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Overview

Uniprot IDQ16543
Protein NameHsp90 co-chaperone Cdc37
Gene NameCDC37
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
110 EEMRKKEKSMPWNVD
121 WNVDTLSKDGFSKSM
126 LSKDGFSKSMVNTKP
240 CFRQFFTKIKTADRQ
60 GCRECKRKVAECQRK
69 AECQRKLKELEVAEG

Function

Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity (PubMed:8666233). Inhibits HSP90AA1 ATPase activity (PubMed:23569206)

Protein Sequence

10 MVDYSVWDHI 20 EVSDDEDETH 30 PNIDTASLFR 40 WRHQARVERM 50 EQFQKEKEEL 60 DRGCRECKRK 70 VAECQRKLKE 80 LEVAEGGKAE 90 LERLQAEAQQ 100 LRKEERSWEQ 110 KLEEMRKKEK 120 SMPWNVDTLS 130 KDGFSKSMVN 140 TKPEKTEEDS 150 EEVREQKHKT 160 FVEKYEKQIK 170 HFGMLRRWDD 180 SQKYLSDNVH 190 LVCEETANYL 200 VIWCIDLEVE 210 EKCALMEQVA 220 HQTIVMQFIL 230 ELAKSLKVDP 240 RACFRQFFTK 250 IKTADRQYME 260 GFNDELEAFK 270 ERVRGRAKLR 280 IEKAMKEYEE 290 EERKKRLGPG 300 GLDPVEVYES 310 LPEELQKCFD 320 VKDVQMLQDA 330 ISKMDPTDAK 340 YHMQRCIDSG 350 LWVPNSKASE 360 AKEGEEAGPG 370 DPLLEAVPKT GDEKDVSV

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:1990565 HSP90-CDC37 chaperone complex
Cellular Component GO:0101031 protein folding chaperone complex
Molecular Function GO:0031072 heat shock protein binding
Molecular Function GO:0051879 Hsp90 protein binding
Molecular Function GO:0019900 kinase binding
Molecular Function GO:0019901 protein kinase binding
Molecular Function GO:0019887 protein kinase regulator activity
Molecular Function GO:0051087 protein-folding chaperone binding
Molecular Function GO:0097110 scaffold protein binding
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:1905091 positive regulation of type 2 mitophagy
Biological Process GO:0010608 post-transcriptional regulation of gene expression
Biological Process GO:0006457 protein folding
Biological Process GO:0050821 protein stabilization
Biological Process GO:0006605 protein targeting
Biological Process GO:0000079 regulation of cyclin-dependent protein serine/threonine kinase activity
Biological Process GO:0060338 regulation of type I interferon-mediated signaling pathway
Biological Process GO:0060334 regulation of type II interferon-mediated signaling pathway

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 C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[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.