Search Results

Overview

Uniprot IDQ12888
Protein NameTP53-binding protein 1
Gene NameTP53BP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1141 TNKENPSKALIERPS
1332 HSSGSSGKGAGPLRG
1340 GAGPLRGKTSGTEPA
1360 SSRGGPGKLSPRKGV
1626 LDNLVEGKRKRRSNV
1628 NLVEGKRKRRSNVSS
1652 SSTTPTRKITESPRA
1667 SMGVLSGKRKLITSE
1669 GVLSGKRKLITSEEE
1685 SPAKRGRKSATVKPG
868 NSLTEDSKMANAKQL

Function

Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:17190600, PubMed:21144835, PubMed:22553214, PubMed:23333306, PubMed:27153538, PubMed:28241136, PubMed:31135337, PubMed:37696958). Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ)-mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23333306, PubMed:23727112, PubMed:27153538, PubMed:31135337). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136). Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:17190600, PubMed:23760478, PubMed:27153538, PubMed:28241136). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates in the repair and the orientation of the broken DNA ends during CSR (By similarity). In contrast, it is not required for classic NHEJ and V(D)J recombination (By similarity). Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112)

Protein Sequence

10 MDPTGSQLDS 20 DFSQQDTPCL 30 IIEDSQPESQ 40 VLEDDSGSHF 50 SMLSRHLPNL 60 QTHKENPVLD 70 VVSNPEQTAG 80 EERGDGNSGF 90 NEHLKENKVA 100 DPVDSSNLDT 110 CGSISQVIEQ 120 LPQPNRTSSV 130 LGMSVESAPA 140 VEEEKGEELE 150 QKEKEKEEDT 160 SGNTTHSLGA 170 EDTASSQLGF 180 GVLELSQSQD 190 VEENTVPYEV 200 DKEQLQSVTT 210 NSGYTRLSDV 220 DANTAIKHEE 230 QSNEDIPIAE 240 QSSKDIPVTA 250 QPSKDVHVVK 260 EQNPPPARSE 270 DMPFSPKASV 280 AAMEAKEQLS 290 AQELMESGLQ 300 IQKSPEPEVL 310 STQEDLFDQS 320 NKTVSSDGCS 330 TPSREEGGCS 340 LASTPATTLH 350 LLQLSGQRSL 360 VQDSLSTNSS 370 DLVAPSPDAF 380 RSTPFIVPSS 390 PTEQEGRQDK 400 PMDTSVLSEE 410 GGEPFQKKLQ 420 SGEPVELENP 430 PLLPESTVSP 440 QASTPISQST 450 PVFPPGSLPI 460 PSQPQFSHDI 470 FIPSPSLEEQ 480 SNDGKKDGDM 490 HSSSLTVECS 500 KTSEIEPKNS 510 PEDLGLSLTG 520 DSCKLMLSTS 530 EYSQSPKMES 540 LSSHRIDEDG 550 ENTQIEDTEP 560 MSPVLNSKFV 570 PAENDSILMN 580 PAQDGEVQLS 590 QNDDKTKGDD 600 TDTRDDISIL 610 ATGCKGREET 620 VAEDVCIDLT 630 CDSGSQAVPS 640 PATRSEALSS 650 VLDQEEAMEI 660 KEHHPEEGSS 670 GSEVEEIPET 680 PCESQGEELK 690 EENMESVPLH 700 LSLTETQSQG 710 LCLQKEMPKK 720 ECSEAMEVET 730 SVISIDSPQK 740 LAILDQELEH 750 KEQEAWEEAT 760 SEDSSVVIVD 770 VKEPSPRVDV 780 SCEPLEGVEK 790 CSDSQSWEDI 800 APEIEPCAEN 810 RLDTKEEKSV 820 EYEGDLKSGT 830 AETEPVEQDS 840 SQPSLPLVRA 850 DDPLRLDQEL 860 QQPQTQEKTS 870 NSLTEDSKMA 880 NAKQLSSDAE 890 AQKLGKPSAH 900 ASQSFCESSS 910 ETPFHFTLPK 920 EGDIIPPLTG 930 ATPPLIGHLK 940 LEPKRHSTPI 950 GISNYPESTI 960 ATSDVMSESM 970 VETHDPILGS 980 GKGDSGAAPD 990 VDDKLCLRMK 1000 LVSPETEASE 1010 ESLQFNLEKP 1020 ATGERKNGST 1030 AVAESVASPQ 1040 KTMSVLSCIC 1050 EARQENEARS 1060 EDPPTTPIRG 1070 NLLHFPSSQG 1080 EEEKEKLEGD 1090 HTIRQSQQPM 1100 KPISPVKDPV 1110 SPASQKMVIQ 1120 GPSSPQGEAM 1130 VTDVLEDQKE 1140 GRSTNKENPS 1150 KALIERPSQN 1160 NIGIQTMECS 1170 LRVPETVSAA 1180 TQTIKNVCEQ 1190 GTSTVDQNFG 1200 KQDATVQTER 1210 GSGEKPVSAP 1220 GDDTESLHSQ 1230 GEEEFDMPQP 1240 PHGHVLHRHM 1250 RTIREVRTLV 1260 TRVITDVYYV 1270 DGTEVERKVT 1280 EETEEPIVEC 1290 QECETEVSPS 1300 QTGGSSGDLG 1310 DISSFSSKAS 1320 SLHRTSSGTS 1330 LSAMHSSGSS 1340 GKGAGPLRGK 1350 TSGTEPADFA 1360 LPSSRGGPGK 1370 LSPRKGVSQT 1380 GTPVCEEDGD 1390 AGLGIRQGGK 1400 APVTPRGRGR 1410 RGRPPSRTTG 1420 TRETAVPGPL 1430 GIEDISPNLS 1440 PDDKSFSRVV 1450 PRVPDSTRRT 1460 DVGAGALRRS 1470 DSPEIPFQAA 1480 AGPSDGLDAS 1490 SPGNSFVGLR 1500 VVAKWSSNGY 1510 FYSGKITRDV 1520 GAGKYKLLFD 1530 DGYECDVLGK 1540 DILLCDPIPL 1550 DTEVTALSED 1560 EYFSAGVVKG 1570 HRKESGELYY 1580 SIEKEGQRKW 1590 YKRMAVILSL 1600 EQGNRLREQY 1610 GLGPYEAVTP 1620 LTKAADISLD 1630 NLVEGKRKRR 1640 SNVSSPATPT 1650 ASSSSSTTPT 1660 RKITESPRAS 1670 MGVLSGKRKL 1680 ITSEEERSPA 1690 KRGRKSATVK 1700 PGAVGAGEFV 1710 SPCESGDNTG 1720 EPSALEEQRG 1730 PLPLNKTLFL 1740 GYAFLLTMAT 1750 TSDKLASRSK 1760 LPDGPTGSSE 1770 EEEEFLEIPP 1780 FNKQYTESQL 1790 RAGAGYILED 1800 FNEAQCNTAY 1810 QCLLIADQHC 1820 RTRKYFLCLA 1830 SGIPCVSHVW 1840 VHDSCHANQL 1850 QNYRNYLLPA 1860 GYSLEEQRIL 1870 DWQPRENPFQ 1880 NLKVLLVSDQ 1890 QQNFLELWSE 1900 ILMTGGAASV 1910 KQHHSSAHNK 1920 DIALGVFDVV 1930 VTDPSCPASV 1940 LKCAEALQLP 1950 VVSQEWVIQC 1960 LIVGERIGFK 1970 QHPKYKHDYV SH

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0000776 kinetochore
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0035861 site of double-strand break
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0042393 histone binding
Molecular Function GO:0140941 histone H4K20me methyltransferase activity
Molecular Function GO:0140005 histone H4K20me2 reader activity
Molecular Function GO:0140566 histone reader activity
Molecular Function GO:0002039 p53 binding
Molecular Function GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding
Molecular Function GO:0003713 transcription coactivator activity
Molecular Function GO:0003712 transcription coregulator activity
Molecular Function GO:0061649 ubiquitin-modified histone reader activity
Biological Process GO:0000077 DNA damage checkpoint signaling
Biological Process GO:0006974 DNA damage response
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0097680 double-strand break repair via classical nonhomologous end joining
Biological Process GO:0006303 double-strand break repair via nonhomologous end joining
Biological Process GO:2000042 negative regulation of double-strand break repair via homologous recombination
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:1902255 positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator
Biological Process GO:0045830 positive regulation of isotype switching
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0051260 protein homooligomerization
Biological Process GO:1990166 protein localization to site of double-strand break

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] 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.

[3] 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.

[4] 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.

[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[6] 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.