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Protein

TP53-binding protein 1

Gene

Tp53bp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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). In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites. Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites. Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:15159415, PubMed:15077110). Participates to the repair and the orientation of the broken DNA ends during CSR (PubMed:26308889). In contrast, it is not required for classic NHEJ and V(D)J recombination (PubMed:15159415). Promotes NHEJ of dysfunctional telomeres (By similarity).By similarity6 Publications

GO - Molecular functioni

  • damaged DNA binding Source: MGI
  • histone binding Source: GO_Central
  • methylated histone binding Source: UniProtKB
  • p53 binding Source: MGI
  • RNA polymerase II activating transcription factor binding Source: MGI
  • RNA polymerase II transcription cofactor activity Source: MGI
  • sequence-specific DNA binding Source: MGI
  • telomeric DNA binding Source: MGI
  • transcription factor binding Source: MGI

GO - Biological processi

Keywordsi

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

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componentsi: Chromosome 2, Unplaced

Organism-specific databases

MGIiMGI:1351320. Trp53bp1.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • DNA repair complex Source: MGI
  • kinetochore Source: MGI
  • nuclear body Source: MGI
  • nuclear chromosome, telomeric region Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • replication fork Source: MGI

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000726441 – 1969TP53-binding protein 1Add BLAST1969

Amino acid modifications

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

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

EPDiP70399.
MaxQBiP70399.
PaxDbiP70399.
PeptideAtlasiP70399.
PRIDEiP70399.

PTM databases

iPTMnetiP70399.
PhosphoSitePlusiP70399.

Interactioni

Subunit structurei

Homoligomer (By similarity). Interacts with p53/TP53 (via the central domain) (By similarity). Interacts with DCLRE1C (By similarity). Interacts with histone H2AFX and this requires phosphorylation of H2AFX on 'Ser-139' (By similarity). Interacts with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2) (PubMed:23209566). Has low affinity for histone H4 containing monomethylated 'Lys-20' (H4K20me1) (By similarity). Does not bind histone H4 containing unmethylated or trimethylated 'Lys-20' (H4K20me3) (By similarity). Has low affinity for histone H3 that has been dimethylated on 'Lys-79' (By similarity). Has very low affinity for histone H3 that has been monomethylated on 'Lys-79' (in vitro) (By similarity). Does not bind unmethylated histone H3 (By similarity). Interacts with histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) (By similarity). Interacts with MUM1/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).By similarity4 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi205144. 30 interactors.
DIPiDIP-31595N.
IntActiP70399. 6 interactors.
MINTiMINT-136714.
STRINGi10090.ENSMUSP00000106278.

Structurei

Secondary structure

11969
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1487 – 1490Combined sources4
Beta strandi1495 – 1505Combined sources11
Turni1508 – 1510Combined sources3
Beta strandi1511 – 1515Combined sources5
Beta strandi1521 – 1525Combined sources5
Turni1526 – 1528Combined sources3
Beta strandi1529 – 1532Combined sources4
Beta strandi1537 – 1545Combined sources9
Turni1547 – 1549Combined sources3
Beta strandi1551 – 1561Combined sources11
Beta strandi1564 – 1571Combined sources8
Beta strandi1574 – 1578Combined sources5
Helixi1580 – 1582Combined sources3
Beta strandi1583 – 1586Combined sources4
Helixi1587 – 1591Combined sources5
Turni1592 – 1596Combined sources5
Beta strandi1597 – 1599Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SSFNMR-A1475-1629[»]
ProteinModelPortaliP70399.
SMRiP70399.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70399.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1749 – 1845BRCT 1PROSITE-ProRule annotationAdd BLAST97
Domaini1861 – 1961BRCT 2PROSITE-ProRule annotationAdd BLAST101

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1481 – 1600Tudor-likeBy similarityAdd BLAST120
Regioni1492 – 1520Interaction with dimethylated histone H4By similarityAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1393 – 1400GARBy similarity8
Motifi1601 – 1628UDRBy similarityAdd BLAST28

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi136 – 149Poly-GluAdd BLAST14
Compositional biasi637 – 814Glu-richAdd BLAST178
Compositional biasi1285 – 1327Ser-richAdd BLAST43
Compositional biasi1476 – 1479Poly-Ser4
Compositional biasi1640 – 1643Poly-Ser4
Compositional biasi1757 – 1761Poly-Glu5

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

eggNOGiKOG3548. Eukaryota.
ENOG411075K. LUCA.
GeneTreeiENSGT00390000011891.
HOGENOMiHOG000231961.
HOVERGENiHBG060882.
InParanoidiP70399.
KOiK20915.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di2.30.30.30. 1 hit.
3.40.50.10190. 2 hits.
InterProiView protein in InterPro
IPR015125. 53-BP1_Tudor.
IPR001357. BRCT_dom.
IPR014722. Rib_L2_dom2.
PfamiView protein in Pfam
PF09038. 53-BP1_Tudor. 1 hit.
SMARTiView protein in SMART
SM00292. BRCT. 2 hits.
SUPFAMiSSF52113. SSF52113. 2 hits.
PROSITEiView protein in PROSITE
PS50172. BRCT. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P70399-1) [UniParc]FASTAAdd 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
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
GO
Isoform 2 (identifier: P70399-5) [UniParc]FASTAAdd to basket

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

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

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

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

Sequence cautioni

The sequence AAH79906 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti145Missing in CAC94013 (PubMed:11801725).Curated1
Sequence conflicti401V → A in CAC94013 (PubMed:11801725).Curated1
Sequence conflicti427A → T in CAC94013 (PubMed:11801725).Curated1
Sequence conflicti675P → A in CAC94013 (PubMed:11801725).Curated1
Sequence conflicti1070P → L in AAH79906 (PubMed:15489334).Curated1
Sequence conflicti1071K → N in AAH35206 (PubMed:15489334).Curated1
Sequence conflicti1183 – 1184EQ → DE in AAC52876 (PubMed:8910340).Curated2
Sequence conflicti1187G → R in CAC94013 (PubMed:11801725).Curated1
Sequence conflicti1206A → T in AAC52876 (PubMed:8910340).Curated1
Sequence conflicti1271E → G in AAC52876 (PubMed:8910340).Curated1
Sequence conflicti1359 – 1408Missing in AAH79906 (PubMed:15489334).CuratedAdd BLAST50
Sequence conflicti1771Q → H in AAH79906 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0589261 – 949Missing in isoform 3. Add BLAST949
Alternative sequenceiVSP_0589271101 – 1106Missing in isoform 2 and isoform 3. 6

Sequence databases

Select the link destinations:
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.
RefSeqiNP_001277759.1. NM_001290830.1.
NP_038763.3. NM_013735.4.
UniGeneiMm.215389.
Mm.383499.
Mm.481841.

Genome annotation databases

EnsembliENSMUST00000110647; ENSMUSP00000106277; ENSMUSG00000043909.
ENSMUST00000110648; ENSMUSP00000106278; ENSMUSG00000043909.
GeneIDi27223.
KEGGimmu:27223.
UCSCiuc008lye.4. mouse.
uc012cco.3. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

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.
RefSeqiNP_001277759.1. NM_001290830.1.
NP_038763.3. NM_013735.4.
UniGeneiMm.215389.
Mm.383499.
Mm.481841.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SSFNMR-A1475-1629[»]
ProteinModelPortaliP70399.
SMRiP70399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205144. 30 interactors.
DIPiDIP-31595N.
IntActiP70399. 6 interactors.
MINTiMINT-136714.
STRINGi10090.ENSMUSP00000106278.

PTM databases

iPTMnetiP70399.
PhosphoSitePlusiP70399.

Proteomic databases

EPDiP70399.
MaxQBiP70399.
PaxDbiP70399.
PeptideAtlasiP70399.
PRIDEiP70399.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000110647; ENSMUSP00000106277; ENSMUSG00000043909.
ENSMUST00000110648; ENSMUSP00000106278; ENSMUSG00000043909.
GeneIDi27223.
KEGGimmu:27223.
UCSCiuc008lye.4. mouse.
uc012cco.3. mouse.

Organism-specific databases

CTDi27223.
MGIiMGI:1351320. Trp53bp1.

Phylogenomic databases

eggNOGiKOG3548. Eukaryota.
ENOG411075K. LUCA.
GeneTreeiENSGT00390000011891.
HOGENOMiHOG000231961.
HOVERGENiHBG060882.
InParanoidiP70399.
KOiK20915.

Miscellaneous databases

EvolutionaryTraceiP70399.
PROiPR:P70399.
SOURCEiSearch...

Family and domain databases

CDDicd00027. BRCT. 1 hit.
Gene3Di2.30.30.30. 1 hit.
3.40.50.10190. 2 hits.
InterProiView protein in InterPro
IPR015125. 53-BP1_Tudor.
IPR001357. BRCT_dom.
IPR014722. Rib_L2_dom2.
PfamiView protein in Pfam
PF09038. 53-BP1_Tudor. 1 hit.
SMARTiView protein in SMART
SM00292. BRCT. 2 hits.
SUPFAMiSSF52113. SSF52113. 2 hits.
PROSITEiView protein in PROSITE
PS50172. BRCT. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiTP53B_MOUSE
AccessioniPrimary (citable) accession number: P70399
Secondary accession number(s): A2AU89
, A2AU91, Q68FD0, Q8CI97, Q91YC9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 10, 2017
Last modified: May 10, 2017
This is version 148 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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.