UniProtKB - P70399 (TP53B_MOUSE)
TP53-binding protein 1
Tp53bp1
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 PublicationsGO - Molecular functioni
- damaged DNA binding Source: MGI
- histone binding Source: GO_Central
- methylated histone binding Source: UniProtKB
- p53 binding Source: MGI
- RNA polymerase II-specific DNA-binding transcription factor binding Source: MGI
- sequence-specific DNA binding Source: MGI
- telomeric DNA binding Source: MGI
- transcription coregulator activity Source: MGI
- ubiquitin modification-dependent histone binding Source: UniProtKB
GO - Biological processi
- cellular response to DNA damage stimulus Source: MGI
- cellular response to X-ray Source: Ensembl
- DNA damage checkpoint signaling Source: GO_Central
- DNA repair Source: MGI
- double-strand break repair via nonhomologous end joining Source: UniProtKB
- negative regulation of double-strand break repair via homologous recombination Source: UniProtKB
- positive regulation of isotype switching Source: UniProtKB
- positive regulation of transcription by RNA polymerase II Source: MGI
- protein homooligomerization Source: UniProtKB
- regulation of transcription, DNA-templated Source: MGI
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 |
Names & Taxonomyi
Protein namesi | Recommended name: TP53-binding protein 1CuratedShort 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 | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1351320, Trp53bp1 |
VEuPathDBi | HostDB:ENSMUSG00000043909 |
Subcellular locationi
Nucleus
- Nucleus 1 Publication
Other locations
- Chromosome 5 Publications
- kinetochore 1 Publication
Note: Localizes to the nucleus in absence of DNA damage (PubMed:11801725). Following DNA damage, recruited to sites of DNA damage, such as double stand breaks (DSBs) (PubMed:11673449, PubMed:23209566, PubMed:23333305, PubMed:23306439). 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:23209566). Associated with kinetochores during mitosis (PubMed:11801725).5 Publications
Nucleus
- nuclear body Source: MGI
- nucleoplasm Source: MGI
- nucleus Source: MGI
Other locations
- chromosome, telomeric region Source: MGI
- cytoplasm Source: MGI
- DNA repair complex Source: MGI
- kinetochore Source: MGI
- replication fork Source: MGI
- site of double-strand break Source: UniProtKB
Keywords - Cellular componenti
Centromere, Chromosome, Kinetochore, NucleusPathology & Biotechi
Disruption phenotypei
Chemistry databases
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 | Graphical view | 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
Keywords - PTMi
Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | P70399 |
jPOSTi | P70399 |
MaxQBi | P70399 |
PaxDbi | P70399 |
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 PublicationsBinary interactionsi
Isoform 1 [P70399-1]
With | #Exp. | IntAct |
---|---|---|
PLK1 [P53350] from Homo sapiens. | 2 | EBI-15790796,EBI-476768 |
GO - Molecular functioni
- histone binding Source: GO_Central
- methylated histone binding Source: UniProtKB
- p53 binding Source: MGI
- RNA polymerase II-specific DNA-binding transcription factor binding Source: MGI
- ubiquitin modification-dependent histone binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 205144, 43 interactors |
DIPi | DIP-31595N |
IntActi | P70399, 30 interactors |
MINTi | P70399 |
STRINGi | 10090.ENSMUSP00000106278 |
Miscellaneous databases
RNActi | P70399, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P70399 |
BMRBi | P70399 |
SMRi | P70399 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
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 | Graphical view | 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 | Graphical view | 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
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG3548, Eukaryota |
GeneTreei | ENSGT00390000011891 |
InParanoidi | P70399 |
OMAi | PIVDDTC |
TreeFami | TF350227 |
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 |
s (3+)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 3 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A5H1ZRL7 | A0A5H1ZRL7_MOUSE | Transformation-related protein 53-b... | Trp53bp1 | 1,919 | Annotation score: | ||
F6ZRL3 | F6ZRL3_MOUSE | Transformation-related protein 53-b... | Trp53bp1 | 166 | Annotation score: | ||
F6QNC8 | F6QNC8_MOUSE | Transformation-related protein 53-b... | Trp53bp1 | 190 | Annotation score: | ||
F6VCK5 | F6VCK5_MOUSE | Transformation-related protein 53-b... | Trp53bp1 | 59 | Annotation score: | ||
A2AU90 | A2AU90_MOUSE | Transformation-related protein 53-b... | Trp53bp1 | 1,018 | Annotation score: | ||
F6S5E4 | F6S5E4_MOUSE | Transformation-related protein 53-b... | Trp53bp1 | 81 | Annotation score: | ||
F7CE65 | F7CE65_MOUSE | Transformation-related protein 53-b... | Trp53bp1 | 48 | Annotation score: |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | 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 |
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] |
Genome annotation databases
Ensembli | ENSMUST00000110648; ENSMUSP00000106278; ENSMUSG00000043909 [P70399-1] |
GeneIDi | 27223 |
KEGGi | mmu:27223 |
UCSCi | uc008lye.4, mouse |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
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: PDBei RCSB PDBi 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 |
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 |
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 |
Miscellaneous databases
BioGRID-ORCSi | 27223, 4 hits in 110 CRISPR screens |
ChiTaRSi | Trp53bp1, mouse |
EvolutionaryTracei | P70399 |
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 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 proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references