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Overview

Uniprot ID	P17066
Protein Name	Heat shock 70 kDa protein 6
Gene Name	HSPA6
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
330	LRDAKLDKAQIHDVV
359	LQDFFNGKELNKSIN
502	RSTGKANKITITNDK

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)

Protein Sequence

10 MQAPRELAVG 20 IDLGTTYSCV 30 GVFQQGRVEI 40 LANDQGNRTT 50 PSYVAFTDTE 60 RLVGDAAKSQ 70 AALNPHNTVF 80 DAKRLIGRKF 90 ADTTVQSDMK 100 HWPFRVVSEG 110 GKPKVRVCYR 120 GEDKTFYPEE 130 ISSMVLSKMK 140 ETAEAYLGQP 150 VKHAVITVPA 160 YFNDSQRQAT 170 KDAGAIAGLN 180 VLRIINEPTA 190 AAIAYGLDRR 200 GAGERNVLIF 210 DLGGGTFDVS 220 VLSIDAGVFE 230 VKATAGDTHL 240 GGEDFDNRLV 250 NHFMEEFRRK 260 HGKDLSGNKR 270 ALRRLRTACE 280 RAKRTLSSST 290 QATLEIDSLF 300 EGVDFYTSIT 310 RARFEELCSD 320 LFRSTLEPVE 330 KALRDAKLDK 340 AQIHDVVLVG 350 GSTRIPKVQK 360 LLQDFFNGKE 370 LNKSINPDEA 380 VAYGAAVQAA 390 VLMGDKCEKV 400 QDLLLLDVAP 410 LSLGLETAGG 420 VMTTLIQRNA 430 TIPTKQTQTF 440 TTYSDNQPGV 450 FIQVYEGERA 460 MTKDNNLLGR 470 FELSGIPPAP 480 RGVPQIEVTF 490 DIDANGILSV 500 TATDRSTGKA 510 NKITITNDKG 520 RLSKEEVERM 530 VHEAEQYKAE 540 DEAQRDRVAA 550 KNSLEAHVFH 560 VKGSLQEESL 570 RDKIPEEDRR 580 KMQDKCREVL 590 AWLEHNQLAE 600 KEEYEHQKRE 610 LEQICRPIFS 620 RLYGGPGVPG 630 GSSCGTQARQ 640 GDPSTGPIIE EVD

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0072562	blood microparticle
Cellular Component	GO:0005814	centriole
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0070062	extracellular exosome
Cellular Component	GO:0005576	extracellular region
Cellular Component	GO:1904813	ficolin-1-rich granule lumen
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0005886	plasma membrane
Cellular Component	GO:0034774	secretory granule lumen
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0016887	ATP hydrolysis activity
Molecular Function	GO:0019899	enzyme binding
Molecular Function	GO:0031072	heat shock protein binding
Molecular Function	GO:0044183	protein folding chaperone
Molecular Function	GO:0051082	unfolded protein binding
Biological Process	GO:0034605	cellular response to heat
Biological Process	GO:0042026	protein refolding
Biological Process	GO:0006986	response to unfolded protein

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.