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Q8CG79

- ASPP2_MOUSE

UniProt

Q8CG79 - ASPP2_MOUSE

Protein

Apoptosis-stimulating of p53 protein 2

Gene

Tp53bp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 3 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    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.By similarity

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. central nervous system development Source: MGI
    3. embryo development ending in birth or egg hatching Source: MGI
    4. heart development Source: MGI
    5. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
    6. response to ionizing radiation Source: MGI

    Keywords - Biological processi

    Apoptosis, Cell cycle

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:Tp53bp2
    Synonyms:Aspp2, Trp53bp2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:2138319. Trp53bp2.

    Subcellular locationi

    Cytoplasmperinuclear region By similarity. Nucleus By similarity
    Note: Predominantly found in the perinuclear region. Some small fraction is nuclear.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11281128Apoptosis-stimulating of p53 protein 2PRO_0000066965Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei479 – 4791PhosphoserineBy similarity
    Modified residuei555 – 5551PhosphoserineBy similarity
    Modified residuei571 – 5711PhosphoserineBy similarity
    Modified residuei697 – 6971Phosphoserine1 Publication
    Modified residuei713 – 7131Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8CG79.
    PaxDbiQ8CG79.
    PRIDEiQ8CG79.

    PTM databases

    PhosphoSiteiQ8CG79.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8CG79.
    BgeeiQ8CG79.
    GenevestigatoriQ8CG79.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    IntActiQ8CG79. 3 interactions.
    MINTiMINT-1753644.
    STRINGi10090.ENSMUSP00000112508.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CG79.
    SMRiQ8CG79. Positions 1-83, 920-1121.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati958 – 98730ANK 1Add
    BLAST
    Repeati991 – 102030ANK 2Add
    BLAST
    Domaini1057 – 111963SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni332 – 34817Interaction with APPBP1By similarityAdd
    BLAST
    Regioni876 – 1128253Mediates interaction with APC2By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi866 – 87510SH3-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi92 – 13342Gln-richAdd
    BLAST
    Compositional biasi132 – 17342Gln-richAdd
    BLAST

    Domaini

    The ankyrin repeats and the SH3 domain are required for a specific interactions with p53/TP53.By similarity

    Sequence similaritiesi

    Belongs to the ASPP family.Curated
    Contains 2 ANK repeats.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat, SH3 domain, SH3-binding

    Phylogenomic databases

    eggNOGiNOG283717.
    HOGENOMiHOG000034106.
    HOVERGENiHBG050596.
    InParanoidiQ8CG79.
    KOiK16823.
    PhylomeDBiQ8CG79.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001452. SH3_domain.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF12796. Ank_2. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    SMARTiSM00248. ANK. 2 hits.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 2 hits.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8CG79-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMPMFLTVYL SNSEQHFTEV PVTPETICRD VVDLCKEPGE NDCHLAEVWC     50
    GSERPVADNE RMFDVLQRFG SQRNEVRFFL RHERPPNRDI VSGPRSQDPS 100
    VKRNGVKVPG EHRRKENGVN SPRLDLTLAE LQEMASRQQQ QIEAQQQMLA 150
    TKEQRLKFLK QQDQRQQQQA AEQEKLKRLR EIAESQEAKL KKVRALKGHV 200
    EQKRLSNGKL VEEIEQMNSL FQQKQRELVL AVSKVEELTR QLEMLKNGRI 250
    DGHHDNQSAV AELDRLYKEL QLRNKLNQEQ NAKLQQQREC LNKRNSEVAV 300
    MDKRVSELRD RLWKKKAALQ QKENLPVSPD GNLPQQAVSA PSRVAAVGPY 350
    IQSSTMPRMP SRPELLVKPA LPDGSLLMQS AEGPMKIQTL PNMRSGAASQ 400
    SKGSKAHPAS PDWNPSNADL LPSQGSSVPQ SAGTALDQVD DGEIAVREKE 450
    KKVRPFSMFD TVDQCAAPPS FGTLRKNQSS EDILRDAQAV NKNVAKVPPP 500
    VPTKPKQIHL PYFGQTAQSP SDMKPDGNAQ QLPIAATSVG AKLKPAGPQA 550
    RMLLSPGAPS GGQDQVLSPA SKQESPPAAA VRPFTPQPSK DTFPPAFRKP 600
    QTVAASSIYS MYTQQQAPGK NFQQAVQSAL TKTQPRGPHF SSVYGKPVIA 650
    AAQNPQQHPE NIYSCSQGKP GSPEPETETV SSVHESHENE RIPRPLSPTK 700
    LLPFLSNPYR NQSDADLEAL RKKLSNAPRP LKKRSSITEP EGPNGPNIQK 750
    LLYQRTTIAA METISVPSHP SKSPGSVTVN PESSVEIPNP YLHVEPEKEV 800
    GSLVPEPLSP EDMGSASTEN SDVPAPSAGL EYVSEGVTDS STNLQNNVEE 850
    TNPEAPHLLE VYLEEYPPYP PPPYPSGEPE VSEEDSARMR PPEITGQVSL 900
    PPGKRTNLRK TGSERIAHGM RVKFNPLALL LDSSLEGEFD LVQRIIYEVD 950
    DPSLPNDEGI TALHNAVCAG HTEIVKFLVQ FGVNVNAADS DGWTPLHCAA 1000
    SCNNVQVCKF LVESGAAVFA MTYSDMQTAA DKCEEMEEGY TQCSQFLYGV 1050
    QEKMGIMNKG VIYALWDYEP QHDDELLMKE GDCMTVIRRE DEEEIEWWWA 1100
    RLNDKEGYVP RNLLGLYPRI KPRQRSLA 1128
    Length:1,128
    Mass (Da):125,301
    Last modified:January 9, 2007 - v3
    Checksum:iC5FF5D37D73187A0
    GO

    Sequence cautioni

    The sequence BC042874 differs from that shown. Reason: Frameshift at position 23.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti270 – 2701L → V in BAE22185. (PubMed:16141072)Curated
    Sequence conflicti367 – 38216VKPAL…MQSAE → DAWVAHASAHASAHAS in AAH30894. (PubMed:15489334)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqiNP_775554.2. NM_173378.2.
    UniGeneiMm.287450.

    Genome annotation databases

    GeneIDi209456.
    KEGGimmu:209456.
    UCSCiuc007dyd.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    RefSeqi NP_775554.2. NM_173378.2.
    UniGenei Mm.287450.

    3D structure databases

    ProteinModelPortali Q8CG79.
    SMRi Q8CG79. Positions 1-83, 920-1121.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8CG79. 3 interactions.
    MINTi MINT-1753644.
    STRINGi 10090.ENSMUSP00000112508.

    PTM databases

    PhosphoSitei Q8CG79.

    Proteomic databases

    MaxQBi Q8CG79.
    PaxDbi Q8CG79.
    PRIDEi Q8CG79.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 209456.
    KEGGi mmu:209456.
    UCSCi uc007dyd.1. mouse.

    Organism-specific databases

    CTDi 209456.
    MGIi MGI:2138319. Trp53bp2.

    Phylogenomic databases

    eggNOGi NOG283717.
    HOGENOMi HOG000034106.
    HOVERGENi HBG050596.
    InParanoidi Q8CG79.
    KOi K16823.
    PhylomeDBi Q8CG79.

    Miscellaneous databases

    NextBioi 372677.
    PROi Q8CG79.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8CG79.
    Bgeei Q8CG79.
    Genevestigatori Q8CG79.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001452. SH3_domain.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF12796. Ank_2. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    SMARTi SM00248. ANK. 2 hits.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF54236. SSF54236. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 2 hits.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiASPP2_MOUSE
    AccessioniPrimary (citable) accession number: Q8CG79
    Secondary accession number(s): Q3UYM7, Q8K2L5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 15, 2003
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 106 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3