Search Results

Overview

Uniprot IDP25685
Protein NameDnaJ homolog subfamily B member 1
Gene NameDNAJB1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
159 AQEPARKKQDPPVTH
181 EIYSGCTKKMKISHK
195 KRLNPDGKSIRNEDK

Function

Interacts with HSP70 and can stimulate its ATPase activity. Acts also with TTC1 as a chaperone adapter that regulates HSP70-dependent folding process by interacting with the HSP70 amino terminal region (PubMed:14503850). Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) (PubMed:24318877)

Protein Sequence

10 MGKDYYQTLG 20 LARGASDEEI 30 KRAYRRQALR 40 YHPDKNKEPG 50 AEEKFKEIAE 60 AYDVLSDPRK 70 REIFDRYGEE 80 GLKGSGPSGG 90 SGGGANGTSF 100 SYTFHGDPHA 110 MFAEFFGGRN 120 PFDTFFGQRN 130 GEEGMDIDDP 140 FSGFPMGMGG 150 FTNVNFGRSR 160 SAQEPARKKQ 170 DPPVTHDLRV 180 SLEEIYSGCT 190 KKMKISHKRL 200 NPDGKSIRNE 210 DKILTIEVKK 220 GWKEGTKITF 230 PKEGDQTSNN 240 IPADIVFVLK 250 DKPHNIFKRD 260 GSDVIYPARI 270 SLREALCGCT 280 VNVPTLDGRT 290 IPVVFKDVIR 300 PGMRRKVPGE 310 GLPLPKTPEK 320 RGDLIIEFEV 330 IFPERIPQTS 340 RTVLEQVLPI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0043197 dendritic spine
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0043025 neuronal cell body
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0014069 postsynaptic density
Cellular Component GO:0061827 sperm head
Molecular Function GO:0001671 ATPase activator activity
Molecular Function GO:0051117 ATPase binding
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0030544 Hsp70 protein binding
Molecular Function GO:0044183 protein folding chaperone
Molecular Function GO:0051087 protein-folding chaperone binding
Molecular Function GO:0003714 transcription corepressor activity
Molecular Function GO:0140416 transcription regulator inhibitor activity
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:0034605 cellular response to heat
Biological Process GO:0030900 forebrain development
Biological Process GO:0090084 negative regulation of inclusion body assembly
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:1903334 positive regulation of protein folding
Biological Process GO:0006457 protein folding
Biological Process GO:1900034 regulation of cellular response to heat
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] 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.

[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] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[5] 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.