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UniProtKB - P70399 (TP53B_MOUSE)

>sp|P70399|TP53B_MOUSE TP53-binding protein 1 OS=Mus musculus OX=10090 GN=Tp53bp1 PE=1 SV=3
MPGEQMDPTGSQLDSDFSQQDTPCLIIEDSQPESQVLEEDAGSHFSVLSRHLPNLQMHKE
NPVLDIVSNPEQSAVEQGDSNSSFNEHLKEKKASDPVESSHLGTSGSISQVIERLPQPNR
TSSALAVTVEAASLPEEEKEEEELEEEKEGVGANAPGADSLAAEDSASSQLGFGVLELSQ
SQDVEEHTVPYDVNQEHLQLVTTNSGSSPLSDVDASTAIKCEEQPTEDIAMIEQPSKDIP
VTVQPGKGIHVVEEQNLPLVRSEDRPSSPQVSVAAVETKEQVPARELLEEGPQVQPSSEP
EVSSTQEDLFDQSSKTASDGCSTPSREEGGCSPVSTPATTLQLLQLSGQKPLVQESLSTN
SSDLVAPSPDAFRSTPFIVPSSPTEQGGRKDEPMDMSVIPVGGEPFQKLHDDEAMETEKP
LLPSQPAVSPQASTPVSRSTPVFTPGSLPIPSQPEFSHDIFIPSPSLEEPSDDVKKGGGL
HSSSLTVECSKTSESEPKNFTDDLGLSMTGDSCKLMLSTSEYSQSSKMESLGSPRTEEDR
ENTQIDDTEPLSPVSNSKLPADSENVLVTPSQDDQVEMSQNVDKAKEDETEDRGDCKGRE
DAVAEDVCIDLTCDSGSQAVPSPATRSEALSSVLDQEEAMDTKEHHPEEGFSGSEVEEVP
ETPCGSHREEPKEEPMESIPLHLSLTETQSEALCLQKEAPKEECPEAMEVETSVISIDSP
QKLQVLDQELEHKDPDTWEEATSEDSSVVIVDVKEPSPRADVSCEPLEEVEKCSDSQSWE
GVAPEEEPCAENRLDTPEEKRIECDGDSKAETTEKDAVTEDSPQPPLPSVRDEPVRPDQE
TQQPQVQEKESPVTVDAEVADDKQLGPEGACQQLEKAPACASQSFCESSSETPFHFTLPK
EGDIIPPLTGATPPLIGHLKLEPKRHSTPIGISNYPESTIATSDVTSESMVEINDPLLGN
EKGDSESAPEMDGKLSLKMKLVSPETEASEESLQFSLEKPTTAERKNGSTAIAEPVASLQ
KPVPVFGCIYEAQQEKEAQSEAPPSAPDRANLLHFPSAQEEDKERPDVTPKLRQSEQPVK
PVGPVMDDAAPEDSASPVSQQRASQEQRASQEPFSPAEDVMETDLLEGLAANQDRPSKML
MDRPTQSNIGIQTVDHSLCAPETVSAATQTVKSVCEQGTSTAEQNSGKQDATVQTERGSG
EKPASAPVDDTESLHSQGEEEFEMPQPPHGHVLHRHMRTIREVRTLVTRVITDVYYVDGT
EVERKVTEETEEPIVECQECETEVSPSQTGGSSGDLGDISSFSSKASSSHHTSSGTSLSA
IHSSGSSGRGAGPLKGKASGTEAADFALPSSRGGPGKLSPRKGISQTGAPVCEEDGDAGL
GIRQGGKAPVTPRGRGRRGRPPSRTTGTRETVVSGPLGVEDISPSMSPDDKSFTRIMPRV
PDSTKRTDASSSTLRRSDSPEIPFQAATGSSDGLDSSSSGNSFVGLRVVAKWSSNGYFYS
GKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTEVTALSEDEYFSAGVVKGHRK
ESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLGPYEAVTPLTKAADISLDNLV
EGKRKRRSNISSPVTPTAASSSSTTPTRKATESPRASTGVPSGKRKLPTSEEERSPAKRG
RKSATVKPGTVGAAEFVSPCETGDNIGEPSVLEEPRGPLPLNKTLFLGYAFLLTMATTSD
KLASRSKLLDGPTGSSEEEEEFLEIPPFNKQYTECQLRAGAGYILEDFNEAQCNTAYQCL
LIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQ
PRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVFDVVVTD
PSCPASVLKCAEALQLPVVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH

Entry version 182 (25 May 2022)
Sequence version 3 (10 May 2017)
Previous versions | rss

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Protein

TP53-binding protein 1

Gene

Tp53bp1

Organism

Mus musculus (Mouse)

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: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, PubMed:30297459).

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 in 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 similarity7 Publications

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

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

Enzyme and pathway databases

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

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

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:Tp53bp1By similarity Synonyms:Trp53bp1Imported
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 2

Organism-specific databases

MGIⁱ	MGI:1351320, Trp53bp1
VEuPathDBⁱ	HostDB:ENSMUSG00000043909

Keywords - Cellular componentⁱ

Centromere, Chromosome, Kinetochore, Nucleus

Pathology & Biotechⁱ

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

Chemistry databases

ChEMBLⁱ	CHEMBL4295790

ChEMBLⁱ

CHEMBL4295790

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000072644	1 – 1969	TP53-binding protein 1Add BLAST		1969

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	30	PhosphoserineBy similarity	1
Modified residueⁱ	68	PhosphoserineBy similarity	1
Modified residueⁱ	73	PhosphoserineCombined sources	1
Modified residueⁱ	109	PhosphoserineBy similarity	1
Modified residueⁱ	169	PhosphoserineBy similarity	1
Modified residueⁱ	179	PhosphoserineBy similarity	1
Modified residueⁱ	181	PhosphoserineBy similarity	1
Cross-linkⁱ	220	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linkⁱ	220	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residueⁱ	267	PhosphoserineCombined sources	1
Modified residueⁱ	268	PhosphoserineCombined sources	1
Modified residueⁱ	297	PhosphoserineBy similarity	1
Modified residueⁱ	305	PhosphothreonineBy similarity	1
Modified residueⁱ	368	PhosphoserineBy similarity	1
Modified residueⁱ	382	PhosphoserineCombined sources	1
Modified residueⁱ	397	PhosphoserineBy similarity	1
Modified residueⁱ	429	PhosphoserineCombined sources	1
Modified residueⁱ	452	PhosphoserineBy similarity	1
Modified residueⁱ	464	PhosphoserineCombined sources	1
Modified residueⁱ	507	PhosphoserineBy similarity	1
Modified residueⁱ	518	PhosphoserineBy similarity	1
Modified residueⁱ	523	PhosphoserineBy similarity	1
Modified residueⁱ	525	PhosphoserineBy similarity	1
Modified residueⁱ	543	PhosphothreonineBy similarity	1
Modified residueⁱ	548	PhosphothreonineBy similarity	1
Modified residueⁱ	552	PhosphoserineCombined sources	1
Modified residueⁱ	579	PhosphoserineBy similarity	1
Modified residueⁱ	622	PhosphoserineBy similarity	1
Modified residueⁱ	627	PhosphoserineCombined sources	1
Modified residueⁱ	631	PhosphoserineCombined sources	1
Modified residueⁱ	632	PhosphoserineCombined sources	1
Modified residueⁱ	684	PhosphoserineBy similarity	1
Modified residueⁱ	716	PhosphoserineCombined sources	1
Modified residueⁱ	719	PhosphoserineCombined sources	1
Modified residueⁱ	763	PhosphoserineBy similarity	1
Modified residueⁱ	822	PhosphoserineCombined sources	1
Modified residueⁱ	912	PhosphothreonineBy similarity	1
Cross-linkⁱ	920	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	965	PhosphoserineBy similarity	1
Cross-linkⁱ	974	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	1018	PhosphoserineBy similarity	1
Modified residueⁱ	1075	PhosphoserineBy similarity	1
Modified residueⁱ	1096	PhosphoserineCombined sources	1
Modified residueⁱ	1115	PhosphoserineCombined sources	1
Modified residueⁱ	1211	PhosphothreonineBy similarity	1
Modified residueⁱ	1213	PhosphoserineBy similarity	1
Modified residueⁱ	1216	PhosphoserineBy similarity	1
Modified residueⁱ	1314	PhosphoserineBy similarity	1
Modified residueⁱ	1329	Omega-N-methylarginineCombined sources	1
Modified residueⁱ	1339	PhosphoserineBy similarity	1
Modified residueⁱ	1352	Omega-N-methylarginineCombined sources	1
Modified residueⁱ	1359	PhosphoserineBy similarity	1
Cross-linkⁱ	1362	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	1365	PhosphoserineBy similarity	1
Modified residueⁱ	1423	PhosphoserineCombined sources	1
Modified residueⁱ	1427	PhosphoserineCombined sources	1
Cross-linkⁱ	1431	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linkⁱ	1431	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residueⁱ	1457	PhosphoserineBy similarity	1
Modified residueⁱ	1459	PhosphoserineCombined sources	1
Modified residueⁱ	1470	PhosphoserineCombined sources	1
Modified residueⁱ	1471	PhosphoserineBy similarity	1
Cross-linkⁱ	1560	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linkⁱ	1560	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residueⁱ	1606	PhosphothreonineBy similarity	1
Modified residueⁱ	1615	PhosphoserineBy similarity	1
Modified residueⁱ	1628	PhosphoserineCombined sources	1
Modified residueⁱ	1632	PhosphoserineBy similarity	1
Modified residueⁱ	1635	PhosphothreonineBy similarity	1
Modified residueⁱ	1645	PhosphothreonineBy similarity	1
Modified residueⁱ	1653	PhosphoserineBy similarity	1
Modified residueⁱ	1670	PhosphoserineBy similarity	1
Modified residueⁱ	1675	PhosphoserineBy similarity	1
Modified residueⁱ	1698	PhosphoserineBy similarity	1
Modified residueⁱ	1756	PhosphoserineBy similarity	1

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

EPDⁱ	P70399
jPOSTⁱ	P70399
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P70399
PaxDbⁱ	P70399
PeptideAtlas More...PeptideAtlasⁱ	P70399
PRIDEⁱ	P70399
ProteomicsDBⁱ	260722 [P70399-1] 260723 [P70399-5] 260724 [P70399-6]

PTM databases

iPTMnetⁱ	P70399
PhosphoSitePlusⁱ	P70399
SwissPalmⁱ	P70399

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSMUSG00000043909, Expressed in secondary oocyte and 313 other tissues
ExpressionAtlasⁱ	P70399, baseline and differential

Interactionⁱ

Subunit structureⁱ

Homoligomer (By similarity).

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

Interacts with DCLRE1C (By similarity).

Interacts with histone H2AX and this requires phosphorylation of H2AX 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

Binary interactionsⁱ

Isoform 1 [P70399-1]

With	#Exp.	IntAct
PLK1 [P53350] from Homo sapiens.	2	EBI-15790796,EBI-476768

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	205144, 43 interactors
Database of interacting proteins More...DIPⁱ	DIP-31595N
IntActⁱ	P70399, 30 interactors
Molecular INTeraction database More...MINTⁱ	P70399
STRINGⁱ	10090.ENSMUSP00000106278

Miscellaneous databases

RNActⁱ	P70399, protein

RNActⁱ

P70399, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	1487 – 1490	Combined sources	4
Beta strandⁱ	1495 – 1505	Combined sources	11
Turnⁱ	1508 – 1510	Combined sources	3
Beta strandⁱ	1511 – 1515	Combined sources	5
Beta strandⁱ	1521 – 1525	Combined sources	5
Turnⁱ	1526 – 1528	Combined sources	3
Beta strandⁱ	1529 – 1532	Combined sources	4
Beta strandⁱ	1537 – 1545	Combined sources	9
Turnⁱ	1547 – 1549	Combined sources	3
Beta strandⁱ	1551 – 1561	Combined sources	11
Beta strandⁱ	1564 – 1571	Combined sources	8
Beta strandⁱ	1574 – 1578	Combined sources	5
Helixⁱ	1580 – 1582	Combined sources	3
Beta strandⁱ	1583 – 1586	Combined sources	4
Helixⁱ	1587 – 1591	Combined sources	5
Turnⁱ	1592 – 1596	Combined sources	5
Beta strandⁱ	1597 – 1599	Combined sources	3

Show more details

3D structure databases

AlphaFoldDBⁱ	P70399
BMRBⁱ	P70399
SMRⁱ	P70399
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P70399

EvolutionaryTraceⁱ

P70399

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	1749 – 1845	BRCT 1PROSITE-ProRule annotationAdd BLAST		97
Domainⁱ	1861 – 1961	BRCT 2PROSITE-ProRule annotationAdd BLAST		101

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 24	DisorderedSequence analysisAdd BLAST	24
Regionⁱ	67 – 168	DisorderedSequence analysisAdd BLAST	102
Regionⁱ	254 – 337	DisorderedSequence analysisAdd BLAST	84
Regionⁱ	352 – 599	DisorderedSequence analysisAdd BLAST	248
Regionⁱ	614 – 707	DisorderedSequence analysisAdd BLAST	94
Regionⁱ	754 – 870	DisorderedSequence analysisAdd BLAST	117
Regionⁱ	927 – 1017	DisorderedSequence analysisAdd BLAST	91
Regionⁱ	1034 – 1144	DisorderedSequence analysisAdd BLAST	111
Regionⁱ	1178 – 1231	DisorderedSequence analysisAdd BLAST	54
Regionⁱ	1267 – 1478	DisorderedSequence analysisAdd BLAST	212
Regionⁱ	1481 – 1600	Tudor-likeBy similarityAdd BLAST	120
Regionⁱ	1492 – 1520	Interaction with dimethylated histone H4By similarityAdd BLAST	29
Regionⁱ	1624 – 1715	DisorderedSequence analysisAdd BLAST	92

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	1393 – 1400	GARBy similarity		8
Motifⁱ	1601 – 1628	UDRBy similarityAdd BLAST		28

Compositional bias

Feature key	Position(s)	DescriptionActions	Length
Compositional biasⁱ	8 – 24	Polar residuesSequence analysisAdd BLAST	17
Compositional biasⁱ	67 – 82	Polar residuesSequence analysisAdd BLAST	16
Compositional biasⁱ	83 – 97	Basic and acidic residuesSequence analysisAdd BLAST	15
Compositional biasⁱ	98 – 128	Polar residuesSequence analysisAdd BLAST	31
Compositional biasⁱ	261 – 275	Polar residuesSequence analysisAdd BLAST	15
Compositional biasⁱ	296 – 337	Polar residuesSequence analysisAdd BLAST	42
Compositional biasⁱ	352 – 368	Polar residuesSequence analysisAdd BLAST	17
Compositional biasⁱ	424 – 446	Polar residuesSequence analysisAdd BLAST	23
Compositional biasⁱ	483 – 531	Polar residuesSequence analysisAdd BLAST	49
Compositional biasⁱ	532 – 546	Basic and acidic residuesSequence analysisAdd BLAST	15
Compositional biasⁱ	547 – 578	Polar residuesSequence analysisAdd BLAST	32
Compositional biasⁱ	579 – 599	Basic and acidic residuesSequence analysisAdd BLAST	21
Compositional biasⁱ	615 – 632	Polar residuesSequence analysisAdd BLAST	18
Compositional biasⁱ	637 – 653	Basic and acidic residuesSequence analysisAdd BLAST	17
Compositional biasⁱ	661 – 677	Basic and acidic residuesSequence analysisAdd BLAST	17
Compositional biasⁱ	758 – 775	Basic and acidic residuesSequence analysisAdd BLAST	18
Compositional biasⁱ	786 – 818	Basic and acidic residuesSequence analysisAdd BLAST	33
Compositional biasⁱ	931 – 950	Polar residuesSequence analysisAdd BLAST	20
Compositional biasⁱ	987 – 1008	Polar residuesSequence analysisAdd BLAST	22
Compositional biasⁱ	1055 – 1071	Basic and acidic residuesSequence analysisAdd BLAST	17
Compositional biasⁱ	1094 – 1112	Polar residuesSequence analysisAdd BLAST	19
Compositional biasⁱ	1178 – 1199	Polar residuesSequence analysisAdd BLAST	22
Compositional biasⁱ	1213 – 1230	Basic and acidic residuesSequence analysisAdd BLAST	18
Compositional biasⁱ	1281 – 1326	Polar residuesSequence analysisAdd BLAST	46
Compositional biasⁱ	1444 – 1478	Polar residuesSequence analysisAdd BLAST	35
Compositional biasⁱ	1629 – 1658	Polar residuesSequence analysisAdd BLAST	30
Compositional biasⁱ	1666 – 1680	Basic and acidic residuesSequence analysisAdd BLAST	15

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

eggNOGⁱ	KOG3548, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000011891
InParanoidⁱ	P70399
OMAⁱ	PIVDDTC
TreeFamⁱ	TF350227

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd04508, TUDOR, 1 hit
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 IPR036420, BRCT_dom_sf IPR014722, Rib_L2_dom2 IPR002999, Tudor
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

This entry has 3 described isoforms and 7 potential isoforms that are computationally mapped.Show all Align All

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

This isoform has been chosen as the 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.

« Hide

        10         20         30         40         50
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

Checksum:ⁱF673EA87B3BA1FDE

Isoform 2 (identifier: P70399-5) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
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
QRASQEPFSP AEDVMETDLL EGLAANQDRP SKMLMDRPTQ SNIGIQTVDH 
      1160       1170       1180       1190       1200
SLCAPETVSA ATQTVKSVCE QGTSTAEQNS GKQDATVQTE RGSGEKPASA 
      1210       1220       1230       1240       1250
PVDDTESLHS QGEEEFEMPQ PPHGHVLHRH MRTIREVRTL VTRVITDVYY 
      1260       1270       1280       1290       1300
VDGTEVERKV TEETEEPIVE CQECETEVSP SQTGGSSGDL GDISSFSSKA 
      1310       1320       1330       1340       1350
SSSHHTSSGT SLSAIHSSGS SGRGAGPLKG KASGTEAADF ALPSSRGGPG 
      1360       1370       1380       1390       1400
KLSPRKGISQ TGAPVCEEDG DAGLGIRQGG KAPVTPRGRG RRGRPPSRTT 
      1410       1420       1430       1440       1450
GTRETVVSGP LGVEDISPSM SPDDKSFTRI MPRVPDSTKR TDASSSTLRR 
      1460       1470       1480       1490       1500
SDSPEIPFQA ATGSSDGLDS SSSGNSFVGL RVVAKWSSNG YFYSGKITRD 
      1510       1520       1530       1540       1550
VGAGKYKLLF DDGYECDVLG KDILLCDPIP LDTEVTALSE DEYFSAGVVK 
      1560       1570       1580       1590       1600
GHRKESGELY YSIEKEGQRK WYKRMAVILS LEQGNRLREQ YGLGPYEAVT 
      1610       1620       1630       1640       1650
PLTKAADISL DNLVEGKRKR RSNISSPVTP TAASSSSTTP TRKATESPRA 
      1660       1670       1680       1690       1700
STGVPSGKRK LPTSEEERSP AKRGRKSATV KPGTVGAAEF VSPCETGDNI 
      1710       1720       1730       1740       1750
GEPSVLEEPR GPLPLNKTLF LGYAFLLTMA TTSDKLASRS KLLDGPTGSS 
      1760       1770       1780       1790       1800
EEEEEFLEIP PFNKQYTECQ LRAGAGYILE DFNEAQCNTA YQCLLIADQH 
      1810       1820       1830       1840       1850
CRTRKYFLCL ASGIPCVSHV WVHDSCHANQ LQNYRNYLLP AGYSLEEQRI 
      1860       1870       1880       1890       1900
LDWQPRENPF QNLKVLLVSD QQQNFLELWS EILMTGGAAS VKQHHSSAHN 
      1910       1920       1930       1940       1950
KDIALGVFDV VVTDPSCPAS VLKCAEALQL PVVSQEWVIQ CLIVGERIGF 
      1960 
KQHPKYKHDY VSH

Show »

Length:1,963

Mass (Da):212,035

Checksum:ⁱ1F0204D04D0E7129

Isoform 3 (identifier: P70399-6) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MVEINDPLLG NEKGDSESAP EMDGKLSLKM KLVSPETEAS EESLQFSLEK 
        60         70         80         90        100
PTTAERKNGS TAIAEPVASL QKPVPVFGCI YEAQQEKEAQ SEAPPSAPDR 
       110        120        130        140        150
ANLLHFPSAQ EEDKERPDVT PKLRQSEQPV KPVGPVMDDA APEDSASPVS 
       160        170        180        190        200
QQRASQEPFS PAEDVMETDL LEGLAANQDR PSKMLMDRPT QSNIGIQTVD 
       210        220        230        240        250
HSLCAPETVS AATQTVKSVC EQGTSTAEQN SGKQDATVQT ERGSGEKPAS 
       260        270        280        290        300
APVDDTESLH SQGEEEFEMP QPPHGHVLHR HMRTIREVRT LVTRVITDVY 
       310        320        330        340        350
YVDGTEVERK VTEETEEPIV ECQECETEVS PSQTGGSSGD LGDISSFSSK 
       360        370        380        390        400
ASSSHHTSSG TSLSAIHSSG SSGRGAGPLK GKASGTEAAD FALPSSRGGP 
       410        420        430        440        450
GKLSPRKGIS QTGAPVCEED GDAGLGIRQG GKAPVTPRGR GRRGRPPSRT 
       460        470        480        490        500
TGTRETVVSG PLGVEDISPS MSPDDKSFTR IMPRVPDSTK RTDASSSTLR 
       510        520        530        540        550
RSDSPEIPFQ AATGSSDGLD SSSSGNSFVG LRVVAKWSSN GYFYSGKITR 
       560        570        580        590        600
DVGAGKYKLL FDDGYECDVL GKDILLCDPI PLDTEVTALS EDEYFSAGVV 
       610        620        630        640        650
KGHRKESGEL YYSIEKEGQR KWYKRMAVIL SLEQGNRLRE QYGLGPYEAV 
       660        670        680        690        700
TPLTKAADIS LDNLVEGKRK RRSNISSPVT PTAASSSSTT PTRKATESPR 
       710        720        730        740        750
ASTGVPSGKR KLPTSEEERS PAKRGRKSAT VKPGTVGAAE FVSPCETGDN 
       760        770        780        790        800
IGEPSVLEEP RGPLPLNKTL FLGYAFLLTM ATTSDKLASR SKLLDGPTGS 
       810        820        830        840        850
SEEEEEFLEI PPFNKQYTEC QLRAGAGYIL EDFNEAQCNT AYQCLLIADQ 
       860        870        880        890        900
HCRTRKYFLC LASGIPCVSH VWVHDSCHAN QLQNYRNYLL PAGYSLEEQR 
       910        920        930        940        950
ILDWQPRENP FQNLKVLLVS DQQQNFLELW SEILMTGGAA SVKQHHSSAH 
       960        970        980        990       1000
NKDIALGVFD VVVTDPSCPA SVLKCAEALQ LPVVSQEWVI QCLIVGERIG 
      1010 
FKQHPKYKHD YVSH

Show »

Length:1,014

Mass (Da):109,745

Checksum:ⁱ52E51794028163EA

Computationally mapped potential isoform sequencesⁱ

There are 7 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0A5H1ZRL7	A0A5H1ZRL7_MOUSE	Transformation-related protein 53-b... Transformation-related protein 53-binding protein 1	Trp53bp1	1,919	Annotation score:
F6ZRL3	F6ZRL3_MOUSE	Transformation-related protein 53-b... Transformation-related protein 53-binding protein 1	Trp53bp1	166	Annotation score:
F6QNC8	F6QNC8_MOUSE	Transformation-related protein 53-b... Transformation-related protein 53-binding protein 1	Trp53bp1	190	Annotation score:
F6VCK5	F6VCK5_MOUSE	Transformation-related protein 53-b... Transformation-related protein 53-binding protein 1	Trp53bp1	59	Annotation score:
A2AU90	A2AU90_MOUSE	Transformation-related protein 53-b... Transformation-related protein 53-binding protein 1	Trp53bp1	1,018	Annotation score:
F6S5E4	F6S5E4_MOUSE	Transformation-related protein 53-b... Transformation-related protein 53-binding protein 1	Trp53bp1	81	Annotation score:
F7CE65	F7CE65_MOUSE	Transformation-related protein 53-b... Transformation-related protein 53-binding protein 1	Trp53bp1	48	Annotation score:

Sequence cautionⁱ

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

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	145	Missing in CAC94013 (PubMed:11801725).Curated	1
Sequence conflictⁱ	401	V → A in CAC94013 (PubMed:11801725).Curated	1
Sequence conflictⁱ	427	A → T in CAC94013 (PubMed:11801725).Curated	1
Sequence conflictⁱ	675	P → A in CAC94013 (PubMed:11801725).Curated	1
Sequence conflictⁱ	1070	P → L in AAH79906 (PubMed:15489334).Curated	1
Sequence conflictⁱ	1071	K → N in AAH35206 (PubMed:15489334).Curated	1
Sequence conflictⁱ	1183 – 1184	EQ → DE in AAC52876 (PubMed:8910340).Curated	2
Sequence conflictⁱ	1187	G → R in CAC94013 (PubMed:11801725).Curated	1
Sequence conflictⁱ	1206	A → T in AAC52876 (PubMed:8910340).Curated	1
Sequence conflictⁱ	1271	E → G in AAC52876 (PubMed:8910340).Curated	1
Sequence conflictⁱ	1359 – 1408	Missing in AAH79906 (PubMed:15489334).CuratedAdd BLAST	50
Sequence conflictⁱ	1771	Q → H in AAH79906 (PubMed:15489334).Curated	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_058926	1 – 949	Missing in isoform 3. Add BLAST		949
Alternative sequenceⁱVSP_058927	1101 – 1106	Missing in isoform 2 and isoform 3.		6

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
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

Ensemblⁱ	ENSMUST00000110648; ENSMUSP00000106278; ENSMUSG00000043909 [P70399-1]
GeneIDⁱ	27223
KEGGⁱ	mmu:27223
UCSC genome browser More...UCSCⁱ	uc008lye.4, mouse

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P70399	Uncharacterized protein (Fragment)		MOUSE		689	UniRef100_P70399
+4

Protein	Similar proteins		Species	Score	Length	Source
P70399	Uncharacterized protein (Fragment)		MOUSE		689	UniRef90_P70399
Transformation related protein 53 binding protein 1		MUSSI		1968
Tumor protein p53-binding protein 1		RAT		1932
Isoform 2 of TP53-binding protein 1		MOUSE		1963
Isoform 3 of TP53-binding protein 1		MOUSE		1014
+18

Protein	Similar proteins		Species	Score	Length	Source
P70399	TP53-binding protein 1	)	HUMAN		1972	UniRef50_Q12888
Tumor protein p53 binding protein 1		CERAT		1979
Tumor protein p53 binding protein 1		MACFA		1977
tumor suppressor p53-binding protein 1 isoform X2		MICMU		1977
TP53-binding protein 1		Ugandan red Colobus		1977
+882

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
CCDSⁱ	CCDS50684.1 [P70399-1]
RefSeqⁱ	NP_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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1SSF	NMR	-	A	1475-1629	[»]
AlphaFoldDBⁱ	P70399
BMRBⁱ	P70399
SMRⁱ	P70399
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	205144, 43 interactors
DIPⁱ	DIP-31595N
IntActⁱ	P70399, 30 interactors
MINTⁱ	P70399
STRINGⁱ	10090.ENSMUSP00000106278

Chemistry databases

ChEMBLⁱ	CHEMBL4295790

ChEMBLⁱ

CHEMBL4295790

PTM databases

iPTMnetⁱ	P70399
PhosphoSitePlusⁱ	P70399
SwissPalmⁱ	P70399

Proteomic databases

EPDⁱ	P70399
jPOSTⁱ	P70399
MaxQBⁱ	P70399
PaxDbⁱ	P70399
PeptideAtlasⁱ	P70399
PRIDEⁱ	P70399
ProteomicsDBⁱ	260722 [P70399-1] 260723 [P70399-5] 260724 [P70399-6]

Protocols and materials databases

Antibodypediaⁱ	1749, 960 antibodies from 40 providers
The DNASU plasmid repository More...DNASUⁱ	27223

Genome annotation databases

Ensemblⁱ	ENSMUST00000110648; ENSMUSP00000106278; ENSMUSG00000043909 [P70399-1]
GeneIDⁱ	27223
KEGGⁱ	mmu:27223
UCSCⁱ	uc008lye.4, mouse

Organism-specific databases

CTDⁱ	27223
MGIⁱ	MGI:1351320, Trp53bp1
VEuPathDBⁱ	HostDB:ENSMUSG00000043909

Phylogenomic databases

eggNOGⁱ	KOG3548, Eukaryota
GeneTreeⁱ	ENSGT00390000011891
InParanoidⁱ	P70399
OMAⁱ	PIVDDTC
TreeFamⁱ	TF350227

Enzyme and pathway databases

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

Reactomeⁱ

Miscellaneous databases

BioGRID-ORCSⁱ	27223, 4 hits in 110 CRISPR screens
ChiTaRSⁱ	Trp53bp1, mouse
EvolutionaryTraceⁱ	P70399
Protein Ontology More...PROⁱ	PR:P70399
RNActⁱ	P70399, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000043909, Expressed in secondary oocyte and 313 other tissues
ExpressionAtlasⁱ	P70399, baseline and differential

Family and domain databases

CDDⁱ	cd04508, TUDOR, 1 hit
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 IPR036420, BRCT_dom_sf IPR014722, Rib_L2_dom2 IPR002999, Tudor
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
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	TP53B_MOUSE
Accessionⁱ	P70399Primary (citable) accession number: P70399 Secondary accession number(s): A2AU89 , A2AU91, Q68FD0, Q8CI97, Q91YC9
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
	Last sequence update:	May 10, 2017
	Last modified:	May 25, 2022
	This is version 182 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P70399 (TP53B_MOUSE)

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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

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

Nucleus

Other locations

Nucleus

Other locations

Keywords - 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

Chemistry 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

Keywords - PTMi

Proteomic databases

PTM 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

<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

Isoform 1 [P70399-1]

GO - Molecular functioni

Protein-protein interaction databases

Miscellaneous 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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<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

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

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Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM 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

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<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

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ