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Q9JJP2

- P73_MOUSE

UniProt

Q9JJP2 - P73_MOUSE

Protein

Tumor protein p73

Gene

Tp73

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein.By similarity2 Publications

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi186 – 1861ZincBy similarity
    Metal bindingi189 – 1891ZincBy similarity
    Metal bindingi250 – 2501ZincBy similarity
    Metal bindingi254 – 2541ZincBy similarity

    GO - Molecular functioni

    1. chromatin binding Source: RefGenome
    2. damaged DNA binding Source: RefGenome
    3. DNA binding Source: MGI
    4. double-stranded DNA binding Source: RefGenome
    5. metal ion binding Source: UniProtKB-KW
    6. p53 binding Source: MGI
    7. protein binding Source: IntAct
    8. sequence-specific DNA binding Source: RefGenome
    9. sequence-specific DNA binding transcription factor activity Source: MGI
    10. transcription regulatory region DNA binding Source: InterPro

    GO - Biological processi

    1. cell cycle arrest Source: MGI
    2. cellular response to DNA damage stimulus Source: MGI
    3. cellular response to UV Source: RefGenome
    4. cerebrospinal fluid secretion Source: MGI
    5. digestive tract morphogenesis Source: MGI
    6. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: RefGenome
    7. forebrain development Source: MGI
    8. hippocampus development Source: MGI
    9. inflammatory response Source: MGI
    10. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
    11. mitotic G1 DNA damage checkpoint Source: RefGenome
    12. negative regulation of JUN kinase activity Source: MGI
    13. negative regulation of neuron apoptotic process Source: MGI
    14. negative regulation of transcription from RNA polymerase II promoter Source: RefGenome
    15. neuron development Source: MGI
    16. positive regulation of apoptotic signaling pathway Source: MGI
    17. positive regulation of cell size Source: MGI
    18. positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
    19. positive regulation of transcription, DNA-templated Source: MGI
    20. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    21. post-embryonic development Source: MGI
    22. protein tetramerization Source: InterPro
    23. regulation of neuron apoptotic process Source: MGI
    24. release of cytochrome c from mitochondria Source: MGI
    25. response to gamma radiation Source: RefGenome
    26. response to X-ray Source: RefGenome
    27. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Apoptosis, Cell cycle, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor protein p73By similarity
    Alternative name(s):
    p53-like transcription factorBy similarity
    p53-related proteinBy similarity
    Gene namesi
    Name:Tp73
    Synonyms:P73Imported, Trp73Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1336991. Trp73.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm By similarity
    Note: Accumulates in the nucleus in response to DNA damage.1 Publication

    GO - Cellular componenti

    1. chromatin Source: RefGenome
    2. cytosol Source: RefGenome
    3. nucleus Source: MGI
    4. transcription factor complex Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice lacking Tp73 display a runting phenotype and high rates of mortality due to massive gastrointestinal hemorrhages or intracranial bleeding. The gastrointestinal tract suffers loss of enterocytes and excessive mucosecretions in the duodenum, ileum and cecum. Survivors exhibit hippocampal dysgenesis, hydrocephalus, chronic infections and inflammation, as well as abnormalities in pheromone sensory pathways.1 Publication

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 631631Tumor protein p73PRO_0000370211Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241Phosphothreonine; by PLK1By similarity
    Modified residuei25 – 251Phosphotyrosine; by SRC and HCKBy similarity
    Modified residuei91 – 911Phosphotyrosine; by ABL1By similarity
    Cross-linki622 – 622Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    Sumoylated on Lys-622, which potentiates proteasomal degradation but does not affect transcriptional activity.By similarity
    Phosphorylation by PLK1 and PLK3 inhibits the transcription regulator activity and pro-apoptotic function By similarity. Higher levels of phosphorylation seen in striatal neurons of. mutant huntingtin (htt) transgenic mice.By similarity1 Publication
    Polyubiquitinated by RCHY1/PIRH2; leading to its degradation by the proteasome.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ9JJP2.

    PTM databases

    PhosphoSiteiQ9JJP2.

    Expressioni

    Tissue specificityi

    Found in striatal neurons of mutant huntingtin (htt) transgenic mice (at protein level). Isoform 1 is expressed in the nasal epithelium, the vomeronasal organ, the hippocampus and the hypothalamus.2 Publications

    Gene expression databases

    ArrayExpressiQ9JJP2.
    BgeeiQ9JJP2.
    GenevestigatoriQ9JJP2.

    Interactioni

    Subunit structurei

    Found in a complex with p53/TP53 and CABLES1. The C-terminal oligomerization domain binds to the ABL1 tyrosine kinase SH3 domain. Interacts with HECW2, HIPK2, RANBP9 and WWOX By similarity. Interacts (via SAM domain) with FBXO45 (via B30.2/SPRY domain) By similarity. Interacts with YAP1 (phosphorylated form) By similarity. Interacts with HCK (via SH3 domain); this inhibits TP73 activity and degradation By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Yap1P469382EBI-1770138,EBI-1211949

    Protein-protein interaction databases

    BioGridi204326. 5 interactions.
    DIPiDIP-41942N.
    IntActiQ9JJP2. 2 interactions.
    MINTiMINT-3388880.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JJP2.
    SMRiQ9JJP2. Positions 107-381, 486-542.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini479 – 54567SAMSequence AnalysisAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 4343TransactivationBy similarityAdd
    BLAST
    Regioni123 – 302180DNA-bindingBy similarityAdd
    BLAST
    Regioni337 – 37842OligomerizationSequence AnalysisAdd
    BLAST
    Regioni337 – 37236Interaction with HIPK2By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi477 – 4815WW-bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi5 – 106Poly-SerSequence Analysis
    Compositional biasi383 – 3886Poly-GlnSequence Analysis

    Domaini

    Possesses an acidic transactivation domain, a central DNA binding domain and a C-terminal oligomerization domain that binds to the ABL1 tyrosine kinase SH3 domain.By similarity
    The WW-binding motif mediates interaction with WWOX.By similarity

    Sequence similaritiesi

    Belongs to the p53 family.By similarity
    Contains 1 SAM (sterile alpha motif) domain.Sequence Analysis

    Phylogenomic databases

    eggNOGiNOG80479.
    GeneTreeiENSGT00390000015092.
    InParanoidiB1AX90.
    KOiK10148.
    OrthoDBiEOG7JQBNW.
    PhylomeDBiQ9JJP2.
    TreeFamiTF106101.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    2.60.40.720. 1 hit.
    4.10.170.10. 1 hit.
    InterProiIPR008967. p53-like_TF_DNA-bd.
    IPR012346. p53/RUNT-type_TF_DNA-bd.
    IPR011615. p53_DNA-bd.
    IPR010991. p53_tetrameristn.
    IPR002117. p53_tumour_suppressor.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    [Graphical view]
    PANTHERiPTHR11447. PTHR11447. 1 hit.
    PfamiPF00870. P53. 1 hit.
    PF07710. P53_tetramer. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view]
    PRINTSiPR00386. P53SUPPRESSR.
    SMARTiSM00454. SAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF47719. SSF47719. 1 hit.
    SSF47769. SSF47769. 1 hit.
    SSF49417. SSF49417. 1 hit.
    PROSITEiPS00348. P53. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 11 Publication (identifier: Q9JJP2-1) [UniParc]FASTAAdd to Basket

    Also known as: AlphaBy similarity

    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

    MAQTSSSSSS TFEHLWSSLE PDSTYFDLPQ PSQGTSEASG SEESNMDVFH    50
    LQGMAQFNLL SSAMDQMGSR AAPASPYTPE HAASAPTHSP YAQPSSTFDT 100
    MSPAPVIPSN TDYPGPHHFE VTFQQSSTAK SATWTYSPLL KKLYCQIAKT 150
    CPIQIKVSTP PPPGTAIRAM PVYKKAEHVT DIVKRCPNHE LGRDFNEGQS 200
    APASHLIRVE GNNLAQYVDD PVTGRQSVVV PYEPPQVGTE FTTILYNFMC 250
    NSSCVGGMNR RPILVIITLE TRDGQVLGRR SFEGRICACP GRDRKADEDH 300
    YREQQALNES TTKNGAASKR AFKQSPPAIP ALGTNVKKRR HGDEDMFYMH 350
    VRGRENFEIL MKVKESLELM ELVPQPLVDS YRQQQQQQLL QRPSHLQPPS 400
    YGPVLSPMNK VHGGVNKLPS VNQLVGQPPP HSSAAGPNLG PMGSGMLNSH 450
    GHSMPANGEM NGGHSSQTMV SGSHCTPPPP YHADPSLVSF LTGLGCPNCI 500
    ECFTSQGLQS IYHLQNLTIE DLGALKVPDQ YRMTIWRGLQ DLKQSHDCGQ 550
    QLLRSSSNAA TISIGGSGEL QRQRVMEAVH FRVRHTITIP NRGGAGAVTG 600
    PDEWADFGFD LPDCKSRKQP IKEEFTETES H 631
    Length:631
    Mass (Da):69,096
    Last modified:October 1, 2000 - v1
    Checksum:iE364D566A90CBF1D
    GO
    Isoform 22 Publications (identifier: Q9JJP2-2) [UniParc]FASTAAdd to Basket

    Also known as: dN-AlphaBy similarity

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: MAQTSSSSSSTFEHLWSSLEPDSTYFDLPQPSQGTSEASGSEESNMDVFHLQGM → MLYVGDPMRHLAT

    Note: Produced by alternative promoter usage.1 Publication

    Curated

    Show »
    Length:590
    Mass (Da):64,725
    Checksum:i8580C7EFA21B5797
    GO
    Isoform 3 (identifier: Q9JJP2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: MAQTSSSSSSTFEHLWSSLEPDSTYFDLPQPSQGTSEASGSEESNMDVFHLQGM → MLYVGDPMRHLAT
         489-493: SFLTG → RTLGL
         494-631: Missing.

    Note: Produced by alternative splicing of isoform 2. No experimental confirmation available.1 Publication

    Curated

    Show »
    Length:452
    Mass (Da):49,392
    Checksum:i13C8757F5A4A5FFC
    GO
    Isoform 41 Publication (identifier: Q9JJP2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: MAQTSSSSSSTFEHLWSSLEPDSTYFDLPQPSQGTSEASGSEESNMDVFHLQGM → MLYVGDPMRHLAT
         394-489: Missing.

    Note: Produced by alternative splicing of isoform 2. No experimental confirmation available.1 Publication

    Curated

    Show »
    Length:494
    Mass (Da):55,025
    Checksum:iFA7D89986822E491
    GO

    Sequence cautioni

    The sequence CAM18775.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti118 – 1181H → D in BAB30732. (PubMed:16141072)Curated
    Sequence conflicti127 – 1271S → G in BAE24089. (PubMed:16141072)Curated
    Sequence conflicti254 – 2541C → S in AAD32213. (PubMed:15489334)Curated
    Sequence conflicti352 – 3532RG → SAS in AAD32213. (PubMed:15489334)Curated
    Sequence conflicti376 – 3761P → H in AAD32213. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5454MAQTS…HLQGM → MLYVGDPMRHLAT in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_053081Add
    BLAST
    Alternative sequencei394 – 48996Missing in isoform 4. 1 PublicationVSP_053082Add
    BLAST
    Alternative sequencei489 – 4935SFLTG → RTLGL in isoform 3. CuratedVSP_053083
    Alternative sequencei494 – 631138Missing in isoform 3. CuratedVSP_053084Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y19234 mRNA. Translation: CAB81953.1.
    Y19235 mRNA. Translation: CAB81954.1.
    AK017412 mRNA. Translation: BAB30732.1.
    AK139633 mRNA. Translation: BAE24089.1.
    AL806525 Genomic DNA. Translation: CAM18773.1.
    AL806525 Genomic DNA. Translation: CAM18774.1.
    AL806525 Genomic DNA. Translation: CAM18775.1. Different initiation.
    CH466594 Genomic DNA. Translation: EDL14957.1.
    BC066045 mRNA. Translation: AAH66045.1.
    AF138873 Genomic DNA. Translation: AAD32213.1.
    CCDSiCCDS51396.1. [Q9JJP2-4]
    CCDS51397.1. [Q9JJP2-2]
    RefSeqiNP_001119802.1. NM_001126330.1. [Q9JJP2-2]
    NP_001119803.1. NM_001126331.1. [Q9JJP2-4]
    NP_035772.2. NM_011642.3.
    UniGeneiMm.78015.

    Genome annotation databases

    EnsembliENSMUST00000097762; ENSMUSP00000095368; ENSMUSG00000029026. [Q9JJP2-4]
    ENSMUST00000105643; ENSMUSP00000101268; ENSMUSG00000029026. [Q9JJP2-3]
    ENSMUST00000133533; ENSMUSP00000114418; ENSMUSG00000029026. [Q9JJP2-2]
    GeneIDi22062.
    KEGGimmu:22062.
    UCSCiuc008wbg.2. mouse. [Q9JJP2-2]
    uc008wbh.2. mouse. [Q9JJP2-1]
    uc012dqi.1. mouse. [Q9JJP2-4]

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y19234 mRNA. Translation: CAB81953.1 .
    Y19235 mRNA. Translation: CAB81954.1 .
    AK017412 mRNA. Translation: BAB30732.1 .
    AK139633 mRNA. Translation: BAE24089.1 .
    AL806525 Genomic DNA. Translation: CAM18773.1 .
    AL806525 Genomic DNA. Translation: CAM18774.1 .
    AL806525 Genomic DNA. Translation: CAM18775.1 . Different initiation.
    CH466594 Genomic DNA. Translation: EDL14957.1 .
    BC066045 mRNA. Translation: AAH66045.1 .
    AF138873 Genomic DNA. Translation: AAD32213.1 .
    CCDSi CCDS51396.1. [Q9JJP2-4 ]
    CCDS51397.1. [Q9JJP2-2 ]
    RefSeqi NP_001119802.1. NM_001126330.1. [Q9JJP2-2 ]
    NP_001119803.1. NM_001126331.1. [Q9JJP2-4 ]
    NP_035772.2. NM_011642.3.
    UniGenei Mm.78015.

    3D structure databases

    ProteinModelPortali Q9JJP2.
    SMRi Q9JJP2. Positions 107-381, 486-542.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204326. 5 interactions.
    DIPi DIP-41942N.
    IntActi Q9JJP2. 2 interactions.
    MINTi MINT-3388880.

    PTM databases

    PhosphoSitei Q9JJP2.

    Proteomic databases

    PRIDEi Q9JJP2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000097762 ; ENSMUSP00000095368 ; ENSMUSG00000029026 . [Q9JJP2-4 ]
    ENSMUST00000105643 ; ENSMUSP00000101268 ; ENSMUSG00000029026 . [Q9JJP2-3 ]
    ENSMUST00000133533 ; ENSMUSP00000114418 ; ENSMUSG00000029026 . [Q9JJP2-2 ]
    GeneIDi 22062.
    KEGGi mmu:22062.
    UCSCi uc008wbg.2. mouse. [Q9JJP2-2 ]
    uc008wbh.2. mouse. [Q9JJP2-1 ]
    uc012dqi.1. mouse. [Q9JJP2-4 ]

    Organism-specific databases

    CTDi 22062.
    MGIi MGI:1336991. Trp73.

    Phylogenomic databases

    eggNOGi NOG80479.
    GeneTreei ENSGT00390000015092.
    InParanoidi B1AX90.
    KOi K10148.
    OrthoDBi EOG7JQBNW.
    PhylomeDBi Q9JJP2.
    TreeFami TF106101.

    Miscellaneous databases

    NextBioi 301868.
    PROi Q9JJP2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JJP2.
    Bgeei Q9JJP2.
    Genevestigatori Q9JJP2.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    2.60.40.720. 1 hit.
    4.10.170.10. 1 hit.
    InterProi IPR008967. p53-like_TF_DNA-bd.
    IPR012346. p53/RUNT-type_TF_DNA-bd.
    IPR011615. p53_DNA-bd.
    IPR010991. p53_tetrameristn.
    IPR002117. p53_tumour_suppressor.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    [Graphical view ]
    PANTHERi PTHR11447. PTHR11447. 1 hit.
    Pfami PF00870. P53. 1 hit.
    PF07710. P53_tetramer. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00386. P53SUPPRESSR.
    SMARTi SM00454. SAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47719. SSF47719. 1 hit.
    SSF47769. SSF47769. 1 hit.
    SSF49417. SSF49417. 1 hit.
    PROSITEi PS00348. P53. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "p73-deficient mice have neurological, pheromonal and inflammatory defects but lack spontaneous tumours."
      Yang A., Walker N., Bronson R., Kaghad M., Oosterwegel M., Bonnin J., Vagner C., Bonnet H., Dikkes P., Sharpe A., McKeon F., Caput D.
      Nature 404:99-103(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    2. "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] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-631 (ISOFORM 1/2).
      Strain: C57BL/6JImported.
      Tissue: EggImported and HeadImported.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      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 2).
      Strain: C57BL/6Imported.
      Tissue: Fetal brainImported.
    6. "Mouse p73 gene maps to the distal part of chromosome 4 and might be involved in the progression of gamma-radiation-induced T-cell lymphomas."
      Herranz M., Santos J., Salido E., Fernandez-Piqueras J., Serrano M.
      Cancer Res. 59:2068-2071(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 136-631 (ISOFORMS 1/2), FUNCTION.
      Strain: 129/SvImported.
    7. "p63 and p73 are required for p53-dependent apoptosis in response to DNA damage."
      Flores E.R., Tsai K.Y., Crowley D., Sengupta S., Yang A., McKeon F., Jacks T.
      Nature 416:560-564(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "p73alpha is a candidate effector in the p53 independent apoptosis pathway of cisplatin damaged primary murine colonocytes."
      Oniscu A., Sphyris N., Morris R.G., Bader S., Harrison D.J.
      J. Clin. Pathol. 57:492-498(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Transcriptional repression induces a slowly progressive atypical neuronal death associated with changes of YAP isoforms and p73."
      Hoshino M., Qi M.-L., Yoshimura N., Tagawa K., Wada Y.-I., Enokido Y., Marubuchi S., Harjes P., Arai N., Oyanagi K., Blandino G., Sudol M., Rich T., Kanazawa I., Wanker E.E., Saitoe M., Okazawa H.
      J. Cell Biol. 172:589-604(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiP73_MOUSE
    AccessioniPrimary (citable) accession number: Q9JJP2
    Secondary accession number(s): B1AX89
    , B1AX90, Q3UT91, Q9CU77, Q9JJP1, Q9WUJ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Activated and stabilized by interaction with RANBP9.By similarity

    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