ASPP2_MOUSE
ID ASPP2_MOUSE Reviewed; 1128 AA.
AC Q8CG79; Q3UYM7; Q8K2L5;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Apoptosis-stimulating of p53 protein 2;
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, Trp53bp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 270-1128.
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). Regulates p53/TP53 by enhancing the DNA binding
CC and transactivation function of p53/TP53 on the promoters of
CC proapoptotic genes in vivo. Inhibits the ability of APPBP1 to conjugate
CC NEDD8 to CUL1, and thereby decreases APPBP1 ability to induce
CC apoptosis. Impedes cell cycle progression at G2/M. Its apoptosis-
CC stimulating activity is inhibited by its interaction with DDX42 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q13625}.
CC -!- SUBUNIT: Interacts with P53/TP53; the interaction promotes pro-
CC apoptotic activity (By similarity). Interacts with BCL2 (By
CC similarity). Interacts with protein phosphatase 1. Interacts with RELA
CC NF-kappa-B subunit. This interaction probably prevents the activation
CC of apoptosis, possibly by preventing its interaction with p53/TP53.
CC Interacts with APC2 and APPBP1. Interacts with DDX42 (via the C-
CC terminus); the interaction is not inhibited by TP53BP2 ubiquitination
CC and is independent of p53/TP53 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q13625}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC Nucleus {ECO:0000250}. Note=Predominantly found in the perinuclear
CC region. Some small fraction is nuclear. {ECO:0000250}.
CC -!- DOMAIN: The ankyrin repeats and the SH3 domain are required for a
CC specific interactions with p53/TP53. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ASPP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC042874; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC131742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030894; AAH30894.1; -; mRNA.
DR EMBL; BC042874; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CB248714; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK134556; BAE22185.1; -; mRNA.
DR RefSeq; NP_775554.2; NM_173378.2.
DR AlphaFoldDB; Q8CG79; -.
DR SMR; Q8CG79; -.
DR BioGRID; 229080; 4.
DR IntAct; Q8CG79; 5.
DR STRING; 10090.ENSMUSP00000112508; -.
DR iPTMnet; Q8CG79; -.
DR PhosphoSitePlus; Q8CG79; -.
DR EPD; Q8CG79; -.
DR jPOST; Q8CG79; -.
DR MaxQB; Q8CG79; -.
DR PaxDb; Q8CG79; -.
DR PRIDE; Q8CG79; -.
DR DNASU; 209456; -.
DR GeneID; 209456; -.
DR KEGG; mmu:209456; -.
DR UCSC; uc007dyd.1; mouse.
DR CTD; 209456; -.
DR MGI; MGI:2138319; Trp53bp2.
DR eggNOG; KOG0515; Eukaryota.
DR InParanoid; Q8CG79; -.
DR OrthoDB; 1041229at2759; -.
DR PhylomeDB; Q8CG79; -.
DR Reactome; R-MMU-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR BioGRID-ORCS; 209456; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Trp53bp2; mouse.
DR PRO; PR:Q8CG79; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CG79; protein.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISS:UniProtKB.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:MGI.
DR Gene3D; 1.25.40.20; -; 1.
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; PF14604; SH3_9; 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 ANK repeat; Apoptosis; Cell cycle; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; SH3-binding.
FT CHAIN 1..1128
FT /note="Apoptosis-stimulating of p53 protein 2"
FT /id="PRO_0000066965"
FT REPEAT 958..987
FT /note="ANK 1"
FT REPEAT 991..1020
FT /note="ANK 2"
FT DOMAIN 1057..1119
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 85..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..348
FT /note="Interaction with APPBP1"
FT /evidence="ECO:0000250"
FT REGION 393..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..1128
FT /note="Mediates interaction with APC2"
FT /evidence="ECO:0000250"
FT MOTIF 866..875
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 105..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13625"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13625"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13625"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13625"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13625"
FT CONFLICT 270
FT /note="L -> V (in Ref. 3; BAE22185)"
FT /evidence="ECO:0000305"
FT CONFLICT 367..382
FT /note="VKPALPDGSLLMQSAE -> DAWVAHASAHASAHAS (in Ref. 2;
FT AAH30894)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1128 AA; 125301 MW; C5FF5D37D73187A0 CRC64;
MMPMFLTVYL SNSEQHFTEV PVTPETICRD VVDLCKEPGE NDCHLAEVWC GSERPVADNE
RMFDVLQRFG SQRNEVRFFL RHERPPNRDI VSGPRSQDPS VKRNGVKVPG EHRRKENGVN
SPRLDLTLAE LQEMASRQQQ QIEAQQQMLA TKEQRLKFLK QQDQRQQQQA AEQEKLKRLR
EIAESQEAKL KKVRALKGHV EQKRLSNGKL VEEIEQMNSL FQQKQRELVL AVSKVEELTR
QLEMLKNGRI DGHHDNQSAV AELDRLYKEL QLRNKLNQEQ NAKLQQQREC LNKRNSEVAV
MDKRVSELRD RLWKKKAALQ QKENLPVSPD GNLPQQAVSA PSRVAAVGPY IQSSTMPRMP
SRPELLVKPA LPDGSLLMQS AEGPMKIQTL PNMRSGAASQ SKGSKAHPAS PDWNPSNADL
LPSQGSSVPQ SAGTALDQVD DGEIAVREKE KKVRPFSMFD TVDQCAAPPS FGTLRKNQSS
EDILRDAQAV NKNVAKVPPP VPTKPKQIHL PYFGQTAQSP SDMKPDGNAQ QLPIAATSVG
AKLKPAGPQA RMLLSPGAPS GGQDQVLSPA SKQESPPAAA VRPFTPQPSK DTFPPAFRKP
QTVAASSIYS MYTQQQAPGK NFQQAVQSAL TKTQPRGPHF SSVYGKPVIA AAQNPQQHPE
NIYSCSQGKP GSPEPETETV SSVHESHENE RIPRPLSPTK LLPFLSNPYR NQSDADLEAL
RKKLSNAPRP LKKRSSITEP EGPNGPNIQK LLYQRTTIAA METISVPSHP SKSPGSVTVN
PESSVEIPNP YLHVEPEKEV GSLVPEPLSP EDMGSASTEN SDVPAPSAGL EYVSEGVTDS
STNLQNNVEE TNPEAPHLLE VYLEEYPPYP PPPYPSGEPE VSEEDSARMR PPEITGQVSL
PPGKRTNLRK TGSERIAHGM RVKFNPLALL LDSSLEGEFD LVQRIIYEVD DPSLPNDEGI
TALHNAVCAG HTEIVKFLVQ FGVNVNAADS DGWTPLHCAA SCNNVQVCKF LVESGAAVFA
MTYSDMQTAA DKCEEMEEGY TQCSQFLYGV QEKMGIMNKG VIYALWDYEP QHDDELLMKE
GDCMTVIRRE DEEEIEWWWA RLNDKEGYVP RNLLGLYPRI KPRQRSLA
