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Q12888 (TP53B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor suppressor p53-binding protein 1

Short name=53BP1
Short name=p53-binding protein 1
Short name=p53BP1
Gene names
Name:TP53BP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1972 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a key role in the response to DNA damage. May have a role in checkpoint signaling during mitosis. Enhances TP53-mediated transcriptional activation. Ref.10 Ref.29 Ref.34

Subunit structure

Interacts with IFI202A By similarity. Binds to the central domain of p53/TP53. 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. Interacts with MSL1; this interaction may be required for MSL1 DNA repair activity, but not for histone acetyltransferase activity. Ref.10 Ref.11 Ref.13 Ref.15 Ref.24 Ref.26 Ref.33 Ref.34

Subcellular location

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. Ref.1 Ref.9 Ref.14 Ref.15 Ref.23 Ref.29 Ref.33

Domain

The Tudor-like region mediates binding to H4K20me2.

Post-translational modification

Asymmetrically dimethylated on Arg residues by PRMT1. Methylation is required for DNA binding. Ref.14 Ref.15

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. Ref.8 Ref.9 Ref.18 Ref.23 Ref.29

Involvement in disease

A chromosomal aberration involving TP53BP1 is found in a form of myeloproliferative disorder chronic with eosinophilia. Translocation t(5;15)(q33;q22) with PDGFRB creating a TP53BP1-PDGFRB fusion protein.

Sequence similarities

Contains 2 BRCT domains.

Sequence caution

The sequence BAE06107.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentCentromere
Chromosome
Kinetochore
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
   PTMMethylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement. Source: Reactome

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 17500065. Source: MGI

double-strand break repair

Traceable author statement. Source: Reactome

double-strand break repair via homologous recombination

Traceable author statement. Source: Reactome

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred by curator PubMed 17805299. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17805299. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17805299. Source: GOC

   Cellular_componentcondensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.1. Source: ProtInc

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

replication fork

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA polymerase II activating transcription factor binding

Inferred from physical interaction PubMed 17805299. Source: BHF-UCL

RNA polymerase II transcription cofactor activity

Inferred from mutant phenotype PubMed 17805299. Source: BHF-UCL

damaged DNA binding

Inferred from electronic annotation. Source: Ensembl

methylated histone binding

Inferred from direct assay PubMed 22373579. Source: UniProtKB

p53 binding

Inferred from physical interaction PubMed 17805299. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 16901786Ref.26. Source: UniProtKB

telomeric DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12888-1)

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.
Isoform 2 (identifier: Q12888-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPGEQM
Note: No experimental confirmation available.
Isoform 3 (identifier: Q12888-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPGEQM
     1692-1693: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19721972Tumor suppressor p53-binding protein 1
PRO_0000072643

Regions

Domain1724 – 1848125BRCT 1
Domain1864 – 1964101BRCT 2
Region1483 – 1604122Tudor-like
Region1495 – 152329Interaction with dimethylated histone H4
Motif1396 – 14038GAR
Compositional bias1642 – 16465Poly-Ser
Compositional bias1760 – 17645Poly-Glu

Amino acid modifications

Modified residue251Phosphoserine Ref.23
Modified residue1051Phosphoserine Ref.19
Modified residue1241Phosphoserine Ref.27
Modified residue1661Phosphoserine Ref.18
Modified residue1761Phosphoserine Probable
Modified residue1781Phosphoserine Probable
Modified residue2221Phosphoserine Ref.16 Ref.21 Ref.30
Modified residue2651Phosphoserine Ref.21
Modified residue2941Phosphoserine Ref.16 Ref.18 Ref.25 Ref.27 Ref.30
Modified residue3021Phosphothreonine Ref.18 Ref.19
Modified residue3661Phosphoserine Ref.25
Modified residue3801Phosphoserine Ref.18 Ref.25
Modified residue3951Phosphoserine Ref.21
Modified residue3981Phosphoserine Ref.21
Modified residue4521Phosphoserine Ref.18
Modified residue5001Phosphoserine Ref.16 Ref.21 Ref.25 Ref.27 Ref.30
Modified residue5231Phosphoserine Ref.18 Ref.19 Ref.21 Ref.25
Modified residue5251Phosphoserine Ref.21 Ref.25 Ref.27 Ref.30
Modified residue5431Phosphothreonine Ref.19 Ref.25
Modified residue5481Phosphothreonine Ref.19
Modified residue5521Phosphoserine Ref.18 Ref.19 Ref.21 Ref.25 Ref.27 Ref.30
Modified residue5661Phosphoserine Ref.27
Modified residue5801Phosphoserine Ref.27
Modified residue6351Phosphoserine Ref.16
Modified residue6391Phosphoserine Ref.16 Ref.27
Modified residue6401Phosphoserine Ref.16 Ref.27
Modified residue8091Phosphoserine Ref.21 Ref.27 Ref.30
Modified residue8311Phosphoserine Ref.18 Ref.19 Ref.21
Modified residue8341Phosphoserine Ref.17 Ref.25
Modified residue8551Phosphothreonine Ref.19
Modified residue9221Phosphothreonine Ref.27
Modified residue9701Phosphoserine Ref.27
Modified residue9751Phosphoserine Ref.27
Modified residue10281Phosphoserine Ref.18 Ref.21 Ref.25 Ref.27 Ref.30
Modified residue10681Phosphoserine Ref.27
Modified residue10861Phosphoserine Ref.18
Modified residue10941Phosphoserine Ref.16 Ref.21 Ref.27 Ref.30
Modified residue11011Phosphoserine Ref.30
Modified residue11141Phosphoserine Ref.18 Ref.25 Ref.27 Ref.30
Modified residue12141Phosphothreonine Ref.19
Modified residue12161Phosphoserine Ref.19 Ref.21
Modified residue12191Phosphoserine Ref.16 Ref.18 Ref.19 Ref.21
Modified residue13621Phosphoserine Ref.16 Ref.27 Ref.30
Modified residue13681Phosphoserine Ref.21
Modified residue13721Phosphothreonine Ref.21
Modified residue14261Phosphoserine Ref.17 Ref.21 Ref.25 Ref.27
Modified residue14301Phosphoserine Ref.21 Ref.25 Ref.27 Ref.30
Modified residue14601Phosphoserine Ref.25
Modified residue14621Phosphoserine Ref.21 Ref.25
Modified residue14741Phosphoserine Ref.25
Modified residue16091Phosphothreonine Ref.21 Ref.27
Modified residue16181Phosphoserine Ref.27 Ref.30
Modified residue16781Phosphoserine Ref.16 Ref.27 Ref.30
Modified residue17011Phosphoserine Ref.21
Modified residue17591Phosphoserine Ref.21
Modified residue17781Phosphoserine Ref.23 Ref.29

Natural variations

Alternative sequence11M → MPGEQM in isoform 2 and isoform 3.
VSP_018390
Alternative sequence1692 – 16932Missing in isoform 3.
VSP_055062
Natural variant3531D → E. Ref.3 Ref.4
Corresponds to variant rs560191 [ dbSNP | Ensembl ].
VAR_022172
Natural variant4121G → S. Ref.3 Ref.4
Corresponds to variant rs689647 [ dbSNP | Ensembl ].
VAR_022173
Natural variant6481M → V. Ref.4
Corresponds to variant rs45443496 [ dbSNP | Ensembl ].
VAR_022174
Natural variant6991Q → R. Ref.4
Corresponds to variant rs34823068 [ dbSNP | Ensembl ].
VAR_022175
Natural variant8411D → G.
Corresponds to variant rs34185035 [ dbSNP | Ensembl ].
VAR_034558
Natural variant10141E → G. Ref.4
Corresponds to variant rs45470395 [ dbSNP | Ensembl ].
VAR_022176
Natural variant10261V → A. Ref.4
Corresponds to variant rs45482998 [ dbSNP | Ensembl ].
VAR_022177
Natural variant11361K → Q. Ref.3 Ref.4
Corresponds to variant rs2602141 [ dbSNP | Ensembl ].
VAR_022178
Natural variant11371E → K.
Corresponds to variant rs34740611 [ dbSNP | Ensembl ].
VAR_034559
Natural variant11701A → G. Ref.4
Corresponds to variant rs45500399 [ dbSNP | Ensembl ].
VAR_022179
Natural variant11741I → V. Ref.4
Corresponds to variant rs3803339 [ dbSNP | Ensembl ].
VAR_022180
Natural variant14421R → Q.
Corresponds to variant rs2230449 [ dbSNP | Ensembl ].
VAR_034560
Natural variant14881G → W.
Corresponds to variant rs11554564 [ dbSNP | Ensembl ].
VAR_038689

Experimental info

Mutagenesis176 – 1783SQS → AQA: Loss of phosphorylation site. Ref.18
Mutagenesis13961R → A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1398; A-1400; A-1401 and A-1403. Ref.14 Ref.15
Mutagenesis13961R → K: No detectable effect on methylation by PRMT1 (in vitro). Ref.14 Ref.15
Mutagenesis13981R → A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1400; A-1401 and A-1403. Ref.14 Ref.15
Mutagenesis13981R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1400. Strongly reduced methylation; when associated with K-1401. Ref.14 Ref.15
Mutagenesis14001R → A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1401 and A-1403. Ref.14 Ref.15
Mutagenesis14001R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1401. Ref.14 Ref.15
Mutagenesis14011R → A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1400 and A-1403. Ref.14 Ref.15
Mutagenesis14011R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1400. Ref.14 Ref.15
Mutagenesis14031R → A: No detectable effect on methylation by PRMT1 (in vitro). Loss of methylation; when associated with A-1396; A-1398; A-1400 and A-1401. Ref.14 Ref.15
Mutagenesis14031R → K: No detectable effect on methylation by PRMT1 (in vitro). Ref.14 Ref.15
Mutagenesis14951W → A or H: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20'. Ref.33 Ref.34
Mutagenesis14951W → F: No effect on recruitment to double strand breaks. Ref.33 Ref.34
Mutagenesis14951W → V: Reduces recruitment to double strand breaks. Ref.33 Ref.34
Mutagenesis15001Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. Ref.34
Mutagenesis15021Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. Ref.33 Ref.34
Mutagenesis15021Y → L or Q: Abolishes recruitment to double strand breaks. Ref.33 Ref.34
Mutagenesis15211D → A: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20'. Abolishes recruitment to double strand breaks. Ref.33 Ref.34
Mutagenesis15211D → R: Abolishes recruitment to double strand breaks. Ref.33 Ref.34
Mutagenesis15231Y → A: Increases affinity for histone H4 that has been dimethylated at 'Lys-20'. No effect on recruitment to double strand breaks. Ref.34
Mutagenesis15231Y → S: Decreases affinity for histone H4 that has been dimethylated at 'Lys-20'. Ref.34
Sequence conflict7961P → S in CAD97660. Ref.3
Sequence conflict16001Y → C in CAD97660. Ref.3
Sequence conflict19581G → R in CAD97660. Ref.3

Secondary structure

........................................................................ 1972
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 13E2CC8A265F9D2A

FASTA1,972213,574
        10         20         30         40         50         60 
MDPTGSQLDS DFSQQDTPCL IIEDSQPESQ VLEDDSGSHF SMLSRHLPNL QTHKENPVLD 

        70         80         90        100        110        120 
VVSNPEQTAG EERGDGNSGF NEHLKENKVA DPVDSSNLDT CGSISQVIEQ LPQPNRTSSV 

       130        140        150        160        170        180 
LGMSVESAPA VEEEKGEELE QKEKEKEEDT SGNTTHSLGA EDTASSQLGF GVLELSQSQD 

       190        200        210        220        230        240 
VEENTVPYEV DKEQLQSVTT NSGYTRLSDV DANTAIKHEE QSNEDIPIAE QSSKDIPVTA 

       250        260        270        280        290        300 
QPSKDVHVVK EQNPPPARSE DMPFSPKASV AAMEAKEQLS AQELMESGLQ IQKSPEPEVL 

       310        320        330        340        350        360 
STQEDLFDQS NKTVSSDGCS TPSREEGGCS LASTPATTLH LLQLSGQRSL VQDSLSTNSS 

       370        380        390        400        410        420 
DLVAPSPDAF RSTPFIVPSS PTEQEGRQDK PMDTSVLSEE GGEPFQKKLQ SGEPVELENP 

       430        440        450        460        470        480 
PLLPESTVSP QASTPISQST PVFPPGSLPI PSQPQFSHDI FIPSPSLEEQ SNDGKKDGDM 

       490        500        510        520        530        540 
HSSSLTVECS KTSEIEPKNS PEDLGLSLTG DSCKLMLSTS EYSQSPKMES LSSHRIDEDG 

       550        560        570        580        590        600 
ENTQIEDTEP MSPVLNSKFV PAENDSILMN PAQDGEVQLS QNDDKTKGDD TDTRDDISIL 

       610        620        630        640        650        660 
ATGCKGREET VAEDVCIDLT CDSGSQAVPS PATRSEALSS VLDQEEAMEI KEHHPEEGSS 

       670        680        690        700        710        720 
GSEVEEIPET PCESQGEELK EENMESVPLH LSLTETQSQG LCLQKEMPKK ECSEAMEVET 

       730        740        750        760        770        780 
SVISIDSPQK LAILDQELEH KEQEAWEEAT SEDSSVVIVD VKEPSPRVDV SCEPLEGVEK 

       790        800        810        820        830        840 
CSDSQSWEDI APEIEPCAEN RLDTKEEKSV EYEGDLKSGT AETEPVEQDS SQPSLPLVRA 

       850        860        870        880        890        900 
DDPLRLDQEL QQPQTQEKTS NSLTEDSKMA NAKQLSSDAE AQKLGKPSAH ASQSFCESSS 

       910        920        930        940        950        960 
ETPFHFTLPK EGDIIPPLTG ATPPLIGHLK LEPKRHSTPI GISNYPESTI ATSDVMSESM 

       970        980        990       1000       1010       1020 
VETHDPILGS GKGDSGAAPD VDDKLCLRMK LVSPETEASE ESLQFNLEKP ATGERKNGST 

      1030       1040       1050       1060       1070       1080 
AVAESVASPQ KTMSVLSCIC EARQENEARS EDPPTTPIRG NLLHFPSSQG EEEKEKLEGD 

      1090       1100       1110       1120       1130       1140 
HTIRQSQQPM KPISPVKDPV SPASQKMVIQ GPSSPQGEAM VTDVLEDQKE GRSTNKENPS 

      1150       1160       1170       1180       1190       1200 
KALIERPSQN NIGIQTMECS LRVPETVSAA TQTIKNVCEQ GTSTVDQNFG KQDATVQTER 

      1210       1220       1230       1240       1250       1260 
GSGEKPVSAP GDDTESLHSQ GEEEFDMPQP PHGHVLHRHM RTIREVRTLV TRVITDVYYV 

      1270       1280       1290       1300       1310       1320 
DGTEVERKVT EETEEPIVEC QECETEVSPS QTGGSSGDLG DISSFSSKAS SLHRTSSGTS 

      1330       1340       1350       1360       1370       1380 
LSAMHSSGSS GKGAGPLRGK TSGTEPADFA LPSSRGGPGK LSPRKGVSQT GTPVCEEDGD 

      1390       1400       1410       1420       1430       1440 
AGLGIRQGGK APVTPRGRGR RGRPPSRTTG TRETAVPGPL GIEDISPNLS PDDKSFSRVV 

      1450       1460       1470       1480       1490       1500 
PRVPDSTRRT DVGAGALRRS DSPEIPFQAA AGPSDGLDAS SPGNSFVGLR VVAKWSSNGY 

      1510       1520       1530       1540       1550       1560 
FYSGKITRDV GAGKYKLLFD DGYECDVLGK DILLCDPIPL DTEVTALSED EYFSAGVVKG 

      1570       1580       1590       1600       1610       1620 
HRKESGELYY SIEKEGQRKW YKRMAVILSL EQGNRLREQY GLGPYEAVTP LTKAADISLD 

      1630       1640       1650       1660       1670       1680 
NLVEGKRKRR SNVSSPATPT ASSSSSTTPT RKITESPRAS MGVLSGKRKL ITSEEERSPA 

      1690       1700       1710       1720       1730       1740 
KRGRKSATVK PGAVGAGEFV SPCESGDNTG EPSALEEQRG PLPLNKTLFL GYAFLLTMAT 

      1750       1760       1770       1780       1790       1800 
TSDKLASRSK LPDGPTGSSE EEEEFLEIPP FNKQYTESQL RAGAGYILED FNEAQCNTAY 

      1810       1820       1830       1840       1850       1860 
QCLLIADQHC RTRKYFLCLA SGIPCVSHVW VHDSCHANQL QNYRNYLLPA GYSLEEQRIL 

      1870       1880       1890       1900       1910       1920 
DWQPRENPFQ NLKVLLVSDQ QQNFLELWSE ILMTGGAASV KQHHSSAHNK DIALGVFDVV 

      1930       1940       1950       1960       1970 
VTDPSCPASV LKCAEALQLP VVSQEWVIQC LIVGERIGFK QHPKYKHDYV SH 

« Hide

Isoform 2 [UniParc].

Checksum: B8C43ACE26E9A204
Show »

FASTA1,977214,117
Isoform 3 [UniParc].

Checksum: 14467931B27D109D
Show »

FASTA1,975213,989

References

« Hide 'large scale' references
[1]"Stimulation of p53-mediated transcriptional activation by the p53-binding proteins, 53BP1 and 53BP2."
Iwabuchi K., Li B., Massa H.F., Trask B.J., Date T., Fields S.
J. Biol. Chem. 273:26061-26068(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
Tissue: Skeletal muscle.
[2]"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Myeloid leukemia cell.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS GLU-353; SER-412 AND GLN-1136.
Tissue: Cervix.
[4]NIEHS SNPs program
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-353; SER-412; VAL-648; ARG-699; GLY-1014; ALA-1026; GLN-1136; GLY-1170 AND VAL-1174.
[5]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1).
Tissue: Cerebellum.
[7]"Two cellular proteins that bind to wild-type but not mutant p53."
Iwabuchi K., Bartel P.L., Li B., Marraccino R., Fields S.
Proc. Natl. Acad. Sci. U.S.A. 91:6098-6102(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 946-1972.
[8]"Negative cell cycle regulation and DNA-damage inducible phosphorylation of the BRCT protein 53BP1."
Xia Z., Morales J.C., Dunphy W.G., Carpenter P.B.
J. Biol. Chem. 276:2708-2718(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[9]"Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA damage-signaling pathways."
Rappold I., Iwabuchi K., Date T., Chen J.
J. Cell Biol. 153:613-620(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[10]"53BP1, a mediator of the DNA damage checkpoint."
Wang B., Matsuoka S., Carpenter P.B., Elledge S.J.
Science 298:1435-1438(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA DAMAGE CHECKPOINT, INTERACTION WITH CHEK2.
[11]"MDC1 is a mediator of the mammalian DNA damage checkpoint."
Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.
Nature 421:961-966(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH H2AFX.
[12]"p53-Binding protein 1 is fused to the platelet-derived growth factor receptor beta in a patient with a t(5;15)(q33;q22) and an imatinib-responsive eosinophilic myeloproliferative disorder."
Grand F.H., Burgstaller S., Kuhr T., Baxter E.J., Webersinke G., Thaler J., Chase A.J., Cross N.C.
Cancer Res. 64:7216-7219(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH PDGFRB.
[13]"A pathway of double-strand break rejoining dependent upon ATM, Artemis, and proteins locating to gamma-H2AX foci."
Riballo E., Kuehne M., Rief N., Doherty A., Smith G.C.M., Recio M.-J., Reis C., Dahm K., Fricke A., Krempler A., Parker A.R., Jackson S.P., Gennery A., Jeggo P.A., Loebrich M.
Mol. Cell 16:715-724(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DCLRE1C.
[14]"The GAR motif of 53BP1 is arginine methylated by PRMT1 and is necessary for 53BP1 DNA binding activity."
Boisvert F.-M., Rhie A., Richard S., Doherty A.J.
Cell Cycle 4:1834-1841(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION, MUTAGENESIS OF ARG-1396; ARG-1398; ARG-1400; ARG-1401 AND ARG-1403, SUBCELLULAR LOCATION, DNA-BINDING.
[15]"53BP1 oligomerization is independent of its methylation by PRMT1."
Adams M.M., Wang B., Xia Z., Morales J.C., Lu X., Donehower L.A., Bochar D.A., Elledge S.J., Carpenter P.B.
Cell Cycle 4:1854-1861(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION, MUTAGENESIS OF ARG-1396; ARG-1398; ARG-1400; ARG-1401 AND ARG-1403, SUBUNIT, SUBCELLULAR LOCATION, DNA-BINDING.
[16]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-294; SER-500; SER-635; SER-639; SER-640; SER-1094; SER-1219; SER-1362 AND SER-1678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-834 AND SER-1426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Characterisation of the sites of DNA damage-induced 53BP1 phosphorylation catalysed by ATM and ATR."
Jowsey P., Morrice N.A., Hastie C.J., McLauchlan H., Toth R., Rouse J.
DNA Repair 6:1536-1544(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-166; SER-176; SER-178; SER-294; THR-302; SER-380; SER-452; SER-523; SER-552; SER-831; SER-1028; SER-1086; SER-1114 AND SER-1219, MUTAGENESIS OF 176-SER--SER-178.
[19]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-302; SER-523; THR-543; THR-548; SER-552; SER-831; THR-855; THR-1214; SER-1216 AND SER-1219, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[20]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-265; SER-395; SER-398; SER-500; SER-523; SER-525; SER-552; SER-809; SER-831; SER-1028; SER-1094; SER-1216; SER-1219; SER-1368; THR-1372; SER-1426; SER-1430; SER-1462; THR-1609; SER-1701 AND SER-1759, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Protein phosphatase 5 regulates the function of 53BP1 after neocarzinostatin-induced DNA damage."
Kang Y., Lee J.H., Hoan N.N., Sohn H.M., Chang I.Y., You H.J.
J. Biol. Chem. 284:9845-9853(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-25 AND SER-1778, DEPHOSPHORYLATION AT SER-25 AND SER-1778 BY PPP5C, SUBCELLULAR LOCATION.
[24]"p8/nupr1 regulates DNA-repair activity after double-strand gamma irradiation-induced DNA damage."
Gironella M., Malicet C., Cano C., Sandi M.J., Hamidi T., Tauil R.M., Baston M., Valaco P., Moreno S., Lopez F., Neira J.L., Dagorn J.C., Iovanna J.L.
J. Cell. Physiol. 221:594-602(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MSL1.
[25]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294; SER-366; SER-380; SER-500; SER-523; SER-525; THR-543; SER-552; SER-834; SER-1028; SER-1114; SER-1426; SER-1430; SER-1460; SER-1462 AND SER-1474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[26]"Regulation of chromatin architecture by the PWWP domain-containing DNA damage-responsive factor EXPAND1/MUM1."
Huen M.S., Huang J., Leung J.W., Sy S.M., Leung K.M., Ching Y.P., Tsao S.W., Chen J.
Mol. Cell 37:854-864(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MUM1.
[27]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-294; SER-500; SER-525; SER-552; SER-566; SER-580; SER-639; SER-640; SER-809; THR-922; SER-970; SER-975; SER-1028; SER-1068; SER-1094; SER-1114; SER-1362; SER-1426; SER-1430; THR-1609; SER-1618 AND SER-1678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Protein phosphatase 5 is necessary for ATR-mediated DNA repair."
Kang Y., Cheong H.M., Lee J.H., Song P.I., Lee K.H., Kim S.Y., Jun J.Y., You H.J.
Biochem. Biophys. Res. Commun. 404:476-481(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA DAMAGE RESPONSE, PHOSPHORYLATION AT SER-1778, SUBCELLULAR LOCATION.
[30]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-294; SER-500; SER-525; SER-552; SER-809; SER-1028; SER-1094; SER-1101; SER-1114; SER-1362; SER-1430; SER-1618 AND SER-1678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"Crystal structure of human 53BP1 BRCT domains bound to p53 tumour suppressor."
Derbyshire D.J., Basu B.P., Serpell L.C., Joo W.S., Date T., Iwabuchi K., Doherty A.J.
EMBO J. 21:3863-3872(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1722-1971 IN COMPLEX WITH TP53.
[32]"Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure."
Joo W.S., Jeffrey P.D., Cantor S.B., Finnin M.S., Livingston D.M., Pavletich N.P.
Genes Dev. 16:583-593(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1714-1972 IN COMPLEX WITH TP53.
[33]"Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks."
Huyen Y., Zgheib O., Ditullio R.A. Jr., Gorgoulis V.G., Zacharatos P., Petty T.J., Sheston E.A., Mellert H.S., Stavridi E.S., Halazonetis T.D.
Nature 432:406-411(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1485-1602, INTERACTION WITH METHYLATED HISTONE H3 AND HISTONE H4, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-1495; TYR-1502 AND ASP-1521.
[34]"Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair."
Botuyan M.V., Lee J., Ward I.M., Kim J.-E., Thompson J.R., Chen J., Mer G.
Cell 127:1361-1373(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1484-1603 IN COMPLEX WITH HISTONE H4, SUBUNIT, FUNCTION, MUTAGENESIS OF TRP-1495; TYR-1500; TYR-1502; ASP-1521 AND TYR-1523.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF078776 mRNA. Translation: AAC62018.1.
AB210025 mRNA. Translation: BAE06107.1. Different initiation.
BX537418 mRNA. Translation: CAD97660.1.
AY904026 Genomic DNA. Translation: AAW69392.1.
AC018924 Genomic DNA. No translation available.
BC112161 mRNA. Translation: AAI12162.1.
U09477 mRNA. Translation: AAA21596.1.
CCDSCCDS10096.1. [Q12888-1]
CCDS45250.1. [Q12888-2]
PIRI38604.
RefSeqNP_001135451.1. NM_001141979.1.
NP_001135452.1. NM_001141980.1. [Q12888-2]
NP_005648.1. NM_005657.2. [Q12888-1]
XP_005254691.1. XM_005254634.2. [Q12888-1]
UniGeneHs.440968.
Hs.584887.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GZHX-ray2.60B/D1724-1972[»]
1KZYX-ray2.50C/D1714-1972[»]
1XNIX-ray2.80A/B/C/D/E/F/G/H/I/J1485-1602[»]
2G3RX-ray1.25A1484-1603[»]
2IG0X-ray1.70A1484-1603[»]
2LVMNMR-A1484-1603[»]
3LGFX-ray1.50A1484-1603[»]
3LGLX-ray1.60A1484-1603[»]
3LH0X-ray1.90A1484-1603[»]
ProteinModelPortalQ12888.
SMRQ12888. Positions 1485-1603, 1724-1971.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113011. 115 interactions.
DIPDIP-5978N.
IntActQ12888. 24 interactions.
MINTMINT-276057.
STRING9606.ENSP00000371475.

Chemistry

ChEMBLCHEMBL2424509.

PTM databases

PhosphoSiteQ12888.

Polymorphism databases

DMDM8928568.

Proteomic databases

MaxQBQ12888.
PaxDbQ12888.
PRIDEQ12888.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263801; ENSP00000263801; ENSG00000067369. [Q12888-1]
ENST00000382044; ENSP00000371475; ENSG00000067369. [Q12888-2]
ENST00000450115; ENSP00000393497; ENSG00000067369.
GeneID7158.
KEGGhsa:7158.
UCSCuc001zrr.4. human. [Q12888-2]
uc001zrs.3. human. [Q12888-1]

Organism-specific databases

CTD7158.
GeneCardsGC15M043699.
HGNCHGNC:11999. TP53BP1.
HPACAB004083.
HPA008788.
HPA022133.
MIM605230. gene.
neXtProtNX_Q12888.
PharmGKBPA36680.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264535.
HOGENOMHOG000231961.
HOVERGENHBG060882.
InParanoidQ12888.
OMAPEIPFQA.
OrthoDBEOG7RZ5P1.
PhylomeDBQ12888.
TreeFamTF350227.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressQ12888.
BgeeQ12888.
CleanExHS_TP53BP1.
GenevestigatorQ12888.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
3.40.50.10190. 2 hits.
InterProIPR015125. 53-BP1_Tudor.
IPR001357. BRCT_dom.
IPR014722. Rib_L2_dom2.
[Graphical view]
PfamPF09038. 53-BP1_Tudor. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 2 hits.
[Graphical view]
SUPFAMSSF52113. SSF52113. 2 hits.
PROSITEPS50172. BRCT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTP53BP1. human.
EvolutionaryTraceQ12888.
GeneWikiTP53BP1.
GenomeRNAi7158.
NextBio28010.
PMAP-CutDBQ12888.
PROQ12888.
SOURCESearch...

Entry information

Entry nameTP53B_HUMAN
AccessionPrimary (citable) accession number: Q12888
Secondary accession number(s): F8VY86 expand/collapse secondary AC list , Q2M1Z7, Q4LE46, Q5FWZ3, Q7Z3U4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM