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Q12888

- TP53B_HUMAN

UniProt

Q12888 - TP53B_HUMAN

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Protein

Tumor suppressor p53-binding protein 1

Gene

TP53BP1

Organism
Homo sapiens (Human)
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.3 Publications

GO - Molecular functioni

  1. damaged DNA binding Source: Ensembl
  2. methylated histone binding Source: UniProtKB
  3. p53 binding Source: BHF-UCL
  4. RNA polymerase II activating transcription factor binding Source: BHF-UCL
  5. RNA polymerase II transcription cofactor activity Source: BHF-UCL
  6. telomeric DNA binding Source: Ensembl

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: MGI
  2. DNA repair Source: Reactome
  3. double-strand break repair Source: Reactome
  4. double-strand break repair via homologous recombination Source: Reactome
  5. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  6. positive regulation of transcription, DNA-templated Source: UniProtKB
  7. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  8. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_97. Recruitment of repair and signaling proteins to double-strand breaks.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:11999. TP53BP1.

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.

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. kinetochore Source: UniProtKB-KW
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
  5. replication fork Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi176 – 1783SQS → AQA: Loss of phosphorylation site. 1 Publication
Mutagenesisi1396 – 13961R → 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. 2 Publications
Mutagenesisi1396 – 13961R → K: No detectable effect on methylation by PRMT1 (in vitro). 2 Publications
Mutagenesisi1398 – 13981R → 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. 2 Publications
Mutagenesisi1398 – 13981R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1400. Strongly reduced methylation; when associated with K-1401. 2 Publications
Mutagenesisi1400 – 14001R → 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. 2 Publications
Mutagenesisi1400 – 14001R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1401. 2 Publications
Mutagenesisi1401 – 14011R → 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. 2 Publications
Mutagenesisi1401 – 14011R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1400. 2 Publications
Mutagenesisi1403 – 14031R → 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. 2 Publications
Mutagenesisi1403 – 14031R → K: No detectable effect on methylation by PRMT1 (in vitro). 2 Publications
Mutagenesisi1495 – 14951W → A or H: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20'. 2 Publications
Mutagenesisi1495 – 14951W → F: No effect on recruitment to double strand breaks. 2 Publications
Mutagenesisi1495 – 14951W → V: Reduces recruitment to double strand breaks. 2 Publications
Mutagenesisi1500 – 15001Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. 1 Publication
Mutagenesisi1502 – 15021Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. 2 Publications
Mutagenesisi1502 – 15021Y → L or Q: Abolishes recruitment to double strand breaks. 2 Publications
Mutagenesisi1521 – 15211D → A: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20'. Abolishes recruitment to double strand breaks. 2 Publications
Mutagenesisi1521 – 15211D → R: Abolishes recruitment to double strand breaks. 2 Publications
Mutagenesisi1523 – 15231Y → A: Increases affinity for histone H4 that has been dimethylated at 'Lys-20'. No effect on recruitment to double strand breaks. 1 Publication
Mutagenesisi1523 – 15231Y → S: Decreases affinity for histone H4 that has been dimethylated at 'Lys-20'. 1 Publication

Organism-specific databases

PharmGKBiPA36680.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19721972Tumor suppressor p53-binding protein 1PRO_0000072643Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Phosphoserine1 Publication
Modified residuei105 – 1051Phosphoserine1 Publication
Modified residuei124 – 1241Phosphoserine1 Publication
Modified residuei166 – 1661Phosphoserine1 Publication
Modified residuei176 – 1761Phosphoserine1 Publication
Modified residuei178 – 1781Phosphoserine1 Publication
Modified residuei222 – 2221Phosphoserine3 Publications
Modified residuei265 – 2651Phosphoserine1 Publication
Modified residuei294 – 2941Phosphoserine5 Publications
Modified residuei302 – 3021Phosphothreonine2 Publications
Modified residuei366 – 3661Phosphoserine1 Publication
Modified residuei380 – 3801Phosphoserine2 Publications
Modified residuei395 – 3951Phosphoserine1 Publication
Modified residuei398 – 3981Phosphoserine1 Publication
Modified residuei452 – 4521Phosphoserine1 Publication
Modified residuei500 – 5001Phosphoserine5 Publications
Modified residuei523 – 5231Phosphoserine4 Publications
Modified residuei525 – 5251Phosphoserine4 Publications
Modified residuei543 – 5431Phosphothreonine2 Publications
Modified residuei548 – 5481Phosphothreonine1 Publication
Modified residuei552 – 5521Phosphoserine6 Publications
Modified residuei566 – 5661Phosphoserine1 Publication
Modified residuei580 – 5801Phosphoserine1 Publication
Modified residuei635 – 6351Phosphoserine1 Publication
Modified residuei639 – 6391Phosphoserine2 Publications
Modified residuei640 – 6401Phosphoserine2 Publications
Modified residuei809 – 8091Phosphoserine3 Publications
Modified residuei831 – 8311Phosphoserine3 Publications
Modified residuei834 – 8341Phosphoserine2 Publications
Modified residuei855 – 8551Phosphothreonine1 Publication
Modified residuei922 – 9221Phosphothreonine1 Publication
Modified residuei970 – 9701Phosphoserine1 Publication
Modified residuei975 – 9751Phosphoserine1 Publication
Modified residuei1028 – 10281Phosphoserine5 Publications
Modified residuei1068 – 10681Phosphoserine1 Publication
Modified residuei1086 – 10861Phosphoserine1 Publication
Modified residuei1094 – 10941Phosphoserine4 Publications
Modified residuei1101 – 11011Phosphoserine1 Publication
Modified residuei1114 – 11141Phosphoserine4 Publications
Modified residuei1214 – 12141Phosphothreonine1 Publication
Modified residuei1216 – 12161Phosphoserine2 Publications
Modified residuei1219 – 12191Phosphoserine4 Publications
Modified residuei1362 – 13621Phosphoserine3 Publications
Modified residuei1368 – 13681Phosphoserine1 Publication
Modified residuei1372 – 13721Phosphothreonine1 Publication
Modified residuei1426 – 14261Phosphoserine4 Publications
Modified residuei1430 – 14301Phosphoserine4 Publications
Modified residuei1460 – 14601Phosphoserine1 Publication
Modified residuei1462 – 14621Phosphoserine2 Publications
Modified residuei1474 – 14741Phosphoserine1 Publication
Modified residuei1609 – 16091Phosphothreonine2 Publications
Modified residuei1618 – 16181Phosphoserine2 Publications
Modified residuei1678 – 16781Phosphoserine3 Publications
Modified residuei1701 – 17011Phosphoserine1 Publication
Modified residuei1759 – 17591Phosphoserine1 Publication
Modified residuei1778 – 17781Phosphoserine2 Publications

Post-translational modificationi

Asymmetrically dimethylated on Arg residues by PRMT1. Methylation is required for DNA binding.2 Publications
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.12 Publications

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ12888.
PaxDbiQ12888.
PRIDEiQ12888.

PTM databases

PhosphoSiteiQ12888.

Miscellaneous databases

PMAP-CutDBQ12888.

Expressioni

Gene expression databases

BgeeiQ12888.
CleanExiHS_TP53BP1.
ExpressionAtlasiQ12888. baseline and differential.
GenevestigatoriQ12888.

Organism-specific databases

HPAiCAB004083.
HPA008788.
HPA022133.

Interactioni

Subunit structurei

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.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST1H3DP684315EBI-396540,EBI-79722
HIST2H4BP628058EBI-396540,EBI-302023
PAXIP1Q6ZW494EBI-396540,EBI-743225
Paxip1Q6NZQ42EBI-396540,EBI-1395317From a different organism.
TP53P046372EBI-396540,EBI-366083
VRK1Q999868EBI-396540,EBI-1769146
ZNHIT1O432572EBI-396540,EBI-347522

Protein-protein interaction databases

BioGridi113011. 120 interactions.
DIPiDIP-5978N.
IntActiQ12888. 24 interactions.
MINTiMINT-276057.
STRINGi9606.ENSP00000371475.

Structurei

Secondary structure

1
1972
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1490 – 14945
Turni1496 – 14983
Beta strandi1501 – 151111
Beta strandi1514 – 15196
Beta strandi1524 – 15285
Helixi1529 – 15313
Beta strandi1532 – 15354
Beta strandi1543 – 15475
Beta strandi1553 – 156412
Beta strandi1567 – 15748
Beta strandi1577 – 15826
Helixi1583 – 15853
Beta strandi1586 – 15883
Helixi1590 – 15945
Helixi1597 – 16004
Helixi1715 – 17195
Turni1726 – 17316
Beta strandi1732 – 17365
Helixi1741 – 17455
Helixi1773 – 17819
Turni1782 – 17843
Turni1793 – 17997
Beta strandi1801 – 18088
Helixi1813 – 18219
Beta strandi1825 – 18273
Helixi1829 – 18379
Helixi1843 – 18453
Beta strandi1851 – 18533
Turni1854 – 18574
Beta strandi1858 – 18603
Turni1868 – 18714
Beta strandi1873 – 18797
Turni1881 – 18844
Helixi1885 – 189410
Beta strandi1898 – 190811
Helixi1914 – 19163
Beta strandi1918 – 19225
Helixi1928 – 193710
Helixi1944 – 195310
Helixi1963 – 19653

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4CRIX-ray2.35A/B1459-1634[»]
ProteinModelPortaliQ12888.
SMRiQ12888. Positions 1485-1603, 1724-1971.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12888.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1724 – 1848125BRCT 1PROSITE-ProRule annotationAdd
BLAST
Domaini1864 – 1964101BRCT 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1483 – 1604122Tudor-likeAdd
BLAST
Regioni1495 – 152329Interaction with dimethylated histone H4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1396 – 14038GAR

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1642 – 16465Poly-Ser
Compositional biasi1760 – 17645Poly-Glu

Domaini

The Tudor-like region mediates binding to H4K20me2.

Sequence similaritiesi

Contains 2 BRCT domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG264535.
GeneTreeiENSGT00390000011891.
HOGENOMiHOG000231961.
HOVERGENiHBG060882.
InParanoidiQ12888.
OMAiPEIPFQA.
OrthoDBiEOG7RZ5P1.
PhylomeDBiQ12888.
TreeFamiTF350227.

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: Q12888-1) [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
MDPTGSQLDS DFSQQDTPCL IIEDSQPESQ VLEDDSGSHF SMLSRHLPNL
60 70 80 90 100
QTHKENPVLD VVSNPEQTAG EERGDGNSGF NEHLKENKVA DPVDSSNLDT
110 120 130 140 150
CGSISQVIEQ LPQPNRTSSV LGMSVESAPA VEEEKGEELE QKEKEKEEDT
160 170 180 190 200
SGNTTHSLGA EDTASSQLGF GVLELSQSQD VEENTVPYEV DKEQLQSVTT
210 220 230 240 250
NSGYTRLSDV DANTAIKHEE QSNEDIPIAE QSSKDIPVTA QPSKDVHVVK
260 270 280 290 300
EQNPPPARSE DMPFSPKASV AAMEAKEQLS AQELMESGLQ IQKSPEPEVL
310 320 330 340 350
STQEDLFDQS NKTVSSDGCS TPSREEGGCS LASTPATTLH LLQLSGQRSL
360 370 380 390 400
VQDSLSTNSS DLVAPSPDAF RSTPFIVPSS PTEQEGRQDK PMDTSVLSEE
410 420 430 440 450
GGEPFQKKLQ SGEPVELENP PLLPESTVSP QASTPISQST PVFPPGSLPI
460 470 480 490 500
PSQPQFSHDI FIPSPSLEEQ SNDGKKDGDM HSSSLTVECS KTSEIEPKNS
510 520 530 540 550
PEDLGLSLTG DSCKLMLSTS EYSQSPKMES LSSHRIDEDG ENTQIEDTEP
560 570 580 590 600
MSPVLNSKFV PAENDSILMN PAQDGEVQLS QNDDKTKGDD TDTRDDISIL
610 620 630 640 650
ATGCKGREET VAEDVCIDLT CDSGSQAVPS PATRSEALSS VLDQEEAMEI
660 670 680 690 700
KEHHPEEGSS GSEVEEIPET PCESQGEELK EENMESVPLH LSLTETQSQG
710 720 730 740 750
LCLQKEMPKK ECSEAMEVET SVISIDSPQK LAILDQELEH KEQEAWEEAT
760 770 780 790 800
SEDSSVVIVD VKEPSPRVDV SCEPLEGVEK CSDSQSWEDI APEIEPCAEN
810 820 830 840 850
RLDTKEEKSV EYEGDLKSGT AETEPVEQDS SQPSLPLVRA DDPLRLDQEL
860 870 880 890 900
QQPQTQEKTS NSLTEDSKMA NAKQLSSDAE AQKLGKPSAH ASQSFCESSS
910 920 930 940 950
ETPFHFTLPK EGDIIPPLTG ATPPLIGHLK LEPKRHSTPI GISNYPESTI
960 970 980 990 1000
ATSDVMSESM VETHDPILGS GKGDSGAAPD VDDKLCLRMK LVSPETEASE
1010 1020 1030 1040 1050
ESLQFNLEKP ATGERKNGST AVAESVASPQ KTMSVLSCIC EARQENEARS
1060 1070 1080 1090 1100
EDPPTTPIRG NLLHFPSSQG EEEKEKLEGD HTIRQSQQPM KPISPVKDPV
1110 1120 1130 1140 1150
SPASQKMVIQ GPSSPQGEAM VTDVLEDQKE GRSTNKENPS KALIERPSQN
1160 1170 1180 1190 1200
NIGIQTMECS LRVPETVSAA TQTIKNVCEQ GTSTVDQNFG KQDATVQTER
1210 1220 1230 1240 1250
GSGEKPVSAP GDDTESLHSQ GEEEFDMPQP PHGHVLHRHM RTIREVRTLV
1260 1270 1280 1290 1300
TRVITDVYYV DGTEVERKVT EETEEPIVEC QECETEVSPS QTGGSSGDLG
1310 1320 1330 1340 1350
DISSFSSKAS SLHRTSSGTS LSAMHSSGSS GKGAGPLRGK TSGTEPADFA
1360 1370 1380 1390 1400
LPSSRGGPGK LSPRKGVSQT GTPVCEEDGD AGLGIRQGGK APVTPRGRGR
1410 1420 1430 1440 1450
RGRPPSRTTG TRETAVPGPL GIEDISPNLS PDDKSFSRVV PRVPDSTRRT
1460 1470 1480 1490 1500
DVGAGALRRS DSPEIPFQAA AGPSDGLDAS SPGNSFVGLR VVAKWSSNGY
1510 1520 1530 1540 1550
FYSGKITRDV GAGKYKLLFD DGYECDVLGK DILLCDPIPL DTEVTALSED
1560 1570 1580 1590 1600
EYFSAGVVKG HRKESGELYY SIEKEGQRKW YKRMAVILSL EQGNRLREQY
1610 1620 1630 1640 1650
GLGPYEAVTP LTKAADISLD NLVEGKRKRR SNVSSPATPT ASSSSSTTPT
1660 1670 1680 1690 1700
RKITESPRAS MGVLSGKRKL ITSEEERSPA KRGRKSATVK PGAVGAGEFV
1710 1720 1730 1740 1750
SPCESGDNTG EPSALEEQRG PLPLNKTLFL GYAFLLTMAT TSDKLASRSK
1760 1770 1780 1790 1800
LPDGPTGSSE EEEEFLEIPP FNKQYTESQL RAGAGYILED FNEAQCNTAY
1810 1820 1830 1840 1850
QCLLIADQHC RTRKYFLCLA SGIPCVSHVW VHDSCHANQL QNYRNYLLPA
1860 1870 1880 1890 1900
GYSLEEQRIL DWQPRENPFQ NLKVLLVSDQ QQNFLELWSE ILMTGGAASV
1910 1920 1930 1940 1950
KQHHSSAHNK DIALGVFDVV VTDPSCPASV LKCAEALQLP VVSQEWVIQC
1960 1970
LIVGERIGFK QHPKYKHDYV SH
Length:1,972
Mass (Da):213,574
Last modified:December 1, 2000 - v2
Checksum:i13E2CC8A265F9D2A
GO
Isoform 2 (identifier: Q12888-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPGEQM

Note: No experimental confirmation available.

Show »
Length:1,977
Mass (Da):214,117
Checksum:iB8C43ACE26E9A204
GO
Isoform 3 (identifier: Q12888-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPGEQM
     1692-1693: Missing.

Note: No experimental confirmation available.

Show »
Length:1,975
Mass (Da):213,989
Checksum:i14467931B27D109D
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti796 – 7961P → S in CAD97660. (PubMed:17974005)Curated
Sequence conflicti1600 – 16001Y → C in CAD97660. (PubMed:17974005)Curated
Sequence conflicti1958 – 19581G → R in CAD97660. (PubMed:17974005)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti353 – 3531D → E.2 Publications
Corresponds to variant rs560191 [ dbSNP | Ensembl ].
VAR_022172
Natural varianti412 – 4121G → S.2 Publications
Corresponds to variant rs689647 [ dbSNP | Ensembl ].
VAR_022173
Natural varianti648 – 6481M → V.1 Publication
Corresponds to variant rs45443496 [ dbSNP | Ensembl ].
VAR_022174
Natural varianti699 – 6991Q → R.1 Publication
Corresponds to variant rs34823068 [ dbSNP | Ensembl ].
VAR_022175
Natural varianti841 – 8411D → G.
Corresponds to variant rs34185035 [ dbSNP | Ensembl ].
VAR_034558
Natural varianti1014 – 10141E → G.1 Publication
Corresponds to variant rs45470395 [ dbSNP | Ensembl ].
VAR_022176
Natural varianti1026 – 10261V → A.1 Publication
Corresponds to variant rs45482998 [ dbSNP | Ensembl ].
VAR_022177
Natural varianti1136 – 11361K → Q.2 Publications
Corresponds to variant rs2602141 [ dbSNP | Ensembl ].
VAR_022178
Natural varianti1137 – 11371E → K.
Corresponds to variant rs34740611 [ dbSNP | Ensembl ].
VAR_034559
Natural varianti1170 – 11701A → G.1 Publication
Corresponds to variant rs45500399 [ dbSNP | Ensembl ].
VAR_022179
Natural varianti1174 – 11741I → V.1 Publication
Corresponds to variant rs3803339 [ dbSNP | Ensembl ].
VAR_022180
Natural varianti1442 – 14421R → Q.
Corresponds to variant rs2230449 [ dbSNP | Ensembl ].
VAR_034560
Natural varianti1488 – 14881G → W.
Corresponds to variant rs11554564 [ dbSNP | Ensembl ].
VAR_038689

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MPGEQM in isoform 2 and isoform 3. 2 PublicationsVSP_018390
Alternative sequencei1692 – 16932Missing in isoform 3. 1 PublicationVSP_055062

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS10096.1. [Q12888-1]
CCDS45250.1. [Q12888-2]
CCDS45251.1. [Q12888-3]
PIRiI38604.
RefSeqiNP_001135451.1. NM_001141979.1. [Q12888-3]
NP_001135452.1. NM_001141980.1. [Q12888-2]
NP_005648.1. NM_005657.2. [Q12888-1]
XP_005254691.1. XM_005254634.2. [Q12888-1]
UniGeneiHs.440968.
Hs.584887.

Genome annotation databases

EnsembliENST00000263801; ENSP00000263801; ENSG00000067369. [Q12888-1]
ENST00000382044; ENSP00000371475; ENSG00000067369. [Q12888-2]
ENST00000450115; ENSP00000393497; ENSG00000067369. [Q12888-3]
GeneIDi7158.
KEGGihsa:7158.
UCSCiuc001zrr.4. human. [Q12888-2]
uc001zrs.3. human. [Q12888-1]

Polymorphism databases

DMDMi8928568.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS10096.1. [Q12888-1 ]
CCDS45250.1. [Q12888-2 ]
CCDS45251.1. [Q12888-3 ]
PIRi I38604.
RefSeqi NP_001135451.1. NM_001141979.1. [Q12888-3 ]
NP_001135452.1. NM_001141980.1. [Q12888-2 ]
NP_005648.1. NM_005657.2. [Q12888-1 ]
XP_005254691.1. XM_005254634.2. [Q12888-1 ]
UniGenei Hs.440968.
Hs.584887.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4CRI X-ray 2.35 A/B 1459-1634 [» ]
ProteinModelPortali Q12888.
SMRi Q12888. Positions 1485-1603, 1724-1971.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113011. 120 interactions.
DIPi DIP-5978N.
IntActi Q12888. 24 interactions.
MINTi MINT-276057.
STRINGi 9606.ENSP00000371475.

Chemistry

ChEMBLi CHEMBL2424509.

PTM databases

PhosphoSitei Q12888.

Polymorphism databases

DMDMi 8928568.

Proteomic databases

MaxQBi Q12888.
PaxDbi Q12888.
PRIDEi Q12888.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263801 ; ENSP00000263801 ; ENSG00000067369 . [Q12888-1 ]
ENST00000382044 ; ENSP00000371475 ; ENSG00000067369 . [Q12888-2 ]
ENST00000450115 ; ENSP00000393497 ; ENSG00000067369 . [Q12888-3 ]
GeneIDi 7158.
KEGGi hsa:7158.
UCSCi uc001zrr.4. human. [Q12888-2 ]
uc001zrs.3. human. [Q12888-1 ]

Organism-specific databases

CTDi 7158.
GeneCardsi GC15M043699.
HGNCi HGNC:11999. TP53BP1.
HPAi CAB004083.
HPA008788.
HPA022133.
MIMi 605230. gene.
neXtProti NX_Q12888.
PharmGKBi PA36680.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG264535.
GeneTreei ENSGT00390000011891.
HOGENOMi HOG000231961.
HOVERGENi HBG060882.
InParanoidi Q12888.
OMAi PEIPFQA.
OrthoDBi EOG7RZ5P1.
PhylomeDBi Q12888.
TreeFami TF350227.

Enzyme and pathway databases

Reactomei REACT_97. Recruitment of repair and signaling proteins to double-strand breaks.

Miscellaneous databases

ChiTaRSi TP53BP1. human.
EvolutionaryTracei Q12888.
GeneWikii TP53BP1.
GenomeRNAii 7158.
NextBioi 28010.
PMAP-CutDB Q12888.
PROi Q12888.
SOURCEi Search...

Gene expression databases

Bgeei Q12888.
CleanExi HS_TP53BP1.
ExpressionAtlasi Q12888. baseline and differential.
Genevestigatori Q12888.

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. "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. 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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. 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. 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.

Entry informationi

Entry nameiTP53B_HUMAN
AccessioniPrimary (citable) accession number: Q12888
Secondary accession number(s): F8VY86
, Q2M1Z7, Q4LE46, Q5FWZ3, Q7Z3U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 1, 2000
Last modified: October 29, 2014
This is version 161 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3