Search Results

Overview

Uniprot IDQ9UHD1
Protein NameCysteine and histidine-rich domain-containing protein 1
Gene NameCHORDC1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
107 PKPVEAIKRPSPDEP
127 LKISASLKQALDKLK
134 KQALDKLKLSSGNEE
198 YWSCCRRKTSDFNTF
213 LAQEGCTKGKHMWTK
322 LELPAAKKQEKQKDA
89 KKELCELKPKFQEHI
91 ELCELKPKFQEHIIQ

Function

Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2 (PubMed:20230755). Proposed to act as co-chaperone for HSP90 (PubMed:20230755). May play a role in the regulation of NOD1 via a HSP90 chaperone complex (PubMed:20230755). In vitro, has intrinsic chaperone activity (PubMed:20230755). This function may be achieved by inhibiting association of ROCK2 with NPM1 (PubMed:20230755). Plays a role in ensuring the localization of the tyrosine kinase receptor EGFR to the plasma membrane, and thus ensures the subsequent regulation of EGFR activity and EGF-induced actin cytoskeleton remodeling (PubMed:32053105). Involved in stress response (PubMed:20230755). Prevents tumorigenesis (PubMed:20230755)

Protein Sequence

10 MALLCYNRGC 20 GQRFDPETNS 30 DDACTYHPGV 40 PVFHDALKGW 50 SCCKRRTTDF 60 SDFLSIVGCT 70 KGRHNSEKPP 80 EPVKPEVKTT 90 EKKELCELKP 100 KFQEHIIQAP 110 KPVEAIKRPS 120 PDEPMTNLEL 130 KISASLKQAL 140 DKLKLSSGNE 150 ENKKEEDNDE 160 IKIGTSCKNG 170 GCSKTYQGLE 180 SLEEVCVYHS 190 GVPIFHEGMK 200 YWSCCRRKTS 210 DFNTFLAQEG 220 CTKGKHMWTK 230 KDAGKKVVPC 240 RHDWHQTGGE 250 VTISVYAKNS 260 LPELSRVEAN 270 STLLNVHIVF 280 EGEKEFDQNV 290 KLWGVIDVKR 300 SYVTMTATKI 310 EITMRKAEPM 320 QWASLELPAA 330 KKQEKQKDAT TD

Gene Ontology

Classification GO ID Description
Molecular Function GO:0043531 ADP binding
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0051879 Hsp90 protein binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0051298 centrosome duplication
Biological Process GO:0006457 protein folding
Biological Process GO:1900034 regulation of cellular response to heat
Biological Process GO:0010824 regulation of centrosome duplication

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] 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] 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.

[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.