Search Results

Overview

Uniprot ID	Q9Y3Y2
Protein Name	Chromatin target of PRMT1 protein
Gene Name	CHTOP
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
12	SAPKVVLKSTTKMSL
16	VVLKSTTKMSLNERF
228	DAYMSKTKGHLDAEL
30	FTNMLKNKQPTPVNI
70	PSVQAALKLKQSLKQ
81	SLKQRLGKSNIQARL

Function

Plays an important role in the ligand-dependent activation of estrogen receptor target genes (PubMed:19858291). May play a role in the silencing of fetal globin genes (PubMed:20688955). Recruits the 5FMC complex to ZNF148, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (By similarity). Plays an important role in the tumorigenicity of glioblastoma cells. Binds to 5-hydroxymethylcytosine (5hmC) and associates with the methylosome complex containing PRMT1, PRMT5, MEP50 and ERH. The CHTOP-methylosome complex associated with 5hmC is recruited to selective sites on the chromosome, where it methylates H4R3 and activates the transcription of genes involved in glioblastomagenesis (PubMed:25284789)

Protein Sequence

10 MAAQSAPKVV 20 LKSTTKMSLN 30 ERFTNMLKNK 40 QPTPVNIRAS 50 MQQQQQLASA 60 RNRRLAQQME 70 NRPSVQAALK 80 LKQSLKQRLG 90 KSNIQARLGR 100 PIGALARGAI 110 GGRGLPIIQR 120 GLPRGGLRGG 130 RATRTLLRGG 140 MSLRGQNLLR 150 GGRAVAPRMG 160 LRRGGVRGRG 170 GPGRGGLGRG 180 AMGRGGIGGR 190 GRGMIGRGRG 200 GFGGRGRGRG 210 RGRGALARPV 220 LTKEQLDNQL 230 DAYMSKTKGH 240 LDAELDAYMA QTDPETND

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0016607	nuclear speck
Cellular Component	GO:0005730	nucleolus
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0000346	transcription export complex
Molecular Function	GO:0008327	methyl-CpG binding
Molecular Function	GO:0003723	RNA binding
Biological Process	GO:0006338	chromatin remodeling
Biological Process	GO:0006351	DNA-templated transcription
Biological Process	GO:0006406	mRNA export from nucleus
Biological Process	GO:0032781	positive regulation of ATP-dependent activity
Biological Process	GO:0051096	positive regulation of helicase activity

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] 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.

[3] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[4] 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.