Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

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

Q12888

- TP53B_HUMAN

UniProt

Q12888 - TP53B_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: UniProtKB
    5. RNA polymerase II activating transcription factor binding Source: BHF-UCL
    6. RNA polymerase II transcription cofactor activity Source: BHF-UCL
    7. 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

    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. condensed chromosome kinetochore Source: UniProtKB-SubCell
    2. cytoplasm Source: ProtInc
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA
    5. replication fork Source: Ensembl

    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. 3 Publications
    Mutagenesisi1396 – 13961R → K: No detectable effect on methylation by PRMT1 (in vitro). 3 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. 3 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. 3 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. 3 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. 3 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. 3 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. 3 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. 3 Publications
    Mutagenesisi1403 – 14031R → K: No detectable effect on methylation by PRMT1 (in vitro). 3 Publications
    Mutagenesisi1495 – 14951W → A or H: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20'. 3 Publications
    Mutagenesisi1495 – 14951W → F: No effect on recruitment to double strand breaks. 3 Publications
    Mutagenesisi1495 – 14951W → V: Reduces recruitment to double strand breaks. 3 Publications
    Mutagenesisi1500 – 15001Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. 2 Publications
    Mutagenesisi1502 – 15021Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. 3 Publications
    Mutagenesisi1502 – 15021Y → L or Q: Abolishes recruitment to double strand breaks. 3 Publications
    Mutagenesisi1521 – 15211D → A: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20'. Abolishes recruitment to double strand breaks. 3 Publications
    Mutagenesisi1521 – 15211D → R: Abolishes recruitment to double strand breaks. 3 Publications
    Mutagenesisi1523 – 15231Y → A: Increases affinity for histone H4 that has been dimethylated at 'Lys-20'. No effect on recruitment to double strand breaks. 2 Publications
    Mutagenesisi1523 – 15231Y → S: Decreases affinity for histone H4 that has been dimethylated at 'Lys-20'. 2 Publications

    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

    ArrayExpressiQ12888.
    BgeeiQ12888.
    CleanExiHS_TP53BP1.
    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. 116 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[»]
    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.
    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

    MDPTGSQLDS DFSQQDTPCL IIEDSQPESQ VLEDDSGSHF SMLSRHLPNL     50
    QTHKENPVLD VVSNPEQTAG EERGDGNSGF NEHLKENKVA DPVDSSNLDT 100
    CGSISQVIEQ LPQPNRTSSV LGMSVESAPA VEEEKGEELE QKEKEKEEDT 150
    SGNTTHSLGA EDTASSQLGF GVLELSQSQD VEENTVPYEV DKEQLQSVTT 200
    NSGYTRLSDV DANTAIKHEE QSNEDIPIAE QSSKDIPVTA QPSKDVHVVK 250
    EQNPPPARSE DMPFSPKASV AAMEAKEQLS AQELMESGLQ IQKSPEPEVL 300
    STQEDLFDQS NKTVSSDGCS TPSREEGGCS LASTPATTLH LLQLSGQRSL 350
    VQDSLSTNSS DLVAPSPDAF RSTPFIVPSS PTEQEGRQDK PMDTSVLSEE 400
    GGEPFQKKLQ SGEPVELENP PLLPESTVSP QASTPISQST PVFPPGSLPI 450
    PSQPQFSHDI FIPSPSLEEQ SNDGKKDGDM HSSSLTVECS KTSEIEPKNS 500
    PEDLGLSLTG DSCKLMLSTS EYSQSPKMES LSSHRIDEDG ENTQIEDTEP 550
    MSPVLNSKFV PAENDSILMN PAQDGEVQLS QNDDKTKGDD TDTRDDISIL 600
    ATGCKGREET VAEDVCIDLT CDSGSQAVPS PATRSEALSS VLDQEEAMEI 650
    KEHHPEEGSS GSEVEEIPET PCESQGEELK EENMESVPLH LSLTETQSQG 700
    LCLQKEMPKK ECSEAMEVET SVISIDSPQK LAILDQELEH KEQEAWEEAT 750
    SEDSSVVIVD VKEPSPRVDV SCEPLEGVEK CSDSQSWEDI APEIEPCAEN 800
    RLDTKEEKSV EYEGDLKSGT AETEPVEQDS SQPSLPLVRA DDPLRLDQEL 850
    QQPQTQEKTS NSLTEDSKMA NAKQLSSDAE AQKLGKPSAH ASQSFCESSS 900
    ETPFHFTLPK EGDIIPPLTG ATPPLIGHLK LEPKRHSTPI GISNYPESTI 950
    ATSDVMSESM VETHDPILGS GKGDSGAAPD VDDKLCLRMK LVSPETEASE 1000
    ESLQFNLEKP ATGERKNGST AVAESVASPQ KTMSVLSCIC EARQENEARS 1050
    EDPPTTPIRG NLLHFPSSQG EEEKEKLEGD HTIRQSQQPM KPISPVKDPV 1100
    SPASQKMVIQ GPSSPQGEAM VTDVLEDQKE GRSTNKENPS KALIERPSQN 1150
    NIGIQTMECS LRVPETVSAA TQTIKNVCEQ GTSTVDQNFG KQDATVQTER 1200
    GSGEKPVSAP GDDTESLHSQ GEEEFDMPQP PHGHVLHRHM RTIREVRTLV 1250
    TRVITDVYYV DGTEVERKVT EETEEPIVEC QECETEVSPS QTGGSSGDLG 1300
    DISSFSSKAS SLHRTSSGTS LSAMHSSGSS GKGAGPLRGK TSGTEPADFA 1350
    LPSSRGGPGK LSPRKGVSQT GTPVCEEDGD AGLGIRQGGK APVTPRGRGR 1400
    RGRPPSRTTG TRETAVPGPL GIEDISPNLS PDDKSFSRVV PRVPDSTRRT 1450
    DVGAGALRRS DSPEIPFQAA AGPSDGLDAS SPGNSFVGLR VVAKWSSNGY 1500
    FYSGKITRDV GAGKYKLLFD DGYECDVLGK DILLCDPIPL DTEVTALSED 1550
    EYFSAGVVKG HRKESGELYY SIEKEGQRKW YKRMAVILSL EQGNRLREQY 1600
    GLGPYEAVTP LTKAADISLD NLVEGKRKRR SNVSSPATPT ASSSSSTTPT 1650
    RKITESPRAS MGVLSGKRKL ITSEEERSPA KRGRKSATVK PGAVGAGEFV 1700
    SPCESGDNTG EPSALEEQRG PLPLNKTLFL GYAFLLTMAT TSDKLASRSK 1750
    LPDGPTGSSE EEEEFLEIPP FNKQYTESQL RAGAGYILED FNEAQCNTAY 1800
    QCLLIADQHC RTRKYFLCLA SGIPCVSHVW VHDSCHANQL QNYRNYLLPA 1850
    GYSLEEQRIL DWQPRENPFQ NLKVLLVSDQ QQNFLELWSE ILMTGGAASV 1900
    KQHHSSAHNK DIALGVFDVV VTDPSCPASV LKCAEALQLP VVSQEWVIQC 1950
    LIVGERIGFK QHPKYKHDYV SH 1972
    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.
    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.
    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 [» ]
    ProteinModelPortali Q12888.
    SMRi Q12888. Positions 1485-1603, 1724-1971.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113011. 116 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.
    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

    ArrayExpressi Q12888.
    Bgeei Q12888.
    CleanExi HS_TP53BP1.
    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

    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 1, 2014
    This is version 160 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