Search Results

Overview

Uniprot IDQ9Y620
Protein NameDNA repair and recombination protein RAD54B
Gene NameRAD54B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
16 QLQGNSFKKPKFIPP
17 LQGNSFKKPKFIPPG
233 KCFSNPFKSVCKPSS
454 LISLSCEKRIILTGT

Function

Multifunctional ATPase that could play with RAD54, a redundant role in homologous recombination (HR), a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks (PubMed:11884632, PubMed:16428451). Could act as a molecular motor during the homology search and guide RAD51 ssDNA along a donor dsDNA thereby changing the homology search from the diffusion-based mechanism to a motor-guided mechanism (PubMed:11782437, PubMed:11884632, PubMed:16428451). Once DNA strand exchange occured, could dissociate RAD51 from nucleoprotein filaments formed on dsDNA (By similarity). May also function as a molecular adapter, promoting MDM2-MDM4 heterodimerization to facilitate the ubiquitin-dependent degradation of p53, thereby modulating the cellular decision between cell cycle arrest and progression in response to DNA damage (PubMed:25384516)

Protein Sequence

10 MRRSAAPSQL 20 QGNSFKKPKF 30 IPPGRSNPGL 40 NEEITKLNPD 50 IKLFEGVAIN 60 NTFLPSQNDL 70 RICSLNLPSE 80 ESTREINNRD 90 NCSGKYCFEA 100 PTLATLDPPH 110 TVHSAPKEVA 120 VSKEQEEKSD 130 SLVKYFSVVW 140 CKPSKKKHKK 150 WEGDAVLIVK 160 GKSFILKNLE 170 GKDIGRGIGY 180 KFKELEKIEE 190 GQTLMICGKE 200 IEVMGVISPD 210 DFSSGRCFQL 220 GGGSTAISHS 230 SQVARKCFSN 240 PFKSVCKPSS 250 KENRQNDFQN 260 CKPRHDPYTP 270 NSLVMPRPDK 280 NHQWVFNKNC 290 FPLVDVVIDP 300 YLVYHLRPHQ 310 KEGIIFLYEC 320 VMGMRMNGRC 330 GAILADEMGL 340 GKTLQCISLI 350 WTLQCQGPYG 360 GKPVIKKTLI 370 VTPGSLVNNW 380 KKEFQKWLGS 390 ERIKIFTVDQ 400 DHKVEEFIKS 410 IFYSVLIISY 420 EMLLRSLDQI 430 KNIKFDLLIC 440 DEGHRLKNSA 450 IKTTTALISL 460 SCEKRIILTG 470 TPIQNDLQEF 480 FALIDFVNPG 490 ILGSLSSYRK 500 IYEEPIILSR 510 EPSASEEEKE 520 LGERRAAELT 530 CLTGLFILRR 540 TQEIINKYLP 550 PKIENVVFCR 560 PGALQIELYR 570 KLLNSQVVRF 580 CLQGLLENSP 590 HLICIGALKK 600 LCNHPCLLFN 610 SIKEKECSST 620 CDKNEEKSLY 630 KGLLSVFPAD 640 YNPLLFTEKE 650 SGKLQVLSKL 660 LAVIHELRPT 670 EKVVLVSNYT 680 QTLNILQEVC 690 KRHGYAYTRL 700 DGQTPISQRQ 710 QIVDGFNSQH 720 SSFFIFLLSS 730 KAGGVGLNLI 740 GGSHLILYDI 750 DWNPATDIQA 760 MSRVWRDGQK 770 YPVHIYRLLT 780 TGTIEEKIYQ 790 RQISKQGLCG 800 AVVDLTKTSE 810 HIQFSVEELK 820 NLFTLHESSD 830 CVTHDLLDCE 840 CTGEEVHTGD 850 SLEKFIVSRD 860 CQLGPHHQKS 870 NSLKPLSMSQ 880 LKQWKHFSGD 890 HLNLTDPFLE 900 RITENVSFIF 910 QNITTQATGT

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0035861 site of double-strand break
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0008094 ATP-dependent activity, acting on DNA
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0015616 DNA translocase activity
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Biological Process GO:0000724 double-strand break repair via homologous recombination
Biological Process GO:0035825 homologous recombination
Biological Process GO:1901797 negative regulation of signal transduction by p53 class mediator
Biological Process GO:0007131 reciprocal meiotic recombination

Reference

[1] 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.