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P70399

- TP53B_MOUSE

UniProt

P70399 - TP53B_MOUSE

Protein

Tumor suppressor p53-binding protein 1

Gene

Tp53bp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (10 Jan 2006)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    DNA damage, DNA repair, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

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

    Organism-specific databases

    MGIiMGI:1351320. Trp53bp1.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Centromere, Chromosome, Kinetochore, Nucleus

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251PhosphoserineBy similarity
    Modified residuei104 – 1041PhosphoserineBy similarity
    Modified residuei163 – 1631PhosphoserineBy similarity
    Modified residuei262 – 2621PhosphoserineBy similarity
    Modified residuei291 – 2911PhosphoserineBy similarity
    Modified residuei299 – 2991PhosphothreonineBy similarity
    Modified residuei362 – 3621PhosphoserineBy similarity
    Modified residuei376 – 3761PhosphoserineBy similarity
    Modified residuei391 – 3911PhosphoserineBy similarity
    Modified residuei446 – 4461PhosphoserineBy similarity
    Modified residuei517 – 5171PhosphoserineBy similarity
    Modified residuei519 – 5191PhosphoserineBy similarity
    Modified residuei537 – 5371PhosphothreonineBy similarity
    Modified residuei542 – 5421PhosphothreonineBy similarity
    Modified residuei546 – 5461Phosphoserine2 Publications
    Modified residuei573 – 5731PhosphoserineBy similarity
    Modified residuei621 – 6211PhosphoserineBy similarity
    Modified residuei625 – 6251PhosphoserineBy similarity
    Modified residuei626 – 6261PhosphoserineBy similarity
    Modified residuei906 – 9061PhosphothreonineBy similarity
    Modified residuei959 – 9591PhosphoserineBy similarity
    Modified residuei1012 – 10121PhosphoserineBy similarity
    Modified residuei1069 – 10691PhosphoserineBy similarity
    Modified residuei1090 – 10901PhosphoserineBy similarity
    Modified residuei1103 – 11031Phosphoserine2 Publications
    Modified residuei1199 – 11991PhosphothreonineBy similarity
    Modified residuei1201 – 12011PhosphoserineBy similarity
    Modified residuei1204 – 12041PhosphoserineBy similarity
    Modified residuei1347 – 13471PhosphoserineBy similarity
    Modified residuei1353 – 13531PhosphoserineBy similarity
    Modified residuei1411 – 14111PhosphoserineBy similarity
    Modified residuei1415 – 14151PhosphoserineBy similarity
    Modified residuei1445 – 14451PhosphoserineBy similarity
    Modified residuei1447 – 14471PhosphoserineBy similarity
    Modified residuei1459 – 14591PhosphoserineBy similarity
    Modified residuei1594 – 15941PhosphothreonineBy similarity
    Modified residuei1603 – 16031PhosphoserineBy similarity
    Modified residuei1663 – 16631PhosphoserineBy similarity
    Modified residuei1686 – 16861PhosphoserineBy similarity
    Modified residuei1744 – 17441PhosphoserineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP70399.
    PaxDbiP70399.
    PRIDEiP70399.

    PTM databases

    PhosphoSiteiP70399.

    Expressioni

    Gene expression databases

    GenevestigatoriP70399.

    Interactioni

    Subunit structurei

    May form homooligomers. Interacts with DCLRE1C. Interacts with histone H2AFX and this requires phosphorylation of H2AFX on 'Ser-139'. Interacts with histone H4 that has been dimethylated at 'Lys-20' (H4K20me2). Has low affinity for histone H4 containing monomethylated 'Lys-20' (H4K20me1). Does not bind histone H4 containing unmethylated or trimethylated 'Lys-20' (H4K20me3). Has low affinity for histone H3 that has been dimethylated on 'Lys-79'. Has very low affinity for histone H3 that has been monomethylated on 'Lys-79' (in vitro). Does not bind unmethylated histone H3. Interacts with MUM1/EXPAND1. Interacts with CHEK2; modulates CHEK2 phosphorylation at 'Thr-68' in response to infrared By similarity. Binds to the central domain of p53/TP53. Interacts with IFI202A. Interacts with MSL1; this interaction may be required for MSL1 DNA repair activity, but not for histone acetyltransferase activity.By similarity1 Publication

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

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

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP70399.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1737 – 183397BRCT 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1849 – 1949101BRCT 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1468 – 1589122Tudor-likeBy similarityAdd
    BLAST
    Regioni1480 – 150829Interaction with dimethylated histone H4By similarityAdd
    BLAST

    Motif

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

    Compositional bias

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

    Sequence similaritiesi

    Contains 2 BRCT domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG264535.
    HOGENOMiHOG000231961.
    HOVERGENiHBG060882.
    InParanoidiP70399.

    Family and domain databases

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

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P70399-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

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

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

    Note: No experimental confirmation available.

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

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

    Note: No experimental confirmation available.

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti141 – 1411E → EE in AAH79906. (PubMed:15489334)Curated
    Sequence conflicti395 – 3951A → V in AAH79906. (PubMed:15489334)Curated
    Sequence conflicti421 – 4211T → A in AAH79906. (PubMed:15489334)Curated
    Sequence conflicti669 – 6691A → P in AAH79906. (PubMed:15489334)Curated
    Sequence conflicti1064 – 10641P → L in AAH79906. (PubMed:15489334)Curated
    Sequence conflicti1065 – 10651K → N in AAH35206. (PubMed:15489334)Curated
    Sequence conflicti1171 – 11722EQ → DE in AAC52876. (PubMed:8910340)Curated
    Sequence conflicti1175 – 11751G → R in CAC94013. (PubMed:11801725)Curated
    Sequence conflicti1194 – 11941A → T in AAC52876. (PubMed:8910340)Curated
    Sequence conflicti1259 – 12591E → G in AAC52876. (PubMed:8910340)Curated
    Sequence conflicti1759 – 17591Q → H in AAH79906. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 943943Missing in isoform 2. 1 PublicationVSP_016899Add
    BLAST
    Alternative sequencei1100 – 11001E → EQRASQE in isoform 3. 1 PublicationVSP_016900
    Alternative sequencei1347 – 139650Missing in isoform 3. 1 PublicationVSP_016901Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ414734 mRNA. Translation: CAC94013.1.
    BC035206 mRNA. Translation: AAH35206.1.
    BC079906 mRNA. Translation: AAH79906.1.
    U67885 mRNA. Translation: AAC52876.1.
    RefSeqiNP_001277759.1. NM_001290830.1.
    NP_038763.3. NM_013735.4.
    UniGeneiMm.215389.
    Mm.383499.
    Mm.481841.

    Genome annotation databases

    GeneIDi27223.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

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

    3D structure databases

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

    Protein-protein interaction databases

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

    PTM databases

    PhosphoSitei P70399.

    Proteomic databases

    MaxQBi P70399.
    PaxDbi P70399.
    PRIDEi P70399.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 27223.

    Organism-specific databases

    MGIi MGI:1351320. Trp53bp1.

    Phylogenomic databases

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

    Miscellaneous databases

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

    Gene expression databases

    Genevestigatori P70399.

    Family and domain databases

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

    Publicationsi

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

    Entry informationi

    Entry nameiTP53B_MOUSE
    AccessioniPrimary (citable) accession number: P70399
    Secondary accession number(s): Q68FD0, Q8CI97, Q91YC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 10, 2006
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3