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Q8CG79 (ASPP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1128 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11281128Apoptosis-stimulating of p53 protein 2
PRO_0000066965

Regions

Repeat958 – 98730ANK 1
Repeat991 – 102030ANK 2
Domain1057 – 111963SH3
Region332 – 34817Interaction with APPBP1 By similarity
Region876 – 1128253Mediates interaction with APC2 By similarity
Motif866 – 87510SH3-binding Potential
Compositional bias92 – 13342Gln-rich
Compositional bias132 – 17342Gln-rich

Amino acid modifications

Modified residue4791Phosphoserine By similarity
Modified residue5551Phosphoserine By similarity
Modified residue5711Phosphoserine By similarity
Modified residue6971Phosphoserine Ref.5
Modified residue7131Phosphoserine Ref.4

Experimental info

Sequence conflict2701L → V in BAE22185. Ref.3
Sequence conflict367 – 38216VKPAL…MQSAE → DAWVAHASAHASAHAS in AAH30894. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8CG79 [UniParc].

Last modified January 9, 2007. Version 3.
Checksum: C5FF5D37D73187A0

FASTA1,128125,301
        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

« Hide

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. expand/collapse author list , 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. expand/collapse author list , 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-713, 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.
RefSeqNP_775554.2. NM_173378.2.
UniGeneMm.287450.

3D structure databases

ProteinModelPortalQ8CG79.
SMRQ8CG79. Positions 1-83, 920-1121.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8CG79. 3 interactions.
MINTMINT-1753644.
STRING10090.ENSMUSP00000112508.

PTM databases

PhosphoSiteQ8CG79.

Proteomic databases

PaxDbQ8CG79.
PRIDEQ8CG79.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID209456.
KEGGmmu:209456.
UCSCuc007dyd.1. mouse.

Organism-specific databases

CTD209456.
MGIMGI:2138319. Trp53bp2.

Phylogenomic databases

eggNOGNOG283717.
HOGENOMHOG000034106.
HOVERGENHBG050596.
InParanoidQ8CG79.
KOK16823.

Gene expression databases

ArrayExpressQ8CG79.
BgeeQ8CG79.
GenevestigatorQ8CG79.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF12796. Ank_2. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio372677.
PROQ8CG79.
SOURCESearch...

Entry information

Entry nameASPP2_MOUSE
AccessionPrimary (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: January 22, 2014
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents