Search Results

Overview

Uniprot ID	Q9NV56
Protein Name	MRG/MORF4L-binding protein
Gene Name	MRGBP
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
185	KRSRVTDKVLTANSN
200	PSSPSAAKRRRT***

Function

Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage

Protein Sequence

10 MGEAEVGGGG 20 AAGDKGPGEA 30 ATSPAEETVV 40 WSPEVEVCLF 50 HAMLGHKPVG 60 VNRHFHMICI 70 RDKFSQNIGR 80 QVPSKVIWDH 90 LSTMYDMQAL 100 HESEILPFPN 110 PERNFVLPEE 120 IIQEVREGKV 130 MIEEEMKEEM 140 KEDVDPHNGA 150 DDVFSSSGSL 160 GKASEKSSKD 170 KEKNSSDLGC 180 KEGADKRKRS 190 RVTDKVLTAN 200 SNPSSPSAAK RRRT

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0035267	NuA4 histone acetyltransferase complex
Biological Process	GO:2000779	regulation of double-strand break repair
Biological Process	GO:0006357	regulation of transcription by RNA polymerase II
Cellular Component	GO:0005654	nucleoplasm
Biological Process	GO:0006325	chromatin organization
Biological Process	GO:0006351	DNA-templated transcription
Biological Process	GO:0045893	positive regulation of DNA-templated transcription
Biological Process	GO:1905168	positive regulation of double-strand break repair via homologous recombination
Biological Process	GO:0042981	regulation of apoptotic process
Biological Process	GO:0051726	regulation of cell cycle

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] 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] 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.