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Protein

Tumor suppressor p53-binding protein 1

Gene

TP53BP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • DNA binding Source: UniProtKB-KW
  • methylated histone binding Source: UniProtKB
  • p53 binding Source: AgBase
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL
  • RNA polymerase II transcription cofactor activity Source: BHF-UCL

GO - Biological processi

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

BioCyciZFISH:ENSG00000067369-MONOMER.
ReactomeiR-HSA-3232118. SUMOylation of transcription factors.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-69473. G2/M DNA damage checkpoint.
SIGNORiQ12888.

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
Proteomesi
  • UP000005640 Componenti: 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

  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: ProtInc
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
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)DescriptionActionsGraphical viewLength
Mutagenesisi176 – 178SQS → AQA: Loss of phosphorylation site. 1 Publication3
Mutagenesisi1396R → 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 Publications1
Mutagenesisi1396R → K: No detectable effect on methylation by PRMT1 (in vitro). 2 Publications1
Mutagenesisi1398R → 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 Publications1
Mutagenesisi1398R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1400. Strongly reduced methylation; when associated with K-1401. 2 Publications1
Mutagenesisi1400R → 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 Publications1
Mutagenesisi1400R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1401. 2 Publications1
Mutagenesisi1401R → 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 Publications1
Mutagenesisi1401R → K: Reduced methylation by PRMT1 (in vitro). Strongly reduced methylation; when associated with K-1398. Strongly reduced methylation; when associated with K-1400. 2 Publications1
Mutagenesisi1403R → 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 Publications1
Mutagenesisi1403R → K: No detectable effect on methylation by PRMT1 (in vitro). 2 Publications1
Mutagenesisi1495W → A or H: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20'. 2 Publications1
Mutagenesisi1495W → F: No effect on recruitment to double strand breaks. 2 Publications1
Mutagenesisi1495W → V: Reduces recruitment to double strand breaks. 2 Publications1
Mutagenesisi1500Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. 1 Publication1
Mutagenesisi1502Y → A: Reduces affinity for histone H4 that has been dimethylated at 'Lys-20'. 2 Publications1
Mutagenesisi1502Y → L or Q: Abolishes recruitment to double strand breaks. 2 Publications1
Mutagenesisi1521D → A: Loss of interaction with histone H4 that has been dimethylated at 'Lys-20'. Abolishes recruitment to double strand breaks. 2 Publications1
Mutagenesisi1521D → R: Abolishes recruitment to double strand breaks. 2 Publications1
Mutagenesisi1523Y → A: Increases affinity for histone H4 that has been dimethylated at 'Lys-20'. No effect on recruitment to double strand breaks. 1 Publication1
Mutagenesisi1523Y → S: Decreases affinity for histone H4 that has been dimethylated at 'Lys-20'. 1 Publication1

Organism-specific databases

DisGeNETi7158.
OpenTargetsiENSG00000067369.
PharmGKBiPA36680.

Chemistry databases

ChEMBLiCHEMBL2424509.

Polymorphism and mutation databases

BioMutaiTP53BP1.
DMDMi8928568.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000726431 – 1972Tumor suppressor p53-binding protein 1Add BLAST1972

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei25Phosphoserine1 Publication1
Modified residuei63PhosphoserineCombined sources1
Modified residuei105PhosphoserineCombined sources1
Modified residuei124PhosphoserineCombined sources1
Modified residuei166Phosphoserine1 Publication1
Modified residuei176Phosphoserine1 Publication1
Modified residuei178Phosphoserine1 Publication1
Cross-linki217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki217Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei222PhosphoserineCombined sources1
Modified residuei265PhosphoserineCombined sources1
Modified residuei294PhosphoserineCombined sources1 Publication1
Modified residuei302PhosphothreonineCombined sources1 Publication1
Modified residuei366PhosphoserineCombined sources1
Modified residuei380PhosphoserineCombined sources1 Publication1
Modified residuei395PhosphoserineCombined sources1
Modified residuei398PhosphoserineCombined sources1
Modified residuei452Phosphoserine1 Publication1
Modified residuei464PhosphoserineBy similarity1
Modified residuei500PhosphoserineCombined sources1
Modified residuei507PhosphoserineCombined sources1
Modified residuei518PhosphoserineCombined sources1
Modified residuei523PhosphoserineCombined sources1 Publication1
Modified residuei525PhosphoserineCombined sources1
Modified residuei543PhosphothreonineCombined sources1
Modified residuei548PhosphothreonineCombined sources1
Modified residuei552PhosphoserineCombined sources1 Publication1
Modified residuei566PhosphoserineCombined sources1
Modified residuei580PhosphoserineCombined sources1
Modified residuei630PhosphoserineCombined sources1
Modified residuei635PhosphoserineCombined sources1
Modified residuei639PhosphoserineCombined sources1
Modified residuei640PhosphoserineCombined sources1
Modified residuei692PhosphoserineCombined sources1
Modified residuei724PhosphoserineBy similarity1
Modified residuei727PhosphoserineCombined sources1
Modified residuei771PhosphoserineCombined sources1
Modified residuei809PhosphoserineCombined sources1
Modified residuei830PhosphoserineBy similarity1
Modified residuei831PhosphoserineCombined sources1 Publication1
Modified residuei834PhosphoserineCombined sources1
Modified residuei855PhosphothreonineCombined sources1
Cross-linki868Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei922PhosphothreonineCombined sources1
Cross-linki930Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei970PhosphoserineCombined sources1
Modified residuei975PhosphoserineCombined sources1
Modified residuei1028PhosphoserineCombined sources1 Publication1
Modified residuei1056PhosphothreonineCombined sources1
Modified residuei1068PhosphoserineCombined sources1
Modified residuei1086Phosphoserine1 Publication1
Modified residuei1094PhosphoserineCombined sources1
Modified residuei1101PhosphoserineCombined sources1
Modified residuei1114PhosphoserineCombined sources1 Publication1
Modified residuei1148PhosphoserineCombined sources1
Modified residuei1214PhosphothreonineCombined sources1
Modified residuei1216PhosphoserineCombined sources1
Modified residuei1219PhosphoserineCombined sources1 Publication1
Modified residuei1317PhosphoserineCombined sources1
Modified residuei1342PhosphoserineCombined sources1
Modified residuei1355Omega-N-methylarginineBy similarity1
Modified residuei1362PhosphoserineCombined sources1
Modified residuei1368PhosphoserineCombined sources1
Modified residuei1372PhosphothreonineCombined sources1
Modified residuei1426PhosphoserineCombined sources1
Modified residuei1430PhosphoserineCombined sources1
Cross-linki1434Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1434Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1460PhosphoserineCombined sources1
Modified residuei1462PhosphoserineCombined sources1
Modified residuei1474PhosphoserineCombined sources1
Cross-linki1563Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1563Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1609PhosphothreonineCombined sources1
Modified residuei1618PhosphoserineCombined sources1
Modified residuei1631PhosphoserineBy similarity1
Modified residuei1635PhosphoserineCombined sources1
Modified residuei1638PhosphothreonineCombined sources1
Modified residuei1648PhosphothreonineCombined sources1
Modified residuei1656PhosphoserineCombined sources1
Modified residuei1673PhosphoserineCombined sources1
Modified residuei1678PhosphoserineCombined sources1
Modified residuei1701PhosphoserineCombined sources1
Modified residuei1759PhosphoserineCombined sources1
Modified residuei1778Phosphoserine2 Publications1

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.5 Publications

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ12888.
MaxQBiQ12888.
PaxDbiQ12888.
PeptideAtlasiQ12888.
PRIDEiQ12888.

PTM databases

iPTMnetiQ12888.
PhosphoSitePlusiQ12888.

Miscellaneous databases

PMAP-CutDBQ12888.

Expressioni

Gene expression databases

BgeeiENSG00000067369.
CleanExiHS_TP53BP1.
ExpressionAtlasiQ12888. baseline and differential.
GenevisibleiQ12888. HS.

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
MEOX2A4D1273EBI-396540,EBI-10172134
PAXIP1Q6ZW494EBI-396540,EBI-743225
Paxip1Q6NZQ45EBI-396540,EBI-1395317From a different organism.
TP53P046372EBI-396540,EBI-366083
VAC14Q08AM65EBI-396540,EBI-2107455
VRK1Q999868EBI-396540,EBI-1769146
ZNHIT1O432572EBI-396540,EBI-347522

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB
  • p53 binding Source: AgBase
  • RNA polymerase II activating transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi113011. 139 interactors.
DIPiDIP-5978N.
IntActiQ12888. 34 interactors.
MINTiMINT-276057.
STRINGi9606.ENSP00000371475.

Chemistry databases

BindingDBiQ12888.

Structurei

Secondary structure

11972
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1490 – 1494Combined sources5
Turni1496 – 1498Combined sources3
Beta strandi1501 – 1511Combined sources11
Beta strandi1514 – 1519Combined sources6
Beta strandi1524 – 1528Combined sources5
Helixi1529 – 1531Combined sources3
Beta strandi1532 – 1535Combined sources4
Beta strandi1543 – 1547Combined sources5
Beta strandi1548 – 1551Combined sources4
Beta strandi1553 – 1564Combined sources12
Beta strandi1567 – 1574Combined sources8
Beta strandi1577 – 1582Combined sources6
Helixi1583 – 1585Combined sources3
Beta strandi1586 – 1588Combined sources3
Helixi1590 – 1594Combined sources5
Helixi1597 – 1600Combined sources4
Helixi1715 – 1719Combined sources5
Turni1726 – 1731Combined sources6
Beta strandi1732 – 1736Combined sources5
Helixi1741 – 1745Combined sources5
Helixi1773 – 1781Combined sources9
Turni1782 – 1784Combined sources3
Turni1793 – 1799Combined sources7
Beta strandi1801 – 1808Combined sources8
Helixi1813 – 1821Combined sources9
Beta strandi1825 – 1827Combined sources3
Helixi1829 – 1837Combined sources9
Helixi1843 – 1845Combined sources3
Beta strandi1851 – 1853Combined sources3
Turni1854 – 1857Combined sources4
Beta strandi1858 – 1860Combined sources3
Turni1868 – 1871Combined sources4
Beta strandi1873 – 1879Combined sources7
Turni1881 – 1884Combined sources4
Helixi1885 – 1894Combined sources10
Beta strandi1898 – 1908Combined sources11
Helixi1914 – 1916Combined sources3
Beta strandi1918 – 1922Combined sources5
Helixi1928 – 1937Combined sources10
Helixi1944 – 1953Combined sources10
Helixi1963 – 1965Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2MWONMR-A1484-1603[»]
2MWPNMR-A1484-1603[»]
3LGFX-ray1.50A1484-1603[»]
3LGLX-ray1.60A1484-1603[»]
3LH0X-ray1.90A1484-1603[»]
4CRIX-ray2.35A/B1459-1634[»]
4RG2X-ray1.50A/B1483-1606[»]
4X34X-ray1.80A/B1484-1603[»]
5ECGX-ray3.00C/D1713-1972[»]
5KGFelectron microscopy4.54K/L1611-1631[»]
ProteinModelPortaliQ12888.
SMRiQ12888.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12888.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1724 – 1848BRCT 1PROSITE-ProRule annotationAdd BLAST125
Domaini1864 – 1964BRCT 2PROSITE-ProRule annotationAdd BLAST101

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1484 – 1603Tudor-like1 PublicationAdd BLAST120
Regioni1495 – 1523Interaction with dimethylated histone H41 PublicationAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1396 – 1403GAR8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1642 – 1646Poly-Ser5
Compositional biasi1760 – 1764Poly-Glu5

Domaini

The Tudor-like region mediates binding to H4K20me2.1 Publication

Sequence similaritiesi

Contains 2 BRCT domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3548. Eukaryota.
ENOG411075K. LUCA.
GeneTreeiENSGT00390000011891.
HOGENOMiHOG000231961.
HOVERGENiHBG060882.
InParanoidiQ12888.
OMAiCIDLTCD.
OrthoDBiEOG091G0BHF.
PhylomeDBiQ12888.
TreeFamiTF350227.

Family and domain databases

CDDicd00027. BRCT. 2 hits.
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. AlignAdd to basket

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti796P → S in CAD97660 (PubMed:17974005).Curated1
Sequence conflicti1600Y → C in CAD97660 (PubMed:17974005).Curated1
Sequence conflicti1958G → R in CAD97660 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_022172353D → E.2 PublicationsCorresponds to variant rs560191dbSNPEnsembl.1
Natural variantiVAR_022173412G → S.2 PublicationsCorresponds to variant rs689647dbSNPEnsembl.1
Natural variantiVAR_022174648M → V.1 PublicationCorresponds to variant rs45443496dbSNPEnsembl.1
Natural variantiVAR_022175699Q → R.1 PublicationCorresponds to variant rs34823068dbSNPEnsembl.1
Natural variantiVAR_034558841D → G.Corresponds to variant rs34185035dbSNPEnsembl.1
Natural variantiVAR_0221761014E → G.1 PublicationCorresponds to variant rs45470395dbSNPEnsembl.1
Natural variantiVAR_0221771026V → A.1 PublicationCorresponds to variant rs45482998dbSNPEnsembl.1
Natural variantiVAR_0221781136K → Q.2 PublicationsCorresponds to variant rs2602141dbSNPEnsembl.1
Natural variantiVAR_0345591137E → K.Corresponds to variant rs34740611dbSNPEnsembl.1
Natural variantiVAR_0221791170A → G.1 PublicationCorresponds to variant rs45500399dbSNPEnsembl.1
Natural variantiVAR_0221801174I → V.1 PublicationCorresponds to variant rs3803339dbSNPEnsembl.1
Natural variantiVAR_0345601442R → Q.Corresponds to variant rs2230449dbSNPEnsembl.1
Natural variantiVAR_0386891488G → W.Corresponds to variant rs11554564dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0183901M → MPGEQM in isoform 2 and isoform 3. 2 Publications1
Alternative sequenceiVSP_0550621692 – 1693Missing in isoform 3. 1 Publication2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
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.
UCSCiuc001zrq.5. human. [Q12888-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
UniGeneiHs.440968.
Hs.584887.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2MWONMR-A1484-1603[»]
2MWPNMR-A1484-1603[»]
3LGFX-ray1.50A1484-1603[»]
3LGLX-ray1.60A1484-1603[»]
3LH0X-ray1.90A1484-1603[»]
4CRIX-ray2.35A/B1459-1634[»]
4RG2X-ray1.50A/B1483-1606[»]
4X34X-ray1.80A/B1484-1603[»]
5ECGX-ray3.00C/D1713-1972[»]
5KGFelectron microscopy4.54K/L1611-1631[»]
ProteinModelPortaliQ12888.
SMRiQ12888.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113011. 139 interactors.
DIPiDIP-5978N.
IntActiQ12888. 34 interactors.
MINTiMINT-276057.
STRINGi9606.ENSP00000371475.

Chemistry databases

BindingDBiQ12888.
ChEMBLiCHEMBL2424509.

PTM databases

iPTMnetiQ12888.
PhosphoSitePlusiQ12888.

Polymorphism and mutation databases

BioMutaiTP53BP1.
DMDMi8928568.

Proteomic databases

EPDiQ12888.
MaxQBiQ12888.
PaxDbiQ12888.
PeptideAtlasiQ12888.
PRIDEiQ12888.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263801; ENSP00000263801; ENSG00000067369. [Q12888-1]
ENST00000382044; ENSP00000371475; ENSG00000067369. [Q12888-2]
ENST00000450115; ENSP00000393497; ENSG00000067369. [Q12888-3]
GeneIDi7158.
KEGGihsa:7158.
UCSCiuc001zrq.5. human. [Q12888-1]

Organism-specific databases

CTDi7158.
DisGeNETi7158.
GeneCardsiTP53BP1.
HGNCiHGNC:11999. TP53BP1.
HPAiCAB004083.
HPA008788.
HPA022133.
MIMi605230. gene.
neXtProtiNX_Q12888.
OpenTargetsiENSG00000067369.
PharmGKBiPA36680.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3548. Eukaryota.
ENOG411075K. LUCA.
GeneTreeiENSGT00390000011891.
HOGENOMiHOG000231961.
HOVERGENiHBG060882.
InParanoidiQ12888.
OMAiCIDLTCD.
OrthoDBiEOG091G0BHF.
PhylomeDBiQ12888.
TreeFamiTF350227.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000067369-MONOMER.
ReactomeiR-HSA-3232118. SUMOylation of transcription factors.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-69473. G2/M DNA damage checkpoint.
SIGNORiQ12888.

Miscellaneous databases

ChiTaRSiTP53BP1. human.
EvolutionaryTraceiQ12888.
GeneWikiiTP53BP1.
GenomeRNAii7158.
PMAP-CutDBQ12888.
PROiQ12888.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000067369.
CleanExiHS_TP53BP1.
ExpressionAtlasiQ12888. baseline and differential.
GenevisibleiQ12888. HS.

Family and domain databases

CDDicd00027. BRCT. 2 hits.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 184 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.