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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • damaged DNA binding Source: Ensembl
  • histone binding Source: GO_Central
  • methylated histone binding Source: UniProtKB
  • p53 binding Source: AgBase
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • telomeric DNA binding Source: Ensembl
  • transcription coregulator activity Source: BHF-UCL
  • ubiquitin modification-dependent histone binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-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

SIGNOR Signaling Network Open Resource

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SIGNORi
Q12888

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
TP53-binding protein 1Curated
Short name:
53BP11 Publication
Short name:
p53-binding protein 11 Publication
Short name:
p53BP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TP53BP1Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000067369.13

Human Gene Nomenclature Database

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HGNCi
HGNC:11999 TP53BP1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
605230 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q12888

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...
DisGeNETi
7158

Open Targets

More...
OpenTargetsi
ENSG00000067369

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA36680

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2424509

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
TP53BP1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
8928568

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000726431 – 1972TP53-binding protein 1Add BLAST1972

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei25Phosphoserine1 Publication1
Modified residuei63PhosphoserineCombined sources1
Modified residuei105PhosphoserineCombined sources1
Modified residuei124PhosphoserineCombined sources1
Modified residuei166Phosphoserine1 Publication1
Modified residuei176Phosphoserine1 Publication1
Modified residuei178Phosphoserine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined 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); alternateCombined sources
Cross-linki868Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined 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); alternateCombined sources
Cross-linki1434Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei1460PhosphoserineCombined sources1
Modified residuei1462PhosphoserineCombined sources1
Modified residuei1474PhosphoserineCombined sources1
Cross-linki1563Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki1563Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined 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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
Q12888

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q12888

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q12888

PeptideAtlas

More...
PeptideAtlasi
Q12888

PRoteomics IDEntifications database

More...
PRIDEi
Q12888

ProteomicsDB human proteome resource

More...
ProteomicsDBi
59003
59004 [Q12888-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q12888

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q12888

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
Q12888

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000067369 Expressed in 222 organ(s), highest expression level in lung

CleanEx database of gene expression profiles

More...
CleanExi
HS_TP53BP1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q12888 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q12888 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB004083
HPA008788
HPA022133

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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). Interacts with SHLD2 (PubMed:29789392).By similarity15 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
113011, 147 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q12888

Database of interacting proteins

More...
DIPi
DIP-5978N

Protein interaction database and analysis system

More...
IntActi
Q12888, 320 interactors

Molecular INTeraction database

More...
MINTi
Q12888

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000371475

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q12888

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11972
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q12888

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q12888

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q12888

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1724 – 1848BRCT 1PROSITE-ProRule annotationAdd BLAST125
Domaini1864 – 1964BRCT 2PROSITE-ProRule annotationAdd BLAST101

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1484 – 1603Tudor-like1 PublicationAdd BLAST120
Regioni1495 – 1523Interaction with dimethylated histone H41 PublicationAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1396 – 1403GAR1 Publication8
Motifi1604 – 1631UDR1 PublicationAdd BLAST28

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1642 – 1646Poly-Ser5
Compositional biasi1760 – 1764Poly-Glu5

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The Tudor-like region mediates binding to histone H4 dimethylated at 'Lys-20' (H4K20me2) (PubMed:17190600). Interaction with NUDT16L1/TIRR masks the Tudor-like domain and prevents recruitment to chromatin (PubMed:28241136).2 Publications
The UDR (ubiquitin-dependent recruitment) motif specifically recognizes and binds histone H2A monoubiquitinated at 'Lys-15' (H2AK15ub) (PubMed: