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Q13625

- ASPP2_HUMAN

UniProt

Q13625 - ASPP2_HUMAN

Protein

Apoptosis-stimulating of p53 protein 2

Gene

TP53BP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 2 (15 Aug 2003)
      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 TP53 by enhancing the DNA binding and transactivation function of 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 DDX42.3 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. NF-kappaB binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. SH3/SH2 adaptor activity Source: ProtInc

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. central nervous system development Source: Ensembl
    3. embryo development ending in birth or egg hatching Source: Ensembl
    4. heart development Source: Ensembl
    5. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
    6. negative regulation of cell cycle Source: UniProtKB
    7. positive regulation of signal transduction Source: GOC
    8. response to ionizing radiation Source: Ensembl
    9. signal transduction Source: ProtInc

    Keywords - Biological processi

    Apoptosis, Cell cycle

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Apoptosis-stimulating of p53 protein 2
    Alternative name(s):
    Bcl2-binding protein
    Short name:
    Bbp
    Renal carcinoma antigen NY-REN-51
    Tumor suppressor p53-binding protein 2
    Short name:
    53BP2
    Short name:
    p53-binding protein 2
    Short name:
    p53BP2
    Gene namesi
    Name:TP53BP2
    Synonyms:ASPP2, BBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12000. TP53BP2.

    Subcellular locationi

    Cytoplasmperinuclear region. Nucleus
    Note: Predominantly found in the perinuclear region. Some small fraction is nuclear. Sequester in the cytoplasm on overexpression of DDX42.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1098 – 10981W → K: Loss of interaction with APC2. 1 Publication

    Organism-specific databases

    PharmGKBiPA36681.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11281128Apoptosis-stimulating of p53 protein 2PRO_0000066964Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei480 – 4801Phosphoserine4 Publications
    Modified residuei556 – 5561Phosphoserine2 Publications
    Modified residuei572 – 5721Phosphoserine1 Publication
    Modified residuei698 – 6981PhosphoserineBy similarity
    Modified residuei714 – 7141PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13625.
    PaxDbiQ13625.
    PRIDEiQ13625.

    PTM databases

    PhosphoSiteiQ13625.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocyte. Reduced expression in breast carcinomas expressing a wild-type TP53 protein. Overexpressed in lung cancer cell lines.3 Publications

    Inductioni

    Following DNA damage induced by UV irradiation. Down-regulated by wild-type, but not mutant, p53/TP53.1 Publication

    Gene expression databases

    ArrayExpressiQ13625.
    BgeeiQ13625.
    CleanExiHS_TP53BP2.
    GenevestigatoriQ13625.

    Organism-specific databases

    HPAiHPA021603.

    Interactioni

    Subunit structurei

    Binds to the central domain of 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 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/TP53.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself7EBI-77642,EBI-77642
    APC2O959964EBI-77642,EBI-1053045
    APPP050673EBI-77642,EBI-77613
    BCL2P1041513EBI-77642,EBI-77694
    BCL2L1Q07817-14EBI-77642,EBI-287195
    BCL2L2Q928432EBI-77642,EBI-707714
    EP300Q094722EBI-77642,EBI-447295
    Irs1P355692EBI-287091,EBI-400825From a different organism.
    Irs1P355704EBI-287091,EBI-520230From a different organism.
    PPP1CAP621367EBI-77642,EBI-357253
    PPP1CCP368736EBI-77642,EBI-356283
    RELAQ042066EBI-287091,EBI-73886
    TP53P046372EBI-77642,EBI-366083
    YAP1P469366EBI-287091,EBI-7804091From a different organism.
    YAP1P469379EBI-287091,EBI-1044059

    Protein-protein interaction databases

    BioGridi113012. 37 interactions.
    DIPiDIP-24266N.
    DIP-29587N.
    DIP-426N.
    IntActiQ13625. 55 interactions.
    MINTiMINT-106406.
    STRINGi9606.ENSP00000341957.

    Structurei

    Secondary structure

    1
    1128
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 98
    Beta strandi17 – 226
    Helixi29 – 346
    Beta strandi40 – 423
    Beta strandi44 – 496
    Beta strandi52 – 565
    Helixi62 – 698
    Helixi73 – 753
    Beta strandi77 – 815
    Helixi747 – 76014
    Turni761 – 7644
    Helixi927 – 93610
    Helixi939 – 9457
    Helixi946 – 9483
    Helixi962 – 9698
    Helixi972 – 98110
    Helixi995 – 10017
    Helixi1005 – 10139
    Beta strandi1023 – 10253
    Helixi1029 – 10324
    Beta strandi1035 – 10373
    Helixi1043 – 105311
    Turni1054 – 10574
    Helixi1058 – 10603
    Beta strandi1061 – 10666
    Beta strandi1083 – 10864
    Beta strandi1091 – 10933
    Beta strandi1095 – 11028
    Beta strandi1105 – 11106
    Helixi1111 – 11133
    Beta strandi1114 – 11174

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YCSX-ray2.20B892-1126[»]
    2UWQNMR-A1-83[»]
    4A63X-ray2.27B/D/F/H/J/L892-1128[»]
    4IRVX-ray2.04E/F/G/H726-782[»]
    ProteinModelPortaliQ13625.
    SMRiQ13625. Positions 1-83, 926-1118.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13625.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati958 – 99033ANK 1Add
    BLAST
    Repeati991 – 102333ANK 2Add
    BLAST
    Domaini1057 – 111963SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni332 – 34817Interaction with APPBP1Add
    BLAST
    Regioni876 – 1128253Mediates interaction with APC2Add
    BLAST

    Motif

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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi132 – 17342Gln-richAdd
    BLAST
    Compositional biasi824 – 90279Pro-richAdd
    BLAST

    Domaini

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

    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.
    KOiK16823.
    OMAiYRNQSDA.
    OrthoDBiEOG73FQKX.
    PhylomeDBiQ13625.
    TreeFamiTF105545.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001452. SH3_domain.
    IPR013315. Spectrin_alpha_SH3.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF00023. Ank. 2 hits.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR01887. SPECTRNALPHA.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13625-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MMPMFLTVYL SNNEQHFTEV PVTPETICRD VVDLCKEPGE SDCHLAEVWC     50
    GSERPVADNE RMFDVLQRFG SQRNEVRFFL RHERPPGRDI VSGPRSQDPS 100
    LKRNGVKVPG EYRRKENGVN SPRMDLTLAE LQEMASRQQQ QIEAQQQLLA 150
    TKEQRLKFLK QQDQRQQQQV AEQEKLKRLK EIAENQEAKL KKVRALKGHV 200
    EQKRLSNGKL VEEIEQMNNL FQQKQRELVL AVSKVEELTR QLEMLKNGRI 250
    DSHHDNQSAV AELDRLYKEL QLRNKLNQEQ NAKLQQQREC LNKRNSEVAV 300
    MDKRVNELRD RLWKKKAALQ QKENLPVSSD GNLPQQAASA PSRVAAVGPY 350
    IQSSTMPRMP SRPELLVKPA LPDGSLVIQA SEGPMKIQTL PNMRSGAASQ 400
    TKGSKIHPVG PDWSPSNADL FPSQGSASVP QSTGNALDQV DDGEVPLREK 450
    EKKVRPFSMF DAVDQSNAPP SFGTLRKNQS SEDILRDAQV ANKNVAKVPP 500
    PVPTKPKQIN LPYFGQTNQP PSDIKPDGSS QQLSTVVPSM GTKPKPAGQQ 550
    PRVLLSPSIP SVGQDQTLSP GSKQESPPAA AVRPFTPQPS KDTLLPPFRK 600
    PQTVAASSIY SMYTQQQAPG KNFQQAVQSA LTKTHTRGPH FSSVYGKPVI 650
    AAAQNQQQHP ENIYSNSQGK PGSPEPETEP VSSVQENHEN ERIPRPLSPT 700
    KLLPFLSNPY RNQSDADLEA LRKKLSNAPR PLKKRSSITE PEGPNGPNIQ 750
    KLLYQRTTIA AMETISVPSY PSKSASVTAS SESPVEIQNP YLHVEPEKEV 800
    VSLVPESLSP EDVGNASTEN SDMPAPSPGL DYEPEGVPDN SPNLQNNPEE 850
    PNPEAPHVLD VYLEEYPPYP PPPYPSGEPE GPGEDSVSMR PPEITGQVSL 900
    PPGKRTNLRK TGSERIAHGM RVKFNPLALL LDSSLEGEFD LVQRIIYEVD 950
    DPSLPNDEGI TALHNAVCAG HTEIVKFLVQ FGVNVNAADS DGWTPLHCAA 1000
    SCNNVQVCKF LVESGAAVFA MTYSDMQTAA DKCEEMEEGY TQCSQFLYGV 1050
    QEKMGIMNKG VIYALWDYEP QNDDELPMKE GDCMTIIHRE DEDEIEWWWA 1100
    RLNDKEGYVP RNLLGLYPRI KPRQRSLA 1128
    Length:1,128
    Mass (Da):125,616
    Last modified:August 15, 2003 - v2
    Checksum:iC75D056FBC1DAD75
    GO
    Isoform 2 (identifier: Q13625-2) [UniParc]FASTAAdd to Basket

    Also known as: Bbp

    The sequence of this isoform differs from the canonical sequence as follows:
         1-123: Missing.

    Note: Due to Alu sequence insertion that creates a shorter but existing form that may have an alternative function.

    Show »
    Length:1,005
    Mass (Da):111,431
    Checksum:i3DF4FF49EB589F20
    GO
    Isoform 3 (identifier: Q13625-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MRFGSKM

    Note: No experimental confirmation available.

    Show »
    Length:1,134
    Mass (Da):126,323
    Checksum:i2C7683F88B171926
    GO

    Sequence cautioni

    The sequence AAH46150.2 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH46150.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH58918.2 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 123123Missing in isoform 2. 1 PublicationVSP_008010Add
    BLAST
    Alternative sequencei1 – 11M → MRFGSKM in isoform 3. 1 PublicationVSP_043509

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58334 mRNA. Translation: AAC50557.1.
    AJ318888 mRNA. Translation: CAC83012.1.
    AK294432 mRNA. Translation: BAG57677.1.
    AC096542 Genomic DNA. No translation available.
    BC046150 mRNA. Translation: AAH46150.2. Sequence problems.
    BC058918 mRNA. Translation: AAH58918.2. Different initiation.
    U09582 mRNA. Translation: AAA21597.1.
    CCDSiCCDS1538.1. [Q13625-2]
    CCDS44319.1. [Q13625-3]
    PIRiI38607.
    RefSeqiNP_001026855.2. NM_001031685.2. [Q13625-3]
    NP_005417.1. NM_005426.2. [Q13625-2]
    UniGeneiHs.523968.

    Genome annotation databases

    EnsembliENST00000343537; ENSP00000341957; ENSG00000143514. [Q13625-3]
    ENST00000391878; ENSP00000375750; ENSG00000143514. [Q13625-2]
    GeneIDi7159.
    KEGGihsa:7159.
    UCSCiuc001hod.3. human. [Q13625-1]

    Polymorphism databases

    DMDMi33860140.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58334 mRNA. Translation: AAC50557.1 .
    AJ318888 mRNA. Translation: CAC83012.1 .
    AK294432 mRNA. Translation: BAG57677.1 .
    AC096542 Genomic DNA. No translation available.
    BC046150 mRNA. Translation: AAH46150.2 . Sequence problems.
    BC058918 mRNA. Translation: AAH58918.2 . Different initiation.
    U09582 mRNA. Translation: AAA21597.1 .
    CCDSi CCDS1538.1. [Q13625-2 ]
    CCDS44319.1. [Q13625-3 ]
    PIRi I38607.
    RefSeqi NP_001026855.2. NM_001031685.2. [Q13625-3 ]
    NP_005417.1. NM_005426.2. [Q13625-2 ]
    UniGenei Hs.523968.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YCS X-ray 2.20 B 892-1126 [» ]
    2UWQ NMR - A 1-83 [» ]
    4A63 X-ray 2.27 B/D/F/H/J/L 892-1128 [» ]
    4IRV X-ray 2.04 E/F/G/H 726-782 [» ]
    ProteinModelPortali Q13625.
    SMRi Q13625. Positions 1-83, 926-1118.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113012. 37 interactions.
    DIPi DIP-24266N.
    DIP-29587N.
    DIP-426N.
    IntActi Q13625. 55 interactions.
    MINTi MINT-106406.
    STRINGi 9606.ENSP00000341957.

    PTM databases

    PhosphoSitei Q13625.

    Polymorphism databases

    DMDMi 33860140.

    Proteomic databases

    MaxQBi Q13625.
    PaxDbi Q13625.
    PRIDEi Q13625.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343537 ; ENSP00000341957 ; ENSG00000143514 . [Q13625-3 ]
    ENST00000391878 ; ENSP00000375750 ; ENSG00000143514 . [Q13625-2 ]
    GeneIDi 7159.
    KEGGi hsa:7159.
    UCSCi uc001hod.3. human. [Q13625-1 ]

    Organism-specific databases

    CTDi 7159.
    GeneCardsi GC01M223967.
    HGNCi HGNC:12000. TP53BP2.
    HPAi HPA021603.
    MIMi 602143. gene.
    neXtProti NX_Q13625.
    PharmGKBi PA36681.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG283717.
    HOGENOMi HOG000034106.
    HOVERGENi HBG050596.
    KOi K16823.
    OMAi YRNQSDA.
    OrthoDBi EOG73FQKX.
    PhylomeDBi Q13625.
    TreeFami TF105545.

    Miscellaneous databases

    ChiTaRSi TP53BP2. human.
    EvolutionaryTracei Q13625.
    GeneWikii TP53BP2.
    GenomeRNAii 7159.
    NextBioi 28014.
    PROi Q13625.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13625.
    Bgeei Q13625.
    CleanExi HS_TP53BP2.
    Genevestigatori Q13625.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR001452. SH3_domain.
    IPR013315. Spectrin_alpha_SH3.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF00023. Ank. 2 hits.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR01887. SPECTRNALPHA.
    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. "The p53-binding protein 53BP2 also interacts with Bcl2 and impedes cell cycle progression at G2/M."
      Naumovski L., Cleary M.L.
      Mol. Cell. Biol. 16:3884-3892(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH BCL2.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TP53.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Amygdala.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Testis and Uterus.
    6. "Two cellular proteins that bind to wild-type but not mutant p53."
      Iwabuchi K., Bartel P.L., Li B., Marraccino R., Fields S.
      Proc. Natl. Acad. Sci. U.S.A. 91:6098-6102(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 600-1128, INTERACTION WITH TP53.
    7. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    8. "NF-kappaB subunit p65 binds to 53BP2 and inhibits cell death induced by 53BP2."
      Yang J.-P., Hori M., Takahashi N., Kawabe T., Kato H., Okamoto T.
      Oncogene 18:5177-5186(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INTERACTION WITH RELA.
    9. "APCL, a central nervous system-specific homologue of adenomatous polyposis coli tumor suppressor, binds to p53-binding protein 2 and translocates it to the perinucleus."
      Nakagawa H., Koyama K., Murata Y., Morito M., Akiyama T., Nakamura Y.
      Cancer Res. 60:101-105(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APC2, MUTAGENESIS OF TRP-1098, SUBCELLULAR LOCATION.
    10. "Proapoptotic p53-interacting protein 53BP2 is induced by UV irradiation but suppressed by p53."
      Lopez C.D., Ao Y., Rohde L.H., Perez T.D., O'Connor D.J., Lu X., Ford J.M., Naumovski L.
      Mol. Cell. Biol. 20:8018-8025(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    11. "Aberrant overexpression of 53BP2 mRNA in lung cancer cell lines."
      Mori T., Okamoto H., Takahashi N., Ueda R., Okamoto T.
      FEBS Lett. 465:124-128(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    12. "ASPP2 inhibits APP-BP1-mediated NEDD8 conjugation to cullin-1 and decreases APP-BP1-induced cell proliferation and neuronal apoptosis."
      Chen Y., Liu W., Naumovski L., Neve R.L.
      J. Neurochem. 85:801-809(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH APPBP1.
    13. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480 AND SER-556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "The DEAD box protein Ddx42p modulates the function of ASPP2, a stimulator of apoptosis."
      Uhlmann-Schiffler H., Kiermayer S., Stahl H.
      Oncogene 28:2065-2073(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DDX42, SUBCELLULAR LOCATION.
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480; SER-556 AND SER-572, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2."
      Gorina S., Pavletich N.P.
      Science 274:1001-1005(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 892-1128.
    22. "Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a ubiquitin-like fold."
      Tidow H., Andreeva A., Rutherford T.J., Fersht A.R.
      J. Mol. Biol. 371:948-958(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-83.

    Entry informationi

    Entry nameiASPP2_HUMAN
    AccessioniPrimary (citable) accession number: Q13625
    Secondary accession number(s): B4DG66
    , Q12892, Q86X75, Q96KQ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: August 15, 2003
    Last modified: October 1, 2014
    This is version 155 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3