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TP53BP2 (tumor protein p53 binding protein, 2)

Written2011-01Kathryn Van Hook, Zhiping Wang, Charles Lopez
Department of Medicine, Division of Hematology, Medical Oncology, Oregon Health, Science University, Portland, OR, USA

(Note : for Links provided by Atlas : click)


Alias (NCBI)53BP2
HGNC (Hugo) TP53BP2
HGNC Alias symbPPP1R13A
HGNC Previous nametumor protein p53-binding protein, 2
LocusID (NCBI) 7159
Atlas_Id 42667
Location 1q41  [Link to chromosome band 1q41]
Location_base_pair Starts at 223779893 and ends at 223845972 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping TP53BP2.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
TP53BP2 (1q41)::RPL30 (8q22.2)TP53BP2 (1q41)::WDR26 (1q42.11)


  TSS=transcription start site.
Description The TP53BP2 gene spans about 66 kb on chromosome 1q42.1 on the minus strand (Yang et al., 1997). There are two transcripts as a result of alternative splicing (Takahashi et al., 2004). The transcript variant 1, which is shorter (4670 bp), does not contain exon 3 and gives rise to a longer form of the protein named TP53BPL (long) or ASPP2. The transcript variant 2, which is longer (4802 bp), contains exon 3 which harbors a stop codon. As a result, the transcription initiates at exon 6 giving rise to a shorter form of the protein named TP53BPS (short) or BBP.
Transcription ASPP2 is a serum inducible protein and subject to transcriptional regulation by E2F and its family members (Chen et al., 2005; Fogal et al., 2005).
Pseudogene Not known.


  ASPP2 protein domains. RA=Ras-association domain; PP=polyproline domain; AR=ankyrin repeats.
Description ASPP2 is a pro-apoptotic protein with a predicted size of approximately 135 kDa. It is the founding member of a family of ASPP proteins that all share the common motifs of four Ankyrin-repeats, a Src-homology 3 (SH3) domain, and a Polyproline domain in their C-terminus (Iwabuchi et al., 1994). The N-terminus of ASPP2 is thought to be important for regulating its apoptotic function and contains a putative Ras-association domain as well as a ubiquitin-like fold (Tidow et al., 2007). ASPP2 has been most widely studied for its ability to interact with and stimulate the apoptotic function of the tumor suppressor p53 (and p63/p73) but several studies have also demonstrated p53-independent as well as apoptosis-independent functions for ASPP2 as well (Kampa et al., 2009a).
ASPP2 was originally pulled out of a yeast two-hybrid screen using the p53-binding domain as bait as a partial C-terminal clone named 53BP2 (Iwabuchi et al., 1994). In 1996, Naumovski and Cleary determined that 53BP2 was a partial clone of a longer transcript they named Bcl-2 binding protein (Bbp or Bbp/53BP2) for its ability to bind the anti-apoptotic protein Bcl-2. It was later determined that Bbp is a splice isoform of the full length gene product from this locus, ASPP2 (Samuels-Lev et al., 2001).
Expression Northern blot analysis, using a C-terminal probe, shows elevated levels of ASPP2 mRNA in several human tissues including heart, testis, and peripheral blood leukocytes (Yang et al., 1999). ASPP2 protein levels are controlled by proteasomal degradation (Zhu et al., 2005).
Localisation ASPP2 contains a nuclear localization signal within its ankyrin repeat domain (amino acid residues 795-894) that when expressed alone or as a fusion with other proteins localizes in the nucleus of cells (Sachdev et al., 1998; Yang et al., 1999). Despite this signal however, full length ASPP2 is predominantly located in the cytoplasm and often seen near the cell periphery (Naumovski and Cleary, 1996; Iwabuchi et al., 1998; Yang et al., 1999).
Function Apoptosis. Before ASPP2 was known to be the full length gene product from the TP53BP2 locus, Yang and colleagues showed that overexpression of Bbp/53BP2 in cells induces apoptosis (Yang et al., 1999). In 2000, Lopez et al. demonstrated that Bbp/53BP2 was UV-damage inducible and that loss of this endogenous protein promotes cell survival in response to damage, thus implicating a function in the damage response pathway. In 2001, Samuels-Lev et al. provided evidence that not only does full length ASPP2 promote apoptosis but that it does so, at least in part, through a p53-mediated mechanism that may involve preferential binding of p53 to its apoptotic target genes. ASPP2 has also been shown to modulate the apoptotic activity of the p53 family members, p63/p73 (Bergamaschi et al., 2004), and is known to bind other proteins involved in apoptosis such as Bcl-2 and NF-kappaB (Naumovski and Cleary, 1996; Yang et al., 1999). However, the functional ramifications of these interactions remain unclear. Additionally, there is evidence to indicate ASPP2 as a player in mitochondrial-mediated apoptosis (Kobayashi et al., 2005).
Tumor suppressor. Several clinical studies demonstrate low ASPP2 expression in a variety of human tumors (breast, lung, lymphoma) and this low expression often correlates with poor clinical outcome, suggesting that ASPP2 may function as a tumor suppressor (Mori et al., 2000; Samuels-Lev et al., 2001; Lossos et al., 2002; Cobleigh et al., 2005). In support of this concept, Iwabuchi et al. demonstrated in 1998 that transfection of 53BP2 inhibits Ras/E1A-mediated transformation in rat embryonic fibroblasts. Since then two separate mouse models targeting the ASPP2 locus via homologous recombination have demonstrated that loss of only one copy of ASPP2 increases spontaneous and irradiation-induced tumor formation in vivo (Vives et al., 2006; Kampa et al., 2009b). Taken together these data strongly suggest that ASPP2 is a haplo-insufficient tumor suppressor.
Cell cycle. Bbp, a splice isoform of ASPP2, can induce accumulation of cells in G2/M and thus impede cell cycle progression (Naumovski and Cleary, 1996). Additionally, ASPP2 appears to play a role in the G0/G1 cell cycle checkpoint in response to gamma-irradiation as murine thymocytes that lack one copy of the ASPP2 locus did not arrest at G0/G1 as efficiently as wild type thymocytes (Kampa et al., 2009b).
Cell polarity. ASPP2 is often seen near the cell periphery and has been shown to co-localize with and bind to the tight junction protein PAR-3. Furthermore, loss of ASPP2 expression correlates with a loss of tight junction integrity and an impaired ability to maintain apical domains in polarized cells in culture (Cong et al., 2010). Interestingly these findings hold true in vivo as well. ASPP2 co-localizes with the PAR-3 complex and apical junctions in the brain and is necessary for tight junction integrity. Targeted deletion of ASPP2 in the mouse leads to defects associated with a loss of structural organization in the brain and retina (Sottocornola et al., 2010).
Senescence. Senescence, a type of irreversible cell cycle arrest, is considered an intrinsic protective response against malignant transformation. Wang et al. recently identified ASPP2 as a mediator of Ras-induced senescence by demonstrating that mouse embryonic fibroblasts with a targeted deletion of exon 3 of the ASPP2 gene (TP53BP2) are less prone to senescence in the presence of activated Ras as compared to wild type fibroblasts (as measured by beta-galactosidase staining). Data also suggests that Ras-induced senescence may be mediated by ASPP2 through its ability to inhibit Ras from inducing accumulation of cyclin D1 in the nucleus (Wang et al., 2011).
  Potential functions and putative interacting partners of ASPP2. Modified from Kampa et al., 2009a.
Homology ASPP2 is a member of the ASPP family of proteins that share a significant amount of homology in their C-terminal domains. ASPP1, ASPP2, and the splice isoform of ASPP2, BBP, share homology in both their N-terminal and C-terminal domains while the family member iASPP only retains C-terminal homology (Samuels-Lev et al., 2001; Bergamaschi et al., 2003).


Note No mutations at the ASPP2 locus, TP53BP2, have been reported. However, single nucleotide polymorphisms in TP53BP2 have been found associated with gastric cancer susceptibility (Ju et al., 2005) and epigenetic silencing of the promoter by methylation is frequently observed (Sarraf and Stancheva, 2004; Liu et al., 2005; Zhao et al., 2010).

Implicated in

Entity Breast cancer
Note ASPP2 mRNA expression is frequently downregulated in human breast cancer samples as compared to adjacent normal tissue (Sgroi et al., 1999; Samuels-Lev et al., 2001; Cobleigh et al., 2005). Reduced levels of ASPP2 expression are seen in both invasive and metastatic breast tumor tissue (Sgroi et al., 1999) and ASPP2 downregulation may be favored in tumor cells expressing wild type but not mutant p53 (Samuels-Lev et al., 2001).
Prognosis Elevated levels of ASPP2 mRNA were correlated with a lower risk of distant recurrence of disease among a panel of 78 patients with extensive lymph node involvement (Cobleigh et al., 2005).
Entity Non-Hodgkin's lymphoma specifically diffuse large B-cell lymphoma, follicular center lymphoma, and Burkitt's lymphoma
Note Overall, ASPP2 expression (as measured by Real-time RT-PCR) was found to be significantly higher in diffuse large B-cell lymphoma as compared to follicular center lymphoma. However, the variability of ASPP2 expression in diffuse large B-cell lymphoma was much greater than that seen in follicular center lymphoma. ASPP2 expression appeared inversely proportional to serum lactate dehydrogenase levels. Additionally, levels of ASPP2 expression are extremely low or undetectable in cell lines derived from Burkitt's lymphoma (Lossos et al., 2002).
Prognosis In general, patients with high ASPP2 expression tended to have a longer median survival than those with low ASPP2 expression (Lossos et al., 2002).
Entity Gastric cancer
Note Four single nucleotide polymorphisms within the ASPP2 gene locus, TP53BP2, show significant correlation with gastric cancer susceptibility (Ju et al., 2005).
Entity Hepatitis B virus-positive hepatocellular carcinoma
Note Downregulation of ASPP2 (and ASPP1) as a result of promoter hypermethylation (as measured by methylation-specific PCR) is frequently observed in human patient samples of HBV-positive hepatocellular carcinoma as compared to surrounding non-tumor tissue (Zhao et al., 2010).


ASPP1 and ASPP2: common activators of p53 family members.
Bergamaschi D, Samuels Y, Jin B, Duraisingham S, Crook T, Lu X.
Mol Cell Biol. 2004 Feb;24(3):1341-50.
PMID 14729977
Hepatitis C virus core protein interacts with p53-binding protein, 53BP2/Bbp/ASPP2, and inhibits p53-mediated apoptosis.
Cao Y, Hamada T, Matsui T, Date T, Iwabuchi K.
Biochem Biophys Res Commun. 2004 Mar 19;315(4):788-95.
PMID 14985081
Apoptosis-stimulating protein of p53-2 (ASPP2/53BP2L) is an E2F target gene.
Chen D, Padiernos E, Ding F, Lossos IS, Lopez CD.
Cell Death Differ. 2005 Apr;12(4):358-68.
PMID 15592436
ASPP2 inhibits APP-BP1-mediated NEDD8 conjugation to cullin-1 and decreases APP-BP1-induced cell proliferation and neuronal apoptosis.
Chen Y, Liu W, Naumovski L, Neve RL.
J Neurochem. 2003 May;85(3):801-9.
PMID 12694406
Tumor gene expression and prognosis in breast cancer patients with 10 or more positive lymph nodes.
Cobleigh MA, Tabesh B, Bitterman P, Baker J, Cronin M, Liu ML, Borchik R, Mosquera JM, Walker MG, Shak S.
Clin Cancer Res. 2005 Dec 15;11(24 Pt 1):8623-31.
PMID 16361546
ASPP2 regulates epithelial cell polarity through the PAR complex.
Cong W, Hirose T, Harita Y, Yamashita A, Mizuno K, Hirano H, Ohno S.
Curr Biol. 2010 Aug 10;20(15):1408-14. Epub 2010 Jul 8.
PMID 20619648
Yes-associated protein and p53-binding protein-2 interact through their WW and SH3 domains.
Espanel X, Sudol M.
J Biol Chem. 2001 Apr 27;276(17):14514-23. Epub 2001 Jan 31.
PMID 11278422
ASPP1 and ASPP2 are new transcriptional targets of E2F.
Fogal V, Kartasheva NN, Trigiante G, Llanos S, Yap D, Vousden KH, Lu X.
Cell Death Differ. 2005 Apr;12(4):369-76.
PMID 15731768
53BP2S, interacting with insulin receptor substrates, modulates insulin signaling.
Hakuno F, Kurihara S, Watson RT, Pessin JE, Takahashi S.
J Biol Chem. 2007 Dec 28;282(52):37747-58. Epub 2007 Oct 26.
PMID 17965023
Protein phosphatase 1 interacts with p53BP2, a protein which binds to the tumour suppressor p53.
Helps NR, Barker HM, Elledge SJ, Cohen PT.
FEBS Lett. 1995 Dec 27;377(3):295-300.
PMID 8549741
Novel link between E2F and p53: proapoptotic cofactors of p53 are transcriptionally upregulated by E2F.
Hershko T, Chaussepied M, Oren M, Ginsberg D.
Cell Death Differ. 2005 Apr;12(4):377-83.
PMID 15706352
Stimulation of p53-mediated transcriptional activation by the p53-binding proteins, 53BP1 and 53BP2.
Iwabuchi K, Li B, Massa HF, Trask BJ, Date T, Fields S.
J Biol Chem. 1998 Oct 2;273(40):26061-8.
PMID 9748285
TP53BP2 locus is associated with gastric cancer susceptibility.
Ju H, Lee KA, Yang M, Kim HJ, Kang CP, Sohn TS, Rhee JC, Kang C, Kim JW.
Int J Cancer. 2005 Dec 20;117(6):957-60.
PMID 15986435
Apoptosis-stimulating protein of p53 (ASPP2) heterozygous mice are tumor-prone and have attenuated cellular damage-response thresholds.
Kampa KM, Acoba JD, Chen D, Gay J, Lee H, Beemer K, Padiernos E, Boonmark N, Zhu Z, Fan AC, Bailey AS, Fleming WH, Corless C, Felsher DW, Naumovski L, Lopez CD.
Proc Natl Acad Sci U S A. 2009b Mar 17;106(11):4390-5. Epub 2009 Feb 26.
PMID 19251665
New insights into the expanding complexity of the tumor suppressor ASPP2.
Kampa KM, Bonin M, Lopez CD.
Cell Cycle. 2009a Sep 15;8(18):2871-6. Epub 2009 Sep 8. (REVIEW)
PMID 19657229
53BP2 induces apoptosis through the mitochondrial death pathway.
Kobayashi S, Kajino S, Takahashi N, Kanazawa S, Imai K, Hibi Y, Ohara H, Itoh M, Okamoto T.
Genes Cells. 2005 Mar;10(3):253-60.
PMID 15743414
Drosophila ASPP regulates C-terminal Src kinase activity.
Langton PF, Colombani J, Aerne BL, Tapon N.
Dev Cell. 2007 Dec;13(6):773-82.
PMID 18061561
PP1 Cooperates with ASPP2 to Dephosphorylate and Activate TAZ.
Liu CY, Lv X, Li T, Xu Y, Zhou X, Zhao S, Xiong Y, Lei QY, Guan KL.
J Biol Chem. 2011 Feb 18;286(7):5558-66. Epub 2010 Dec 28.
PMID 21189257
Downregulated mRNA expression of ASPP and the hypermethylation of the 5'-untranslated region in cancer cell lines retaining wild-type p53.
Liu ZJ, Lu X, Zhang Y, Zhong S, Gu SZ, Zhang XB, Yang X, Xin HM.
FEBS Lett. 2005 Mar 14;579(7):1587-90.
PMID 15757645
Proapoptotic p53-interacting protein 53BP2 is induced by UV irradiation but suppressed by p53.
Lopez CD, Ao Y, Rohde LH, Perez TD, O'Connor DJ, Lu X, Ford JM, Naumovski L.
Mol Cell Biol. 2000 Nov;20(21):8018-25.
PMID 11027272
Apoptosis stimulating protein of p53 (ASPP2) expression differs in diffuse large B-cell and follicular center lymphoma: correlation with clinical outcome.
Lossos IS, Natkunam Y, Levy R, Lopez CD.
Leuk Lymphoma. 2002 Dec;43(12):2309-17.
PMID 12613517
Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins.
Meek SE, Lane WS, Piwnica-Worms H.
J Biol Chem. 2004 Jul 30;279(31):32046-54. Epub 2004 May 25.
PMID 15161933
Aberrant overexpression of 53BP2 mRNA in lung cancer cell lines.
Mori T, Okamoto H, Takahashi N, Ueda R, Okamoto T.
FEBS Lett. 2000 Jan 14;465(2-3):124-8.
PMID 10631318
APCL, a central nervous system-specific homologue of adenomatous polyposis coli tumor suppressor, binds to p53-binding protein 2 and translocates it to the perinucleus.
Nakagawa H, Koyama K, Murata Y, Morito M, Akiyama T, Nakamura Y.
Cancer Res. 2000 Jan 1;60(1):101-5.
PMID 10646860
The p53-binding protein 53BP2 also interacts with Bc12 and impedes cell cycle progression at G2/M.
Naumovski L, Cleary ML.
Mol Cell Biol. 1996 Jul;16(7):3884-92.
PMID 8668206
Nuclear localization of IkappaB alpha is mediated by the second ankyrin repeat: the IkappaB alpha ankyrin repeats define a novel class of cis-acting nuclear import sequences.
Sachdev S, Hoffmann A, Hannink M.
Mol Cell Biol. 1998 May;18(5):2524-34.
PMID 9566872
ASPP proteins specifically stimulate the apoptotic function of p53.
Samuels-Lev Y, O'Connor DJ, Bergamaschi D, Trigiante G, Hsieh JK, Zhong S, Campargue I, Naumovski L, Crook T, Lu X.
Mol Cell. 2001 Oct;8(4):781-94.
PMID 11684014
Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly.
Sarraf SA, Stancheva I.
Mol Cell. 2004 Aug 27;15(4):595-605.
PMID 15327775
In vivo gene expression profile analysis of human breast cancer progression.
Sgroi DC, Teng S, Robinson G, LeVangie R, Hudson JR Jr, Elkahloun AG.
Cancer Res. 1999 Nov 15;59(22):5656-61.
PMID 10582678
ASPP2 binds Par-3 and controls the polarity and proliferation of neural progenitors during CNS development.
Sottocornola R, Royer C, Vives V, Tordella L, Zhong S, Wang Y, Ratnayaka I, Shipman M, Cheung A, Gaston-Massuet C, Ferretti P, Molnar Z, Lu X.
Dev Cell. 2010 Jul 20;19(1):126-37. Epub 2010 Jul 8.
PMID 20619750
p53 target DDA3 binds ASPP2 and inhibits its stimulation on p53-mediated BAX activation.
Sun WT, Hsieh PC, Chiang ML, Wang MC, Wang FF.
Biochem Biophys Res Commun. 2008 Nov 14;376(2):395-8. Epub 2008 Sep 13.
PMID 18793611
Inhibition of the 53BP2S-mediated apoptosis by nuclear factor kappaB and Bcl-2 family proteins.
Takahashi N, Kobayashi S, Kajino S, Imai K, Tomoda K, Shimizu S, Okamoto T.
Genes Cells. 2005 Aug;10(8):803-11.
PMID 16098144
Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a ubiquitin-like fold.
Tidow H, Andreeva A, Rutherford TJ, Fersht AR.
J Mol Biol. 2007 Aug 24;371(4):948-58. Epub 2007 May 13.
PMID 17594908
The DEAD box protein Ddx42p modulates the function of ASPP2, a stimulator of apoptosis.
Uhlmann-Schiffler H, Kiermayer S, Stahl H.
Oncogene. 2009 May 21;28(20):2065-73. Epub 2009 Apr 20.
PMID 19377511
ASPP2 is a haploinsufficient tumor suppressor that cooperates with p53 to suppress tumor growth.
Vives V, Su J, Zhong S, Ratnayaka I, Slee E, Goldin R, Lu X.
Genes Dev. 2006 May 15;20(10):1262-7.
PMID 16702401
SUMO-modified nuclear cyclin D1 bypasses Ras-induced senescence.
Wang XD, Lapi E, Sullivan A, Ratnayaka I, Goldin R, Hay R, Lu X.
Cell Death Differ. 2011 Feb;18(2):304-14. Epub 2010 Aug 27.
PMID 20798689
NF-kappaB subunit p65 binds to 53BP2 and inhibits cell death induced by 53BP2.
Yang JP, Hori M, Takahashi N, Kawabe T, Kato H, Okamoto T.
Oncogene. 1999 Sep 16;18(37):5177-86.
PMID 10498867
Assignment of p53 binding protein (TP53BP2) to human chromosome band 1q42.1 by in situ hybridization.
Yang JP, Ono T, Sonta S, Kawabe T, Okamoto T.
Cytogenet Cell Genet. 1997;78(1):61-2.
PMID 9345910
Epigenetic silence of ankyrin-repeat-containing, SH3-domain-containing, and proline-rich-region- containing protein 1 (ASPP1) and ASPP2 genes promotes tumor growth in hepatitis B virus-positive hepatocellular carcinoma.
Zhao J, Wu G, Bu F, Lu B, Liang A, Cao L, Tong X, Lu X, Wu M, Guo Y.
Hepatology. 2010 Jan;51(1):142-53.
PMID 20034025
Control of ASPP2/(53BP2L) protein levels by proteasomal degradation modulates p53 apoptotic function.
Zhu Z, Ramos J, Kampa K, Adimoolam S, Sirisawad M, Yu Z, Chen D, Naumovski L, Lopez CD.
J Biol Chem. 2005 Oct 14;280(41):34473-80. Epub 2005 Aug 9.
PMID 16091363


This paper should be referenced as such :
Van, Hook K ; Wang, Z ; Lopez, C
TP53BP2 (tumor protein p53 binding protein, 2)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(8):681-685.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)TP53BP2   12000
Entrez_Gene (NCBI)TP53BP2    tumor protein p53 binding protein 2
Aliases53BP2; ASPP2; BBP; P53BP2; 
GeneCards (Weizmann)TP53BP2
Ensembl hg19 (Hinxton)ENSG00000143514 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000143514 [Gene_View]  ENSG00000143514 [Sequence]  chr1:223779893-223845972 [Contig_View]  TP53BP2 [Vega]
ICGC DataPortalENSG00000143514
TCGA cBioPortalTP53BP2
AceView (NCBI)TP53BP2
Genatlas (Paris)TP53BP2
SOURCE (Princeton)TP53BP2
Genetics Home Reference (NIH)TP53BP2
Genomic and cartography
GoldenPath hg38 (UCSC)TP53BP2  -     chr1:223779893-223845972 -  1q41   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)TP53BP2  -     1q41   [Description]    (hg19-Feb_2009)
GoldenPathTP53BP2 - 1q41 [CytoView hg19]  TP53BP2 - 1q41 [CytoView hg38]
Genome Data Viewer NCBITP53BP2 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AA961496 AI042183 AJ318888 AK294432 AK294654
RefSeq transcript (Entrez)NM_001031685 NM_005426
Consensus coding sequences : CCDS (NCBI)TP53BP2
Gene ExpressionTP53BP2 [ NCBI-GEO ]   TP53BP2 [ EBI - ARRAY_EXPRESS ]   TP53BP2 [ SEEK ]   TP53BP2 [ MEM ]
Gene Expression Viewer (FireBrowse)TP53BP2 [ Firebrowse - Broad ]
GenevisibleExpression of TP53BP2 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)7159
GTEX Portal (Tissue expression)TP53BP2
Human Protein AtlasENSG00000143514-TP53BP2 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ13625   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ13625  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ13625
Domaine pattern : Prosite (Expaxy)ANK_REP_REGION (PS50297)    ANK_REPEAT (PS50088)    SH3 (PS50002)   
Domains : Interpro (EBI)Ankyrin_rpt    Ankyrin_rpt-contain_dom    Ankyrin_rpt-contain_sf    SH3-like_dom_sf    SH3_domain    Ubiquitin-like_domsf   
Domain families : Pfam (Sanger)Ank_2 (PF12796)    SH3_1 (PF00018)   
Domain families : Pfam (NCBI)pfam12796    pfam00018   
Domain families : Smart (EMBL)ANK (SM00248)  SH3 (SM00326)  
Conserved Domain (NCBI)TP53BP2
PDB (RSDB)1YCS    2UWQ    4A63    4IRV    6GHM    6HKP   
PDB Europe1YCS    2UWQ    4A63    4IRV    6GHM    6HKP   
PDB (PDBSum)1YCS    2UWQ    4A63    4IRV    6GHM    6HKP   
PDB (IMB)1YCS    2UWQ    4A63    4IRV    6GHM    6HKP   
Structural Biology KnowledgeBase1YCS    2UWQ    4A63    4IRV    6GHM    6HKP   
SCOP (Structural Classification of Proteins)1YCS    2UWQ    4A63    4IRV    6GHM    6HKP   
CATH (Classification of proteins structures)1YCS    2UWQ    4A63    4IRV    6GHM    6HKP   
AlphaFold pdb e-kbQ13625   
Human Protein Atlas [tissue]ENSG00000143514-TP53BP2 [tissue]
Protein Interaction databases
IntAct (EBI)Q13625
Ontologies - Pathways
Ontology : AmiGOp53 binding  p53 binding  protein binding  nucleus  nucleus  nucleoplasm  cytoplasm  cytoplasm  mitochondrion  cytosol  cell cycle  signal transduction  SH3 domain binding  cell junction  identical protein binding  regulation of apoptotic process  negative regulation of cell cycle  perinuclear region of cytoplasm  perinuclear region of cytoplasm  NF-kappaB binding  intrinsic apoptotic signaling pathway by p53 class mediator  positive regulation of execution phase of apoptosis  positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway  positive regulation of neuron death  regulation of signal transduction by p53 class mediator  
Ontology : EGO-EBIp53 binding  p53 binding  protein binding  nucleus  nucleus  nucleoplasm  cytoplasm  cytoplasm  mitochondrion  cytosol  cell cycle  signal transduction  SH3 domain binding  cell junction  identical protein binding  regulation of apoptotic process  negative regulation of cell cycle  perinuclear region of cytoplasm  perinuclear region of cytoplasm  NF-kappaB binding  intrinsic apoptotic signaling pathway by p53 class mediator  positive regulation of execution phase of apoptosis  positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway  positive regulation of neuron death  regulation of signal transduction by p53 class mediator  
Pathways : KEGGHippo signaling pathway   
REACTOMEQ13625 [protein]
REACTOME PathwaysR-HSA-6804759 [pathway]   
NDEx NetworkTP53BP2
Atlas of Cancer Signalling NetworkTP53BP2
Wikipedia pathwaysTP53BP2
Orthology - Evolution
GeneTree (enSembl)ENSG00000143514
Phylogenetic Trees/Animal Genes : TreeFamTP53BP2
Homologs : HomoloGeneTP53BP2
Homology/Alignments : Family Browser (UCSC)TP53BP2
Gene fusions - Rearrangements
Fusion : MitelmanTP53BP2::WDR26 [1q41/1q42.11]  
Fusion : QuiverTP53BP2
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerTP53BP2 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)TP53BP2
Exome Variant ServerTP53BP2
GNOMAD BrowserENSG00000143514
Varsome BrowserTP53BP2
ACMGTP53BP2 variants
Genomic Variants (DGV)TP53BP2 [DGVbeta]
DECIPHERTP53BP2 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisTP53BP2 
ICGC Data PortalTP53BP2 
TCGA Data PortalTP53BP2 
Broad Tumor PortalTP53BP2
OASIS PortalTP53BP2 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICTP53BP2  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DTP53BP2
Mutations and Diseases : HGMDTP53BP2
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)TP53BP2
DoCM (Curated mutations)TP53BP2
CIViC (Clinical Interpretations of Variants in Cancer)TP53BP2
NCG (London)TP53BP2
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry TP53BP2
NextProtQ13625 [Medical]
Target ValidationTP53BP2
Huge Navigator TP53BP2 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDTP53BP2
Pharm GKB GenePA36681
Clinical trialTP53BP2
DataMed IndexTP53BP2
PubMed151 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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