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UniProtKB - P70399 (TP53B_MOUSE)

Entry version 169 (16 Oct 2019)
Sequence version 3 (10 May 2017)
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Protein

TP53-binding protein 1

Gene

Tp53bp1

Organism
Mus musculus (Mouse)
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:15159415, PubMed:15077110, PubMed:20453858, PubMed:23333305, PubMed:26308889, PubMed:20362325). 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:23333305, PubMed:20362325). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites. 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. Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:15159415, PubMed:15077110). Participates to the repair and the orientation of the broken DNA ends during CSR (PubMed:26308889). In contrast, it is not required for classic NHEJ and V(D)J recombination (PubMed:15159415). Promotes NHEJ of dysfunctional telomeres (By similarity).By similarity6 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

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

<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:Tp53bp1By similarity
Synonyms:Trp53bp1Imported
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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 2

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:1351320 Trp53bp1

<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 & Seán O’Donoghue; 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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice display growth retardation and are immune deficient, radiation-sensitive and cancer-prone (PubMed:12640136). Cells show a slight S-phase checkpoint defect and prolonged G2/M arrest after treatment with ionizing radiation (PubMed:12640136). Cells show defects in the DNA damage response (PubMed:12640136). Mice display defects in immunoglobulin class-switch recombination (CSR) during antibody genesis (PubMed:15159415, PubMed:15077110). In contrast, no defects are observed in classic NHEJ and V(D)J recombination (PubMed:15159415).3 Publications

<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_00000726441 – 1969TP53-binding protein 1Add BLAST1969

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 residuei30PhosphoserineBy similarity1
Modified residuei68PhosphoserineBy similarity1
Modified residuei73PhosphoserineCombined sources1
Modified residuei109PhosphoserineBy similarity1
Modified residuei169PhosphoserineBy similarity1
Modified residuei179PhosphoserineBy similarity1
Modified residuei181PhosphoserineBy similarity1
<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-linki220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei267PhosphoserineCombined sources1
Modified residuei268PhosphoserineCombined sources1
Modified residuei297PhosphoserineBy similarity1
Modified residuei305PhosphothreonineBy similarity1
Modified residuei368PhosphoserineBy similarity1
Modified residuei382PhosphoserineCombined sources1
Modified residuei397PhosphoserineBy similarity1
Modified residuei429PhosphoserineCombined sources1
Modified residuei452PhosphoserineBy similarity1
Modified residuei464PhosphoserineCombined sources1
Modified residuei507PhosphoserineBy similarity1
Modified residuei518PhosphoserineBy similarity1
Modified residuei523PhosphoserineBy similarity1
Modified residuei525PhosphoserineBy similarity1
Modified residuei543PhosphothreonineBy similarity1
Modified residuei548PhosphothreonineBy similarity1
Modified residuei552PhosphoserineCombined sources1
Modified residuei579PhosphoserineBy similarity1
Modified residuei622PhosphoserineBy similarity1
Modified residuei627PhosphoserineCombined sources1
Modified residuei631PhosphoserineCombined sources1
Modified residuei632PhosphoserineCombined sources1
Modified residuei684PhosphoserineBy similarity1
Modified residuei716PhosphoserineCombined sources1
Modified residuei719PhosphoserineCombined sources1
Modified residuei763PhosphoserineBy similarity1
Modified residuei822PhosphoserineCombined sources1
Modified residuei912PhosphothreonineBy similarity1
Cross-linki920Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei965PhosphoserineBy similarity1
Cross-linki974Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1018PhosphoserineBy similarity1
Modified residuei1075PhosphoserineBy similarity1
Modified residuei1096PhosphoserineCombined sources1
Modified residuei1115PhosphoserineCombined sources1
Modified residuei1211PhosphothreonineBy similarity1
Modified residuei1213PhosphoserineBy similarity1
Modified residuei1216PhosphoserineBy similarity1
Modified residuei1314PhosphoserineBy similarity1
Modified residuei1329Omega-N-methylarginineCombined sources1
Modified residuei1339PhosphoserineBy similarity1
Modified residuei1352Omega-N-methylarginineCombined sources1
Modified residuei1359PhosphoserineBy similarity1
Cross-linki1362Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1365PhosphoserineBy similarity1
Modified residuei1423PhosphoserineCombined sources1
Modified residuei1427PhosphoserineCombined sources1
Cross-linki1431Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki1431Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei1457PhosphoserineBy similarity1
Modified residuei1459PhosphoserineCombined sources1
Modified residuei1470PhosphoserineCombined sources1
Modified residuei1471PhosphoserineBy similarity1
Cross-linki1560Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki1560Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei1606PhosphothreonineBy similarity1
Modified residuei1615PhosphoserineBy similarity1
Modified residuei1628PhosphoserineCombined sources1
Modified residuei1632PhosphoserineBy similarity1
Modified residuei1635PhosphothreonineBy similarity1
Modified residuei1645PhosphothreonineBy similarity1
Modified residuei1653PhosphoserineBy similarity1
Modified residuei1670PhosphoserineBy similarity1
Modified residuei1675PhosphoserineBy similarity1
Modified residuei1698PhosphoserineBy similarity1
Modified residuei1756PhosphoserineBy similarity1

<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

Phosphorylated at basal level in the absence of DNA damage (By similarity). 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 11-181) promotes interaction with PAXIP1 and non-homologous end joining (NHEJ) of dysfunctional telomeres (By similarity). Phosphorylation by ATM at residues that are located more C-terminus (residues 300-650) leads to promote interaction with RIF1 (PubMed:23333305, PubMed:23306439). Interaction with RIF1 leads to disrupt interaction with NUDT16L1/TIRR (By similarity). Phosphorylation at Thr-1606 and Ser-1615 in the UDR motif blocks interaction with H2AK15ub (By similarity). Dephosphorylated by PPP4C (By similarity). Hyperphosphorylation during mitosis correlates with its exclusion from chromatin and DNA lesions (By similarity). Hyperphosphorylated in an ATR-dependent manner in response to DNA damage induced by UV irradiation (By similarity). Dephosphorylated by PPP5C (By similarity).By similarity2 Publications
Asymmetrically dimethylated on Arg residues by PRMT1. Methylation is required for DNA binding.By similarity

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P70399

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P70399

MaxQB - The MaxQuant DataBase

More...MaxQBi		P70399

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

More...PaxDbi		P70399

PeptideAtlas

More...PeptideAtlasi		P70399

PRoteomics IDEntifications database

More...PRIDEi		P70399

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P70399

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

More...PhosphoSitePlusi		P70399

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P70399

<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		ENSMUSG00000043909 Expressed in 289 organ(s), highest expression level in secondary oocyte

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P70399 baseline and differential

<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 (By similarity).

Interacts with p53/TP53 (via the central domain) (By similarity).

Interacts with DCLRE1C (By similarity).

Interacts with histone H2AFX and this requires phosphorylation of H2AFX on 'Ser-139' (By similarity).

Interacts with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2) (PubMed:23209566). Has low affinity for histone H4 containing monomethylated 'Lys-20' (H4K20me1) (By similarity). Does not bind histone H4 containing unmethylated or trimethylated 'Lys-20' (H4K20me3) (By similarity). Has low affinity for histone H3 that has been dimethylated on 'Lys-79' (By similarity). Has very low affinity for histone H3 that has been monomethylated on 'Lys-79' (in vitro) (By similarity). Does not bind unmethylated histone H3 (By similarity).

Interacts with histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) (By similarity).

Interacts with PWWP3A/EXPAND1 (By similarity).

Interacts with CHEK2; modulates CHEK2 phosphorylation at 'Thr-68' in response to infrared (By similarity).

Interacts with MSL1; this interaction may be required for MSL1 DNA repair activity, but not for histone acetyltransferase activity (By similarity).

Interacts (when phosphorylated by ATM) with RIF1 (PubMed:23333305, PubMed:23306439).

Interacts (via the Tudor-like domain) with NUDT16L1/TIRR; interaction masks the Tudor-like domain and prevents recruitment to chromatin (By similarity).

Interacts with PAXIP1 (By similarity).

Interacts with IFI202A (PubMed:8910340).

Interacts with SHLD2 (By similarity).

By similarity4 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

WithEntry#Exp.IntActNotes
PLK1P533502EBI-15790796,EBI-476768From Homo sapiens.

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		205144, 40 interactors

Database of interacting proteins

More...DIPi		DIP-31595N

Protein interaction database and analysis system

More...IntActi		P70399, 32 interactors

Molecular INTeraction database

More...MINTi		P70399

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000106278

<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

11969
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P70399

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P70399

<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>Domaini1749 – 1845BRCT 1PROSITE-ProRule annotationAdd BLAST97
Domaini1861 – 1961BRCT 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>Regioni1481 – 1600Tudor-likeBy similarityAdd BLAST120
Regioni1492 – 1520Interaction with dimethylated histone H4By similarityAdd 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>Motifi1393 – 1400GARBy similarity8
Motifi1601 – 1628UDRBy similarityAdd 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 biasi136 – 149Poly-GluAdd BLAST14
Compositional biasi637 – 814Glu-richAdd BLAST178
Compositional biasi1285 – 1327Ser-richAdd BLAST43
Compositional biasi1476 – 1479Poly-Ser4
Compositional biasi1640 – 1643Poly-Ser4
Compositional biasi1757 – 1761Poly-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:23209566). Interaction with NUDT16L1/TIRR masks the Tudor-like domain and prevents recruitment to chromatin (By similarity).By similarity1 Publication
The UDR (ubiquitin-dependent recruitment) motif specifically recognizes and binds histone H2A monoubiquitinated at 'Lys-15' (H2AK15ub). Phosphorylation of the UDR blocks interaction with H2AK15ub.By similarity

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3548 Eukaryota
ENOG411075K LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000011891

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000231961

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P70399

KEGG Orthology (KO)

More...KOi		K20915

Identification of Orthologs from Complete Genome Data

More...OMAi		CVSHLWV

Database of Orthologous Groups

More...OrthoDBi		27155at2759

TreeFam database of animal gene trees

More...TreeFami		TF350227

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.30.30.30, 1 hit
3.40.50.10190, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR015125 53-BP1_Tudor
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR014722 Rib_L2_dom2

Pfam protein domain database

More...Pfami		View protein in Pfam
PF09038 53-BP1_Tudor, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00292 BRCT, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52113 SSF52113, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50172 BRCT, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P70399-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MPGEQMDPTG SQLDSDFSQQ DTPCLIIEDS QPESQVLEED AGSHFSVLSR 
        60         70         80         90        100
HLPNLQMHKE NPVLDIVSNP EQSAVEQGDS NSSFNEHLKE KKASDPVESS 
       110        120        130        140        150
HLGTSGSISQ VIERLPQPNR TSSALAVTVE AASLPEEEKE EEELEEEKEG 
       160        170        180        190        200
VGANAPGADS LAAEDSASSQ LGFGVLELSQ SQDVEEHTVP YDVNQEHLQL 
       210        220        230        240        250
VTTNSGSSPL SDVDASTAIK CEEQPTEDIA MIEQPSKDIP VTVQPGKGIH 
       260        270        280        290        300
VVEEQNLPLV RSEDRPSSPQ VSVAAVETKE QVPARELLEE GPQVQPSSEP 
       310        320        330        340        350
EVSSTQEDLF DQSSKTASDG CSTPSREEGG CSPVSTPATT LQLLQLSGQK 
       360        370        380        390        400
PLVQESLSTN SSDLVAPSPD AFRSTPFIVP SSPTEQGGRK DEPMDMSVIP 
       410        420        430        440        450
VGGEPFQKLH DDEAMETEKP LLPSQPAVSP QASTPVSRST PVFTPGSLPI 
       460        470        480        490        500
PSQPEFSHDI FIPSPSLEEP SDDVKKGGGL HSSSLTVECS KTSESEPKNF 
       510        520        530        540        550
TDDLGLSMTG DSCKLMLSTS EYSQSSKMES LGSPRTEEDR ENTQIDDTEP 
       560        570        580        590        600
LSPVSNSKLP ADSENVLVTP SQDDQVEMSQ NVDKAKEDET EDRGDCKGRE 
       610        620        630        640        650
DAVAEDVCID LTCDSGSQAV PSPATRSEAL SSVLDQEEAM DTKEHHPEEG 
       660        670        680        690        700
FSGSEVEEVP ETPCGSHREE PKEEPMESIP LHLSLTETQS EALCLQKEAP 
       710        720        730        740        750
KEECPEAMEV ETSVISIDSP QKLQVLDQEL EHKDPDTWEE ATSEDSSVVI 
       760        770        780        790        800
VDVKEPSPRA DVSCEPLEEV EKCSDSQSWE GVAPEEEPCA ENRLDTPEEK 
       810        820        830        840        850
RIECDGDSKA ETTEKDAVTE DSPQPPLPSV RDEPVRPDQE TQQPQVQEKE 
       860        870        880        890        900
SPVTVDAEVA DDKQLGPEGA CQQLEKAPAC ASQSFCESSS ETPFHFTLPK 
       910        920        930        940        950
EGDIIPPLTG ATPPLIGHLK LEPKRHSTPI GISNYPESTI ATSDVTSESM 
       960        970        980        990       1000
VEINDPLLGN EKGDSESAPE MDGKLSLKMK LVSPETEASE ESLQFSLEKP 
      1010       1020       1030       1040       1050
TTAERKNGST AIAEPVASLQ KPVPVFGCIY EAQQEKEAQS EAPPSAPDRA 
      1060       1070       1080       1090       1100
NLLHFPSAQE EDKERPDVTP KLRQSEQPVK PVGPVMDDAA PEDSASPVSQ 
      1110       1120       1130       1140       1150
QRASQEQRAS QEPFSPAEDV METDLLEGLA ANQDRPSKML MDRPTQSNIG 
      1160       1170       1180       1190       1200
IQTVDHSLCA PETVSAATQT VKSVCEQGTS TAEQNSGKQD ATVQTERGSG 
      1210       1220       1230       1240       1250
EKPASAPVDD TESLHSQGEE EFEMPQPPHG HVLHRHMRTI REVRTLVTRV 
      1260       1270       1280       1290       1300
ITDVYYVDGT EVERKVTEET EEPIVECQEC ETEVSPSQTG GSSGDLGDIS 
      1310       1320       1330       1340       1350
SFSSKASSSH HTSSGTSLSA IHSSGSSGRG AGPLKGKASG TEAADFALPS 
      1360       1370       1380       1390       1400
SRGGPGKLSP RKGISQTGAP VCEEDGDAGL GIRQGGKAPV TPRGRGRRGR 
      1410       1420       1430       1440       1450
PPSRTTGTRE TVVSGPLGVE DISPSMSPDD KSFTRIMPRV PDSTKRTDAS 
      1460       1470       1480       1490       1500
SSTLRRSDSP EIPFQAATGS SDGLDSSSSG NSFVGLRVVA KWSSNGYFYS 
      1510       1520       1530       1540       1550
GKITRDVGAG KYKLLFDDGY ECDVLGKDIL LCDPIPLDTE VTALSEDEYF 
      1560       1570       1580       1590       1600
SAGVVKGHRK ESGELYYSIE KEGQRKWYKR MAVILSLEQG NRLREQYGLG 
      1610       1620       1630       1640       1650
PYEAVTPLTK AADISLDNLV EGKRKRRSNI SSPVTPTAAS SSSTTPTRKA 
      1660       1670       1680       1690       1700
TESPRASTGV PSGKRKLPTS EEERSPAKRG RKSATVKPGT VGAAEFVSPC 
      1710       1720       1730       1740       1750
ETGDNIGEPS VLEEPRGPLP LNKTLFLGYA FLLTMATTSD KLASRSKLLD 
      1760       1770       1780       1790       1800
GPTGSSEEEE EFLEIPPFNK QYTECQLRAG AGYILEDFNE AQCNTAYQCL 
      1810       1820       1830       1840       1850
LIADQHCRTR KYFLCLASGI PCVSHVWVHD SCHANQLQNY RNYLLPAGYS 
      1860       1870       1880       1890       1900
LEEQRILDWQ PRENPFQNLK VLLVSDQQQN FLELWSEILM TGGAASVKQH 
      1910       1920       1930       1940       1950
HSSAHNKDIA LGVFDVVVTD PSCPASVLKC AEALQLPVVS QEWVIQCLIV 
      1960 
GERIGFKQHP KYKHDYVSH
Length:1,969
Mass (Da):212,735
Last modified:May 10, 2017 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF673EA87B3BA1FDE
GO
Isoform 2 (identifier: P70399-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1101-1106: Missing.

Show »
Length:1,963
Mass (Da):212,035
Checksum:i1F0204D04D0E7129
GO
Isoform 3 (identifier: P70399-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-949: Missing.
     1101-1106: Missing.

Show »
Length:1,014
Mass (Da):109,745
Checksum:i52E51794028163EA
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F6ZRL3F6ZRL3_MOUSE
Transformation-related protein 53-b...
Trp53bp1
166Annotation score:

Annotation score:1 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>
A2AU90A2AU90_MOUSE
Transformation-related protein 53-b...
Trp53bp1
1,018Annotation score:

Annotation score:1 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>
F6QNC8F6QNC8_MOUSE
Transformation-related protein 53-b...
Trp53bp1
190Annotation score:

Annotation score:1 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>
F6VCK5F6VCK5_MOUSE
Transformation-related protein 53-b...
Trp53bp1
59Annotation score:

Annotation score:1 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>
F6S5E4F6S5E4_MOUSE
Transformation-related protein 53-b...
Trp53bp1
81Annotation score:

Annotation score:1 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>
F7CE65F7CE65_MOUSE
Transformation-related protein 53-b...
Trp53bp1
48Annotation score:

Annotation score:1 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH79906 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti145Missing in CAC94013 (PubMed:11801725).Curated1
Sequence conflicti401V → A in CAC94013 (PubMed:11801725).Curated1
Sequence conflicti427A → T in CAC94013 (PubMed:11801725).Curated1
Sequence conflicti675P → A in CAC94013 (PubMed:11801725).Curated1
Sequence conflicti1070P → L in AAH79906 (PubMed:15489334).Curated1
Sequence conflicti1071K → N in AAH35206 (PubMed:15489334).Curated1
Sequence conflicti1183 – 1184EQ → DE in AAC52876 (PubMed:8910340).Curated2
Sequence conflicti1187G → R in CAC94013 (PubMed:11801725).Curated1
Sequence conflicti1206A → T in AAC52876 (PubMed:8910340).Curated1
Sequence conflicti1271E → G in AAC52876 (PubMed:8910340).Curated1
Sequence conflicti1359 – 1408Missing in AAH79906 (PubMed:15489334).CuratedAdd BLAST50
Sequence conflicti1771Q → H in AAH79906 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0589261 – 949Missing in isoform 3. Add BLAST949
Alternative sequenceiVSP_0589271101 – 1106Missing in isoform 2 and isoform 3. 6

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AL929059 Genomic DNA No translation available.
BC035206 mRNA Translation: AAH35206.1
BC079906 mRNA Translation: AAH79906.1 Different initiation.
AJ414734 mRNA Translation: CAC94013.1
U67885 mRNA Translation: AAC52876.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS50684.1 [P70399-1]

NCBI Reference Sequences

More...RefSeqi		NP_001277759.1, NM_001290830.1
NP_038763.3, NM_013735.4 [P70399-1]
XP_011237883.1, XM_011239581.2 [P70399-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000110648; ENSMUSP00000106278; ENSMUSG00000043909 [P70399-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		27223

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:27223

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL929059 Genomic DNA No translation available.
BC035206 mRNA Translation: AAH35206.1
BC079906 mRNA Translation: AAH79906.1 Different initiation.
AJ414734 mRNA Translation: CAC94013.1
U67885 mRNA Translation: AAC52876.1
CCDSiCCDS50684.1 [P70399-1]
RefSeqiNP_001277759.1, NM_001290830.1
NP_038763.3, NM_013735.4 [P70399-1]
XP_011237883.1, XM_011239581.2 [P70399-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SSFNMR-A1475-1629[»]
SMRiP70399
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi205144, 40 interactors
DIPiDIP-31595N
IntActiP70399, 32 interactors
MINTiP70399
STRINGi10090.ENSMUSP00000106278

PTM databases

iPTMnetiP70399
PhosphoSitePlusiP70399
SwissPalmiP70399

Proteomic databases

EPDiP70399
jPOSTiP70399
MaxQBiP70399
PaxDbiP70399
PeptideAtlasiP70399
PRIDEiP70399

Genome annotation databases

EnsembliENSMUST00000110648; ENSMUSP00000106278; ENSMUSG00000043909 [P70399-1]
GeneIDi27223
KEGGimmu:27223

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		27223
MGIiMGI:1351320 Trp53bp1

Phylogenomic databases

eggNOGiKOG3548 Eukaryota
ENOG411075K LUCA
GeneTreeiENSGT00390000011891
HOGENOMiHOG000231961
InParanoidiP70399
KOiK20915
OMAiCVSHLWV
OrthoDBi27155at2759
TreeFamiTF350227

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Trp53bp1 mouse
EvolutionaryTraceiP70399

Protein Ontology

More...PROi		PR:P70399

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000043909 Expressed in 289 organ(s), highest expression level in secondary oocyte
ExpressionAtlasiP70399 baseline and differential

Family and domain databases

Gene3Di2.30.30.30, 1 hit
3.40.50.10190, 2 hits
InterProiView protein in InterPro
IPR015125 53-BP1_Tudor
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR014722 Rib_L2_dom2
PfamiView protein in Pfam
PF09038 53-BP1_Tudor, 1 hit
SMARTiView protein in SMART
SM00292 BRCT, 2 hits
SUPFAMiSSF52113 SSF52113, 2 hits
PROSITEiView protein in PROSITE
PS50172 BRCT, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTP53B_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P70399
Secondary accession number(s): A2AU89
, A2AU91, Q68FD0, Q8CI97, Q91YC9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 10, 2017
Last modified: October 16, 2019
This is version 169 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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