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Overview

Uniprot IDA0A286Y5I8
Protein NameHsp90 co-chaperone Cdc37
Gene NameCDC37
OrganismCavia porcellus

Kla Sites from experimental identification

Position Flanking peptide
121 WNVDTLSKDGFSKSM

Function

Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity

Protein Sequence

10 MVDYSVWDHI 20 EVSDDEDETH 30 PNIDTASLFR 40 WRHQARVERM 50 EQFQKEKEEL 60 DRGCRECKRK 70 VAECQRKLKE 80 LEVAEGGQAE 90 LERLQAEAQQ 100 LRKEERSWEQ 110 KLEEMRKKEK 120 SMPWNVDTLS 130 KDGFSKSMVN 140 TKPEKAEEES 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 EERRKRLGPG 300 GLDPVEVYES 310 LPEELQKCFD 320 VKDVQMLQDA 330 ISKMDPTDAK 340 YHMQRCIDSG 350 LWVPNSKASE 360 PKEGEEAGPR 370 DPLLDTVTKP GDEKDGSA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:1990565 HSP90-CDC37 chaperone complex
Molecular Function GO:0051879 Hsp90 protein 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

Reference

[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.