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P70399

- TP53B_MOUSE

UniProt

P70399 - TP53B_MOUSE

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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

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. sequence-specific DNA 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
Complete GO annotation...

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. kinetochore Source: MGI
  2. nucleus Source: MGI
  3. replication fork Source: MGI
Complete GO annotation...

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 – 5461Phosphoserine1 Publication
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 – 11031Phosphoserine1 Publication
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) [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 VLEEDAGSHF SVLSRHLPNL
60 70 80 90 100
QMHKENPVLD IVSNPEQSAV EQGDSNSSFN EHLKEKKASD PVESSHLGTS
110 120 130 140 150
GSISQVIERL PQPNRTSSAL AVTVEAASLP EEEKEEEELE EKEGVGANAP
160 170 180 190 200
GADSLAAEDS ASSQLGFGVL ELSQSQDVEE HTVPYDVNQE HLQLVTTNSG
210 220 230 240 250
SSPLSDVDAS TAIKCEEQPT EDIAMIEQPS KDIPVTVQPG KGIHVVEEQN
260 270 280 290 300
LPLVRSEDRP SSPQVSVAAV ETKEQVPARE LLEEGPQVQP SSEPEVSSTQ
310 320 330 340 350
EDLFDQSSKT ASDGCSTPSR EEGGCSPVST PATTLQLLQL SGQKPLVQES
360 370 380 390 400
LSTNSSDLVA PSPDAFRSTP FIVPSSPTEQ GGRKDEPMDM SVIPAGGEPF
410 420 430 440 450
QKLHDDEAME TEKPLLPSQP TVSPQASTPV SRSTPVFTPG SLPIPSQPEF
460 470 480 490 500
SHDIFIPSPS LEEPSDDVKK GGGLHSSSLT VECSKTSESE PKNFTDDLGL
510 520 530 540 550
SMTGDSCKLM LSTSEYSQSS KMESLGSPRT EEDRENTQID DTEPLSPVSN
560 570 580 590 600
SKLPADSENV LVTPSQDDQV EMSQNVDKAK EDETEDRGDC KGREDAVAED
610 620 630 640 650
VCIDLTCDSG SQAVPSPATR SEALSSVLDQ EEAMDTKEHH PEEGFSGSEV
660 670 680 690 700
EEVPETPCGS HREEPKEEAM ESIPLHLSLT ETQSEALCLQ KEAPKEECPE
710 720 730 740 750
AMEVETSVIS IDSPQKLQVL DQELEHKDPD TWEEATSEDS SVVIVDVKEP
760 770 780 790 800
SPRADVSCEP LEEVEKCSDS QSWEGVAPEE EPCAENRLDT PEEKRIECDG
810 820 830 840 850
DSKAETTEKD AVTEDSPQPP LPSVRDEPVR PDQETQQPQV QEKESPVTVD
860 870 880 890 900
AEVADDKQLG PEGACQQLEK APACASQSFC ESSSETPFHF TLPKEGDIIP
910 920 930 940 950
PLTGATPPLI GHLKLEPKRH STPIGISNYP ESTIATSDVT SESMVEINDP
960 970 980 990 1000
LLGNEKGDSE SAPEMDGKLS LKMKLVSPET EASEESLQFS LEKPTTAERK
1010 1020 1030 1040 1050
NGSTAIAEPV ASLQKPVPVF GCIYEAQQEK EAQSEAPPSA PDRANLLHFP
1060 1070 1080 1090 1100
SAQEEDKERP DVTPKLRQSE QPVKPVGPVM DDAAPEDSAS PVSQQRASQE
1110 1120 1130 1140 1150
PFSPAEDVME TDLLEGLAAN QDRPSKMLMD RPTQSNIGIQ TVDHSLCAPE
1160 1170 1180 1190 1200
TVSAATQTVK SVCEQGTSTA EQNSGKQDAT VQTERGSGEK PASAPVDDTE
1210 1220 1230 1240 1250
SLHSQGEEEF EMPQPPHGHV LHRHMRTIRE VRTLVTRVIT DVYYVDGTEV
1260 1270 1280 1290 1300
ERKVTEETEE PIVECQECET EVSPSQTGGS SGDLGDISSF SSKASSSHHT
1310 1320 1330 1340 1350
SSGTSLSAIH SSGSSGRGAG PLKGKASGTE AADFALPSSR GGPGKLSPRK
1360 1370 1380 1390 1400
GISQTGAPVC EEDGDAGLGI RQGGKAPVTP RGRGRRGRPP SRTTGTRETV
1410 1420 1430 1440 1450
VSGPLGVEDI SPSMSPDDKS FTRIMPRVPD STKRTDASSS TLRRSDSPEI
1460 1470 1480 1490 1500
PFQAATGSSD GLDSSSSGNS FVGLRVVAKW SSNGYFYSGK ITRDVGAGKY
1510 1520 1530 1540 1550
KLLFDDGYEC DVLGKDILLC DPIPLDTEVT ALSEDEYFSA GVVKGHRKES
1560 1570 1580 1590 1600
GELYYSIEKE GQRKWYKRMA VILSLEQGNR LREQYGLGPY EAVTPLTKAA
1610 1620 1630 1640 1650
DISLDNLVEG KRKRRSNISS PVTPTAASSS STTPTRKATE SPRASTGVPS
1660 1670 1680 1690 1700
GKRKLPTSEE ERSPAKRGRK SATVKPGTVG AAEFVSPCET GDNIGEPSVL
1710 1720 1730 1740 1750
EEPRGPLPLN KTLFLGYAFL LTMATTSDKL ASRSKLLDGP TGSSEEEEEF
1760 1770 1780 1790 1800
LEIPPFNKQY TECQLRAGAG YILEDFNEAQ CNTAYQCLLI ADQHCRTRKY
1810 1820 1830 1840 1850
FLCLASGIPC VSHVWVHDSC HANQLQNYRN YLLPAGYSLE EQRILDWQPR
1860 1870 1880 1890 1900
ENPFQNLKVL LVSDQQQNFL ELWSEILMTG GAASVKQHHS SAHNKDIALG
1910 1920 1930 1940 1950
VFDVVVTDPS CPASVLKCAE ALQLPVVSQE WVIQCLIVGE RIGFKQHPKY

KHDYVSH
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

CTDi 27223.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 122 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