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Overview

Uniprot IDQ5VTR2
Protein NameE3 ubiquitin-protein ligase BRE1A
Gene NameRNF20
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
22 TSMPPEKKAAVEDSG
57 TLQTKNRKLAEMLDQ
694 KEKKENKKMADEDAL
775 IKSNQIHKLLKEEKE

Function

Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role inb histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. Recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator. Mediates the polyubiquitination of isoform 2 of PA2G4 in cancer cells leading to its proteasome-mediated degradation

Protein Sequence

10 MSGIGNKRAA 20 GEPGTSMPPE 30 KKAAVEDSGT 40 TVETIKLGGV 50 SSTEELDIRT 60 LQTKNRKLAE 70 MLDQRQAIED 80 ELREHIEKLE 90 RRQATDDASL 100 LIVNRYWSQF 110 DENIRIILKR 120 YDLEQGLGDL 130 LTERKALVVP 140 EPEPDSDSNQ 150 ERKDDRERGE 160 GQEPAFSFLA 170 TLASSSSEEM 180 ESQLQERVES 190 SRRAVSQIVT 200 VYDKLQEKVE 210 LLSRKLNSGD 220 NLIVEEAVQE 230 LNSFLAQENM 240 RLQELTDLLQ 250 EKHRTMSQEF 260 SKLQSKVETA 270 ESRVSVLESM 280 IDDLQWDIDK 290 IRKREQRLNR 300 HLAEVLERVN 310 SKGYKVYGAG 320 SSLYGGTITI 330 NARKFEEMNA 340 ELEENKELAQ 350 NRLCELEKLR 360 QDFEEVTTQN 370 EKLKVELRSA 380 VEQVVKETPE 390 YRCMQSQFSV 400 LYNESLQLKA 410 HLDEARTLLH 420 GTRGTHQHQV 430 ELIERDEVSL 440 HKKLRTEVIQ 450 LEDTLAQVRK 460 EYEMLRIEFE 470 QTLAANEQAG 480 PINREMRHLI 490 SSLQNHNHQL 500 KGEVLRYKRK 510 LREAQSDLNK 520 TRLRSGSALL 530 QSQSSTEDPK 540 DEPAELKPDS 550 EDLSSQSSAS 560 KASQEDANEI 570 KSKRDEEERE 580 RERREKERER 590 EREREKEKER 600 EREKQKLKES 610 EKERDSAKDK 620 EKGKHDDGRK 630 KEAEIIKQLK 640 IELKKAQESQ 650 KEMKLLLDMY 660 RSAPKEQRDK 670 VQLMAAEKKS 680 KAELEDLRQR 690 LKDLEDKEKK 700 ENKKMADEDA 710 LRKIRAVEEQ 720 IEYLQKKLAM 730 AKQEEEALLS 740 EMDVTGQAFE 750 DMQEQNIRLM 760 QQLREKDDAN 770 FKLMSERIKS 780 NQIHKLLKEE 790 KEELADQVLT 800 LKTQVDAQLQ 810 VVRKLEEKEH 820 LLQSNIGTGE 830 KELGLRTQAL 840 EMNKRKAMEA 850 AQLADDLKAQ 860 LELAQKKLHD 870 FQDEIVENSV 880 TKEKDMFNFK 890 RAQEDISRLR 900 RKLETTKKPD 910 NVPKCDEILM 920 EEIKDYKARL 930 TCPCCNMRKK 940 DAVLTKCFHV 950 FCFECVKTRY 960 DTRQRKCPKC 970 NAAFGANDFH RIYIG

Gene Ontology

Classification GO ID Description
Cellular Component GO:0033503 HULC complex
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0000151 ubiquitin ligase complex
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0042393 histone binding
Molecular Function GO:0140850 histone H2B C-terminal K residue ubiquitin ligase activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0003730 mRNA 3'-UTR binding
Molecular Function GO:0002039 p53 binding
Molecular Function GO:0003713 transcription coactivator activity
Molecular Function GO:0061630 ubiquitin protein ligase activity
Molecular Function GO:0031625 ubiquitin protein ligase binding
Molecular Function GO:0004842 ubiquitin-protein transferase activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0030336 negative regulation of cell migration
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0000209 protein polyubiquitination
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0006511 ubiquitin-dependent protein catabolic process

Reference

[1] 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.

[2] 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.