Search Results

Overview

Uniprot IDP38646
Protein NameStress-70 protein, mitochondrial
Gene NameHSPA9
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
106 RLVGMPAKRQAVTNP
121 NNTFYATKRLIGRRY
135 YDDPEVQKDIKNVPF
138 PEVQKDIKNVPFKIV
175 AFVLMKMKETAENYL
187 NYLGHTAKNAVITVP
206 DSQRQATKDAGQISG
234 ALAYGLDKSEDKVIA
288 ALLRHIVKEFKRETG
300 ETGVDLTKDNMALQR
345 GPKHLNMKLTRAQFE
368 RTIAPCQKAMQDAEV
394 GGMTRMPKVQQTVQD
467 RNTTIPTKKSQVFST
468 NTTIPTKKSQVFSTA
555 QSSGGLSKDDIENMV
563 DDIENMVKNAEKYAE
567 NMVKNAEKYAEEDRR
600 ETKMEEFKDQLPADE
610 LPADECNKLKEEISK
612 ADECNKLKEEISKMR
625 MRELLARKDSETGEN
653 KLFEMAYKKMASERE
654 LFEMAYKKMASEREG
73 CVAVMEGKQAKVLEN
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 (PubMed:18632665, PubMed:25615450, PubMed:28848044, PubMed:30933555, PubMed:31177526). 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, interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU (PubMed:26702583). Regulates erythropoiesis via stabilization of ISC assembly (PubMed:21123823, PubMed:26702583). 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 (By similarity). 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 (PubMed:24625977, PubMed:26634371). May play a role in the control of cell proliferation and cellular aging (By similarity). Protects against reactive oxygen species (ROS) (By similarity). Extracellular HSPA9 plays a cytoprotective role by preventing cell lysis following immune attack by the membrane attack complex by disrupting formation of the complex (PubMed:16091382)

Protein Sequence

10 MISASRAAAA 20 RLVGAAASRG 30 PTAARHQDSW 40 NGLSHEAFRL 50 VSRRDYASEA 60 IKGAVVGIDL 70 GTTNSCVAVM 80 EGKQAKVLEN 90 AEGARTTPSV 100 VAFTADGERL 110 VGMPAKRQAV 120 TNPNNTFYAT 130 KRLIGRRYDD 140 PEVQKDIKNV 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 YLTMDSSGPK 350 HLNMKLTRAQ 360 FEGIVTDLIR 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 LKEEISKMRE 630 LLARKDSETG 640 ENIRQAASSL 650 QQASLKLFEM 660 AYKKMASERE 670 GSGSSGTGEQ KEDQKEEKQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0140275 MIB complex
Cellular Component GO:0005743 mitochondrial inner membrane
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0042645 mitochondrial nucleoid
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0001401 SAM complex
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0031072 heat shock protein binding
Molecular Function GO:0044183 protein folding chaperone
Molecular Function GO:0003723 RNA 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:0007007 inner mitochondrial membrane organization
Biological Process GO:0006886 intracellular protein transport
Biological Process GO:0016226 iron-sulfur cluster assembly
Biological Process GO:0043066 negative regulation of apoptotic process
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:0042026 protein refolding
Biological Process GO:0045646 regulation of erythrocyte differentiation

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] 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.

[5] 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.

[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.