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Overview

Uniprot IDP54652
Protein NameHeat shock-related 70 kDa protein 2
Gene NameHSPA2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
139 AEAYLGGKVHSAVIT
160 DSQRQATKDAGTITG
249 SHLAEEFKRKHKKDI
254 EFKRKHKKDIGPNKR
322 GTLEPVEKALRDAKL
331 LRDAKLDKGQIQEIV
510 KITITNDKGRLSKDD
515 NDKGRLSKDDIDRMV
560 KQTVEDEKLRGKISE
72 TNTIFDAKRLIGRKF
78 AKRLIGRKFEDATVQ

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)

Protein Sequence

10 MSARGPAIGI 20 DLGTTYSCVG 30 VFQHGKVEII 40 ANDQGNRTTP 50 SYVAFTDTER 60 LIGDAAKNQV 70 AMNPTNTIFD 80 AKRLIGRKFE 90 DATVQSDMKH 100 WPFRVVSEGG 110 KPKVQVEYKG 120 ETKTFFPEEI 130 SSMVLTKMKE 140 IAEAYLGGKV 150 HSAVITVPAY 160 FNDSQRQATK 170 DAGTITGLNV 180 LRIINEPTAA 190 AIAYGLDKKG 200 CAGGEKNVLI 210 FDLGGGTFDV 220 SILTIEDGIF 230 EVKSTAGDTH 240 LGGEDFDNRM 250 VSHLAEEFKR 260 KHKKDIGPNK 270 RAVRRLRTAC 280 ERAKRTLSSS 290 TQASIEIDSL 300 YEGVDFYTSI 310 TRARFEELNA 320 DLFRGTLEPV 330 EKALRDAKLD 340 KGQIQEIVLV 350 GGSTRIPKIQ 360 KLLQDFFNGK 370 ELNKSINPDE 380 AVAYGAAVQA 390 AILIGDKSEN 400 VQDLLLLDVT 410 PLSLGIETAG 420 GVMTPLIKRN 430 TTIPTKQTQT 440 FTTYSDNQSS 450 VLVQVYEGER 460 AMTKDNNLLG 470 KFDLTGIPPA 480 PRGVPQIEVT 490 FDIDANGILN 500 VTAADKSTGK 510 ENKITITNDK 520 GRLSKDDIDR 530 MVQEAERYKS 540 EDEANRDRVA 550 AKNALESYTY 560 NIKQTVEDEK 570 LRGKISEQDK 580 NKILDKCQEV 590 INWLDRNQMA 600 EKDEYEHKQK 610 ELERVCNPII 620 SKLYQGGPGG 630 GSGGGGSGAS GGPTIEEVD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0072562 blood microparticle
Cellular Component GO:0036128 CatSper complex
Cellular Component GO:0009986 cell surface
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0001673 male germ cell nucleus
Cellular Component GO:0072687 meiotic spindle
Cellular Component GO:0016020 membrane
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0000795 synaptonemal complex
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0097718 disordered domain specific binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0051861 glycolipid binding
Molecular Function GO:0031072 heat shock protein binding
Molecular Function GO:0044183 protein folding chaperone
Molecular Function GO:0051087 protein-folding chaperone binding
Molecular Function GO:0048156 tau protein binding
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:0007140 male meiotic nuclear division
Biological Process GO:0090084 negative regulation of inclusion body assembly
Biological Process GO:0042026 protein refolding
Biological Process GO:0009409 response to cold
Biological Process GO:0009408 response to heat
Biological Process GO:0006986 response to unfolded protein
Biological Process GO:0007286 spermatid development
Biological Process GO:0007283 spermatogenesis

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[4] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.