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Q8CG79

- ASPP2_MOUSE

UniProt

Q8CG79 - ASPP2_MOUSE

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Protein

Apoptosis-stimulating of p53 protein 2

Gene
Tp53bp2, Aspp2, Trp53bp2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

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
Complete GO annotation...

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 By similarity. 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
Complete GO annotation...

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 – 4791Phosphoserine By similarity
Modified residuei555 – 5551Phosphoserine By similarity
Modified residuei571 – 5711Phosphoserine By 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.

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati958 – 98730ANK 1Add
BLAST
Repeati991 – 102030ANK 2Add
BLAST
Domaini1057 – 111963SH3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni332 – 34817Interaction with APPBP1 By similarityAdd
BLAST
Regioni876 – 1128253Mediates interaction with APC2 By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi866 – 87510SH3-binding Reviewed prediction

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.
Contains 2 ANK repeats.
Contains 1 SH3 domain.

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti270 – 2701L → V in BAE22185. 1 Publication
Sequence conflicti367 – 38216VKPAL…MQSAE → DAWVAHASAHASAHAS in AAH30894. 1 PublicationAdd
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: September 3, 2014
This is version 105 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

Similar proteinsi