ASPP2_HUMAN
ID ASPP2_HUMAN Reviewed; 1128 AA.
AC Q13625; B4DG66; Q12892; Q86X75; Q96KQ3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Apoptosis-stimulating of p53 protein 2;
DE AltName: Full=Bcl2-binding protein;
DE Short=Bbp;
DE AltName: Full=Renal carcinoma antigen NY-REN-51;
DE AltName: Full=Tumor suppressor p53-binding protein 2;
DE Short=53BP2;
DE Short=p53-binding protein 2;
DE Short=p53BP2;
GN Name=TP53BP2; Synonyms=ASPP2, BBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH BCL2.
RX PubMed=8668206; DOI=10.1128/mcb.16.7.3884;
RA Naumovski L., Cleary M.L.;
RT "The p53-binding protein 53BP2 also interacts with Bcl2 and impedes cell
RT cycle progression at G2/M.";
RL Mol. Cell. Biol. 16:3884-3892(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH TP53.
RX PubMed=11684014; DOI=10.1016/s1097-2765(01)00367-7;
RA Samuels-Lev Y., O'Connor D.J., Bergamaschi D., Trigiante G., Hsieh J.-K.,
RA Zhong S., Campargue I., Naumovski L., Crook T., Lu X.;
RT "ASPP proteins specifically stimulate the apoptotic function of p53.";
RL Mol. Cell 8:781-794(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 600-1128, AND INTERACTION WITH TP53.
RX PubMed=8016121; DOI=10.1073/pnas.91.13.6098;
RA Iwabuchi K., Bartel P.L., Li B., Marraccino R., Fields S.;
RT "Two cellular proteins that bind to wild-type but not mutant p53.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6098-6102(1994).
RN [7]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [8]
RP TISSUE SPECIFICITY, AND INTERACTION WITH RELA.
RX PubMed=10498867; DOI=10.1038/sj.onc.1202904;
RA Yang J.-P., Hori M., Takahashi N., Kawabe T., Kato H., Okamoto T.;
RT "NF-kappaB subunit p65 binds to 53BP2 and inhibits cell death induced by
RT 53BP2.";
RL Oncogene 18:5177-5186(1999).
RN [9]
RP INTERACTION WITH APC2, MUTAGENESIS OF TRP-1098, AND SUBCELLULAR LOCATION.
RX PubMed=10646860;
RA Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.;
RT "APCL, a central nervous system-specific homologue of adenomatous polyposis
RT coli tumor suppressor, binds to p53-binding protein 2 and translocates it
RT to the perinucleus.";
RL Cancer Res. 60:101-105(2000).
RN [10]
RP INDUCTION.
RX PubMed=11027272; DOI=10.1128/mcb.20.21.8018-8025.2000;
RA Lopez C.D., Ao Y., Rohde L.H., Perez T.D., O'Connor D.J., Lu X., Ford J.M.,
RA Naumovski L.;
RT "Proapoptotic p53-interacting protein 53BP2 is induced by UV irradiation
RT but suppressed by p53.";
RL Mol. Cell. Biol. 20:8018-8025(2000).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=10631318; DOI=10.1016/s0014-5793(99)01726-3;
RA Mori T., Okamoto H., Takahashi N., Ueda R., Okamoto T.;
RT "Aberrant overexpression of 53BP2 mRNA in lung cancer cell lines.";
RL FEBS Lett. 465:124-128(2000).
RN [12]
RP FUNCTION, AND INTERACTION WITH NAE1.
RX PubMed=12694406; DOI=10.1046/j.1471-4159.2003.01727.x;
RA Chen Y., Liu W., Naumovski L., Neve R.L.;
RT "ASPP2 inhibits APP-BP1-mediated NEDD8 conjugation to cullin-1 and
RT decreases APP-BP1-induced cell proliferation and neuronal apoptosis.";
RL J. Neurochem. 85:801-809(2003).
RN [13]
RP FUNCTION, AND INTERACTION WITH TP53.
RX PubMed=12524540; DOI=10.1038/ng1070;
RA Bergamaschi D., Samuels Y., O'Neil N.J., Trigiante G., Crook T.,
RA Hsieh J.-K., O'Connor D.J., Zhong S., Campargue I., Tomlinson M.L.,
RA Kuwabara P.E., Lu X.;
RT "iASPP oncoprotein is a key inhibitor of p53 conserved from worm to
RT human.";
RL Nat. Genet. 33:162-167(2003).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480 AND SER-556, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP FUNCTION, INTERACTION WITH DDX42, AND SUBCELLULAR LOCATION.
RX PubMed=19377511; DOI=10.1038/onc.2009.75;
RA Uhlmann-Schiffler H., Kiermayer S., Stahl H.;
RT "The DEAD box protein Ddx42p modulates the function of ASPP2, a stimulator
RT of apoptosis.";
RL Oncogene 28:2065-2073(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480; SER-556 AND SER-572, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480; SER-556; SER-569;
RP SER-576; SER-714 AND SER-737, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP ANKYRIN REPEATS.
RX PubMed=25547411; DOI=10.1186/s12859-014-0440-9;
RA Chakrabarty B., Parekh N.;
RT "Identifying tandem Ankyrin repeats in protein structures.";
RL BMC Bioinformatics 15:6599-6599(2014).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 892-1128.
RX PubMed=8875926; DOI=10.1126/science.274.5289.1001;
RA Gorina S., Pavletich N.P.;
RT "Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains
RT of 53BP2.";
RL Science 274:1001-1005(1996).
RN [25]
RP STRUCTURE BY NMR OF 1-83.
RX PubMed=17594908; DOI=10.1016/j.jmb.2007.05.024;
RA Tidow H., Andreeva A., Rutherford T.J., Fersht A.R.;
RT "Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a
RT ubiquitin-like fold.";
RL J. Mol. Biol. 371:948-958(2007).
CC -!- FUNCTION: Regulator that plays a central role in regulation of
CC apoptosis and cell growth via its interactions with proteins such as
CC TP53 (PubMed:12524540). Regulates TP53 by enhancing the DNA binding and
CC transactivation function of TP53 on the promoters of proapoptotic genes
CC in vivo. Inhibits the ability of NAE1 to conjugate NEDD8 to CUL1, and
CC thereby decreases NAE1 ability to induce apoptosis. Impedes cell cycle
CC progression at G2/M. Its apoptosis-stimulating activity is inhibited by
CC its interaction with DDX42. {ECO:0000269|PubMed:11684014,
CC ECO:0000269|PubMed:12524540, ECO:0000269|PubMed:12694406,
CC ECO:0000269|PubMed:19377511}.
CC -!- SUBUNIT: Interacts with P53/TP53; the interaction promotes pro-
CC apoptotic activity (PubMed:11684014, PubMed:8016121, PubMed:12524540).
CC Interacts with BCL2 (PubMed:8668206). Interacts with protein
CC phosphatase 1. Interacts with RELA NF-kappa-B subunit. This interaction
CC probably prevents the activation of apoptosis, possibly by preventing
CC its interaction with TP53. Interacts with APC2 and NAE1. Interacts with
CC DDX42 (via the C-terminus); the interaction is not inhibited by TP53BP2
CC ubiquitination and is independent of p53/TP53.
CC {ECO:0000269|PubMed:10498867, ECO:0000269|PubMed:10646860,
CC ECO:0000269|PubMed:11684014, ECO:0000269|PubMed:12524540,
CC ECO:0000269|PubMed:12694406, ECO:0000269|PubMed:19377511,
CC ECO:0000269|PubMed:8016121, ECO:0000269|PubMed:8668206}.
CC -!- INTERACTION:
CC Q13625; O95996: APC2; NbExp=4; IntAct=EBI-77642, EBI-1053045;
CC Q13625; P05067: APP; NbExp=3; IntAct=EBI-77642, EBI-77613;
CC Q13625; P10415: BCL2; NbExp=10; IntAct=EBI-77642, EBI-77694;
CC Q13625; Q07817-1: BCL2L1; NbExp=3; IntAct=EBI-77642, EBI-287195;
CC Q13625; Q92843: BCL2L2; NbExp=4; IntAct=EBI-77642, EBI-707714;
CC Q13625; P35222: CTNNB1; NbExp=5; IntAct=EBI-77642, EBI-491549;
CC Q13625; Q09472: EP300; NbExp=2; IntAct=EBI-77642, EBI-447295;
CC Q13625; Q96J02: ITCH; NbExp=2; IntAct=EBI-77642, EBI-1564678;
CC Q13625; P62136: PPP1CA; NbExp=9; IntAct=EBI-77642, EBI-357253;
CC Q13625; P36873: PPP1CC; NbExp=8; IntAct=EBI-77642, EBI-356283;
CC Q13625; P62826: RAN; NbExp=5; IntAct=EBI-77642, EBI-286642;
CC Q13625; Q04206: RELA; NbExp=4; IntAct=EBI-77642, EBI-73886;
CC Q13625; P04637: TP53; NbExp=9; IntAct=EBI-77642, EBI-366083;
CC Q13625; Q13625: TP53BP2; NbExp=7; IntAct=EBI-77642, EBI-77642;
CC Q13625; Q9H3D4: TP63; NbExp=2; IntAct=EBI-77642, EBI-2337775;
CC Q13625; O15350: TP73; NbExp=2; IntAct=EBI-77642, EBI-389606;
CC Q13625; P46937: YAP1; NbExp=6; IntAct=EBI-77642, EBI-1044059;
CC Q13625; P63104: YWHAZ; NbExp=3; IntAct=EBI-77642, EBI-347088;
CC Q13625; PRO_0000037566 [P27958]; Xeno; NbExp=5; IntAct=EBI-77642, EBI-6377335;
CC Q13625-2; Q04206: RELA; NbExp=6; IntAct=EBI-287091, EBI-73886;
CC Q13625-2; P46937: YAP1; NbExp=9; IntAct=EBI-287091, EBI-1044059;
CC Q13625-2; P35569: Irs1; Xeno; NbExp=2; IntAct=EBI-287091, EBI-400825;
CC Q13625-2; P35570: Irs1; Xeno; NbExp=4; IntAct=EBI-287091, EBI-520230;
CC Q13625-2; P46936: YAP1; Xeno; NbExp=6; IntAct=EBI-287091, EBI-7804091;
CC Q13625-3; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-10175039, EBI-1166928;
CC Q13625-3; Q9UQB8: BAIAP2; NbExp=3; IntAct=EBI-10175039, EBI-525456;
CC Q13625-3; Q53HC0: CCDC92; NbExp=3; IntAct=EBI-10175039, EBI-719994;
CC Q13625-3; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-10175039, EBI-5453285;
CC Q13625-3; Q96GG9: DCUN1D1; NbExp=3; IntAct=EBI-10175039, EBI-740086;
CC Q13625-3; P62993: GRB2; NbExp=3; IntAct=EBI-10175039, EBI-401755;
CC Q13625-3; P62807: H2BC8; NbExp=3; IntAct=EBI-10175039, EBI-354552;
CC Q13625-3; Q9BUJ2: HNRNPUL1; NbExp=3; IntAct=EBI-10175039, EBI-1018153;
CC Q13625-3; P61968: LMO4; NbExp=3; IntAct=EBI-10175039, EBI-2798728;
CC Q13625-3; Q8NCE2: MTMR14; NbExp=3; IntAct=EBI-10175039, EBI-5658424;
CC Q13625-3; O14777: NDC80; NbExp=3; IntAct=EBI-10175039, EBI-715849;
CC Q13625-3; Q86Y26: NUTM1; NbExp=3; IntAct=EBI-10175039, EBI-10178410;
CC Q13625-3; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-10175039, EBI-398874;
CC Q13625-3; Q96DC9: OTUB2; NbExp=3; IntAct=EBI-10175039, EBI-746259;
CC Q13625-3; Q494U1: PLEKHN1; NbExp=3; IntAct=EBI-10175039, EBI-10241513;
CC Q13625-3; P62875: POLR2L; NbExp=3; IntAct=EBI-10175039, EBI-359527;
CC Q13625-3; P62140: PPP1CB; NbExp=3; IntAct=EBI-10175039, EBI-352350;
CC Q13625-3; P36873: PPP1CC; NbExp=3; IntAct=EBI-10175039, EBI-356283;
CC Q13625-3; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-10175039, EBI-1567797;
CC Q13625-3; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-10175039, EBI-747107;
CC Q13625-3; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-10175039, EBI-2212028;
CC Q13625-3; Q92844: TANK; NbExp=3; IntAct=EBI-10175039, EBI-356349;
CC Q13625-3; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-10175039, EBI-8787464;
CC Q13625-3; P56279: TCL1A; NbExp=3; IntAct=EBI-10175039, EBI-749995;
CC Q13625-3; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-10175039, EBI-3650647;
CC Q13625-3; P40222: TXLNA; NbExp=3; IntAct=EBI-10175039, EBI-359793;
CC Q13625-3; P57075: UBASH3A; NbExp=3; IntAct=EBI-10175039, EBI-2105393;
CC Q13625-3; Q8N5A5: ZGPAT; NbExp=3; IntAct=EBI-10175039, EBI-3439227;
CC Q13625-3; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-10175039, EBI-10183064;
CC Q13625-3; P17031: ZNF26; NbExp=5; IntAct=EBI-10175039, EBI-2841331;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus.
CC Note=Predominantly found in the perinuclear region. Some small fraction
CC is nuclear. Sequester in the cytoplasm on overexpression of DDX42.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q13625-1; Sequence=Displayed;
CC Name=2; Synonyms=Bbp;
CC IsoId=Q13625-2; Sequence=VSP_008010;
CC Name=3;
CC IsoId=Q13625-3; Sequence=VSP_043509;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in spleen, thymus,
CC prostate, testis, ovary, small intestine, colon and peripheral blood
CC leukocyte. Reduced expression in breast carcinomas expressing a wild-
CC type TP53 protein. Overexpressed in lung cancer cell lines.
CC {ECO:0000269|PubMed:10498867, ECO:0000269|PubMed:10631318,
CC ECO:0000269|PubMed:11684014}.
CC -!- INDUCTION: Following DNA damage induced by UV irradiation. Down-
CC regulated by wild-type, but not mutant, p53/TP53.
CC {ECO:0000269|PubMed:11027272}.
CC -!- DOMAIN: The ankyrin repeats and the SH3 domain are required for a
CC specific interactions with TP53.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to Alu sequence insertion that creates
CC a shorter but existing form that may have an alternative function.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ASPP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46150.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH46150.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH58918.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TP53BP2ID42667ch1q42.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U58334; AAC50557.1; -; mRNA.
DR EMBL; AJ318888; CAC83012.1; -; mRNA.
DR EMBL; AK294432; BAG57677.1; -; mRNA.
DR EMBL; AC096542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046150; AAH46150.2; ALT_SEQ; mRNA.
DR EMBL; BC058918; AAH58918.2; ALT_INIT; mRNA.
DR EMBL; U09582; AAA21597.1; -; mRNA.
DR CCDS; CCDS1538.1; -. [Q13625-2]
DR CCDS; CCDS44319.1; -. [Q13625-3]
DR PIR; I38607; I38607.
DR RefSeq; NP_001026855.2; NM_001031685.2. [Q13625-3]
DR RefSeq; NP_005417.1; NM_005426.2. [Q13625-2]
DR RefSeq; XP_011542571.1; XM_011544269.2. [Q13625-2]
DR PDB; 1YCS; X-ray; 2.20 A; B=892-1126.
DR PDB; 2UWQ; NMR; -; A=1-83.
DR PDB; 4A63; X-ray; 2.27 A; B/D/F/H/J/L=892-1128.
DR PDB; 4IRV; X-ray; 2.04 A; E/F/G/H=726-782.
DR PDB; 6GHM; X-ray; 2.15 A; C/D=920-1128.
DR PDB; 6HKP; X-ray; 1.90 A; S=970-992.
DR PDBsum; 1YCS; -.
DR PDBsum; 2UWQ; -.
DR PDBsum; 4A63; -.
DR PDBsum; 4IRV; -.
DR PDBsum; 6GHM; -.
DR PDBsum; 6HKP; -.
DR AlphaFoldDB; Q13625; -.
DR SASBDB; Q13625; -.
DR SMR; Q13625; -.
DR BioGRID; 113012; 224.
DR DIP; DIP-426N; -.
DR IntAct; Q13625; 133.
DR MINT; Q13625; -.
DR STRING; 9606.ENSP00000341957; -.
DR GlyGen; Q13625; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q13625; -.
DR MetOSite; Q13625; -.
DR PhosphoSitePlus; Q13625; -.
DR BioMuta; TP53BP2; -.
DR DMDM; 33860140; -.
DR EPD; Q13625; -.
DR jPOST; Q13625; -.
DR MassIVE; Q13625; -.
DR MaxQB; Q13625; -.
DR PaxDb; Q13625; -.
DR PeptideAtlas; Q13625; -.
DR PRIDE; Q13625; -.
DR ProteomicsDB; 59616; -. [Q13625-1]
DR ProteomicsDB; 59617; -. [Q13625-2]
DR ProteomicsDB; 59618; -. [Q13625-3]
DR Antibodypedia; 20749; 288 antibodies from 33 providers.
DR DNASU; 7159; -.
DR Ensembl; ENST00000343537.12; ENSP00000341957.7; ENSG00000143514.17. [Q13625-3]
DR Ensembl; ENST00000391878.6; ENSP00000375750.2; ENSG00000143514.17. [Q13625-2]
DR GeneID; 7159; -.
DR KEGG; hsa:7159; -.
DR MANE-Select; ENST00000343537.12; ENSP00000341957.7; NM_001031685.3; NP_001026855.2. [Q13625-3]
DR UCSC; uc001hod.4; human. [Q13625-1]
DR CTD; 7159; -.
DR DisGeNET; 7159; -.
DR GeneCards; TP53BP2; -.
DR HGNC; HGNC:12000; TP53BP2.
DR HPA; ENSG00000143514; Low tissue specificity.
DR MIM; 602143; gene.
DR neXtProt; NX_Q13625; -.
DR OpenTargets; ENSG00000143514; -.
DR PharmGKB; PA36681; -.
DR VEuPathDB; HostDB:ENSG00000143514; -.
DR eggNOG; KOG0515; Eukaryota.
DR GeneTree; ENSGT00940000153463; -.
DR HOGENOM; CLU_008234_0_0_1; -.
DR InParanoid; Q13625; -.
DR OMA; MREGDCM; -.
DR OrthoDB; 1041229at2759; -.
DR PhylomeDB; Q13625; -.
DR TreeFam; TF105545; -.
DR PathwayCommons; Q13625; -.
DR Reactome; R-HSA-139915; Activation of PUMA and translocation to mitochondria.
DR Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR Reactome; R-HSA-6803211; TP53 Regulates Transcription of Death Receptors and Ligands.
DR Reactome; R-HSA-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR SignaLink; Q13625; -.
DR SIGNOR; Q13625; -.
DR BioGRID-ORCS; 7159; 21 hits in 1081 CRISPR screens.
DR ChiTaRS; TP53BP2; human.
DR EvolutionaryTrace; Q13625; -.
DR GeneWiki; TP53BP2; -.
DR GenomeRNAi; 7159; -.
DR Pharos; Q13625; Tbio.
DR PRO; PR:Q13625; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13625; protein.
DR Bgee; ENSG00000143514; Expressed in ventricular zone and 194 other tissues.
DR ExpressionAtlas; Q13625; baseline and differential.
DR Genevisible; Q13625; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:AgBase.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IDA:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; TAS:UniProtKB.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IMP:AgBase.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR DisProt; DP01164; -.
DR Gene3D; 1.25.40.20; -; 1.
DR IDEAL; IID00124; -.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Apoptosis; Cell cycle;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW SH3-binding.
FT CHAIN 1..1128
FT /note="Apoptosis-stimulating of p53 protein 2"
FT /id="PRO_0000066964"
FT REPEAT 926..957
FT /note="ANK 1"
FT REPEAT 958..990
FT /note="ANK 2"
FT REPEAT 991..1024
FT /note="ANK 3"
FT REPEAT 1025..1067
FT /note="ANK 4"
FT DOMAIN 1057..1119
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 86..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..348
FT /note="Interaction with APPBP1"
FT /evidence="ECO:0000269|PubMed:12694406"
FT REGION 494..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..1128
FT /note="Mediates interaction with APC2"
FT /evidence="ECO:0000269|PubMed:10646860"
FT MOTIF 866..875
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 322..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..879
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CG79"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8668206"
FT /id="VSP_008010"
FT VAR_SEQ 1
FT /note="M -> MRFGSKM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043509"
FT MUTAGEN 1098
FT /note="W->K: Loss of interaction with APC2."
FT /evidence="ECO:0000269|PubMed:10646860"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:2UWQ"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:2UWQ"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:2UWQ"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2UWQ"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:2UWQ"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:2UWQ"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:2UWQ"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2UWQ"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2UWQ"
FT HELIX 747..760
FT /evidence="ECO:0007829|PDB:4IRV"
FT TURN 761..764
FT /evidence="ECO:0007829|PDB:4IRV"
FT HELIX 926..936
FT /evidence="ECO:0007829|PDB:6GHM"
FT HELIX 939..945
FT /evidence="ECO:0007829|PDB:6GHM"
FT TURN 946..948
FT /evidence="ECO:0007829|PDB:6GHM"
FT HELIX 962..968
FT /evidence="ECO:0007829|PDB:6GHM"
FT TURN 976..979
FT /evidence="ECO:0007829|PDB:6HKP"
FT HELIX 995..1001
FT /evidence="ECO:0007829|PDB:6GHM"
FT HELIX 1005..1012
FT /evidence="ECO:0007829|PDB:6GHM"
FT TURN 1013..1015
FT /evidence="ECO:0007829|PDB:6GHM"
FT TURN 1023..1025
FT /evidence="ECO:0007829|PDB:6GHM"
FT HELIX 1030..1032
FT /evidence="ECO:0007829|PDB:6GHM"
FT STRAND 1035..1037
FT /evidence="ECO:0007829|PDB:1YCS"
FT HELIX 1040..1053
FT /evidence="ECO:0007829|PDB:6GHM"
FT TURN 1054..1056
FT /evidence="ECO:0007829|PDB:6GHM"
FT HELIX 1057..1060
FT /evidence="ECO:0007829|PDB:6GHM"
FT STRAND 1061..1064
FT /evidence="ECO:0007829|PDB:6GHM"
FT STRAND 1083..1090
FT /evidence="ECO:0007829|PDB:6GHM"
FT STRAND 1091..1093
FT /evidence="ECO:0007829|PDB:4A63"
FT STRAND 1095..1102
FT /evidence="ECO:0007829|PDB:6GHM"
FT STRAND 1105..1110
FT /evidence="ECO:0007829|PDB:6GHM"
FT HELIX 1111..1113
FT /evidence="ECO:0007829|PDB:6GHM"
FT STRAND 1114..1117
FT /evidence="ECO:0007829|PDB:6GHM"
SQ SEQUENCE 1128 AA; 125616 MW; C75D056FBC1DAD75 CRC64;
MMPMFLTVYL SNNEQHFTEV PVTPETICRD VVDLCKEPGE SDCHLAEVWC GSERPVADNE
RMFDVLQRFG SQRNEVRFFL RHERPPGRDI VSGPRSQDPS LKRNGVKVPG EYRRKENGVN
SPRMDLTLAE LQEMASRQQQ QIEAQQQLLA TKEQRLKFLK QQDQRQQQQV AEQEKLKRLK
EIAENQEAKL KKVRALKGHV EQKRLSNGKL VEEIEQMNNL FQQKQRELVL AVSKVEELTR
QLEMLKNGRI DSHHDNQSAV AELDRLYKEL QLRNKLNQEQ NAKLQQQREC LNKRNSEVAV
MDKRVNELRD RLWKKKAALQ QKENLPVSSD GNLPQQAASA PSRVAAVGPY IQSSTMPRMP
SRPELLVKPA LPDGSLVIQA SEGPMKIQTL PNMRSGAASQ TKGSKIHPVG PDWSPSNADL
FPSQGSASVP QSTGNALDQV DDGEVPLREK EKKVRPFSMF DAVDQSNAPP SFGTLRKNQS
SEDILRDAQV ANKNVAKVPP PVPTKPKQIN LPYFGQTNQP PSDIKPDGSS QQLSTVVPSM
GTKPKPAGQQ PRVLLSPSIP SVGQDQTLSP GSKQESPPAA AVRPFTPQPS KDTLLPPFRK
PQTVAASSIY SMYTQQQAPG KNFQQAVQSA LTKTHTRGPH FSSVYGKPVI AAAQNQQQHP
ENIYSNSQGK PGSPEPETEP VSSVQENHEN ERIPRPLSPT KLLPFLSNPY RNQSDADLEA
LRKKLSNAPR PLKKRSSITE PEGPNGPNIQ KLLYQRTTIA AMETISVPSY PSKSASVTAS
SESPVEIQNP YLHVEPEKEV VSLVPESLSP EDVGNASTEN SDMPAPSPGL DYEPEGVPDN
SPNLQNNPEE PNPEAPHVLD VYLEEYPPYP PPPYPSGEPE GPGEDSVSMR PPEITGQVSL
PPGKRTNLRK TGSERIAHGM RVKFNPLALL LDSSLEGEFD LVQRIIYEVD DPSLPNDEGI
TALHNAVCAG HTEIVKFLVQ FGVNVNAADS DGWTPLHCAA SCNNVQVCKF LVESGAAVFA
MTYSDMQTAA DKCEEMEEGY TQCSQFLYGV QEKMGIMNKG VIYALWDYEP QNDDELPMKE
GDCMTIIHRE DEDEIEWWWA RLNDKEGYVP RNLLGLYPRI KPRQRSLA
