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Entry version 189 (07 Jun 2017)
Sequence version 2 (01 Dec 2000)
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Protein

TP53-binding protein 1

Gene

TP53BP1

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -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
Inferred from direct assayⁱ
p53 binding
Source: AgBase
Inferred from physical interactionⁱ
- 14985081
RNA polymerase II activating transcription factor binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- 17805299
RNA polymerase II transcription cofactor activity
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 17805299
ubiquitinated histone binding
Source: UniProtKB
Inferred from direct assayⁱ
- 23760478

Complete GO annotation...

GO - Biological processⁱ

cellular response to DNA damage stimulus
Source: UniProtKB
Inferred from direct assayⁱ
- 28241136
cellular response to X-ray Source: Ensembl
DNA damage checkpoint Source: GO_Central
double-strand break repair via nonhomologous end joining
Source: UniProtKB
Inferred from direct assayⁱ
negative regulation of double-strand break repair via homologous recombination
Source: UniProtKB
Inferred from direct assayⁱ
- 23333306
- 23345425
positive regulation of isotype switching
Source: UniProtKB
Inferred from direct assayⁱ
- 23345425
positive regulation of sequence-specific DNA binding transcription factor activity
Source: BHF-UCL
Inferred by curatorⁱ
- 17805299
positive regulation of transcription, DNA-templated
Source: UniProtKB
Non-traceable author statementⁱ
- 9748285
positive regulation of transcription from RNA polymerase II promoter
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 17805299
protein homooligomerization
Source: UniProtKB
Inferred from direct assayⁱ
- 23345425
protein sumoylation Source: Reactome
transcription, DNA-templated Source: UniProtKB-KW

Complete GO annotation...

Keywordsⁱ

Molecular function	Activator, DNA-binding
Biological process	DNA damage, DNA repair, Transcription, Transcription regulation

Enzyme and pathway databases

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.
SIGNORⁱ	Q12888.

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 15

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:11999. TP53BP1.

HGNCⁱ

HGNC:11999. TP53BP1.

Subcellular locationⁱ

Note:

Localizes to the nucleus in absence of DNA damage (PubMed:28241136). Following DNA damage, recruited to sites of DNA damage, such as double stand breaks (DSBs): recognizes and binds 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:23333306, PubMed:23760478, PubMed:24703952, PubMed:28241136, PubMed:17190600). Associated with kinetochores during mitosis (By similarity).By similarity4 Publications

GO - Cellular componentⁱ

condensed chromosome kinetochore Source: UniProtKB-SubCell
cytoplasm
Source: ProtInc
Inferred from direct assayⁱ
- 9748285
nuclear body Source: HPA
nucleoplasm Source: HPA
nucleus
Source: UniProtKB
Inferred from direct assayⁱ
- 28241136
site of double-strand break
Source: UniProtKB
Inferred from direct assayⁱ

Complete GO annotation...

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 key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	6	S → 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 Publications	1
Mutagenesisⁱ	13	S → 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 Publications	1
Mutagenesisⁱ	25	S → 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 Publications	1
Mutagenesisⁱ	29	S → 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 Publications	1
Mutagenesisⁱ	105	S → 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 Publications	1
Mutagenesisⁱ	166	S → 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 Publications	1
Mutagenesisⁱ	176 – 178	SQS → AQA: Loss of phosphorylation site. 1 Publication	3
Mutagenesisⁱ	176	S → 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 Publications	1
Mutagenesisⁱ	178	S → 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 Publications	1
Mutagenesisⁱ	302	T → 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 Publications	1
Mutagenesisⁱ	437	S → 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 Publications	1
Mutagenesisⁱ	452	S → 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 Publications	1
Mutagenesisⁱ	523	S → 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 Publications	1
Mutagenesisⁱ	543	T → 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 Publications	1
Mutagenesisⁱ	580	S → 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 Publications	1
Mutagenesisⁱ	625	S → 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 Publications	1
Mutagenesisⁱ	674	S → 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 Publications	1
Mutagenesisⁱ	696	T → 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 Publications	1
Mutagenesisⁱ	698	S → 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 Publications	1
Mutagenesisⁱ	784	S → 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 Publications	1
Mutagenesisⁱ	831	S → 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 Publications	1
Mutagenesisⁱ	855	T → 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 Publications	1
Mutagenesisⁱ	892	S → 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 Publications	1
Mutagenesisⁱ	1068	S → 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 Publications	1
Mutagenesisⁱ	1086	S → 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 Publications	1
Mutagenesisⁱ	1104	S → 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 Publications	1
Mutagenesisⁱ	1148	S → 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 Publications	1
Mutagenesisⁱ	1171	T → 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 Publications	1
Mutagenesisⁱ	1219	S → 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 Publications	1
Mutagenesisⁱ	1396	R → 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 Publications	1
Mutagenesisⁱ	1396	R → K: No detectable effect on methylation by PRMT1 (in vitro). 2 Publications	1
Mutagenesisⁱ	1398 – 1401	RGRR → AGAA: No effect on in class-switch recombination (CSR). 1 Publication	4
Mutagenesisⁱ	1398	R → 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 Publications	1
Mutagenesisⁱ	1398	R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1400. Strongly reduced methylation; when associated with K-1401. 2 Publications	1
Mutagenesisⁱ	1400	R → 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 Publications	1
Mutagenesisⁱ	1400	R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1401. 2 Publications	1
Mutagenesisⁱ	1401	R → 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 Publications	1
Mutagenesisⁱ	1401	R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1400. 2 Publications	1
Mutagenesisⁱ	1403	R → 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 Publications	1
Mutagenesisⁱ	1403	R → K: No detectable effect on methylation by PRMT1 (in vitro). 2 Publications	1
Mutagenesisⁱ	1495	W → 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 Publications	1
Mutagenesisⁱ	1495	W → F: No effect on recruitment to double strand breaks. 2 Publications	1
Mutagenesisⁱ	1495	W → V: Reduces recruitment to double strand breaks. 2 Publications	1
Mutagenesisⁱ	1500	Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. 1 Publication	1
Mutagenesisⁱ	1502	Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. 2 Publications	1
Mutagenesisⁱ	1502	Y → L or Q: Abolishes recruitment to double strand breaks. 2 Publications	1
Mutagenesisⁱ	1521	D → 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 Publications	1
Mutagenesisⁱ	1521	D → R: Abolishes recruitment to double strand breaks and induces defects in class-switch recombination (CSR). 4 Publications	1
Mutagenesisⁱ	1523	Y → A: Increases affinity for histone H4 that has been dimethylated at 'Lys-20'. No effect on recruitment to double strand breaks. 1 Publication	1
Mutagenesisⁱ	1523	Y → S: Decreases affinity for histone H4 that has been dimethylated at 'Lys-20'. 1 Publication	1
Mutagenesisⁱ	1609	T → A: Constitutive recruitment to mitotic DNA lesions, leading to mitotic defects; when associated with A-1618. 1 Publication	1
Mutagenesisⁱ	1609	T → E: Phosphomimetic mutant that abolishes recruitment to double strand breaks; when associated with D-1618. 1 Publication	1
Mutagenesisⁱ	1613	K → A: Does not affect recruitment to double strand breaks. 1 Publication	1
Mutagenesisⁱ	1616	D → A: Does not affect recruitment to double strand breaks. 1 Publication	1
Mutagenesisⁱ	1617	I → A: Strongly reduced recruitment to double strand breaks. Defects in class-switch recombination (CSR). 1 Publication	1
Mutagenesisⁱ	1618	S → A: Constitutive recruitment to mitotic DNA lesions, leading to mitotic defects; when associated with A-1609. 1 Publication	1
Mutagenesisⁱ	1618	S → D: Phosphomimetic mutant that abolishes recruitment to double strand breaks; when associated with E-1609. 1 Publication	1
Mutagenesisⁱ	1619	L → 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 Publication	1
Mutagenesisⁱ	1621	N → A: Reduced recruitment to double strand breaks. 1 Publication	1
Mutagenesisⁱ	1622	L → A: Reduced recruitment to double strand breaks. 1 Publication	1
Mutagenesisⁱ	1624	E → A: Does not affect recruitment to double strand breaks. 1 Publication	1
Mutagenesisⁱ	1627	R → A: Reduced recruitment to double strand breaks. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	7158.
Open Targets More...OpenTargetsⁱ	ENSG00000067369.
PharmGKBⁱ	PA36680.

Chemistry databases

ChEMBLⁱ	CHEMBL2424509.

ChEMBLⁱ

CHEMBL2424509.

Polymorphism and mutation databases

BioMutaⁱ	TP53BP1.
DMDMⁱ	8928568.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000072643	1 – 1972	TP53-binding protein 1Add BLAST		1972

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	25	Phosphoserine1 Publication	1
Modified residueⁱ	63	PhosphoserineCombined sources	1
Modified residueⁱ	105	PhosphoserineCombined sources	1
Modified residueⁱ	124	PhosphoserineCombined sources	1
Modified residueⁱ	166	Phosphoserine1 Publication	1
Modified residueⁱ	176	Phosphoserine1 Publication	1
Modified residueⁱ	178	Phosphoserine1 Publication	1
Cross-linkⁱ	217	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linkⁱ	217	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	222	PhosphoserineCombined sources	1
Modified residueⁱ	265	PhosphoserineCombined sources	1
Modified residueⁱ	294	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	302	PhosphothreonineCombined sources1 Publication	1
Modified residueⁱ	366	PhosphoserineCombined sources	1
Modified residueⁱ	380	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	395	PhosphoserineCombined sources	1
Modified residueⁱ	398	PhosphoserineCombined sources	1
Modified residueⁱ	452	Phosphoserine1 Publication	1
Modified residueⁱ	464	PhosphoserineBy similarity	1
Modified residueⁱ	500	PhosphoserineCombined sources	1
Modified residueⁱ	507	PhosphoserineCombined sources	1
Modified residueⁱ	518	PhosphoserineCombined sources	1
Modified residueⁱ	523	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	525	PhosphoserineCombined sources	1
Modified residueⁱ	543	PhosphothreonineCombined sources	1
Modified residueⁱ	548	PhosphothreonineCombined sources	1
Modified residueⁱ	552	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	566	PhosphoserineCombined sources	1
Modified residueⁱ	580	PhosphoserineCombined sources	1
Modified residueⁱ	630	PhosphoserineCombined sources	1
Modified residueⁱ	635	PhosphoserineCombined sources	1
Modified residueⁱ	639	PhosphoserineCombined sources	1
Modified residueⁱ	640	PhosphoserineCombined sources	1
Modified residueⁱ	692	PhosphoserineCombined sources	1
Modified residueⁱ	724	PhosphoserineBy similarity	1
Modified residueⁱ	727	PhosphoserineCombined sources	1
Modified residueⁱ	771	PhosphoserineCombined sources	1
Modified residueⁱ	809	PhosphoserineCombined sources	1
Modified residueⁱ	830	PhosphoserineBy similarity	1
Modified residueⁱ	831	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	834	PhosphoserineCombined sources	1
Modified residueⁱ	855	PhosphothreonineCombined sources	1
Cross-linkⁱ	868	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residueⁱ	922	PhosphothreonineCombined sources	1
Cross-linkⁱ	930	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	970	PhosphoserineCombined sources	1
Modified residueⁱ	975	PhosphoserineCombined sources	1
Modified residueⁱ	1028	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	1056	PhosphothreonineCombined sources	1
Modified residueⁱ	1068	PhosphoserineCombined sources	1
Modified residueⁱ	1086	Phosphoserine1 Publication	1
Modified residueⁱ	1094	PhosphoserineCombined sources	1
Modified residueⁱ	1101	PhosphoserineCombined sources	1
Modified residueⁱ	1114	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	1148	PhosphoserineCombined sources	1
Modified residueⁱ	1214	PhosphothreonineCombined sources	1
Modified residueⁱ	1216	PhosphoserineCombined sources	1
Modified residueⁱ	1219	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	1317	PhosphoserineCombined sources	1
Modified residueⁱ	1342	PhosphoserineCombined sources	1
Modified residueⁱ	1355	Omega-N-methylarginineBy similarity	1
Modified residueⁱ	1362	PhosphoserineCombined sources	1
Modified residueⁱ	1368	PhosphoserineCombined sources	1
Modified residueⁱ	1372	PhosphothreonineCombined sources	1
Modified residueⁱ	1426	PhosphoserineCombined sources	1
Modified residueⁱ	1430	PhosphoserineCombined sources	1
Cross-linkⁱ	1434	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linkⁱ	1434	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	1460	PhosphoserineCombined sources	1
Modified residueⁱ	1462	PhosphoserineCombined sources	1
Modified residueⁱ	1474	PhosphoserineCombined sources	1
Cross-linkⁱ	1563	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linkⁱ	1563	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	1609	PhosphothreonineCombined sources1 Publication	1
Modified residueⁱ	1618	PhosphoserineCombined sources1 Publication	1
Modified residueⁱ	1631	PhosphoserineBy similarity	1
Modified residueⁱ	1635	PhosphoserineCombined sources	1
Modified residueⁱ	1638	PhosphothreonineCombined sources	1
Modified residueⁱ	1648	PhosphothreonineCombined sources	1
Modified residueⁱ	1656	PhosphoserineCombined sources	1
Modified residueⁱ	1673	PhosphoserineCombined sources	1
Modified residueⁱ	1678	PhosphoserineCombined sources	1
Modified residueⁱ	1701	PhosphoserineCombined sources	1
Modified residueⁱ	1759	PhosphoserineCombined sources	1
Modified residueⁱ	1778	Phosphoserine2 Publications	1

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

EPDⁱ	Q12888.
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q12888.
PaxDbⁱ	Q12888.
PeptideAtlas More...PeptideAtlasⁱ	Q12888.
PRIDEⁱ	Q12888.

PTM databases

iPTMnetⁱ	Q12888.
PhosphoSitePlusⁱ	Q12888.

Miscellaneous databases

PMAP-CutDBⁱ	Q12888.

PMAP-CutDBⁱ

Q12888.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000067369.
CleanExⁱ	HS_TP53BP1.
ExpressionAtlasⁱ	Q12888. baseline and differential.
Genevisibleⁱ	Q12888. HS.

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB004083. HPA008788. HPA022133.

HPAⁱ

CAB004083.
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

With	Entry	#Exp.	IntAct	Notes
H2AFX	P16104	6	EBI-396540,EBI-494830
HIST1H3D	P68431	5	EBI-396540,EBI-79722
HIST2H4B	P62805	8	EBI-396540,EBI-302023
MEOX2	A4D127	3	EBI-396540,EBI-10172134
PAXIP1	Q6ZW49	4	EBI-396540,EBI-743225
Paxip1	Q6NZQ4	5	EBI-396540,EBI-1395317	From Mus musculus.
TP53	P04637	2	EBI-396540,EBI-366083
VAC14	Q08AM6	5	EBI-396540,EBI-2107455
VRK1	Q99986	8	EBI-396540,EBI-1769146
ZNHIT1	O43257	2	EBI-396540,EBI-347522

Show more details

GO - Molecular functionⁱ

Complete GO annotation...

Protein-protein interaction databases

BioGridⁱ	113011. 140 interactors.
Database of interacting proteins More...DIPⁱ	DIP-5978N.
IntActⁱ	Q12888. 45 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-276057.
STRINGⁱ	9606.ENSP00000371475.

Chemistry databases

BindingDBⁱ	Q12888.

BindingDBⁱ

Q12888.

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	1490 – 1494	Combined sources	5
Turnⁱ	1496 – 1498	Combined sources	3
Beta strandⁱ	1501 – 1511	Combined sources	11
Beta strandⁱ	1514 – 1519	Combined sources	6
Beta strandⁱ	1524 – 1528	Combined sources	5
Helixⁱ	1529 – 1531	Combined sources	3
Beta strandⁱ	1532 – 1535	Combined sources	4
Beta strandⁱ	1543 – 1547	Combined sources	5
Beta strandⁱ	1548 – 1551	Combined sources	4
Beta strandⁱ	1553 – 1564	Combined sources	12
Beta strandⁱ	1567 – 1574	Combined sources	8
Beta strandⁱ	1577 – 1582	Combined sources	6
Helixⁱ	1583 – 1585	Combined sources	3
Beta strandⁱ	1586 – 1588	Combined sources	3
Helixⁱ	1590 – 1594	Combined sources	5
Helixⁱ	1597 – 1600	Combined sources	4
Helixⁱ	1715 – 1719	Combined sources	5
Turnⁱ	1726 – 1731	Combined sources	6
Beta strandⁱ	1732 – 1736	Combined sources	5
Helixⁱ	1741 – 1745	Combined sources	5
Helixⁱ	1773 – 1781	Combined sources	9
Turnⁱ	1782 – 1784	Combined sources	3
Turnⁱ	1793 – 1799	Combined sources	7
Beta strandⁱ	1801 – 1808	Combined sources	8
Helixⁱ	1813 – 1821	Combined sources	9
Beta strandⁱ	1825 – 1827	Combined sources	3
Helixⁱ	1829 – 1837	Combined sources	9
Helixⁱ	1843 – 1845	Combined sources	3
Beta strandⁱ	1851 – 1853	Combined sources	3
Turnⁱ	1854 – 1857	Combined sources	4
Beta strandⁱ	1858 – 1860	Combined sources	3
Turnⁱ	1868 – 1871	Combined sources	4
Beta strandⁱ	1873 – 1879	Combined sources	7
Turnⁱ	1881 – 1884	Combined sources	4
Helixⁱ	1885 – 1894	Combined sources	10
Beta strandⁱ	1898 – 1908	Combined sources	11
Helixⁱ	1914 – 1916	Combined sources	3
Beta strandⁱ	1918 – 1922	Combined sources	5
Helixⁱ	1928 – 1937	Combined sources	10
Helixⁱ	1944 – 1953	Combined sources	10
Helixⁱ	1963 – 1965	Combined sources	3

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1GZH	X-ray	2.60	B/D	1724-1972	[»]
	1KZY	X-ray	2.50	C/D	1714-1972	[»]
	1XNI	X-ray	2.80	A/B/C/D/E/F/G/H/I/J	1485-1602	[»]
	2G3R	X-ray	1.25	A	1484-1603	[»]
	2IG0	X-ray	1.70	A	1484-1603	[»]
	2LVM	NMR	-	A	1484-1603	[»]
	2MWO	NMR	-	A	1484-1603	[»]
	2MWP	NMR	-	A	1484-1603	[»]
	3LGF	X-ray	1.50	A	1484-1603	[»]
	3LGL	X-ray	1.60	A	1484-1603	[»]
	3LH0	X-ray	1.90	A	1484-1603	[»]
	4CRI	X-ray	2.35	A/B	1459-1634	[»]
	4RG2	X-ray	1.50	A/B	1483-1606	[»]
	4X34	X-ray	1.80	A/B	1484-1603	[»]
	5ECG	X-ray	3.00	C/D	1713-1972	[»]
	5J26	X-ray	2.50	A	1487-1603	[»]
	5KGF	electron microscopy	4.54	K/L	1611-1631	[»]
ProteinModelPortalⁱ	Q12888.
SMRⁱ	Q12888.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q12888.

EvolutionaryTraceⁱ

Q12888.

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	1724 – 1848	BRCT 1PROSITE-ProRule annotationAdd BLAST		125
Domainⁱ	1864 – 1964	BRCT 2PROSITE-ProRule annotationAdd BLAST		101

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	1484 – 1603	Tudor-like1 PublicationAdd BLAST		120
Regionⁱ	1495 – 1523	Interaction with dimethylated histone H41 PublicationAdd BLAST		29

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	1396 – 1403	GAR1 Publication		8
Motifⁱ	1604 – 1631	UDR1 PublicationAdd BLAST		28

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	1642 – 1646	Poly-Ser		5
Compositional biasⁱ	1760 – 1764	Poly-Glu		5

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:23760478, PubMed:24703952). Phosphorylation of the UDR blocks interaction with H2AK15ub (PubMed:24703952).2 Publications

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	KOG3548. Eukaryota. ENOG411075K. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000011891.
HOGENOMⁱ	HOG000231961.
HOVERGENⁱ	HBG060882.
InParanoidⁱ	Q12888.
KEGG Orthology (KO) More...KOⁱ	K20915.
OMAⁱ	CIDLTCD.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0BHF.
PhylomeDBⁱ	Q12888.
TreeFamⁱ	TF350227.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00027. BRCT. 2 hits.
Gene3Dⁱ	2.30.30.30. 1 hit. 3.40.50.10190. 2 hits.
InterProⁱ	View protein in InterPro IPR015125. 53-BP1_Tudor. IPR001357. BRCT_dom. IPR014722. Rib_L2_dom2.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF09038. 53-BP1_Tudor. 1 hit.
SMARTⁱ	View protein in SMART SM00292. BRCT. 2 hits.
SUPFAMⁱ	SSF52113. SSF52113. 2 hits.
PROSITEⁱ	View protein in PROSITE PS50172. BRCT. 2 hits.

Sequences (3)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 1 (identifier: Q12888-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

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

Length:1,972

Mass (Da):213,574

Last modified:December 1, 2000 - v2

Checksum:ⁱ13E2CC8A265F9D2A

Isoform 2 (identifier: Q12888-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MPGEQM

« Hide

        10         20         30         40         50
MPGEQMDPTG SQLDSDFSQQ DTPCLIIEDS QPESQVLEDD SGSHFSMLSR 
        60         70         80         90        100
HLPNLQTHKE NPVLDVVSNP EQTAGEERGD GNSGFNEHLK ENKVADPVDS 
       110        120        130        140        150
SNLDTCGSIS QVIEQLPQPN RTSSVLGMSV ESAPAVEEEK GEELEQKEKE 
       160        170        180        190        200
KEEDTSGNTT HSLGAEDTAS SQLGFGVLEL SQSQDVEENT VPYEVDKEQL 
       210        220        230        240        250
QSVTTNSGYT RLSDVDANTA IKHEEQSNED IPIAEQSSKD IPVTAQPSKD 
       260        270        280        290        300
VHVVKEQNPP PARSEDMPFS PKASVAAMEA KEQLSAQELM ESGLQIQKSP 
       310        320        330        340        350
EPEVLSTQED LFDQSNKTVS SDGCSTPSRE EGGCSLASTP ATTLHLLQLS 
       360        370        380        390        400
GQRSLVQDSL STNSSDLVAP SPDAFRSTPF IVPSSPTEQE GRQDKPMDTS 
       410        420        430        440        450
VLSEEGGEPF QKKLQSGEPV ELENPPLLPE STVSPQASTP ISQSTPVFPP 
       460        470        480        490        500
GSLPIPSQPQ FSHDIFIPSP SLEEQSNDGK KDGDMHSSSL TVECSKTSEI 
       510        520        530        540        550
EPKNSPEDLG LSLTGDSCKL MLSTSEYSQS PKMESLSSHR IDEDGENTQI 
       560        570        580        590        600
EDTEPMSPVL NSKFVPAEND SILMNPAQDG EVQLSQNDDK TKGDDTDTRD 
       610        620        630        640        650
DISILATGCK GREETVAEDV CIDLTCDSGS QAVPSPATRS EALSSVLDQE 
       660        670        680        690        700
EAMEIKEHHP EEGSSGSEVE EIPETPCESQ GEELKEENME SVPLHLSLTE 
       710        720        730        740        750
TQSQGLCLQK EMPKKECSEA MEVETSVISI DSPQKLAILD QELEHKEQEA 
       760        770        780        790        800
WEEATSEDSS VVIVDVKEPS PRVDVSCEPL EGVEKCSDSQ SWEDIAPEIE 
       810        820        830        840        850
PCAENRLDTK EEKSVEYEGD LKSGTAETEP VEQDSSQPSL PLVRADDPLR 
       860        870        880        890        900
LDQELQQPQT QEKTSNSLTE DSKMANAKQL SSDAEAQKLG KPSAHASQSF 
       910        920        930        940        950
CESSSETPFH FTLPKEGDII PPLTGATPPL IGHLKLEPKR HSTPIGISNY 
       960        970        980        990       1000
PESTIATSDV MSESMVETHD PILGSGKGDS GAAPDVDDKL CLRMKLVSPE 
      1010       1020       1030       1040       1050
TEASEESLQF NLEKPATGER KNGSTAVAES VASPQKTMSV LSCICEARQE 
      1060       1070       1080       1090       1100
NEARSEDPPT TPIRGNLLHF PSSQGEEEKE KLEGDHTIRQ SQQPMKPISP 
      1110       1120       1130       1140       1150
VKDPVSPASQ KMVIQGPSSP QGEAMVTDVL EDQKEGRSTN KENPSKALIE 
      1160       1170       1180       1190       1200
RPSQNNIGIQ TMECSLRVPE TVSAATQTIK NVCEQGTSTV DQNFGKQDAT 
      1210       1220       1230       1240       1250
VQTERGSGEK PVSAPGDDTE SLHSQGEEEF DMPQPPHGHV LHRHMRTIRE 
      1260       1270       1280       1290       1300
VRTLVTRVIT DVYYVDGTEV ERKVTEETEE PIVECQECET EVSPSQTGGS 
      1310       1320       1330       1340       1350
SGDLGDISSF SSKASSLHRT SSGTSLSAMH SSGSSGKGAG PLRGKTSGTE 
      1360       1370       1380       1390       1400
PADFALPSSR GGPGKLSPRK GVSQTGTPVC EEDGDAGLGI RQGGKAPVTP 
      1410       1420       1430       1440       1450
RGRGRRGRPP SRTTGTRETA VPGPLGIEDI SPNLSPDDKS FSRVVPRVPD 
      1460       1470       1480       1490       1500
STRRTDVGAG ALRRSDSPEI PFQAAAGPSD GLDASSPGNS FVGLRVVAKW 
      1510       1520       1530       1540       1550
SSNGYFYSGK ITRDVGAGKY KLLFDDGYEC DVLGKDILLC DPIPLDTEVT 
      1560       1570       1580       1590       1600
ALSEDEYFSA GVVKGHRKES GELYYSIEKE GQRKWYKRMA VILSLEQGNR 
      1610       1620       1630       1640       1650
LREQYGLGPY EAVTPLTKAA DISLDNLVEG KRKRRSNVSS PATPTASSSS 
      1660       1670       1680       1690       1700
STTPTRKITE SPRASMGVLS GKRKLITSEE ERSPAKRGRK SATVKPGAVG 
      1710       1720       1730       1740       1750
AGEFVSPCES GDNTGEPSAL EEQRGPLPLN KTLFLGYAFL LTMATTSDKL 
      1760       1770       1780       1790       1800
ASRSKLPDGP TGSSEEEEEF LEIPPFNKQY TESQLRAGAG YILEDFNEAQ 
      1810       1820       1830       1840       1850
CNTAYQCLLI ADQHCRTRKY FLCLASGIPC VSHVWVHDSC HANQLQNYRN 
      1860       1870       1880       1890       1900
YLLPAGYSLE EQRILDWQPR ENPFQNLKVL LVSDQQQNFL ELWSEILMTG 
      1910       1920       1930       1940       1950
GAASVKQHHS SAHNKDIALG VFDVVVTDPS CPASVLKCAE ALQLPVVSQE 
      1960       1970 
WVIQCLIVGE RIGFKQHPKY KHDYVSH

Note: No experimental confirmation available.

Show »

Length:1,977

Mass (Da):214,117

Checksum:ⁱB8C43ACE26E9A204

Isoform 3 (identifier: Q12888-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MPGEQM
1692-1693: Missing.

« Hide

        10         20         30         40         50
MPGEQMDPTG SQLDSDFSQQ DTPCLIIEDS QPESQVLEDD SGSHFSMLSR 
        60         70         80         90        100
HLPNLQTHKE NPVLDVVSNP EQTAGEERGD GNSGFNEHLK ENKVADPVDS 
       110        120        130        140        150
SNLDTCGSIS QVIEQLPQPN RTSSVLGMSV ESAPAVEEEK GEELEQKEKE 
       160        170        180        190        200
KEEDTSGNTT HSLGAEDTAS SQLGFGVLEL SQSQDVEENT VPYEVDKEQL 
       210        220        230        240        250
QSVTTNSGYT RLSDVDANTA IKHEEQSNED IPIAEQSSKD IPVTAQPSKD 
       260        270        280        290        300
VHVVKEQNPP PARSEDMPFS PKASVAAMEA KEQLSAQELM ESGLQIQKSP 
       310        320        330        340        350
EPEVLSTQED LFDQSNKTVS SDGCSTPSRE EGGCSLASTP ATTLHLLQLS 
       360        370        380        390        400
GQRSLVQDSL STNSSDLVAP SPDAFRSTPF IVPSSPTEQE GRQDKPMDTS 
       410        420        430        440        450
VLSEEGGEPF QKKLQSGEPV ELENPPLLPE STVSPQASTP ISQSTPVFPP 
       460        470        480        490        500
GSLPIPSQPQ FSHDIFIPSP SLEEQSNDGK KDGDMHSSSL TVECSKTSEI 
       510        520        530        540        550
EPKNSPEDLG LSLTGDSCKL MLSTSEYSQS PKMESLSSHR IDEDGENTQI 
       560        570        580        590        600
EDTEPMSPVL NSKFVPAEND SILMNPAQDG EVQLSQNDDK TKGDDTDTRD 
       610        620        630        640        650
DISILATGCK GREETVAEDV CIDLTCDSGS QAVPSPATRS EALSSVLDQE 
       660        670        680        690        700
EAMEIKEHHP EEGSSGSEVE EIPETPCESQ GEELKEENME SVPLHLSLTE 
       710        720        730        740        750
TQSQGLCLQK EMPKKECSEA MEVETSVISI DSPQKLAILD QELEHKEQEA 
       760        770        780        790        800
WEEATSEDSS VVIVDVKEPS PRVDVSCEPL EGVEKCSDSQ SWEDIAPEIE 
       810        820        830        840        850
PCAENRLDTK EEKSVEYEGD LKSGTAETEP VEQDSSQPSL PLVRADDPLR 
       860        870        880        890        900
LDQELQQPQT QEKTSNSLTE DSKMANAKQL SSDAEAQKLG KPSAHASQSF 
       910        920        930        940        950
CESSSETPFH FTLPKEGDII PPLTGATPPL IGHLKLEPKR HSTPIGISNY 
       960        970        980        990       1000
PESTIATSDV MSESMVETHD PILGSGKGDS GAAPDVDDKL CLRMKLVSPE 
      1010       1020       1030       1040       1050
TEASEESLQF NLEKPATGER KNGSTAVAES VASPQKTMSV LSCICEARQE 
      1060       1070       1080       1090       1100
NEARSEDPPT TPIRGNLLHF PSSQGEEEKE KLEGDHTIRQ SQQPMKPISP 
      1110       1120       1130       1140       1150
VKDPVSPASQ KMVIQGPSSP QGEAMVTDVL EDQKEGRSTN KENPSKALIE 
      1160       1170       1180       1190       1200
RPSQNNIGIQ TMECSLRVPE TVSAATQTIK NVCEQGTSTV DQNFGKQDAT 
      1210       1220       1230       1240       1250
VQTERGSGEK PVSAPGDDTE SLHSQGEEEF DMPQPPHGHV LHRHMRTIRE 
      1260       1270       1280       1290       1300
VRTLVTRVIT DVYYVDGTEV ERKVTEETEE PIVECQECET EVSPSQTGGS 
      1310       1320       1330       1340       1350
SGDLGDISSF SSKASSLHRT SSGTSLSAMH SSGSSGKGAG PLRGKTSGTE 
      1360       1370       1380       1390       1400
PADFALPSSR GGPGKLSPRK GVSQTGTPVC EEDGDAGLGI RQGGKAPVTP 
      1410       1420       1430       1440       1450
RGRGRRGRPP SRTTGTRETA VPGPLGIEDI SPNLSPDDKS FSRVVPRVPD 
      1460       1470       1480       1490       1500
STRRTDVGAG ALRRSDSPEI PFQAAAGPSD GLDASSPGNS FVGLRVVAKW 
      1510       1520       1530       1540       1550
SSNGYFYSGK ITRDVGAGKY KLLFDDGYEC DVLGKDILLC DPIPLDTEVT 
      1560       1570       1580       1590       1600
ALSEDEYFSA GVVKGHRKES GELYYSIEKE GQRKWYKRMA VILSLEQGNR 
      1610       1620       1630       1640       1650
LREQYGLGPY EAVTPLTKAA DISLDNLVEG KRKRRSNVSS PATPTASSSS 
      1660       1670       1680       1690       1700
STTPTRKITE SPRASMGVLS GKRKLITSEE ERSPAKRGRK SATVKPVGAG 
      1710       1720       1730       1740       1750
EFVSPCESGD NTGEPSALEE QRGPLPLNKT LFLGYAFLLT MATTSDKLAS 
      1760       1770       1780       1790       1800
RSKLPDGPTG SSEEEEEFLE IPPFNKQYTE SQLRAGAGYI LEDFNEAQCN 
      1810       1820       1830       1840       1850
TAYQCLLIAD QHCRTRKYFL CLASGIPCVS HVWVHDSCHA NQLQNYRNYL 
      1860       1870       1880       1890       1900
LPAGYSLEEQ RILDWQPREN PFQNLKVLLV SDQQQNFLEL WSEILMTGGA 
      1910       1920       1930       1940       1950
ASVKQHHSSA HNKDIALGVF DVVVTDPSCP ASVLKCAEAL QLPVVSQEWV 
      1960       1970 
IQCLIVGERI GFKQHPKYKH DYVSH

Note: No experimental confirmation available.

Show »

Length:1,975

Mass (Da):213,989

Checksum:ⁱ14467931B27D109D

Sequence cautionⁱ

The sequence BAE06107 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	796	P → S in CAD97660 (PubMed:17974005).Curated	1
Sequence conflictⁱ	1600	Y → C in CAD97660 (PubMed:17974005).Curated	1
Sequence conflictⁱ	1958	G → R in CAD97660 (PubMed:17974005).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_022172	353	D → E2 PublicationsCorresponds to variant dbSNP:rs560191Ensembl.	1
Natural variantⁱVAR_022173	412	G → S2 PublicationsCorresponds to variant dbSNP:rs689647Ensembl.	1
Natural variantⁱVAR_022174	648	M → V1 PublicationCorresponds to variant dbSNP:rs45443496Ensembl.	1
Natural variantⁱVAR_022175	699	Q → R1 PublicationCorresponds to variant dbSNP:rs34823068Ensembl.	1
Natural variantⁱVAR_034558	841	D → G. Corresponds to variant dbSNP:rs34185035Ensembl.	1
Natural variantⁱVAR_022176	1014	E → G1 PublicationCorresponds to variant dbSNP:rs45470395Ensembl.	1
Natural variantⁱVAR_022177	1026	V → A1 PublicationCorresponds to variant dbSNP:rs45482998Ensembl.	1
Natural variantⁱVAR_022178	1136	K → Q2 PublicationsCorresponds to variant dbSNP:rs2602141Ensembl.	1
Natural variantⁱVAR_034559	1137	E → K. Corresponds to variant dbSNP:rs34740611Ensembl.	1
Natural variantⁱVAR_022179	1170	A → G1 PublicationCorresponds to variant dbSNP:rs45500399Ensembl.	1
Natural variantⁱVAR_022180	1174	I → V1 PublicationCorresponds to variant dbSNP:rs3803339Ensembl.	1
Natural variantⁱVAR_034560	1442	R → Q. Corresponds to variant dbSNP:rs2230449Ensembl.	1
Natural variantⁱVAR_038689	1488	G → W. Corresponds to variant dbSNP:rs11554564Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_018390	1	M → MPGEQM in isoform 2 and isoform 3. 2 Publications		1
Alternative sequenceⁱVSP_055062	1692 – 1693	Missing in isoform 3. 1 Publication		2

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF078776 mRNA. Translation: AAC62018.1. AB210025 mRNA. Translation: BAE06107.1. Different initiation. BX537418 mRNA. Translation: CAD97660.1. AY904026 Genomic DNA. Translation: AAW69392.1. AC018924 Genomic DNA. No translation available. BC112161 mRNA. Translation: AAI12162.1. U09477 mRNA. Translation: AAA21596.1.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10096.1. [Q12888-1] CCDS45250.1. [Q12888-2] CCDS45251.1. [Q12888-3]
PIRⁱ	I38604.
NCBI Reference Sequences More...RefSeqⁱ	NP_001135451.1. NM_001141979.1. [Q12888-3] NP_001135452.1. NM_001141980.1. [Q12888-2] NP_005648.1. NM_005657.2. [Q12888-1]
UniGeneⁱ	Hs.440968. Hs.584887.

Genome annotation databases

Ensemblⁱ	ENST00000263801; ENSP00000263801; ENSG00000067369. [Q12888-1] ENST00000382044; ENSP00000371475; ENSG00000067369. [Q12888-2] ENST00000450115; ENSP00000393497; ENSG00000067369. [Q12888-3]
GeneIDⁱ	7158.
KEGGⁱ	hsa:7158.
UCSC genome browser More...UCSCⁱ	uc001zrq.5. human. [Q12888-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Chromosomal rearrangement, Polymorphism

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

BindingDBⁱ	Q12888.
ChEMBLⁱ	CHEMBL2424509.

Structural Biology Knowledgebase	Search...

CTDⁱ	7158.
DisGeNET More...DisGeNETⁱ	7158.
GeneCardsⁱ	TP53BP1.
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:11999. TP53BP1.
Human Protein Atlas More...HPAⁱ	CAB004083. HPA008788. HPA022133.
MIMⁱ	605230. gene.
neXtProtⁱ	NX_Q12888.
Open Targets More...OpenTargetsⁱ	ENSG00000067369.
PharmGKBⁱ	PA36680.
GenAtlas: human gene database More...GenAtlasⁱ	Search...

ChiTaRSⁱ	TP53BP1. human.
EvolutionaryTraceⁱ	Q12888.
GeneWikiⁱ	TP53BP1.
GenomeRNAiⁱ	7158.
PMAP-CutDBⁱ	Q12888.
Protein Ontology More...PROⁱ	PR:Q12888.
SOURCEⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TP53B_HUMAN
Accessionⁱ	Q12888Primary (citable) accession number: Q12888 Secondary accession number(s): F8VY86 , Q2M1Z7, Q4LE46, Q5FWZ3, Q7Z3U4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
	Last sequence update:	December 1, 2000
	Last modified:	June 7, 2017
	This is version 189 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

Human chromosome 15
Human chromosome 15: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

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UniProtKB - Q12888 (TP53B_HUMAN)

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TP53-binding protein 1

TP53BP1

Select a section on the left to see content.

<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

<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

<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 - Biological processi

Enzyme and pathway databases

<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

Organism-specific databases

<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

<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 - Cellular componenti

<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

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Proteomic databases

PTM databases

Miscellaneous databases

<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

Organism-specific databases

<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>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

Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

Miscellaneous databases

<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

Region

Motif

Compositional bias

Phylogenomic databases

Family and domain databases

<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 length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<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

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<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 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

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequences (3)ⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ