Q8CG79 (ASPP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Apoptosis-stimulating of p53 protein 2

Alternative name(s):
Tumor suppressor p53-binding protein 2
Short name=53BP2
Short name=p53-binding protein 2
Short name=p53BP2

Gene names

Name:	Tp53bp2
Synonyms:	Aspp2, Trp53bp2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1128 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulator that plays a central role in regulation of apoptosis and cell growth via its interactions. Regulates p53/TP53 by enhancing the DNA binding and transactivation function of p53/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 By similarity.
Subunit structure	Binds to the central domain of p53/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 p53/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 By similarity.
Subcellular location	Cytoplasm › perinuclear region By similarity. Nucleus By similarity. Note: Predominantly found in the perinuclear region By similarity. Some small fraction is nuclear By similarity.
Domain	The ankyrin repeats and the SH3 domain are required for a specific interactions with p53/TP53 By similarity.
Sequence similarities	Belongs to the ASPP family. Contains 2 ANK repeats. Contains 1 SH3 domain.
Sequence caution	The sequence BC042874 differs from that shown. Reason: Frameshift at position 23.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle
Cellular component	Cytoplasm Nucleus
Domain	ANK repeat Repeat SH3 domain SH3-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW central nervous system development Inferred from mutant phenotype PubMed 16702401. Source: MGI embryo development ending in birth or egg hatching Inferred from genetic interaction PubMed 16702401. Source: MGI heart development Inferred from mutant phenotype PubMed 16702401. Source: MGI induction of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB response to ionizing radiation Inferred from mutant phenotype PubMed 16702401. Source: MGI
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1128	1128	Apoptosis-stimulating of p53 protein 2		PRO_0000066965
Regions
	Repeat	958 – 987	30	ANK 1
	Repeat	991 – 1020	30	ANK 2
	Domain	1057 – 1119	63	SH3
	Region	332 – 348	17	Interaction with APPBP1 By similarity
	Region	876 – 1128	253	Mediates interaction with APC2 By similarity
	Motif	866 – 875	10	SH3-binding Potential
	Compositional bias	92 – 133	42	Gln-rich
	Compositional bias	132 – 173	42	Gln-rich
Amino acid modifications
	Modified residue	479	1	Phosphoserine Ref.4
	Modified residue	555	1	Phosphoserine By similarity
	Modified residue	571	1	Phosphoserine By similarity
	Modified residue	697	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	270	1	L → V in BAE22185. Ref.3
	Sequence conflict	367 – 382	16	VKPAL…MQSAE → DAWVAHASAHASAHAS in AAH30894. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8CG79 [UniParc]. Last modified January 9, 2007. Version 3. Checksum: C5FF5D37D73187A0	FASTA	1,128	125,301
	10 20 30 40 50 60 MMPMFLTVYL SNSEQHFTEV PVTPETICRD VVDLCKEPGE NDCHLAEVWC GSERPVADNE 70 80 90 100 110 120 RMFDVLQRFG SQRNEVRFFL RHERPPNRDI VSGPRSQDPS VKRNGVKVPG EHRRKENGVN 130 140 150 160 170 180 SPRLDLTLAE LQEMASRQQQ QIEAQQQMLA TKEQRLKFLK QQDQRQQQQA AEQEKLKRLR 190 200 210 220 230 240 EIAESQEAKL KKVRALKGHV EQKRLSNGKL VEEIEQMNSL FQQKQRELVL AVSKVEELTR 250 260 270 280 290 300 QLEMLKNGRI DGHHDNQSAV AELDRLYKEL QLRNKLNQEQ NAKLQQQREC LNKRNSEVAV 310 320 330 340 350 360 MDKRVSELRD RLWKKKAALQ QKENLPVSPD GNLPQQAVSA PSRVAAVGPY IQSSTMPRMP 370 380 390 400 410 420 SRPELLVKPA LPDGSLLMQS AEGPMKIQTL PNMRSGAASQ SKGSKAHPAS PDWNPSNADL 430 440 450 460 470 480 LPSQGSSVPQ SAGTALDQVD DGEIAVREKE KKVRPFSMFD TVDQCAAPPS FGTLRKNQSS 490 500 510 520 530 540 EDILRDAQAV NKNVAKVPPP VPTKPKQIHL PYFGQTAQSP SDMKPDGNAQ QLPIAATSVG 550 560 570 580 590 600 AKLKPAGPQA RMLLSPGAPS GGQDQVLSPA SKQESPPAAA VRPFTPQPSK DTFPPAFRKP 610 620 630 640 650 660 QTVAASSIYS MYTQQQAPGK NFQQAVQSAL TKTQPRGPHF SSVYGKPVIA AAQNPQQHPE 670 680 690 700 710 720 NIYSCSQGKP GSPEPETETV SSVHESHENE RIPRPLSPTK LLPFLSNPYR NQSDADLEAL 730 740 750 760 770 780 RKKLSNAPRP LKKRSSITEP EGPNGPNIQK LLYQRTTIAA METISVPSHP SKSPGSVTVN 790 800 810 820 830 840 PESSVEIPNP YLHVEPEKEV GSLVPEPLSP EDMGSASTEN SDVPAPSAGL EYVSEGVTDS 850 860 870 880 890 900 STNLQNNVEE TNPEAPHLLE VYLEEYPPYP PPPYPSGEPE VSEEDSARMR PPEITGQVSL 910 920 930 940 950 960 PPGKRTNLRK TGSERIAHGM RVKFNPLALL LDSSLEGEFD LVQRIIYEVD DPSLPNDEGI 970 980 990 1000 1010 1020 TALHNAVCAG HTEIVKFLVQ FGVNVNAADS DGWTPLHCAA SCNNVQVCKF LVESGAAVFA 1030 1040 1050 1060 1070 1080 MTYSDMQTAA DKCEEMEEGY TQCSQFLYGV QEKMGIMNKG VIYALWDYEP QHDDELLMKE 1090 1100 1110 1120 GDCMTVIRRE DEEEIEWWWA RLNDKEGYVP RNLLGLYPRI KPRQRSLA

References

[1]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and FVB/N. Tissue: Brain and Mammary tumor.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 270-1128. Strain: C57BL/6J. Tissue: Medulla oblongata.
[4]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC131742 Genomic DNA. No translation available. BC030894 mRNA. Translation: AAH30894.1. BC042874 mRNA. No translation available. CB248714 mRNA. No translation available. AK134556 mRNA. Translation: BAE22185.1.
IPI	IPI00229434.
RefSeq	NP_775554.2. NM_173378.2.
UniGene	Mm.287450.
3D structure databases
ProteinModelPortal	Q8CG79.
SMR	Q8CG79. Positions 1-83, 920-1121.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8CG79. 3 interactions.
STRING	10090.ENSMUSP00000112508.
PTM databases
PhosphoSite	Q8CG79.
Proteomic databases
PaxDb	Q8CG79.
PRIDE	Q8CG79.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	209456.
KEGG	mmu:209456.
UCSC	uc007dyc.1. mouse.
Organism-specific databases
CTD	209456.
MGI	MGI:2138319. Trp53bp2.
Phylogenomic databases
eggNOG	NOG283717.
HOGENOM	HOG000034106.
HOVERGEN	HBG050596.
InParanoid	Q8CG79.
KO	K16823.
OrthoDB	EOG4KH2T7.
Gene expression databases
ArrayExpress	Q8CG79.
Bgee	Q8CG79.
Genevestigator	Q8CG79.
GermOnline	ENSMUSG00000026510. Mus musculus.
Family and domain databases
Gene3D	1.25.40.20. 1 hit.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR001452. SH3_domain. [Graphical view]
Pfam	PF12796. Ank_2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
SMART	SM00248. ANK. 2 hits. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit. SSF50044. SH3. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 2 hits. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	372677.
SOURCE	Search...

Entry information

Entry name

ASPP2_MOUSE

Accession

Primary (citable) accession number: Q8CG79
Secondary accession number(s): Q3UYM7, Q8K2L5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	January 9, 2007
Last modified:	April 3, 2013
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program