Search Results

Overview

Uniprot IDP54727
Protein NameLysine-specific demethylase RAD23B
Gene NameRAD23B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
45 AFPVAGQKLIYAGKI
51 QKLIYAGKILNDDTA
60 LNDDTALKEYKIDEK

Function

Multifunctional protein that participates in histone H4K20 demethylation, DNA repair, ubiquitin-dependent protein degradation and transcriptional regulation (PubMed:10488153, PubMed:32209475, PubMed:9372924). Specifically demethylates mono-, di- and trimethylated 'Lys-20' of histone H4 (H4K20me1, H4K20me2, H4K20me3, respectively) into unmethylated forms. Activates the transcription of coding genes by demethylating H4K20me1 and the transcription of repetitive elements by demethylating H4K20me3 (PubMed:32209475). Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome (PubMed:10488153, PubMed:19435460). May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome (PubMed:15358861). Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex, a nucleotide-excision repair complex that is involved in damage sensing during global genome nucleotide excision repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA. Recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix including single-stranded loops, mismatched bubbles or single-stranded overhangs. Cooperatively with CETN2 appears to stabilize XPC (PubMed:10873465, PubMed:12815074, PubMed:9372924)

Protein Sequence

10 MQVTLKTLQQ 20 QTFKIDIDPE 30 ETVKALKEKI 40 ESEKGKDAFP 50 VAGQKLIYAG 60 KILNDDTALK 70 EYKIDEKNFV 80 VVMVTKPKAV 90 STPAPATTQQ 100 SAPASTTAVT 110 SSTTTTVAQA 120 PTPVPALAPT 130 STPASITPAS 140 ATASSEPAPA 150 SAAKQEKPAE 160 KPAETPVATS 170 PTATDSTSGD 180 SSRSNLFEDA 190 TSALVTGQSY 200 ENMVTEIMSM 210 GYEREQVIAA 220 LRASFNNPDR 230 AVEYLLMGIP 240 GDRESQAVVD 250 PPQAASTGAP 260 QSSAVAAAAA 270 TTTATTTTTS 280 SGGHPLEFLR 290 NQPQFQQMRQ 300 IIQQNPSLLP 310 ALLQQIGREN 320 PQLLQQISQH 330 QEHFIQMLNE 340 PVQEAGGQGG 350 GGGGGSGGIA 360 EAGSGHMNYI 370 QVTPQEKEAI 380 ERLKALGFPE 390 GLVIQAYFAC 400 EKNENLAANF LLQQNFDED

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0000502 proteasome complex
Cellular Component GO:0071942 XPC complex
Molecular Function GO:0003684 damaged DNA binding
Molecular Function GO:0140612 DNA damage sensor activity
Molecular Function GO:0035575 histone H4K20 demethylase activity
Molecular Function GO:0031593 polyubiquitin modification-dependent protein binding
Molecular Function GO:0070628 proteasome binding
Molecular Function GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Function GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding
Molecular Function GO:0003697 single-stranded DNA binding
Molecular Function GO:0043130 ubiquitin binding
Biological Process GO:0048568 embryonic organ development
Biological Process GO:0006289 nucleotide-excision repair
Biological Process GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
Biological Process GO:0032434 regulation of proteasomal ubiquitin-dependent protein catabolic process

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] 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.