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Protein

TP53-binding protein 1

Gene

TP53BP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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:22553214, PubMed:23333306, PubMed:17190600, PubMed:21144835, PubMed:28241136). 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:23727112, PubMed:23333306). 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:23760478, PubMed:28241136, PubMed:17190600). Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425). Participates to 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).By similarity9 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • methylated histone binding Source: UniProtKB
  • p53 binding Source: AgBase
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • RNA polymerase II transcription cofactor activity Source: BHF-UCL
  • ubiquitin modification-dependent histone binding Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to X-ray Source: Ensembl
  • DNA damage checkpoint Source: GO_Central
  • double-strand break repair via nonhomologous end joining Source: UniProtKB
  • negative regulation of double-strand break repair via homologous recombination Source: UniProtKB
  • positive regulation of isotype switching Source: UniProtKB
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • protein homooligomerization Source: UniProtKB
  • protein sumoylation Source: Reactome
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Molecular functionActivator, DNA-binding
Biological processDNA damage, DNA repair, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-3232118. SUMOylation of transcription factors.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-69473. G2/M DNA damage checkpoint.
SIGNORiQ12888.

Names & Taxonomyi

Protein namesi
Recommended name:
TP53-binding protein 1Curated
Short name:
53BP11 Publication
Short name:
p53-binding protein 11 Publication
Short name:
p53BP1
Gene namesi
Name:TP53BP1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:11999. TP53BP1.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: ProtInc
  • nuclear body Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • site of double-strand break Source: UniProtKB

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving TP53BP1 is found in a form of myeloproliferative disorder chronic with eosinophilia. Translocation t(5;15)(q33;q22) with PDGFRB creating a TP53BP1-PDGFRB fusion protein.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi6S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-13; A-25; A-29; A-105; A-166; A-176 and A-178. 3 Publications1
Mutagenesisi13S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-25; A-29; A-105; A-166; A-176 and A-178. 3 Publications1
Mutagenesisi25S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-29; A-105; A-166; A-176 and A-178. 3 Publications1
Mutagenesisi29S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-105; A-166; A-176 and A-178. 3 Publications1
Mutagenesisi105S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-166; A-176 and A-178. 3 Publications1
Mutagenesisi166S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-105; A-176 and A-178. 3 Publications1
Mutagenesisi176 – 178SQS → AQA: Loss of phosphorylation site. 1 Publication3
Mutagenesisi176S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-105; A-166 and A-178. 3 Publications1
Mutagenesisi178S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. In 8A: Does not affect interaction with RIF1 and ability to promote immunoglobulin class-switch recombination (CSR), but abolishes interaction with PAXIP1 and ability to promote NHEJ of dysfunctional telomeres; when associated with A-6; A-13; A-25; A-29; A-105; A-166 and A-176. 3 Publications1
Mutagenesisi302T → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi437S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi452S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi523S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi543T → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi580S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi625S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi674S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi696T → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi698S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi784S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi831S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-855; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi855T → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-892; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi892S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-1068; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi1068S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1086; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi1086S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1104; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi1104S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1148; A-1171 and A-1219. 2 Publications1
Mutagenesisi1148S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1171 and A-1219. 2 Publications1
Mutagenesisi1171T → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148 and A-1219. 2 Publications1
Mutagenesisi1219S → A in 28A: Defects in recruitment to double strand breaks (DSBs), abolished interaction with RIF1 and abolished ability to repair DSBs; when associated with A-6; A-13; A-25; A-29; A-105; A-166; A-176; A-178; A-302; A-437; A-452; A-523; A-543; A-580; A-625; A-674; A-696; A-698; A-784; A-831; A-855; A-892; A-1068; A-1086; A-1104; A-1148 and A-1171. 2 Publications1
Mutagenesisi1396R → A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1398; A-1400; A-1401 and A-1403. 2 Publications1
Mutagenesisi1396R → K: No detectable effect on methylation by PRMT1 (in vitro). 2 Publications1
Mutagenesisi1398 – 1401RGRR → AGAA: No effect on in class-switch recombination (CSR). 1 Publication4
Mutagenesisi1398R → A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1400; A-1401 and A-1403. 2 Publications1
Mutagenesisi1398R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1400. Strongly reduced methylation; when associated with K-1401. 2 Publications1
Mutagenesisi1400R → A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1401 and A-1403. 2 Publications1
Mutagenesisi1400R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1401. 2 Publications1
Mutagenesisi1401R → A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1400 and A-1403. 2 Publications1
Mutagenesisi1401R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1400. 2 Publications1
Mutagenesisi1403R → A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1400 and A-1401. 2 Publications1
Mutagenesisi1403R → K: No detectable effect on methylation by PRMT1 (in vitro). 2 Publications1
Mutagenesisi1495W → A or H: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks. Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks; when associated with A-1521. 3 Publications1
Mutagenesisi1495W → F: No effect on recruitment to double strand breaks. 2 Publications1
Mutagenesisi1495W → V: Reduces recruitment to double strand breaks. 2 Publications1
Mutagenesisi1500Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. 1 Publication1
Mutagenesisi1502Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. 2 Publications1
Mutagenesisi1502Y → L or Q: Abolishes recruitment to double strand breaks. 2 Publications1
Mutagenesisi1521D → A: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks. Loss of interaction with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Abolishes recruitment to double strand breaks; when associated with A-1495. 3 Publications1
Mutagenesisi1521D → R: Abolishes recruitment to double strand breaks and induces defects in class-switch recombination (CSR). 4 Publications1
Mutagenesisi1523Y → A: Increases affinity for histone H4 that has been dimethylated at 'Lys-20'. No effect on recruitment to double strand breaks. 1 Publication1
Mutagenesisi1523Y → S: Decreases affinity for histone H4 that has been dimethylated at 'Lys-20'. 1 Publication1
Mutagenesisi1609T → A: Constitutive recruitment to mitotic DNA lesions, leading to mitotic defects; when associated with A-1618. 1 Publication1
Mutagenesisi1609T → E: Phosphomimetic mutant that abolishes recruitment to double strand breaks; when associated with D-1618. 1 Publication1
Mutagenesisi1613K → A: Does not affect recruitment to double strand breaks. 1 Publication1
Mutagenesisi1616D → A: Does not affect recruitment to double strand breaks. 1 Publication1
Mutagenesisi1617I → A: Strongly reduced recruitment to double strand breaks. Defects in class-switch recombination (CSR). 1 Publication1
Mutagenesisi1618S → A: Constitutive recruitment to mitotic DNA lesions, leading to mitotic defects; when associated with A-1609. 1 Publication1
Mutagenesisi1618S → D: Phosphomimetic mutant that abolishes recruitment to double strand breaks; when associated with E-1609. 1 Publication1
Mutagenesisi1619L → A: Strongly reduced recruitment to double strand breaks. Defects in class-switch recombination (CSR). Does not affect interaction with histone H4 dimethylated at 'Lys-20' (H4K20me2). Impaired interaction with histone H2A monoubiquitinated at 'Lys-15' (H2AK15ub). 1 Publication1
Mutagenesisi1621N → A: Reduced recruitment to double strand breaks. 1 Publication1
Mutagenesisi1622L → A: Reduced recruitment to double strand breaks. 1 Publication1
Mutagenesisi1624E → A: Does not affect recruitment to double strand breaks. 1 Publication1
Mutagenesisi1627R → A: Reduced recruitment to double strand breaks. 1 Publication1

Organism-specific databases

DisGeNETi7158.
OpenTargetsiENSG00000067369.
PharmGKBiPA36680.

Chemistry databases

ChEMBLiCHEMBL2424509.

Polymorphism and mutation databases

BioMutaiTP53BP1.
DMDMi8928568.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000726431 – 1972TP53-binding protein 1Add BLAST1972

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25Phosphoserine1 Publication1
Modified residuei63PhosphoserineCombined sources1
Modified residuei105PhosphoserineCombined sources1
Modified residuei124PhosphoserineCombined sources1
Modified residuei166Phosphoserine1 Publication1
Modified residuei176Phosphoserine1 Publication1
Modified residuei178Phosphoserine1 Publication1
Cross-linki217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei222PhosphoserineCombined sources1
Modified residuei265PhosphoserineCombined sources1
Modified residuei294PhosphoserineCombined sources1 Publication1
Modified residuei302PhosphothreonineCombined sources1 Publication1
Modified residuei366PhosphoserineCombined sources1
Modified residuei380PhosphoserineCombined sources1 Publication1
Modified residuei395PhosphoserineCombined sources1
Modified residuei398PhosphoserineCombined sources1
Modified residuei429PhosphoserineBy similarity1
Modified residuei452Phosphoserine1 Publication1
Modified residuei464PhosphoserineBy similarity1
Modified residuei500PhosphoserineCombined sources1
Modified residuei507PhosphoserineCombined sources1
Modified residuei518PhosphoserineCombined sources1
Modified residuei523PhosphoserineCombined sources1 Publication1
Modified residuei525PhosphoserineCombined sources1
Modified residuei543PhosphothreonineCombined sources1
Modified residuei548PhosphothreonineCombined sources1
Modified residuei552PhosphoserineCombined sources1 Publication1
Modified residuei566PhosphoserineCombined sources1
Modified residuei580PhosphoserineCombined sources1
Modified residuei630PhosphoserineCombined sources1
Modified residuei635PhosphoserineCombined sources1
Modified residuei639PhosphoserineCombined sources1
Modified residuei640PhosphoserineCombined sources1
Modified residuei692PhosphoserineCombined sources1
Modified residuei724PhosphoserineBy similarity1
Modified residuei727PhosphoserineCombined sources1
Modified residuei771PhosphoserineCombined sources1
Modified residuei809PhosphoserineCombined sources1
Modified residuei830PhosphoserineBy similarity1
Modified residuei831PhosphoserineCombined sources1 Publication1
Modified residuei834PhosphoserineCombined sources1
Modified residuei855PhosphothreonineCombined sources1
Cross-linki868Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki868Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei922PhosphothreonineCombined sources1
Cross-linki930Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei970PhosphoserineCombined sources1
Modified residuei975PhosphoserineCombined sources1
Cross-linki984Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1028PhosphoserineCombined sources1 Publication1
Modified residuei1056PhosphothreonineCombined sources1
Modified residuei1068PhosphoserineCombined sources1
Modified residuei1086Phosphoserine1 Publication1
Modified residuei1094PhosphoserineCombined sources1
Modified residuei1101PhosphoserineCombined sources1
Modified residuei1114PhosphoserineCombined sources1 Publication1
Modified residuei1148PhosphoserineCombined sources1
Modified residuei1214PhosphothreonineCombined sources1
Modified residuei1216PhosphoserineCombined sources1
Modified residuei1219PhosphoserineCombined sources1 Publication1
Modified residuei1317PhosphoserineCombined sources1
Modified residuei1342PhosphoserineCombined sources1
Modified residuei1355Omega-N-methylarginineBy similarity1
Modified residuei1362PhosphoserineCombined sources1
Cross-linki1365Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1368PhosphoserineCombined sources1
Modified residuei1372PhosphothreonineCombined sources1
Modified residuei1426PhosphoserineCombined sources1
Modified residuei1430PhosphoserineCombined sources1
Cross-linki1434Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1434Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1460PhosphoserineCombined sources1
Modified residuei1462PhosphoserineCombined sources1
Modified residuei1474PhosphoserineCombined sources1
Cross-linki1563Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1563Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1609PhosphothreonineCombined sources1 Publication1
Modified residuei1618PhosphoserineCombined sources1 Publication1
Modified residuei1631PhosphoserineBy similarity1
Modified residuei1635PhosphoserineCombined sources1
Modified residuei1638PhosphothreonineCombined sources1
Modified residuei1648PhosphothreonineCombined sources1
Modified residuei1656PhosphoserineCombined sources1
Modified residuei1673PhosphoserineCombined sources1
Modified residuei1678PhosphoserineCombined sources1
Modified residuei1701PhosphoserineCombined sources1
Modified residuei1759PhosphoserineCombined sources1
Modified residuei1778Phosphoserine2 Publications1

Post-translational modificationi

Asymmetrically dimethylated on Arg residues by PRMT1. Methylation is required for DNA binding.2 Publications
Phosphorylated at basal level in the absence of DNA damage (PubMed:11042216, PubMed:11331310). Phosphorylated by ATM in response to DNA damage: phosphorylation at different sites promotes interaction with different set of proteins: phosphorylation at the N-terminus by ATM (residues from 6-178) promotes interaction with PAXIP1 and non-homologous end joining (NHEJ) of dysfunctional telomeres (PubMed:23727112). Phosphorylation by ATM at residues that are located more C-terminus (residues 300-650) leads to promote interaction with RIF1 (PubMed:23727112, PubMed:23333306, PubMed:28241136). Interaction with RIF1 leads to disrupt interaction with NUDT16L1/TIRR (PubMed:28241136). Phosphorylation at Thr-1609 and Ser-1618 in the UDR motif blocks interaction with H2AK15ub (PubMed:24703952). Dephosphorylated by PPP4C (PubMed:24703952). Hyperphosphorylation during mitosis correlates with its exclusion from chromatin and DNA lesions. Hyperphosphorylated in an ATR-dependent manner in response to DNA damage induced by UV irradiation (PubMed:17553757, PubMed:21144835). Dephosphorylated by PPP5C (PubMed:19176521).9 Publications

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ12888.
MaxQBiQ12888.
PaxDbiQ12888.
PeptideAtlasiQ12888.
PRIDEiQ12888.

PTM databases

iPTMnetiQ12888.
PhosphoSitePlusiQ12888.

Miscellaneous databases

PMAP-CutDBiQ12888.

Expressioni

Gene expression databases

BgeeiENSG00000067369.
CleanExiHS_TP53BP1.
ExpressionAtlasiQ12888. baseline and differential.
GenevisibleiQ12888. HS.

Organism-specific databases

HPAiCAB004083.
HPA008788.
HPA022133.

Interactioni

Subunit structurei

Homoligomer (PubMed:16294047, PubMed:23760478, PubMed:23345425). Interacts with p53/TP53 (via the central domain) (PubMed:12110597, PubMed:11877378). Interacts with DCLRE1C (PubMed:15574327). Interacts with histone H2AFX and this requires phosphorylation of H2AFX on 'Ser-139' (PubMed:12607005). Interacts with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2) (PubMed:17190600). Has low affinity for histone H4 containing monomethylated 'Lys-20' (H4K20me1) (PubMed:17190600). Does not bind histone H4 containing unmethylated or trimethylated 'Lys-20' (H4K20me3) (PubMed:17190600). Has low affinity for histone H3 that has been dimethylated on 'Lys-79' (PubMed:15525939). Has very low affinity for histone H3 that has been monomethylated on 'Lys-79' (in vitro) (PubMed:15525939). Does not bind unmethylated histone H3 (PubMed:15525939). Interacts with histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) (PubMed:23760478). Interacts with MUM1/EXPAND1 (PubMed:20347427). Interacts with CHEK2; modulates CHEK2 phosphorylation at 'Thr-68' in response to infrared (PubMed:12364621). Interacts with MSL1; this interaction may be required for MSL1 DNA repair activity, but not for histone acetyltransferase activity (PubMed:19650074). Interacts (when phosphorylated by ATM) with RIF1 (PubMed:23727112, PubMed:23333306, PubMed:28241136). Interacts (via the Tudor-like domain) with NUDT16L1/TIRR; interaction masks the Tudor-like domain and prevents recruitment to chromatin (PubMed:28241136). Interacts with PAXIP1 (PubMed:23727112). Interacts with IFI202A (By similarity).By similarity14 Publications

Binary interactionsi

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GO - Molecular functioni

  • methylated histone binding Source: UniProtKB
  • p53 binding Source: AgBase
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • ubiquitin modification-dependent histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113011. 141 interactors.
DIPiDIP-5978N.
IntActiQ12888. 45 interactors.
MINTiMINT-276057.
STRINGi9606.ENSP00000371475.

Chemistry databases

BindingDBiQ12888.

Structurei

Secondary structure

11972
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1490 – 1494Combined sources5
Turni1496 – 1498Combined sources3
Beta strandi1501 – 1511Combined sources11
Beta strandi1514 – 1519Combined sources6
Beta strandi1524 – 1528Combined sources5
Helixi1529 – 1531Combined sources3
Beta strandi1532 – 1535Combined sources4
Beta strandi1543 – 1547Combined sources5
Beta strandi1548 – 1551Combined sources4
Beta strandi1553 – 1564Combined sources12
Beta strandi1567 – 1574Combined sources8