SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P70399

- TP53B_MOUSE

UniProt

P70399 - TP53B_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tumor suppressor p53-binding protein 1

Gene
Tp53bp1, Trp53bp1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a key role in the response to DNA damage. May have a role in checkpoint signaling during mitosis. Enhances TP53-mediated transcriptional activation By similarity.1 Publication

GO - Molecular functioni

  1. damaged DNA binding Source: MGI
  2. methylated histone binding Source: UniProtKB
  3. protein binding Source: MGI
  4. telomeric DNA binding Source: MGI
  5. transcription factor binding Source: MGI

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: MGI
  2. DNA repair Source: MGI
  3. regulation of transcription, DNA-templated Source: MGI
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor suppressor p53-binding protein 1
Short name:
53BP1
Short name:
p53-binding protein 1
Short name:
p53BP1
Gene namesi
Name:Tp53bp1
Synonyms:Trp53bp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:1351320. Trp53bp1.

Subcellular locationi

Nucleus. Chromosomecentromerekinetochore
Note: Associated with kinetochores. Both nuclear and cytoplasmic in some cells. Recruited to sites of DNA damage, such as double stand breaks. H4K20me2 is required for efficient localization to double strand breaks and removal of proteins that have a high affinity for H4K20me2 such as L3MBTL1 and KDM4A is needed By similarity.1 Publication

GO - Cellular componenti

  1. condensed chromosome kinetochore Source: UniProtKB-SubCell
  2. kinetochore Source: MGI
  3. nucleus Source: MGI
  4. replication fork Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19571957Tumor suppressor p53-binding protein 1PRO_0000072644Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Phosphoserine By similarity
Modified residuei104 – 1041Phosphoserine By similarity
Modified residuei163 – 1631Phosphoserine By similarity
Modified residuei262 – 2621Phosphoserine By similarity
Modified residuei291 – 2911Phosphoserine By similarity
Modified residuei299 – 2991Phosphothreonine By similarity
Modified residuei362 – 3621Phosphoserine By similarity
Modified residuei376 – 3761Phosphoserine By similarity
Modified residuei391 – 3911Phosphoserine By similarity
Modified residuei446 – 4461Phosphoserine By similarity
Modified residuei517 – 5171Phosphoserine By similarity
Modified residuei519 – 5191Phosphoserine By similarity
Modified residuei537 – 5371Phosphothreonine By similarity
Modified residuei542 – 5421Phosphothreonine By similarity
Modified residuei546 – 5461Phosphoserine1 Publication
Modified residuei573 – 5731Phosphoserine By similarity
Modified residuei621 – 6211Phosphoserine By similarity
Modified residuei625 – 6251Phosphoserine By similarity
Modified residuei626 – 6261Phosphoserine By similarity
Modified residuei906 – 9061Phosphothreonine By similarity
Modified residuei959 – 9591Phosphoserine By similarity
Modified residuei1012 – 10121Phosphoserine By similarity
Modified residuei1069 – 10691Phosphoserine By similarity
Modified residuei1090 – 10901Phosphoserine By similarity
Modified residuei1103 – 11031Phosphoserine1 Publication
Modified residuei1199 – 11991Phosphothreonine By similarity
Modified residuei1201 – 12011Phosphoserine By similarity
Modified residuei1204 – 12041Phosphoserine By similarity
Modified residuei1347 – 13471Phosphoserine By similarity
Modified residuei1353 – 13531Phosphoserine By similarity
Modified residuei1411 – 14111Phosphoserine By similarity
Modified residuei1415 – 14151Phosphoserine By similarity
Modified residuei1445 – 14451Phosphoserine By similarity
Modified residuei1447 – 14471Phosphoserine By similarity
Modified residuei1459 – 14591Phosphoserine By similarity
Modified residuei1594 – 15941Phosphothreonine By similarity
Modified residuei1603 – 16031Phosphoserine By similarity
Modified residuei1663 – 16631Phosphoserine By similarity
Modified residuei1686 – 16861Phosphoserine By similarity
Modified residuei1744 – 17441Phosphoserine By similarity

Post-translational modificationi

Asymmetrically dimethylated on Arg residues by PRMT1. Methylation is required for DNA binding By similarity.
Phosphorylated at basal level in the absence of DNA damage. Hyper-phosphorylated in an ATM-dependent manner in response to DNA damage induced by ionizing radiation. Hyper-phosphorylated in an ATR-dependent manner in response to DNA damage induced by UV irradiation. Dephosphorylated by PPP5C By similarity.1 Publication

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP70399.
PaxDbiP70399.
PRIDEiP70399.

PTM databases

PhosphoSiteiP70399.

Expressioni

Gene expression databases

GenevestigatoriP70399.

Interactioni

Subunit structurei

May form homooligomers. Interacts with DCLRE1C. Interacts with histone H2AFX and this requires phosphorylation of H2AFX on 'Ser-139'. Interacts with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Has low affinity for histone H4 containing monomethylated 'Lys-20' (H4K20me1). Does not bind histone H4 containing unmethylated or trimethylated 'Lys-20' (H4K20me3). Has low affinity for histone H3 that has been dimethylated on 'Lys-79'. Has very low affinity for histone H3 that has been monomethylated on 'Lys-79' (in vitro). Does not bind unmethylated histone H3. Interacts with MUM1/EXPAND1. Interacts with CHEK2; modulates CHEK2 phosphorylation at 'Thr-68' in response to infrared By similarity. Binds to the central domain of p53/TP53. Interacts with IFI202A. Interacts with MSL1; this interaction may be required for MSL1 DNA repair activity, but not for histone acetyltransferase activity.1 Publication

Protein-protein interaction databases

BioGridi205144. 13 interactions.
DIPiDIP-31595N.
IntActiP70399. 5 interactions.
MINTiMINT-136714.

Structurei

Secondary structure

1
1957
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1475 – 14784
Beta strandi1483 – 149311
Turni1496 – 14983
Beta strandi1499 – 15035
Beta strandi1509 – 15135
Turni1514 – 15163
Beta strandi1517 – 15204
Beta strandi1525 – 15339
Turni1535 – 15373
Beta strandi1539 – 154911
Beta strandi1552 – 15598
Beta strandi1562 – 15665
Helixi1568 – 15703
Beta strandi1571 – 15744
Helixi1575 – 15795
Turni1580 – 15845
Beta strandi1585 – 15873

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SSFNMR-A1463-1617[»]
ProteinModelPortaliP70399.
SMRiP70399. Positions 1470-1588, 1709-1956.

Miscellaneous databases

EvolutionaryTraceiP70399.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1737 – 183397BRCT 1Add
BLAST
Domaini1849 – 1949101BRCT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1468 – 1589122Tudor-like By similarityAdd
BLAST
Regioni1480 – 150829Interaction with dimethylated histone H4 By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1381 – 13888GAR

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi131 – 14313Poly-GluAdd
BLAST
Compositional biasi631 – 808178Glu-richAdd
BLAST
Compositional biasi1273 – 131543Ser-richAdd
BLAST
Compositional biasi1464 – 14674Poly-Ser
Compositional biasi1628 – 16314Poly-Ser
Compositional biasi1745 – 17495Poly-Glu

Sequence similaritiesi

Contains 2 BRCT domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG264535.
HOGENOMiHOG000231961.
HOVERGENiHBG060882.
InParanoidiP70399.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
3.40.50.10190. 2 hits.
InterProiIPR015125. 53-BP1_Tudor.
IPR001357. BRCT_dom.
IPR014722. Rib_L2_dom2.
[Graphical view]
PfamiPF09038. 53-BP1_Tudor. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 2 hits.
[Graphical view]
SUPFAMiSSF52113. SSF52113. 2 hits.
PROSITEiPS50172. BRCT. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

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

MDPTGSQLDS DFSQQDTPCL IIEDSQPESQ VLEEDAGSHF SVLSRHLPNL     50
QMHKENPVLD IVSNPEQSAV EQGDSNSSFN EHLKEKKASD PVESSHLGTS 100
GSISQVIERL PQPNRTSSAL AVTVEAASLP EEEKEEEELE EKEGVGANAP 150
GADSLAAEDS ASSQLGFGVL ELSQSQDVEE HTVPYDVNQE HLQLVTTNSG 200
SSPLSDVDAS TAIKCEEQPT EDIAMIEQPS KDIPVTVQPG KGIHVVEEQN 250
LPLVRSEDRP SSPQVSVAAV ETKEQVPARE LLEEGPQVQP SSEPEVSSTQ 300
EDLFDQSSKT ASDGCSTPSR EEGGCSPVST PATTLQLLQL SGQKPLVQES 350
LSTNSSDLVA PSPDAFRSTP FIVPSSPTEQ GGRKDEPMDM SVIPAGGEPF 400
QKLHDDEAME TEKPLLPSQP TVSPQASTPV SRSTPVFTPG SLPIPSQPEF 450
SHDIFIPSPS LEEPSDDVKK GGGLHSSSLT VECSKTSESE PKNFTDDLGL 500
SMTGDSCKLM LSTSEYSQSS KMESLGSPRT EEDRENTQID DTEPLSPVSN 550
SKLPADSENV LVTPSQDDQV EMSQNVDKAK EDETEDRGDC KGREDAVAED 600
VCIDLTCDSG SQAVPSPATR SEALSSVLDQ EEAMDTKEHH PEEGFSGSEV 650
EEVPETPCGS HREEPKEEAM ESIPLHLSLT ETQSEALCLQ KEAPKEECPE 700
AMEVETSVIS IDSPQKLQVL DQELEHKDPD TWEEATSEDS SVVIVDVKEP 750
SPRADVSCEP LEEVEKCSDS QSWEGVAPEE EPCAENRLDT PEEKRIECDG 800
DSKAETTEKD AVTEDSPQPP LPSVRDEPVR PDQETQQPQV QEKESPVTVD 850
AEVADDKQLG PEGACQQLEK APACASQSFC ESSSETPFHF TLPKEGDIIP 900
PLTGATPPLI GHLKLEPKRH STPIGISNYP ESTIATSDVT SESMVEINDP 950
LLGNEKGDSE SAPEMDGKLS LKMKLVSPET EASEESLQFS LEKPTTAERK 1000
NGSTAIAEPV ASLQKPVPVF GCIYEAQQEK EAQSEAPPSA PDRANLLHFP 1050
SAQEEDKERP DVTPKLRQSE QPVKPVGPVM DDAAPEDSAS PVSQQRASQE 1100
PFSPAEDVME TDLLEGLAAN QDRPSKMLMD RPTQSNIGIQ TVDHSLCAPE 1150
TVSAATQTVK SVCEQGTSTA EQNSGKQDAT VQTERGSGEK PASAPVDDTE 1200
SLHSQGEEEF EMPQPPHGHV LHRHMRTIRE VRTLVTRVIT DVYYVDGTEV 1250
ERKVTEETEE PIVECQECET EVSPSQTGGS SGDLGDISSF SSKASSSHHT 1300
SSGTSLSAIH SSGSSGRGAG PLKGKASGTE AADFALPSSR GGPGKLSPRK 1350
GISQTGAPVC EEDGDAGLGI RQGGKAPVTP RGRGRRGRPP SRTTGTRETV 1400
VSGPLGVEDI SPSMSPDDKS FTRIMPRVPD STKRTDASSS TLRRSDSPEI 1450
PFQAATGSSD GLDSSSSGNS FVGLRVVAKW SSNGYFYSGK ITRDVGAGKY 1500
KLLFDDGYEC DVLGKDILLC DPIPLDTEVT ALSEDEYFSA GVVKGHRKES 1550
GELYYSIEKE GQRKWYKRMA VILSLEQGNR LREQYGLGPY EAVTPLTKAA 1600
DISLDNLVEG KRKRRSNISS PVTPTAASSS STTPTRKATE SPRASTGVPS 1650
GKRKLPTSEE ERSPAKRGRK SATVKPGTVG AAEFVSPCET GDNIGEPSVL 1700
EEPRGPLPLN KTLFLGYAFL LTMATTSDKL ASRSKLLDGP TGSSEEEEEF 1750
LEIPPFNKQY TECQLRAGAG YILEDFNEAQ CNTAYQCLLI ADQHCRTRKY 1800
FLCLASGIPC VSHVWVHDSC HANQLQNYRN YLLPAGYSLE EQRILDWQPR 1850
ENPFQNLKVL LVSDQQQNFL ELWSEILMTG GAASVKQHHS SAHNKDIALG 1900
VFDVVVTDPS CPASVLKCAE ALQLPVVSQE WVIQCLIVGE RIGFKQHPKY 1950
KHDYVSH 1957
Length:1,957
Mass (Da):211,340
Last modified:January 10, 2006 - v2
Checksum:i0FFA0C26DD526E7B
GO
Isoform 2 (identifier: P70399-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-943: Missing.

Note: No experimental confirmation available.

Show »
Length:1,014
Mass (Da):109,745
Checksum:i52E51794028163EA
GO
Isoform 3 (identifier: P70399-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1100-1100: E → EQRASQE
     1347-1396: Missing.

Note: No experimental confirmation available.

Show »
Length:1,913
Mass (Da):206,958
Checksum:i919C52122DFE5F93
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 943943Missing in isoform 2. VSP_016899Add
BLAST
Alternative sequencei1100 – 11001E → EQRASQE in isoform 3. VSP_016900
Alternative sequencei1347 – 139650Missing in isoform 3. VSP_016901Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411E → EE in AAH79906. 1 Publication
Sequence conflicti395 – 3951A → V in AAH79906. 1 Publication
Sequence conflicti421 – 4211T → A in AAH79906. 1 Publication
Sequence conflicti669 – 6691A → P in AAH79906. 1 Publication
Sequence conflicti1064 – 10641P → L in AAH79906. 1 Publication
Sequence conflicti1065 – 10651K → N in AAH35206. 1 Publication
Sequence conflicti1171 – 11722EQ → DE in AAC52876. 1 Publication
Sequence conflicti1175 – 11751G → R in CAC94013. 1 Publication
Sequence conflicti1194 – 11941A → T in AAC52876. 1 Publication
Sequence conflicti1259 – 12591E → G in AAC52876. 1 Publication
Sequence conflicti1759 – 17591Q → H in AAH79906. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ414734 mRNA. Translation: CAC94013.1.
BC035206 mRNA. Translation: AAH35206.1.
BC079906 mRNA. Translation: AAH79906.1.
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

GeneIDi27223.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ414734 mRNA. Translation: CAC94013.1 .
BC035206 mRNA. Translation: AAH35206.1 .
BC079906 mRNA. Translation: AAH79906.1 .
U67885 mRNA. Translation: AAC52876.1 .
RefSeqi NP_001277759.1. NM_001290830.1.
NP_038763.3. NM_013735.4.
UniGenei Mm.215389.
Mm.383499.
Mm.481841.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SSF NMR - A 1463-1617 [» ]
ProteinModelPortali P70399.
SMRi P70399. Positions 1470-1588, 1709-1956.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205144. 13 interactions.
DIPi DIP-31595N.
IntActi P70399. 5 interactions.
MINTi MINT-136714.

PTM databases

PhosphoSitei P70399.

Proteomic databases

MaxQBi P70399.
PaxDbi P70399.
PRIDEi P70399.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 27223.

Organism-specific databases

MGIi MGI:1351320. Trp53bp1.

Phylogenomic databases

eggNOGi NOG264535.
HOGENOMi HOG000231961.
HOVERGENi HBG060882.
InParanoidi P70399.

Miscellaneous databases

EvolutionaryTracei P70399.
NextBioi 305136.
PROi P70399.
SOURCEi Search...

Gene expression databases

Genevestigatori P70399.

Family and domain databases

Gene3Di 2.30.30.30. 1 hit.
3.40.50.10190. 2 hits.
InterProi IPR015125. 53-BP1_Tudor.
IPR001357. BRCT_dom.
IPR014722. Rib_L2_dom2.
[Graphical view ]
Pfami PF09038. 53-BP1_Tudor. 1 hit.
[Graphical view ]
SMARTi SM00292. BRCT. 2 hits.
[Graphical view ]
SUPFAMi SSF52113. SSF52113. 2 hits.
PROSITEi PS50172. BRCT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Kinetochore localisation of the DNA damage response component 53BP1 during mitosis."
    Jullien D., Vagnarelli P., Earnshaw W.C., Adachi Y.
    J. Cell Sci. 115:71-79(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    Strain: BALB/c.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6 and FVB/N.
    Tissue: Head and Mammary tumor.
  3. "p202, an interferon-inducible modulator of transcription, inhibits transcriptional activation by the p53 tumor suppressor protein, and a segment from the p53-binding protein 1 that binds to p202 overcomes this inhibition."
    Datta B., Li B., Choubey D., Nallur G., Lengyel P.
    J. Biol. Chem. 271:27544-27555(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1164-1261 (ISOFORMS 1/2/3), INTERACTION WITH IFI202A.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. "The Tudor tandem of 53BP1: a new structural motif involved in DNA and RG-rich peptide binding."
    Charier G., Couprie J., Alpha-Bazin B., Meyer V., Quemeneur E., Guerois R., Callebaut I., Gilquin B., Zinn-Justin S.
    Structure 12:1551-1562(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1463-1617.

Entry informationi

Entry nameiTP53B_MOUSE
AccessioniPrimary (citable) accession number: P70399
Secondary accession number(s): Q68FD0, Q8CI97, Q91YC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 10, 2006
Last modified: September 3, 2014
This is version 120 of the entry and version 2 of the sequence. [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
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi