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Overview

Uniprot IDQ15291
Protein NameRetinoblastoma-binding protein 5
Gene NameRBBP5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
474 VHPLLGVKGDGKSKK
505 PFKPKLYKGDRGLPL
517 LPLEGSAKGKVQAEL
519 LEGSAKGKVQAELSQ

Function

In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). Does not affect ES cell self-renewal (By similarity). Component or associated component of some histone methyltransferase complexes which regulates transcription through recruitment of those complexes to gene promoters (PubMed:19131338). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3 (PubMed:19556245). Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (PubMed:19556245). In association with ASH2L and WDR5, stimulates the histone methyltransferase activities of KMT2A, KMT2B, KMT2C, KMT2D, SETD1A and SETD1B (PubMed:21220120, PubMed:22266653)

Protein Sequence

10 MNLELLESFG 20 QNYPEEADGT 30 LDCISMALTC 40 TFNRWGTLLA 50 VGCNDGRIVI 60 WDFLTRGIAK 70 IISAHIHPVC 80 SLCWSRDGHK 90 LVSASTDNIV 100 SQWDVLSGDC 110 DQRFRFPSPI 120 LKVQYHPRDQ 130 NKVLVCPMKS 140 APVMLTLSDS 150 KHVVLPVDDD 160 SDLNVVASFD 170 RRGEYIYTGN 180 AKGKILVLKT 190 DSQDLVASFR 200 VTTGTSNTTA 210 IKSIEFARKG 220 SCFLINTADR 230 IIRVYDGREI 240 LTCGRDGEPE 250 PMQKLQDLVN 260 RTPWKKCCFS 270 GDGEYIVAGS 280 ARQHALYIWE 290 KSIGNLVKIL 300 HGTRGELLLD 310 VAWHPVRPII 320 ASISSGVVSI 330 WAQNQVENWS 340 AFAPDFKELD 350 ENVEYEERES 360 EFDIEDEDKS 370 EPEQTGADAA 380 EDEEVDVTSV 390 DPIAAFCSSD 400 EELEDSKALL 410 YLPIAPEVED 420 PEENPYGPPP 430 DAVQTSLMDE 440 GASSEKKRQS 450 SADGSQPPKK 460 KPKTTNIELQ 470 GVPNDEVHPL 480 LGVKGDGKSK 490 KKQAGRPKGS 500 KGKEKDSPFK 510 PKLYKGDRGL 520 PLEGSAKGKV 530 QAELSQPLTA GGAISELL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0035097 histone methyltransferase complex
Cellular Component GO:0071339 MLL1 complex
Cellular Component GO:0044666 MLL3/4 complex
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0048188 Set1C/COMPASS complex
Molecular Function GO:0042393 histone binding
Molecular Function GO:0000976 transcription cis-regulatory region binding
Biological Process GO:0006974 DNA damage response
Biological Process GO:0043627 response to estrogen
Biological Process GO:0045815 transcription initiation-coupled chromatin remodeling

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] 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.