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Apoptosis-stimulating of p53 protein 2 (Bcl2-binding protein) (Bbp) (Renal carcinoma antigen NY-REN-51) (Tumor suppressor p53-binding protein 2) (53BP2) (p53-binding protein 2) (p53BP2)

 ASPP2_HUMAN             Reviewed;        1128 AA.
Q13625; B4DG66; Q12892; Q86X75; Q96KQ3;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
15-AUG-2003, sequence version 2.
25-OCT-2017, entry version 187.
RecName: Full=Apoptosis-stimulating of p53 protein 2;
AltName: Full=Bcl2-binding protein;
Short=Bbp;
AltName: Full=Renal carcinoma antigen NY-REN-51;
AltName: Full=Tumor suppressor p53-binding protein 2;
Short=53BP2;
Short=p53-binding protein 2;
Short=p53BP2;
Name=TP53BP2; Synonyms=ASPP2, BBP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH BCL2.
PubMed=8668206; DOI=10.1128/MCB.16.7.3884;
Naumovski L., Cleary M.L.;
"The p53-binding protein 53BP2 also interacts with Bcl2 and impedes
cell cycle progression at G2/M.";
Mol. Cell. Biol. 16:3884-3892(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND INTERACTION WITH TP53.
PubMed=11684014; DOI=10.1016/S1097-2765(01)00367-7;
Samuels-Lev Y., O'Connor D.J., Bergamaschi D., Trigiante G.,
Hsieh J.-K., Zhong S., Campargue I., Naumovski L., Crook T., Lu X.;
"ASPP proteins specifically stimulate the apoptotic function of p53.";
Mol. Cell 8:781-794(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 600-1128, AND INTERACTION WITH TP53.
PubMed=8016121; DOI=10.1073/pnas.91.13.6098;
Iwabuchi K., Bartel P.L., Li B., Marraccino R., Fields S.;
"Two cellular proteins that bind to wild-type but not mutant p53.";
Proc. Natl. Acad. Sci. U.S.A. 91:6098-6102(1994).
[7]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[8]
TISSUE SPECIFICITY, AND INTERACTION WITH RELA.
PubMed=10498867; DOI=10.1038/sj.onc.1202904;
Yang J.-P., Hori M., Takahashi N., Kawabe T., Kato H., Okamoto T.;
"NF-kappaB subunit p65 binds to 53BP2 and inhibits cell death induced
by 53BP2.";
Oncogene 18:5177-5186(1999).
[9]
INTERACTION WITH APC2, MUTAGENESIS OF TRP-1098, AND SUBCELLULAR
LOCATION.
PubMed=10646860;
Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.;
"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.";
Cancer Res. 60:101-105(2000).
[10]
INDUCTION.
PubMed=11027272; DOI=10.1128/MCB.20.21.8018-8025.2000;
Lopez C.D., Ao Y., Rohde L.H., Perez T.D., O'Connor D.J., Lu X.,
Ford J.M., Naumovski L.;
"Proapoptotic p53-interacting protein 53BP2 is induced by UV
irradiation but suppressed by p53.";
Mol. Cell. Biol. 20:8018-8025(2000).
[11]
TISSUE SPECIFICITY.
PubMed=10631318; DOI=10.1016/S0014-5793(99)01726-3;
Mori T., Okamoto H., Takahashi N., Ueda R., Okamoto T.;
"Aberrant overexpression of 53BP2 mRNA in lung cancer cell lines.";
FEBS Lett. 465:124-128(2000).
[12]
FUNCTION, AND INTERACTION WITH APPBP1.
PubMed=12694406;
Chen Y., Liu W., Naumovski L., Neve R.L.;
"ASPP2 inhibits APP-BP1-mediated NEDD8 conjugation to cullin-1 and
decreases APP-BP1-induced cell proliferation and neuronal apoptosis.";
J. Neurochem. 85:801-809(2003).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480 AND SER-556, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
FUNCTION, INTERACTION WITH DDX42, AND SUBCELLULAR LOCATION.
PubMed=19377511; DOI=10.1038/onc.2009.75;
Uhlmann-Schiffler H., Kiermayer S., Stahl H.;
"The DEAD box protein Ddx42p modulates the function of ASPP2, a
stimulator of apoptosis.";
Oncogene 28:2065-2073(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480; SER-556 AND
SER-572, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480; SER-556; SER-569;
SER-576; SER-714 AND SER-737, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
ANKYRIN REPEATS.
PubMed=25547411; DOI=10.1186/s12859-014-0440-9;
Chakrabarty B., Parekh N.;
"Identifying tandem Ankyrin repeats in protein structures.";
BMC Bioinformatics 15:6599-6599(2014).
[23]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 892-1128.
PubMed=8875926; DOI=10.1126/science.274.5289.1001;
Gorina S., Pavletich N.P.;
"Structure of the p53 tumor suppressor bound to the ankyrin and SH3
domains of 53BP2.";
Science 274:1001-1005(1996).
[24]
STRUCTURE BY NMR OF 1-83.
PubMed=17594908; DOI=10.1016/j.jmb.2007.05.024;
Tidow H., Andreeva A., Rutherford T.J., Fersht A.R.;
"Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a
ubiquitin-like fold.";
J. Mol. Biol. 371:948-958(2007).
-!- FUNCTION: Regulator that plays a central role in regulation of
apoptosis and cell growth via its interactions. Regulates TP53 by
enhancing the DNA binding and transactivation function of TP53 on
the promoters of proapoptotic genes in vivo. Inhibits the ability
of APPBP1 to conjugate NEDD8 to CUL1, and thereby decreases APPBP1
ability to induce apoptosis. Impedes cell cycle progression at
G2/M. Its apoptosis-stimulating activity is inhibited by its
interaction with DDX42. {ECO:0000269|PubMed:11684014,
ECO:0000269|PubMed:12694406, ECO:0000269|PubMed:19377511}.
-!- SUBUNIT: Binds to the central domain of TP53 as well as to BCL2.
Interacts with protein phosphatase 1. Interacts with RELA NF-
kappa-B subunit. This interaction probably prevents the activation
of apoptosis, possibly by preventing its interaction with TP53.
Interacts with APC2 and APPBP1. Interacts with DDX42 (via the C-
terminus); the interaction is not inhibited by TP53BP2
ubiquitination and is independent of p53/TP53.
{ECO:0000269|PubMed:10498867, ECO:0000269|PubMed:10646860,
ECO:0000269|PubMed:11684014, ECO:0000269|PubMed:12694406,
ECO:0000269|PubMed:19377511, ECO:0000269|PubMed:8016121,
ECO:0000269|PubMed:8668206}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-77642, EBI-77642;
P27958:- (xeno); NbExp=5; IntAct=EBI-77642, EBI-6377335;
O95996:APC2; NbExp=4; IntAct=EBI-77642, EBI-1053045;
P05067:APP; NbExp=3; IntAct=EBI-77642, EBI-77613;
Q8N5M1:ATPAF2; NbExp=3; IntAct=EBI-10175039, EBI-1166928;
Q9UQB8:BAIAP2; NbExp=3; IntAct=EBI-10175039, EBI-525456;
P10415:BCL2; NbExp=10; IntAct=EBI-77642, EBI-77694;
Q07817-1:BCL2L1; NbExp=3; IntAct=EBI-77642, EBI-287195;
Q92843:BCL2L2; NbExp=4; IntAct=EBI-77642, EBI-707714;
Q53HC0:CCDC92; NbExp=3; IntAct=EBI-10175039, EBI-719994;
P35222:CTNNB1; NbExp=5; IntAct=EBI-77642, EBI-491549;
Q2TBE0:CWF19L2; NbExp=3; IntAct=EBI-10175039, EBI-5453285;
Q96GG9:DCUN1D1; NbExp=3; IntAct=EBI-10175039, EBI-740086;
Q09472:EP300; NbExp=2; IntAct=EBI-77642, EBI-447295;
P62993:GRB2; NbExp=3; IntAct=EBI-10175039, EBI-401755;
P62807:HIST1H2BI; NbExp=3; IntAct=EBI-10175039, EBI-354552;
Q9BUJ2:HNRNPUL1; NbExp=3; IntAct=EBI-10175039, EBI-1018153;
P35569:Irs1 (xeno); NbExp=2; IntAct=EBI-287091, EBI-400825;
P35570:Irs1 (xeno); NbExp=4; IntAct=EBI-287091, EBI-520230;
Q96J02:ITCH; NbExp=2; IntAct=EBI-77642, EBI-1564678;
P61968:LMO4; NbExp=3; IntAct=EBI-10175039, EBI-2798728;
Q8NCE2:MTMR14; NbExp=3; IntAct=EBI-10175039, EBI-5658424;
O14777:NDC80; NbExp=3; IntAct=EBI-10175039, EBI-715849;
Q86Y26:NUTM1; NbExp=3; IntAct=EBI-10175039, EBI-10178410;
Q9UBU9:NXF1; NbExp=3; IntAct=EBI-10175039, EBI-398874;
Q96DC9:OTUB2; NbExp=3; IntAct=EBI-10175039, EBI-746259;
Q494U1:PLEKHN1; NbExp=3; IntAct=EBI-10175039, EBI-10241513;
P62875:POLR2L; NbExp=3; IntAct=EBI-10175039, EBI-359527;
P62136:PPP1CA; NbExp=9; IntAct=EBI-77642, EBI-357253;
P62140:PPP1CB; NbExp=3; IntAct=EBI-10175039, EBI-352350;
P36873:PPP1CC; NbExp=8; IntAct=EBI-77642, EBI-356283;
Q8WWY3:PRPF31; NbExp=3; IntAct=EBI-10175039, EBI-1567797;
P62826:RAN; NbExp=5; IntAct=EBI-77642, EBI-286642;
Q04206:RELA; NbExp=6; IntAct=EBI-287091, EBI-73886;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-10175039, EBI-747107;
Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-10175039, EBI-2212028;
Q92844:TANK; NbExp=3; IntAct=EBI-10175039, EBI-356349;
Q9NU19:TBC1D22B; NbExp=3; IntAct=EBI-10175039, EBI-8787464;
P56279:TCL1A; NbExp=3; IntAct=EBI-10175039, EBI-749995;
P04637:TP53; NbExp=7; IntAct=EBI-77642, EBI-366083;
Q9H3D4:TP63; NbExp=2; IntAct=EBI-77642, EBI-2337775;
O15350:TP73; NbExp=2; IntAct=EBI-77642, EBI-389606;
Q9BUZ4:TRAF4; NbExp=3; IntAct=EBI-10175039, EBI-3650647;
P40222:TXLNA; NbExp=3; IntAct=EBI-10175039, EBI-359793;
P57075:UBASH3A; NbExp=3; IntAct=EBI-10175039, EBI-2105393;
P46936:YAP1 (xeno); NbExp=6; IntAct=EBI-287091, EBI-7804091;
P46937:YAP1; NbExp=9; IntAct=EBI-287091, EBI-1044059;
P63104:YWHAZ; NbExp=2; IntAct=EBI-77642, EBI-347088;
Q8N5A5:ZGPAT; NbExp=3; IntAct=EBI-10175039, EBI-3439227;
Q8N5A5-2:ZGPAT; NbExp=3; IntAct=EBI-10175039, EBI-10183064;
P17031:ZNF26; NbExp=5; IntAct=EBI-10175039, EBI-2841331;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus.
Note=Predominantly found in the perinuclear region. Some small
fraction is nuclear. Sequester in the cytoplasm on overexpression
of DDX42.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q13625-1; Sequence=Displayed;
Name=2; Synonyms=Bbp;
IsoId=Q13625-2; Sequence=VSP_008010;
Note=Due to Alu sequence insertion that creates a shorter but
existing form that may have an alternative function.;
Name=3;
IsoId=Q13625-3; Sequence=VSP_043509;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in spleen, thymus,
prostate, testis, ovary, small intestine, colon and peripheral
blood leukocyte. Reduced expression in breast carcinomas
expressing a wild-type TP53 protein. Overexpressed in lung cancer
cell lines. {ECO:0000269|PubMed:10498867,
ECO:0000269|PubMed:10631318, ECO:0000269|PubMed:11684014}.
-!- INDUCTION: Following DNA damage induced by UV irradiation. Down-
regulated by wild-type, but not mutant, p53/TP53.
{ECO:0000269|PubMed:11027272}.
-!- DOMAIN: The ankyrin repeats and the SH3 domain are required for a
specific interactions with TP53.
-!- SIMILARITY: Belongs to the ASPP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH46150.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH46150.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH58918.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TP53BP2ID42667ch1q42.html";
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EMBL; U58334; AAC50557.1; -; mRNA.
EMBL; AJ318888; CAC83012.1; -; mRNA.
EMBL; AK294432; BAG57677.1; -; mRNA.
EMBL; AC096542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC046150; AAH46150.2; ALT_SEQ; mRNA.
EMBL; BC058918; AAH58918.2; ALT_INIT; mRNA.
EMBL; U09582; AAA21597.1; -; mRNA.
CCDS; CCDS1538.1; -. [Q13625-2]
CCDS; CCDS44319.1; -. [Q13625-3]
PIR; I38607; I38607.
RefSeq; NP_001026855.2; NM_001031685.2. [Q13625-3]
RefSeq; NP_005417.1; NM_005426.2. [Q13625-2]
RefSeq; XP_011542571.1; XM_011544269.2. [Q13625-2]
UniGene; Hs.523968; -.
PDB; 1YCS; X-ray; 2.20 A; B=892-1126.
PDB; 2UWQ; NMR; -; A=1-83.
PDB; 4A63; X-ray; 2.27 A; B/D/F/H/J/L=892-1128.
PDB; 4IRV; X-ray; 2.04 A; E/F/G/H=726-782.
PDBsum; 1YCS; -.
PDBsum; 2UWQ; -.
PDBsum; 4A63; -.
PDBsum; 4IRV; -.
ProteinModelPortal; Q13625; -.
SMR; Q13625; -.
BioGrid; 113012; 115.
DIP; DIP-426N; -.
IntAct; Q13625; 117.
MINT; MINT-106406; -.
STRING; 9606.ENSP00000341957; -.
iPTMnet; Q13625; -.
PhosphoSitePlus; Q13625; -.
BioMuta; TP53BP2; -.
DMDM; 33860140; -.
EPD; Q13625; -.
MaxQB; Q13625; -.
PaxDb; Q13625; -.
PeptideAtlas; Q13625; -.
PRIDE; Q13625; -.
Ensembl; ENST00000343537; ENSP00000341957; ENSG00000143514. [Q13625-3]
Ensembl; ENST00000391878; ENSP00000375750; ENSG00000143514. [Q13625-2]
GeneID; 7159; -.
KEGG; hsa:7159; -.
UCSC; uc001hod.4; human. [Q13625-1]
CTD; 7159; -.
DisGeNET; 7159; -.
EuPathDB; HostDB:ENSG00000143514.16; -.
GeneCards; TP53BP2; -.
HGNC; HGNC:12000; TP53BP2.
HPA; HPA021603; -.
HPA; HPA050429; -.
MIM; 602143; gene.
neXtProt; NX_Q13625; -.
OpenTargets; ENSG00000143514; -.
PharmGKB; PA36681; -.
eggNOG; KOG0515; Eukaryota.
eggNOG; ENOG410Y17W; LUCA.
GeneTree; ENSGT00760000119141; -.
HOGENOM; HOG000034106; -.
HOVERGEN; HBG050596; -.
InParanoid; Q13625; -.
KO; K16823; -.
OMA; QHFTEVP; -.
OrthoDB; EOG091G0R1R; -.
PhylomeDB; Q13625; -.
TreeFam; TF105545; -.
Reactome; R-HSA-139915; Activation of PUMA and translocation to mitochondria.
Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
Reactome; R-HSA-6803211; TP53 Regulates Transcription of Death Receptors and Ligands.
Reactome; R-HSA-6804759; Regulation of TP53 Activity through Association with Co-factors.
SIGNOR; Q13625; -.
ChiTaRS; TP53BP2; human.
EvolutionaryTrace; Q13625; -.
GeneWiki; TP53BP2; -.
GenomeRNAi; 7159; -.
PRO; PR:Q13625; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143514; -.
CleanEx; HS_TP53BP2; -.
ExpressionAtlas; Q13625; baseline and differential.
Genevisible; Q13625; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:AgBase.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IDA:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; TAS:UniProtKB.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IMP:AgBase.
GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR036028; SH3-like_dom.
InterPro; IPR001452; SH3_domain.
InterPro; IPR029071; Ubiquitin-rel_dom.
Pfam; PF12796; Ank_2; 1.
Pfam; PF00018; SH3_1; 1.
SMART; SM00248; ANK; 2.
SMART; SM00326; SH3; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 2.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ANK repeat; Apoptosis; Cell cycle;
Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
Reference proteome; Repeat; SH3 domain; SH3-binding.
CHAIN 1 1128 Apoptosis-stimulating of p53 protein 2.
/FTId=PRO_0000066964.
REPEAT 926 957 ANK 1.
REPEAT 958 990 ANK 2.
REPEAT 991 1024 ANK 3.
REPEAT 1025 1067 ANK 4.
DOMAIN 1057 1119 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 332 348 Interaction with APPBP1.
{ECO:0000269|PubMed:12694406}.
REGION 876 1128 Mediates interaction with APC2.
{ECO:0000269|PubMed:10646860}.
MOTIF 866 875 SH3-binding. {ECO:0000255}.
COMPBIAS 132 173 Gln-rich.
COMPBIAS 824 902 Pro-rich.
MOD_RES 480 480 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 556 556 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 572 572 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 576 576 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 698 698 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CG79}.
MOD_RES 714 714 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 737 737 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 123 Missing (in isoform 2).
{ECO:0000303|PubMed:8668206}.
/FTId=VSP_008010.
VAR_SEQ 1 1 M -> MRFGSKM (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043509.
MUTAGEN 1098 1098 W->K: Loss of interaction with APC2.
{ECO:0000269|PubMed:10646860}.
STRAND 2 9 {ECO:0000244|PDB:2UWQ}.
STRAND 17 22 {ECO:0000244|PDB:2UWQ}.
HELIX 29 34 {ECO:0000244|PDB:2UWQ}.
STRAND 40 42 {ECO:0000244|PDB:2UWQ}.
STRAND 44 49 {ECO:0000244|PDB:2UWQ}.
STRAND 52 56 {ECO:0000244|PDB:2UWQ}.
HELIX 62 69 {ECO:0000244|PDB:2UWQ}.
HELIX 73 75 {ECO:0000244|PDB:2UWQ}.
STRAND 77 81 {ECO:0000244|PDB:2UWQ}.
HELIX 747 760 {ECO:0000244|PDB:4IRV}.
TURN 761 764 {ECO:0000244|PDB:4IRV}.
HELIX 927 936 {ECO:0000244|PDB:1YCS}.
HELIX 939 945 {ECO:0000244|PDB:1YCS}.
HELIX 946 948 {ECO:0000244|PDB:4A63}.
HELIX 962 969 {ECO:0000244|PDB:1YCS}.
HELIX 972 981 {ECO:0000244|PDB:1YCS}.
HELIX 995 1001 {ECO:0000244|PDB:1YCS}.
HELIX 1005 1013 {ECO:0000244|PDB:1YCS}.
STRAND 1023 1025 {ECO:0000244|PDB:1YCS}.
HELIX 1029 1032 {ECO:0000244|PDB:1YCS}.
STRAND 1035 1037 {ECO:0000244|PDB:1YCS}.
HELIX 1043 1053 {ECO:0000244|PDB:1YCS}.
TURN 1054 1057 {ECO:0000244|PDB:1YCS}.
HELIX 1058 1060 {ECO:0000244|PDB:1YCS}.
STRAND 1061 1066 {ECO:0000244|PDB:1YCS}.
STRAND 1083 1086 {ECO:0000244|PDB:1YCS}.
STRAND 1091 1093 {ECO:0000244|PDB:4A63}.
STRAND 1095 1102 {ECO:0000244|PDB:1YCS}.
STRAND 1105 1110 {ECO:0000244|PDB:1YCS}.
HELIX 1111 1113 {ECO:0000244|PDB:1YCS}.
STRAND 1114 1117 {ECO:0000244|PDB:4A63}.
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


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