISS annotation of HSPA2 to meiotic spindle based on manual transfer from mouse ortholog Hsp70-2 (P17156). UniProt notes HSPA2 co-localizes with SHCBP1L at the spindle during meiosis (by similarity). This is a duplicate of the IEA annotation for the same term. Both are supported by the mouse ortholog data. Reason: Meiotic spindle localization is well supported by mouse ortholog data (by similarity to P17156). The ISS annotation is correct and consistent with the IEA annotation.
GO:0009408 response to heat	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: ISS annotation of HSPA2 for response to heat based on manual transfer from orthologs by AgBase. HSPA2 is a member of the HSP70 family, which are classically involved in the heat shock response. However, HSPA2 is notably constitutively expressed rather than heat-inducible. The original characterization (PMID:7829106) describes HSPA2 as constitutively expressed. UniProt keywords include "Stress response" but HSPA2 is not a canonical heat-inducible HSP70 (unlike HSPA1A/HSPA6). While HSPA2 likely participates in protein quality control during heat stress as a constitutive chaperone, "response to heat" may be somewhat misleading for a constitutively expressed member. This is a non-core annotation. Reason: HSPA2 is constitutively expressed (PMID:7829106) rather than heat-inducible, distinguishing it from canonical heat-inducible HSP70s like HSPA1A. It may participate in heat stress response through its constitutive chaperone activity, but "response to heat" is not a core or distinguishing function of HSPA2. Supporting Evidence: PMID:7829106 HSPA2 is constitutively expressed in most tissues, with very high levels in testis and skeletal muscle.
GO:0009409 response to cold	ISS GO_REF:0000024	MARK AS OVER ANNOTATED	Summary: ISS annotation of HSPA2 for response to cold based on manual transfer from orthologs by AgBase. HSP70 family members can be induced by various stresses including cold. However, HSPA2 is constitutively expressed (PMID:7829106) and there is limited direct evidence for its specific involvement in cold stress response in humans. This annotation likely derives from studies of HSP70 orthologs in other organisms (e.g., fish) where cold stress induces HSP70 expression. For HSPA2, this is at best a peripheral function. Reason: HSPA2 is constitutively expressed (PMID:7829106) and there is no strong evidence for specific involvement in cold stress response. This annotation likely derives from studies in distantly related organisms where HSP70 induction by cold is documented, but this is not a core or well-established function of human HSPA2.
GO:0016020 membrane	HDA PMID:19946888 Defining the membrane proteome of NK cells.	KEEP AS NON CORE	Summary: HDA annotation of HSPA2 to membrane based on high-throughput proteomics of NK cell membranes (PMID:19946888). HSPA2 was detected in the membrane proteome of NK cells. HSP70 family members are known to associate with membranes, particularly under stress conditions, and have been detected on cell surfaces. However, "membrane" is a very broad cellular component term and membrane association is not a core localization of HSPA2. Reason: HSPA2 detection in the membrane proteome of NK cells is plausible but represents a non-core localization. The term "membrane" is very broad, and HSPA2's primary functional localization is cytosol and nucleus (synaptonemal complex in meiosis).
GO:0019899 enzyme binding	IPI PMID:23921388 Identification and characterization of a novel human methylt...	KEEP AS NON CORE	Summary: IPI annotation of HSPA2 for enzyme binding based on its interaction with METTL21A (Q8WXB1, also known as HSPA-KMT) demonstrated in Jakobsson et al. (PMID:23921388). METTL21A was identified as the methyltransferase responsible for trimethylation of Lys-564 in HSPA2 and other HSP70 family members. The interaction was demonstrated both in vitro and in vivo, and the K564A mutation abolished methylation. This is a real enzyme-substrate interaction where HSPA2 is the substrate. However, "enzyme binding" is relatively uninformative; the biologically informative aspect is that HSPA2 is a substrate of METTL21A methyltransferase. Reason: The interaction between HSPA2 and METTL21A (PMID:23921388) is real and well-characterized, but HSPA2 is the substrate rather than having enzyme binding as a core molecular function. This is a non-core annotation. Supporting Evidence: PMID:23921388 we identified the methyltransferase METTL21A as the enzyme responsible for trimethylation of a conserved lysine residue found in several human Hsp70 (HSPA) proteins
GO:0005829 cytosol	IDA PMID:21231916 The diverse members of the mammalian HSP70 machine show dist...	ACCEPT	Summary: IDA annotation of HSPA2 to cytosol based on Hageman et al. (PMID:21231916), who demonstrated cytosolic chaperone activities of HSPA2 including luciferase refolding and polyQ aggregation suppression. These functional assays were performed in the cytosol of cultured cells. This is direct experimental evidence for cytosolic localization and is consistent with the IBA annotation for the same term. Reason: Cytosol localization is directly demonstrated by functional chaperone assays (luciferase refolding, polyQ aggregation suppression) performed in the cytosol (PMID:21231916). This is a core localization for HSPA2. Supporting Evidence: PMID:21231916 we assessed the effect of overexpression of each of these HSPs on refolding of heat-denatured luciferase and on the suppression of aggregation of a non-foldable polyQ (polyglutamine)-expanded Huntingtin fragment
GO:0042026 protein refolding	IDA PMID:21231916 The diverse members of the mammalian HSP70 machine show dist...	ACCEPT	Summary: IDA annotation of HSPA2 for protein refolding based on Hageman et al. (PMID:21231916), who directly demonstrated that HSPA2 overexpression supports refolding of heat-denatured luciferase. This is direct experimental evidence from a systematic comparison of all mammalian HSP70 family members. HSPA2 was shown to be competent for luciferase refolding, confirming its function as a protein refolding chaperone. Reason: Direct experimental evidence demonstrating HSPA2 supports luciferase refolding (PMID:21231916). This is a core biological process function of HSPA2 as an HSP70 chaperone. Supporting Evidence: PMID:21231916 we assessed the effect of overexpression of each of these HSPs on refolding of heat-denatured luciferase
GO:0051082 unfolded protein binding	IDA PMID:21231916 The diverse members of the mammalian HSP70 machine show dist...	MODIFY	Summary: Hageman et al. (PMID:21231916) systematically compared the chaperone activities of mammalian HSP70 family members using functional assays for protein refolding and aggregation suppression. The study assessed HSPA2 and other HSPAs for "refolding of heat-denatured luciferase" and "suppression of aggregation of a non-foldable polyQ-expanded Huntingtin fragment." These are assays of active chaperone function (foldase activity), not merely passive binding to unfolded substrates. HSPA2 was shown to support luciferase refolding and suppress protein aggregation, demonstrating it functions as an ATP-dependent protein folding chaperone. The annotation as GO:0051082 "unfolded protein binding" underrepresents this activity; the correct term is GO:0044183 "protein folding chaperone." GO:0051082 is now formally obsolete per go-ontology#30962. Reason: The experimental evidence from PMID:21231916 demonstrates active chaperone function (refolding of denatured luciferase, suppression of polyQ aggregation), which is GO:0044183 "protein folding chaperone" activity, not merely passive binding to unfolded proteins (GO:0051082). Furthermore, GO:0051082 is now formally obsolete (go-ontology#30962) with GO:0044183 as the recommended replacement for foldase-type chaperones. HSPA2 already has an IBA annotation for GO:0044183, and the IDA evidence from this paper directly supports that term. Proposed replacements: protein folding chaperone Supporting Evidence: PMID:21231916 we assessed the effect of overexpression of each of these HSPs on refolding of heat-denatured luciferase and on the suppression of aggregation of a non-foldable polyQ (polyglutamine)-expanded Huntingtin fragment PMID:21231916 even within the highly sequence-conserved HSPA family, functional differentiation is larger than expected
GO:0090084 negative regulation of inclusion body assembly	IDA PMID:21231916 The diverse members of the mammalian HSP70 machine show dist...	ACCEPT	Summary: IDA annotation of HSPA2 for negative regulation of inclusion body assembly based on Hageman et al. (PMID:21231916), who demonstrated that HSPA2 overexpression suppresses aggregation of a polyQ-expanded Huntingtin fragment. This suppression of protein aggregation (inclusion body formation) is a direct consequence of HSPA2 chaperone activity. The annotation accurately describes the experimental observation that HSPA2 can prevent inclusion body formation by maintaining client proteins in a soluble state. Reason: Directly demonstrated by the polyQ aggregation suppression assay in PMID:21231916. Suppression of protein aggregation/inclusion body formation is a core chaperone function of HSPA2. This is a well-supported annotation. Supporting Evidence: PMID:21231916 we assessed the effect of overexpression of each of these HSPs on refolding of heat-denatured luciferase and on the suppression of aggregation of a non-foldable polyQ (polyglutamine)-expanded Huntingtin fragment
GO:0005634 nucleus	HDA PMID:21630459 Proteomic characterization of the human sperm nucleus.	ACCEPT	Summary: HDA annotation of HSPA2 to nucleus based on proteomic characterization of the human sperm nucleus (PMID:21630459). HSPA2 was identified as a component of the sperm nucleus proteome by high-throughput mass spectrometry. This is consistent with HSPA2's known role in spermatogenesis and its association with synaptonemal complexes in the nucleus of meiotic spermatocytes (PMID:8622925). Nuclear localization is a well-supported aspect of HSPA2 biology. Reason: HSPA2 was detected in the human sperm nucleus proteome (PMID:21630459), consistent with its role in meiotic spermatocyte nuclei where it associates with synaptonemal complexes (PMID:8622925). Nuclear localization is supported by multiple independent lines of evidence.
GO:0072562 blood microparticle	HDA PMID:22516433 Proteomic analysis of microvesicles from plasma of healthy d...	KEEP AS NON CORE	Summary: HDA annotation of HSPA2 to blood microparticle based on proteomic analysis of plasma microvesicles (PMID:22516433). HSP70 proteins are commonly detected in extracellular vesicles and blood microparticles, likely reflecting their abundance and their role in extracellular signaling or stress response. Detection in blood microparticles is not a core functional localization for HSPA2. Reason: Detection in blood microparticles is a common finding for abundant intracellular proteins in proteomics studies. This is not a core functional localization for HSPA2 but may reflect real biology (extracellular chaperone function or vesicular secretion).
GO:0070062 extracellular exosome	HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos...	KEEP AS NON CORE	Summary: HDA annotation of HSPA2 to extracellular exosome based on large-scale proteomics of urinary exosomes (PMID:19056867). HSP70 family members are among the most commonly detected proteins in exosome proteomics studies. While this may reflect real biology (HSP70s have roles in exosome biogenesis and can be secreted), it is not a core functional localization for HSPA2. Reason: HSP70 family members are commonly detected in exosome proteomics. While potentially real, extracellular exosome localization is not a core functional localization for HSPA2, whose primary functions are in cytosolic protein folding and meiotic spermatocyte biology.
GO:0036128 CatSper complex	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: ISS annotation of HSPA2 as part of the CatSper complex based on manual transfer from mouse ortholog Hsp70-2 (P17156). UniProt states "Component of the CatSper complex" for HSPA2 (by similarity). CatSper is a sperm-specific calcium channel complex essential for sperm motility and hyperactivation. HSPA2 association with CatSper is consistent with its specialized role in spermatogenesis and sperm function. This duplicates the IEA annotation for the same term. Reason: CatSper complex membership is supported by mouse ortholog data and UniProt annotation. This is a specialized sperm function annotation that is consistent with HSPA2's role in spermatogenesis but is a secondary aspect of its biology.
GO:0006986 response to unfolded protein	TAS PMID:7829106 Cloning, sequencing, and mapping of the human chromosome 14 ...	ACCEPT	Summary: TAS annotation of HSPA2 for response to unfolded protein based on Bonnycastle et al. (PMID:7829106), which cloned and characterized the HSPA2 gene. The paper describes HSPA2 as a member of the HSP70 family and notes its constitutive expression pattern. While the paper does not directly demonstrate response to unfolded protein, it characterizes HSPA2 as an HSP70 gene family member, and HSP70 proteins are fundamentally involved in the unfolded protein response. The TAS evidence code is appropriate for this inference based on family membership. Reason: HSPA2 is an HSP70 family member (PMID:7829106) and involvement in response to unfolded protein is a fundamental function of this family. The TAS annotation is appropriate given the well-established role of HSP70 chaperones in proteostasis. Supporting Evidence: PMID:7829106 A genomic clone for the human heat shock protein (HSP) 70 gene located on chromosome 14 was isolated and sequenced. The gene, designated HSPA2, has a single open reading frame of 1917 bp that encodes a 639-amino acid protein
GO:0051082 unfolded protein binding	TAS PMID:3037489 Structure and expression of a human gene coding for a 71 kd ...	MODIFY	Summary: PMID:3037489 (Dworniczak and Mirault, 1987) describes the structure and expression of a human gene coding for a 71 kDa heat shock cognate protein. The paper characterizes an hsc70 gene (likely HSPA8/HSC70, not HSPA2) as encoding a protein "very likely to be identical to a clathrin uncoating ATPase recently identified as a member of the hsp70-like protein family." This TAS annotation to HSPA2 appears to have been made based on the general understanding that HSP70 family members bind unfolded proteins, but the paper actually describes HSPA8, not HSPA2 specifically. Regardless of the attribution, GO:0051082 is now formally obsolete (go-ontology#30962) and the appropriate replacement for HSP70 foldase-type chaperones is GO:0044183 "protein folding chaperone." HSPA2, like other HSP70 members, functions as an ATP-dependent foldase. Reason: GO:0051082 is now formally obsolete (go-ontology#30962). The cited paper (PMID:3037489) describes a cognate hsc70 gene that may actually correspond to HSPA8 rather than HSPA2. Nonetheless, HSPA2 is a well-established HSP70 family member with documented foldase chaperone activity (PMID:21231916). The correct replacement term is GO:0044183 "protein folding chaperone", reflecting the active ATP-dependent protein folding function of HSP70 family members. Proposed replacements: protein folding chaperone Supporting Evidence: PMID:3037489 In all eukaryotes examined so far, hsp70 gene families include cognate genes (hsc70) encoding proteins of about 70 Kd which are expressed constitutively during normal growth and development PMID:3037489 The latter is very likely to be identical to a clathrin uncoating ATPase recently identified as a member of the hsp70-like protein family
GO:0007140 male meiotic nuclear division	TAS PMID:8622925 Targeted gene disruption of Hsp70-2 results in failed meiosi...	ACCEPT	Summary: TAS annotation of HSPA2 for male meiotic nuclear division based on Dix et al. (PMID:8622925). This landmark paper demonstrated that targeted disruption of the mouse Hsp70-2 gene resulted in failed meiosis in male germ cells. Knockout males "lacked postmeiotic spermatids and mature sperm" and "development rarely progressed to the meiotic divisions." The study concluded that "HSP70-2 participates in synaptonemal complex function during meiosis in male germ cells." This is a core specialized function of HSPA2. Reason: Male meiotic nuclear division is a core specialized function of HSPA2, directly demonstrated by the mouse knockout study where loss of Hsp70-2 prevented meiotic progression (PMID:8622925). This is among the most well-supported annotations for HSPA2. Supporting Evidence: PMID:8622925 Male mice homozygous for the mutant allele (Hsp70-2 -/-) did not synthesize HSP70-2, lacked postmeiotic spermatids and mature sperm, and were infertile. PMID:8622925 These results suggest that HSP70-2 participates in synaptonemal complex function during meiosis in male germ cells and is linked to mechanisms that inhibit apoptosis.
GO:0007286 spermatid development	TAS PMID:8622925 Targeted gene disruption of Hsp70-2 results in failed meiosi...	ACCEPT	Summary: TAS annotation of HSPA2 for spermatid development based on Dix et al. (PMID:8622925). The mouse knockout study showed that Hsp70-2 -/- males "lacked postmeiotic spermatids and mature sperm." This indicates that HSPA2 is required for the meiotic progression that precedes spermatid formation. However, the study shows that meiosis fails before spermatids are formed, so the absence of spermatids is an indirect consequence of failed meiosis rather than a direct role in spermatid development per se. The annotation is still appropriate under TAS evidence as a reasonable inference from the knockout phenotype. Reason: Spermatid development failure is a consequence of HSPA2/Hsp70-2 loss (PMID:8622925). While the primary defect is in meiotic progression, the resulting absence of spermatids means HSPA2 is required for this process. The TAS evidence code is appropriate for this inference. Supporting Evidence: PMID:8622925 Male mice homozygous for the mutant allele (Hsp70-2 -/-) did not synthesize HSP70-2, lacked postmeiotic spermatids and mature sperm, and were infertile. However, neither meiosis nor fertility was affected in female Hsp70-2 -/- mice.

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