Search Results
Overview
| Uniprot ID | P55201 |
|---|---|
| Protein Name | Peregrin |
| Gene Name | BRPF1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 800 | LDEVNASKQSVGRSR |
| 896 | RTSVLFSKKNPKTAG |
| 897 | TSVLFSKKNPKTAGP |
| 983 | GGNQPVKKSFLVYRN |
Function
Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, which have a histone H3 acetyltransferase activity (PubMed:16387653, PubMed:24065767, PubMed:27939640). Plays a key role in HBO1 complex by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac) (PubMed:24065767). Some HAT complexes preferentially mediate histone H3 'Lys-23' (H3K23ac) acetylation (PubMed:27939640). Positively regulates the transcription of RUNX1 and RUNX2 (PubMed:18794358)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0000123 | histone acetyltransferase complex |
| Cellular Component | GO:0070776 | MOZ/MORF histone acetyltransferase complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0010698 | acetyltransferase activator activity |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0140566 | histone reader activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:0050793 | regulation of developmental process |
| Biological Process | GO:0006355 | regulation of DNA-templated transcription |
| Biological Process | GO:1903706 | regulation of hemopoiesis |
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
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 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.
[3] 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.