Search Results

Overview

Uniprot IDP38647
Protein NameStress-70 protein, mitochondrial
Gene NameHspa9
OrganismMus musculus

Kla Sites from experimental identification

Position Flanking peptide
135 YDDPEVQKDTKNVPF
138 PEVQKDTKNVPFKIV
143 DTKNVPFKIVRASNG
206 DSQRQATKDAGQISG
288 ALLRHIVKEFKRETG
300 ETGVDLTKDNMALQR
345 GPKHLNMKLTRAQFE
368 RTIAPCQKAMQDAEV
468 NTTIPTKKSQVFSTA
563 DDIENMVKNAEKYAE
567 NMVKNAEKYAEEDRR
600 ETKMEEFKDQLPADE
610 LPADECNKLKEEISK
612 ADECNKLKEEISKMR
617 KLKEEISKMRALLAG
625 MRALLAGKDSETGEN
76 VMEGKQAKVLENAEG

Function

Mitochondrial chaperone that plays a key role in mitochondrial protein import, folding, and assembly. Plays an essential role in the protein quality control system, the correct folding of proteins, the re-folding of misfolded proteins, and the targeting of proteins for subsequent degradation. These processes are achieved through cycles of ATP binding, ATP hydrolysis, and ADP release, mediated by co-chaperones. In mitochondria, it associates with the TIM (translocase of the inner membrane) protein complex to assist in the import and folding of mitochondrial proteins (By similarity). Plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis (PubMed:26702583). Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU (PubMed:21123823). Regulates erythropoiesis via stabilization of ISC assembly (PubMed:21123823). Regulates mitochondrial calcium-dependent apoptosis by coupling two calcium channels, ITPR1 and VDAC1, at the mitochondria-associated endoplasmic reticulum (ER) membrane to facilitate calcium transport from the ER lumen to the mitochondria intermembrane space, providing calcium for the downstream calcium channel MCU, which releases it into the mitochondrial matrix (PubMed:29907098). Although primarily located in the mitochondria, it is also found in other cellular compartments. In the cytosol, it associates with proteins involved in signaling, apoptosis, or senescence. It may play a role in cell cycle regulation via its interaction with and promotion of degradation of TP53 (By similarity). May play a role in the control of cell proliferation and cellular aging (PubMed:21123823, PubMed:26702583, PubMed:8454632). Protects against reactive oxygen species (ROS) (PubMed:24243970). Extracellular HSPA9 plays a cytoprotective role by preventing cell lysis following immune attack by the membrane attack complex by disrupting formation of the complex (By similarity)

Protein Sequence

10 MISASRAAAA 20 RLVGTAASRS 30 PAAARPQDGW 40 NGLSHEAFRF 50 VSRRDYASEA 60 IKGAVVGIDL 70 GTTNSCVAVM 80 EGKQAKVLEN 90 AEGARTTPSV 100 VAFTADGERL 110 VGMPAKRQAV 120 TNPNNTFYAT 130 KRLIGRRYDD 140 PEVQKDTKNV 150 PFKIVRASNG 160 DAWVEAHGKL 170 YSPSQIGAFV 180 LMKMKETAEN 190 YLGHTAKNAV 200 ITVPAYFNDS 210 QRQATKDAGQ 220 ISGLNVLRVI 230 NEPTAAALAY 240 GLDKSEDKVI 250 AVYDLGGGTF 260 DISILEIQKG 270 VFEVKSTNGD 280 TFLGGEDFDQ 290 ALLRHIVKEF 300 KRETGVDLTK 310 DNMALQRVRE 320 AAEKAKCELS 330 SSVQTDINLP 340 YLTMDASGPK 350 HLNMKLTRAQ 360 FEGIVTDLIK 370 RTIAPCQKAM 380 QDAEVSKSDI 390 GEVILVGGMT 400 RMPKVQQTVQ 410 DLFGRAPSKA 420 VNPDEAVAIG 430 AAIQGGVLAG 440 DVTDVLLLDV 450 TPLSLGIETL 460 GGVFTKLINR 470 NTTIPTKKSQ 480 VFSTAADGQT 490 QVEIKVCQGE 500 REMAGDNKLL 510 GQFTLIGIPP 520 APRGVPQIEV 530 TFDIDANGIV 540 HVSAKDKGTG 550 REQQIVIQSS 560 GGLSKDDIEN 570 MVKNAEKYAE 580 EDRRKKERVE 590 AVNMAEGIIH 600 DTETKMEEFK 610 DQLPADECNK 620 LKEEISKMRA 630 LLAGKDSETG 640 ENIRQAASSL 650 QQASLKLFEM 660 AYKKMASERE 670 GSGSSGTGEQ KEDQKEEKQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0042645 mitochondrial nucleoid
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0043209 myelin sheath
Cellular Component GO:0005730 nucleolus
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0017134 fibroblast growth factor 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:0031625 ubiquitin protein ligase binding
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:0036444 calcium import into the mitochondrion
Biological Process GO:0030218 erythrocyte differentiation
Biological Process GO:0016226 iron-sulfur cluster assembly
Biological Process GO:0045647 negative regulation of erythrocyte differentiation
Biological Process GO:1902037 negative regulation of hematopoietic stem cell differentiation
Biological Process GO:1903707 negative regulation of hemopoiesis
Biological Process GO:0043065 positive regulation of apoptotic process
Biological Process GO:0046777 protein autophosphorylation
Biological Process GO:0006611 protein export from nucleus
Biological Process GO:0042026 protein refolding
Biological Process GO:0045646 regulation of erythrocyte differentiation

Reference

[1] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.

[2] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.

[3] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.