Q12888 (TP53B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tumor suppressor p53-binding protein 1
Short name=53BP1
Short name=p53-binding protein 1
Short name=p53BP1

Gene names

Name:

TP53BP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1972 AA.
Sequence status	Complete.
Protein existence	Evidence 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.9 Ref.30
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.9 Ref.10 Ref.12 Ref.14 Ref.21 Ref.23 Ref.29 Ref.30
Subcellular location	Nucleus. Chromosome › centromere › kinetochore. 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.8 Ref.13 Ref.14 Ref.29
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.13 Ref.14 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. Ref.7 Ref.8 Ref.17
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.

Ontologies

Keywords
Biological process	DNA damage DNA repair Transcription Transcription regulation
Cellular component	Centromere Chromosome Kinetochore Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator
PTM	Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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
Cellular_component	condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from direct assay Ref.1. Source: ProtInc nucleoplasm Traceable author statement. Source: Reactome replication fork Inferred from electronic annotation. Source: Compara
Molecular_function	RNA polymerase II transcription cofactor activity Inferred from mutant phenotype PubMed 17805299. Source: BHF-UCL damaged DNA binding Inferred from electronic annotation. Source: Compara methylated histone residue binding Inferred from direct assay PubMed 22373579. Source: UniProtKB telomeric DNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PAXIP1	Q6ZW49	4	EBI-396540,EBI-743225
Paxip1	Q6NZQ4	2	EBI-396540,EBI-1395317	From a different organism.
VRK1	Q99986	8	EBI-396540,EBI-1769146

Alternative products

This entry describes 2 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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1972

1972

Tumor suppressor p53-binding protein 1

PRO_0000072643

Regions

Domain

1724 – 1848

125

BRCT 1

Domain

1864 – 1964

101

BRCT 2

Region

1483 – 1604

122

Tudor-like

Region

1495 – 1523

29

Interaction with dimethylated histone H4

Motif

1396 – 1403

8

GAR

Compositional bias

1642 – 1646

5

Poly-Ser

Compositional bias

1760 – 1764

5

Poly-Glu

Amino acid modifications

Modified residue

105

1

Phosphoserine Ref.18

Modified residue

124

1

Phosphoserine Ref.24

Modified residue

166

1

Phosphoserine

Modified residue

176

1

Phosphoserine Probable

Modified residue

178

1

Phosphoserine Probable

Modified residue

222

1

Phosphoserine Ref.15 Ref.20 Ref.26

Modified residue

265

1

Phosphoserine Ref.20

Modified residue

294

1

Phosphoserine Ref.15 Ref.17 Ref.22 Ref.24 Ref.26

Modified residue

302

1

Phosphothreonine Ref.17 Ref.18

Modified residue

366

1

Phosphoserine Ref.22

Modified residue

380

1

Phosphoserine Ref.17 Ref.22

Modified residue

395

1

Phosphoserine Ref.20

Modified residue

398

1

Phosphoserine Ref.20

Modified residue

452

1

Phosphoserine Ref.17

Modified residue

500

1

Phosphoserine Ref.15 Ref.20 Ref.22 Ref.24 Ref.26

Modified residue

523

1

Phosphoserine Ref.17 Ref.18 Ref.20 Ref.22

Modified residue

525

1

Phosphoserine Ref.20 Ref.22 Ref.24 Ref.26

Modified residue

543

1

Phosphothreonine Ref.18 Ref.22

Modified residue

548

1

Phosphothreonine Ref.18

Modified residue

552

1

Phosphoserine Ref.17 Ref.18 Ref.20 Ref.22 Ref.24 Ref.26

Modified residue

566

1

Phosphoserine Ref.24

Modified residue

580

1

Phosphoserine Ref.24

Modified residue

635

1

Phosphoserine Ref.15

Modified residue

639

1

Phosphoserine Ref.15 Ref.24

Modified residue

640

1

Phosphoserine Ref.15 Ref.24

Modified residue

809

1

Phosphoserine Ref.20 Ref.24 Ref.26

Modified residue

831

1

Phosphoserine Ref.17 Ref.18 Ref.20

Modified residue

834

1

Phosphoserine Ref.16 Ref.22

Modified residue

855

1

Phosphothreonine Ref.18

Modified residue

922

1

Phosphothreonine Ref.24

Modified residue

970

1

Phosphoserine Ref.24

Modified residue

975

1

Phosphoserine Ref.24

Modified residue

1028

1

Phosphoserine Ref.17 Ref.20 Ref.22 Ref.24 Ref.26

Modified residue

1068

1

Phosphoserine Ref.24

Modified residue

1094

1

Phosphoserine Ref.15 Ref.20 Ref.24 Ref.26

Modified residue

1101

1

Phosphoserine Ref.26

Modified residue

1114

1

Phosphoserine Ref.17 Ref.22 Ref.24 Ref.26

Modified residue

1214

1

Phosphothreonine Ref.18

Modified residue

1216

1

Phosphoserine Ref.18 Ref.20

Modified residue

1219

1

Phosphoserine Ref.15 Ref.17 Ref.18 Ref.20

Modified residue

1362

1

Phosphoserine Ref.15 Ref.24 Ref.26

Modified residue

1368

1

Phosphoserine Ref.20

Modified residue

1372

1

Phosphothreonine Ref.20

Modified residue

1426

1

Phosphoserine Ref.16 Ref.20 Ref.22 Ref.24

Modified residue

1430

1

Phosphoserine Ref.20 Ref.22 Ref.24 Ref.26

Modified residue

1460

1

Phosphoserine Ref.22

Modified residue

1462

1

Phosphoserine Ref.20 Ref.22

Modified residue

1474

1

Phosphoserine Ref.22

Modified residue

1609

1

Phosphothreonine Ref.20 Ref.24

Modified residue

1618

1

Phosphoserine Ref.24 Ref.26

Modified residue

1678

1

Phosphoserine Ref.15 Ref.24 Ref.26

Modified residue

1701

1

Phosphoserine Ref.20

Modified residue

1759

1

Phosphoserine Ref.20

Natural variations

Alternative sequence

1

1

M → MPGEQM in isoform 2.

VSP_018390

Natural variant

353

1

D → E. Ref.3 Ref.4
Corresponds to variant rs560191 [ dbSNP | Ensembl ].

VAR_022172

Natural variant

412

1

G → S. Ref.3 Ref.4
Corresponds to variant rs689647 [ dbSNP | Ensembl ].

VAR_022173

Natural variant

648

1

M → V. Ref.4
Corresponds to variant rs45443496 [ dbSNP | Ensembl ].

VAR_022174

Natural variant

699

1

Q → R. Ref.4
Corresponds to variant rs34823068 [ dbSNP | Ensembl ].

VAR_022175

Natural variant

841

1

D → G.
Corresponds to variant rs34185035 [ dbSNP | Ensembl ].

VAR_034558

Natural variant

1014

1

E → G. Ref.4
Corresponds to variant rs45470395 [ dbSNP | Ensembl ].

VAR_022176

Natural variant

1026

1

V → A. Ref.4
Corresponds to variant rs45482998 [ dbSNP | Ensembl ].

VAR_022177

Natural variant

1136

1

K → Q. Ref.3 Ref.4
Corresponds to variant rs2602141 [ dbSNP | Ensembl ].

VAR_022178

Natural variant

1137

1

E → K.
Corresponds to variant rs34740611 [ dbSNP | Ensembl ].

VAR_034559

Natural variant

1170

1

A → G. Ref.4
Corresponds to variant rs45500399 [ dbSNP | Ensembl ].

VAR_022179

Natural variant

1174

1

I → V. Ref.4
Corresponds to variant rs3803339 [ dbSNP | Ensembl ].

VAR_022180

Natural variant

1442

1

R → Q.
Corresponds to variant rs2230449 [ dbSNP | Ensembl ].

VAR_034560

Natural variant

1488

1

G → W.
Corresponds to variant rs11554564 [ dbSNP | Ensembl ].

VAR_038689

Experimental info

Mutagenesis

176 – 178

3

SQS → AQA: Loss of phosphorylation site. Ref.17

Mutagenesis

1396

1

R → 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.13 Ref.14

Mutagenesis

1396

1

R → K: No detectable effect on methylation by PRMT1 (in vitro). Ref.13 Ref.14

Mutagenesis

1398

1

R → 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.13 Ref.14

Mutagenesis

1398

1

R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1400. Strongly reduced methylation; when associated with K-1401. Ref.13 Ref.14

Mutagenesis

1400

1

R → 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.13 Ref.14

Mutagenesis

1400

1

R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1401. Ref.13 Ref.14

Mutagenesis

1401

1

R → 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.13 Ref.14

Mutagenesis

1401

1

R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1400. Ref.13 Ref.14

Mutagenesis

1403

1

R → 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.13 Ref.14

Mutagenesis

1403

1

R → K: No detectable effect on methylation by PRMT1 (in vitro). Ref.13 Ref.14

Mutagenesis

1495

1

W → A or H: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20'. Ref.29 Ref.30

Mutagenesis

1495

1

W → F: No effect on recruitment to double strand breaks. Ref.29 Ref.30

Mutagenesis

1495

1

W → V: Reduces recruitment to double strand breaks. Ref.29 Ref.30

Mutagenesis

1500

1

Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. Ref.30

Mutagenesis

1502

1

Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. Ref.29 Ref.30

Mutagenesis

1502

1

Y → L or Q: Abolishes recruitment to double strand breaks. Ref.29 Ref.30

Mutagenesis

1521

1

D → A: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20'. Abolishes recruitment to double strand breaks. Ref.29 Ref.30

Mutagenesis

1521

1

D → R: Abolishes recruitment to double strand breaks. Ref.29 Ref.30

Mutagenesis

1523

1

Y → A: Increases affinity for histone H4 that has been dimethylated at 'Lys-20'. No effect on recruitment to double strand breaks. Ref.30

Mutagenesis

1523

1

Y → S: Decreases affinity for histone H4 that has been dimethylated at 'Lys-20'. Ref.30

Sequence conflict

796

1

P → S in CAD97660. Ref.3

Sequence conflict

1600

1

Y → C in CAD97660. Ref.3

Sequence conflict

1692 – 1693

2

Missing in BAE06107. Ref.2

Sequence conflict

1958

1

G → R in CAD97660. Ref.3

Secondary structure

1

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1972

Helix Strand Turn

Details...

Beta strand

1490 – 1494

5

Turn

1496 – 1498

3

Beta strand

1501 – 1511

11

Beta strand

1514 – 1519

6

Beta strand

1524 – 1528

5

Helix

1529 – 1531

3

Beta strand

1532 – 1535

4

Beta strand

1543 – 1547

5

Beta strand

1553 – 1564

12

Beta strand

1567 – 1574

8

Beta strand

1577 – 1582

6

Helix

1583 – 1585

3

Beta strand

1586 – 1588

3

Helix

1590 – 1594

5

Helix

1597 – 1600

4

Helix

1715 – 1719

5

Turn

1726 – 1731

6

Beta strand

1732 – 1736

5

Helix

1741 – 1745

5

Helix

1773 – 1781

9

Turn

1782 – 1784

3

Turn

1793 – 1799

7

Beta strand

1801 – 1808

8

Helix

1813 – 1821

9

Beta strand

1825 – 1827

3

Helix

1829 – 1837

9

Helix

1843 – 1845

3

Beta strand

1851 – 1853

3

Turn

1854 – 1857

4

Beta strand

1858 – 1860

3

Turn

1868 – 1871

4

Beta strand

1873 – 1879

7

Turn

1881 – 1884

4

Helix

1885 – 1894

10

Beta strand

1898 – 1908

11

Helix

1914 – 1916

3

Beta strand

1918 – 1922

5

Helix

1928 – 1937

10

Helix

1944 – 1953

10

Helix

1963 – 1965

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 13E2CC8A265F9D2A	FASTA	1,972	213,574
	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
	Isoform 2 [UniParc]. Checksum: B8C43ACE26E9A204	FASTA	1,977	214,117
	10 20 30 40 50 60 MPGEQMDPTG SQLDSDFSQQ DTPCLIIEDS QPESQVLEDD SGSHFSMLSR HLPNLQTHKE 70 80 90 100 110 120 NPVLDVVSNP EQTAGEERGD GNSGFNEHLK ENKVADPVDS SNLDTCGSIS QVIEQLPQPN 130 140 150 160 170 180 RTSSVLGMSV ESAPAVEEEK GEELEQKEKE KEEDTSGNTT HSLGAEDTAS SQLGFGVLEL 190 200 210 220 230 240 SQSQDVEENT VPYEVDKEQL QSVTTNSGYT RLSDVDANTA IKHEEQSNED IPIAEQSSKD 250 260 270 280 290 300 IPVTAQPSKD VHVVKEQNPP PARSEDMPFS PKASVAAMEA KEQLSAQELM ESGLQIQKSP 310 320 330 340 350 360 EPEVLSTQED LFDQSNKTVS SDGCSTPSRE EGGCSLASTP ATTLHLLQLS GQRSLVQDSL 370 380 390 400 410 420 STNSSDLVAP SPDAFRSTPF IVPSSPTEQE GRQDKPMDTS VLSEEGGEPF QKKLQSGEPV 430 440 450 460 470 480 ELENPPLLPE STVSPQASTP ISQSTPVFPP GSLPIPSQPQ FSHDIFIPSP SLEEQSNDGK 490 500 510 520 530 540 KDGDMHSSSL TVECSKTSEI EPKNSPEDLG LSLTGDSCKL MLSTSEYSQS PKMESLSSHR 550 560 570 580 590 600 IDEDGENTQI EDTEPMSPVL NSKFVPAEND SILMNPAQDG EVQLSQNDDK TKGDDTDTRD 610 620 630 640 650 660 DISILATGCK GREETVAEDV CIDLTCDSGS QAVPSPATRS EALSSVLDQE EAMEIKEHHP 670 680 690 700 710 720 EEGSSGSEVE EIPETPCESQ GEELKEENME SVPLHLSLTE TQSQGLCLQK EMPKKECSEA 730 740 750 760 770 780 MEVETSVISI DSPQKLAILD QELEHKEQEA WEEATSEDSS VVIVDVKEPS PRVDVSCEPL 790 800 810 820 830 840 EGVEKCSDSQ SWEDIAPEIE PCAENRLDTK EEKSVEYEGD LKSGTAETEP VEQDSSQPSL 850 860 870 880 890 900 PLVRADDPLR LDQELQQPQT QEKTSNSLTE DSKMANAKQL SSDAEAQKLG KPSAHASQSF 910 920 930 940 950 960 CESSSETPFH FTLPKEGDII PPLTGATPPL IGHLKLEPKR HSTPIGISNY PESTIATSDV 970 980 990 1000 1010 1020 MSESMVETHD PILGSGKGDS GAAPDVDDKL CLRMKLVSPE TEASEESLQF NLEKPATGER 1030 1040 1050 1060 1070 1080 KNGSTAVAES VASPQKTMSV LSCICEARQE NEARSEDPPT TPIRGNLLHF PSSQGEEEKE 1090 1100 1110 1120 1130 1140 KLEGDHTIRQ SQQPMKPISP VKDPVSPASQ KMVIQGPSSP QGEAMVTDVL EDQKEGRSTN 1150 1160 1170 1180 1190 1200 KENPSKALIE RPSQNNIGIQ TMECSLRVPE TVSAATQTIK NVCEQGTSTV DQNFGKQDAT 1210 1220 1230 1240 1250 1260 VQTERGSGEK PVSAPGDDTE SLHSQGEEEF DMPQPPHGHV LHRHMRTIRE VRTLVTRVIT 1270 1280 1290 1300 1310 1320 DVYYVDGTEV ERKVTEETEE PIVECQECET EVSPSQTGGS SGDLGDISSF SSKASSLHRT 1330 1340 1350 1360 1370 1380 SSGTSLSAMH SSGSSGKGAG PLRGKTSGTE PADFALPSSR GGPGKLSPRK GVSQTGTPVC 1390 1400 1410 1420 1430 1440 EEDGDAGLGI RQGGKAPVTP RGRGRRGRPP SRTTGTRETA VPGPLGIEDI SPNLSPDDKS 1450 1460 1470 1480 1490 1500 FSRVVPRVPD STRRTDVGAG ALRRSDSPEI PFQAAAGPSD GLDASSPGNS FVGLRVVAKW 1510 1520 1530 1540 1550 1560 SSNGYFYSGK ITRDVGAGKY KLLFDDGYEC DVLGKDILLC DPIPLDTEVT ALSEDEYFSA 1570 1580 1590 1600 1610 1620 GVVKGHRKES GELYYSIEKE GQRKWYKRMA VILSLEQGNR LREQYGLGPY EAVTPLTKAA 1630 1640 1650 1660 1670 1680 DISLDNLVEG KRKRRSNVSS PATPTASSSS STTPTRKITE SPRASMGVLS GKRKLITSEE 1690 1700 1710 1720 1730 1740 ERSPAKRGRK SATVKPGAVG AGEFVSPCES GDNTGEPSAL EEQRGPLPLN KTLFLGYAFL 1750 1760 1770 1780 1790 1800 LTMATTSDKL ASRSKLPDGP TGSSEEEEEF LEIPPFNKQY TESQLRAGAG YILEDFNEAQ 1810 1820 1830 1840 1850 1860 CNTAYQCLLI ADQHCRTRKY FLCLASGIPC VSHVWVHDSC HANQLQNYRN YLLPAGYSLE 1870 1880 1890 1900 1910 1920 EQRILDWQPR ENPFQNLKVL LVSDQQQNFL ELWSEILMTG GAASVKQHHS SAHNKDIALG 1930 1940 1950 1960 1970 VFDVVVTDPS CPASVLKCAE ALQLPVVSQE WVIQCLIVGE RIGFKQHPKY KHDYVSH

References

	« Hide 'large scale' referencesShow '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 2). 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]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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-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.
[18]	"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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[19]	"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.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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.
[22]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[23]	"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.
[24]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"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].
[26]	"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, MASS SPECTROMETRY.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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

NIEHS-SNPs

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.
BC112161 mRNA. Translation: AAI12162.1.
U09477 mRNA. Translation: AAA21596.1.

IPI

IPI00029778.
IPI00742743.

PIR

I38604.

RefSeq

NP_001135451.1. NM_001141979.1.
NP_001135452.1. NM_001141980.1.
NP_005648.1. NM_005657.2.

UniGene

Hs.440968.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GZH	X-ray	2.60	B/D	1724-1972	[»]
1KZY	X-ray	2.50	C/D	1714-1972	[»]
1XNI	X-ray	2.80	A/B/C/D/E/F/G/H/I/J	1485-1602	[»]
2G3R	X-ray	1.25	A	1484-1603	[»]
2IG0	X-ray	1.70	A	1484-1603	[»]
2LVM	NMR	-	A	1484-1603	[»]
3LGF	X-ray	1.50	A	1484-1603	[»]
3LGL	X-ray	1.60	A	1484-1603	[»]
3LH0	X-ray	1.90	A	1484-1603	[»]

ProteinModelPortal

Q12888.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5978N.

IntAct

Q12888. 16 interactions.

MINT

MINT-276057.

STRING

9606.ENSP00000371475.

PTM databases

PhosphoSite

Q12888.

Polymorphism databases

DMDM

8928568.

Proteomic databases

PaxDb

Q12888.

PRIDE

Q12888.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263801; ENSP00000263801; ENSG00000067369.
ENST00000382044; ENSP00000371475; ENSG00000067369.

GeneID

7158.

KEGG

hsa:7158.

UCSC

uc001zrr.4. human.
uc001zrs.3. human.

Organism-specific databases

CTD

7158.

GeneCards

GC15M043699.

HGNC

HGNC:11999. TP53BP1.

HPA

CAB004083.
HPA008788.
HPA022133.

MIM

605230. gene.

neXtProt

NX_Q12888.

PharmGKB

PA36680.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG264535.

HOGENOM

HOG000231961.

HOVERGEN

HBG060882.

InParanoid

Q12888.

OMA

PEIPFQA.

OrthoDB

EOG43TZTM.

PhylomeDB

Q12888.

Enzyme and pathway databases

Reactome

REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

Q12888.

Bgee

Q12888.

CleanEx

HS_TP53BP1.

Genevestigator

Q12888.

GermOnline

ENSG00000067369. Homo sapiens.

Family and domain databases

Gene3D

2.30.30.30. 1 hit.

InterPro

IPR015125. 53-BP1_Tudor.
IPR001357. BRCT_dom.
IPR014722. Rib_L2_dom2.
[Graphical view]

Pfam

PF09038. 53-BP1_Tudor. 1 hit.
[Graphical view]

SMART

SM00292. BRCT. 2 hits.
[Graphical view]

SUPFAM

SSF52113. BRCT. 2 hits.

PROSITE

PS50172. BRCT. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TP53BP1. human.

EvolutionaryTrace

Q12888.

GenomeRNAi

7158.

NextBio

28010.

PMAP-CutDB

Q12888.

SOURCE

Search...

Entry information

Entry name

TP53B_HUMAN

Accession

Primary (citable) accession number: Q12888
Secondary accession number(s): Q2M1Z7 , Q4LE46, Q5FWZ3, Q7Z3U4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 145 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.