Search Results

Overview

Uniprot IDP10809
Protein Name60 kDa heat shock protein, mitochondrial
Gene NameHSPD1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
125 VLARSIAKEGFEKIS
130 IAKEGFEKISKGANP
133 EGFEKISKGANPVEI
156 DAVIAELKKQSKPVT
157 AVIAELKKQSKPVTT
160 AELKKQSKPVTTPEE
191 NIISDAMKKVGRKGV
192 IISDAMKKVGRKGVI
196 AMKKVGRKGVITVKD
202 RKGVITVKDGKTLND
233 PYFINTSKGQKCEFQ
236 INTSKGQKCEFQDAY
249 AYVLLSEKKISSIQS
250 YVLLSEKKISSIQSI
292 TLVLNRLKVGLQVVA
301 GLQVVAVKAPGFGDN
31 RAYAKDVKFGADARA
352 VGEVIVTKDDAMLLK
359 KDDAMLLKGKGDKAQ
364 LLKGKGDKAQIEKRI
387 VTTSEYEKEKLNERL
396 KLNERLAKLSDGVAV
405 SDGVAVLKVGGTSDV
417 SDVEVNEKKDRVTDA
418 DVEVNEKKDRVTDAL
469 KIGIEIIKRTLKIPA
473 EIIKRTLKIPAMTIA
481 IPAMTIAKNAGVEGS
523 KGIIDPTKVVRTALL
72 EQSWGSPKVTKDGVT
75 WGSPKVTKDGVTVAK
82 KDGVTVAKSIDLKDK
87 VAKSIDLKDKYKNIG
91 IDLKDKYKNIGAKLV
96 KYKNIGAKLVQDVAN

Function

Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:11422376, PubMed:1346131). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable)

Protein Sequence

10 MLRLPTVFRQ 20 MRPVSRVLAP 30 HLTRAYAKDV 40 KFGADARALM 50 LQGVDLLADA 60 VAVTMGPKGR 70 TVIIEQSWGS 80 PKVTKDGVTV 90 AKSIDLKDKY 100 KNIGAKLVQD 110 VANNTNEEAG 120 DGTTTATVLA 130 RSIAKEGFEK 140 ISKGANPVEI 150 RRGVMLAVDA 160 VIAELKKQSK 170 PVTTPEEIAQ 180 VATISANGDK 190 EIGNIISDAM 200 KKVGRKGVIT 210 VKDGKTLNDE 220 LEIIEGMKFD 230 RGYISPYFIN 240 TSKGQKCEFQ 250 DAYVLLSEKK 260 ISSIQSIVPA 270 LEIANAHRKP 280 LVIIAEDVDG 290 EALSTLVLNR 300 LKVGLQVVAV 310 KAPGFGDNRK 320 NQLKDMAIAT 330 GGAVFGEEGL 340 TLNLEDVQPH 350 DLGKVGEVIV 360 TKDDAMLLKG 370 KGDKAQIEKR 380 IQEIIEQLDV 390 TTSEYEKEKL 400 NERLAKLSDG 410 VAVLKVGGTS 420 DVEVNEKKDR 430 VTDALNATRA 440 AVEEGIVLGG 450 GCALLRCIPA 460 LDSLTPANED 470 QKIGIEIIKR 480 TLKIPAMTIA 490 KNAGVEGSLI 500 VEKIMQSSSE 510 VGYDAMAGDF 520 VNMVEKGIID 530 PTKVVRTALL 540 DAAGVASLLT 550 TAEVVVTEIP 560 KEEKDPGMGA 570 MGGMGGGMGG GMF

Gene Ontology

Classification GO ID Description
Biological Process GO:0050821 protein stabilization
Biological Process GO:0009409 response to cold
Cellular Component GO:0009986 cell surface
Cellular Component GO:0005905 clathrin-coated pit
Cellular Component GO:0030135 coated vesicle
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005769 early endosome
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0046696 lipopolysaccharide receptor complex
Cellular Component GO:0016020 membrane
Cellular Component GO:0140494 migrasome
Cellular Component GO:0005743 mitochondrial inner membrane
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0030141 secretory granule
Cellular Component GO:0097225 sperm midpiece
Molecular Function GO:0034186 apolipoprotein A-I binding
Molecular Function GO:0034185 apolipoprotein binding
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0140662 ATP-dependent protein folding chaperone
Molecular Function GO:0140608 cysteine-type endopeptidase activator activity
Molecular Function GO:0003688 DNA replication origin binding
Molecular Function GO:0003725 double-stranded RNA binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0008035 high-density lipoprotein particle binding
Molecular Function GO:0016853 isomerase activity
Molecular Function GO:0001530 lipopolysaccharide binding
Molecular Function GO:0002039 p53 binding
Molecular Function GO:0051087 protein-folding chaperone binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003697 single-stranded DNA binding
Molecular Function GO:0031625 ubiquitin protein ligase binding
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:0006458 'de novo' protein folding
Biological Process GO:0008637 apoptotic mitochondrial changes
Biological Process GO:0042113 B cell activation
Biological Process GO:0042100 B cell proliferation
Biological Process GO:0051702 biological process involved in interaction with symbiont
Biological Process GO:0051131 chaperone-mediated protein complex assembly
Biological Process GO:0048291 isotype switching to IgG isotypes
Biological Process GO:0034514 mitochondrial unfolded protein response
Biological Process GO:0002755 MyD88-dependent toll-like receptor signaling pathway
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:1900118 negative regulation of execution phase of apoptosis
Biological Process GO:1900119 positive regulation of execution phase of apoptosis
Biological Process GO:0032727 positive regulation of interferon-alpha production
Biological Process GO:0032733 positive regulation of interleukin-10 production
Biological Process GO:0032735 positive regulation of interleukin-12 production
Biological Process GO:0032755 positive regulation of interleukin-6 production
Biological Process GO:0043032 positive regulation of macrophage activation
Biological Process GO:0050870 positive regulation of T cell activation
Biological Process GO:0002842 positive regulation of T cell mediated immune response to tumor cell
Biological Process GO:0032729 positive regulation of type II interferon production
Biological Process GO:0006457 protein folding
Biological Process GO:0045041 protein import into mitochondrial intermembrane space
Biological Process GO:0051604 protein maturation
Biological Process GO:0042026 protein refolding
Biological Process GO:0006986 response to unfolded protein
Biological Process GO:0042110 T cell activation

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] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] 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.

[6] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[7] 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.

[8] 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.