Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O15350

- P73_HUMAN

UniProt

O15350 - P73_HUMAN

Protein

Tumor protein p73

Gene

TP73

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.3 Publications

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi194 – 1941ZincBy similarity
    Metal bindingi197 – 1971ZincBy similarity
    Metal bindingi258 – 2581ZincBy similarity
    Metal bindingi262 – 2621ZincBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. activation of MAPK activity Source: Ensembl
    2. cell cycle arrest Source: Ensembl
    3. cellular response to DNA damage stimulus Source: UniProtKB
    4. cellular response to UV Source: RefGenome
    5. cerebrospinal fluid secretion Source: Ensembl
    6. digestive tract morphogenesis Source: Ensembl
    7. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: RefGenome
    8. hippocampus development Source: Ensembl
    9. inflammatory response Source: Ensembl
    10. intrinsic apoptotic signaling pathway in response to DNA damage Source: ProtInc
    11. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
    12. kidney development Source: Ensembl
    13. mismatch repair Source: ProtInc
    14. mitotic G1 DNA damage checkpoint Source: RefGenome
    15. negative regulation of JUN kinase activity Source: RefGenome
    16. negative regulation of neuron apoptotic process Source: RefGenome
    17. negative regulation of neuron differentiation Source: Ensembl
    18. negative regulation of transcription from RNA polymerase II promoter Source: RefGenome
    19. neuron development Source: Ensembl
    20. positive regulation of apoptotic process Source: Ensembl
    21. positive regulation of cell size Source: Ensembl
    22. positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: Ensembl
    23. positive regulation of oligodendrocyte differentiation Source: Ensembl
    24. positive regulation of transcription, DNA-templated Source: UniProtKB
    25. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    26. post-embryonic development Source: Ensembl
    27. protein tetramerization Source: InterPro
    28. release of cytochrome c from mitochondria Source: Ensembl
    29. response to gamma radiation Source: RefGenome
    30. response to organonitrogen compound Source: Ensembl
    31. response to X-ray Source: RefGenome
    32. 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

    Enzyme and pathway databases

    SignaLinkiO15350.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tumor protein p73
    Alternative name(s):
    p53-like transcription factor
    p53-related protein
    Gene namesi
    Name:TP73
    Synonyms:P73
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12003. TP73.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Accumulates in the nucleus in response to DNA damage.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi27 – 271T → A: Impaired phosphorylation. 1 Publication
    Mutagenesisi99 – 991Y → F: Impaired phosphorylation of isoform beta by ABL1. 1 Publication
    Mutagenesisi487 – 4871Y → A: Loss of interaction with WWOX. 1 Publication
    Mutagenesisi627 – 6271K → R: Strongly diminishes sumoylation but does not affect transcriptional activity. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA36684.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 636636Tumor protein p73PRO_0000185728Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271Phosphothreonine; by PLK12 Publications
    Modified residuei28 – 281Phosphotyrosine; by SRC and HCK1 Publication
    Modified residuei99 – 991Phosphotyrosine; by ABL11 Publication
    Cross-linki627 – 627Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); in isoform Alpha

    Post-translational modificationi

    Isoform alpha (but not isoform beta) is sumoylated on Lys-627, which potentiates proteasomal degradation but does not affect transcriptional activity. Phosphorylation by PLK1 and PLK3 inhibits the transcription regulator activity and pro-apoptotic function.1 Publication
    Higher levels of phosphorylation seen in the brain from patients with Huntington disease.
    Polyubiquitinated by RCHY1/PIRH2; leading to its degradation by the proteasome.2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO15350.
    PaxDbiO15350.
    PRIDEiO15350.

    PTM databases

    PhosphoSiteiO15350.

    Miscellaneous databases

    PMAP-CutDBO15350.

    Expressioni

    Tissue specificityi

    Expressed in striatal neurons of patients with Huntington disease (at protein level). Brain, kidney, placenta, colon, heart, liver, spleen, skeletal muscle, prostate, thymus and pancreas. Highly expressed in fetal tissue.2 Publications

    Inductioni

    Not induced by DNA damage. Isoforms lacking the transactivation domain block gene induction.1 Publication

    Gene expression databases

    ArrayExpressiO15350.
    BgeeiO15350.
    GenevestigatoriO15350.

    Organism-specific databases

    HPAiCAB002514.
    CAB003022.

    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. Isoform Beta interacts homotypically and with p53/TP53, whereas isoform Alpha does not. Isoform Gamma interacts homotypically and with all p73 isoforms. Isoform Delta interacts with isoform Gamma, isoform Alpha, and homotypically. Isoforms Alpha and Beta interact with HIPK2. Isoform Alpha interacts with RANBP9. Isoform Beta interacts with WWOX. Interacts (via SAM domain) with FBXO45 (via B30.2/SPRY domain). Interacts with YAP1 (phosphorylated form). Interacts with HCK (via SH3 domain); this inhibits TP73 activity and degradation.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-389606,EBI-389606
    AURKAO1496511EBI-389606,EBI-448680
    Cables1Q9ESJ13EBI-389606,EBI-604411From a different organism.
    CASP8AP2Q9UKL32EBI-389619,EBI-2339650
    E6P031262EBI-389619,EBI-1177242From a different organism.
    HSPA9P3864611EBI-389606,EBI-354932
    ITCHQ96J025EBI-389619,EBI-1564678
    SIRT1Q96EB64EBI-389606,EBI-1802965
    YAP1P469377EBI-389619,EBI-1044059

    Protein-protein interaction databases

    BioGridi113014. 99 interactions.
    DIPiDIP-24202N.
    IntActiO15350. 18 interactions.
    MINTiMINT-97729.

    Structurei

    Secondary structure

    1
    636
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni123 – 1264
    Beta strandi128 – 1303
    Beta strandi136 – 1383
    Beta strandi141 – 1455
    Turni146 – 1494
    Beta strandi150 – 1534
    Beta strandi157 – 1648
    Beta strandi174 – 1818
    Turni184 – 1885
    Helixi195 – 1995
    Turni202 – 2065
    Beta strandi214 – 2196
    Beta strandi224 – 2274
    Turni229 – 2313
    Beta strandi234 – 2396
    Beta strandi250 – 2567
    Helixi260 – 2623
    Turni263 – 2686
    Beta strandi271 – 2788
    Beta strandi280 – 2823
    Beta strandi284 – 29411
    Helixi298 – 31114
    Beta strandi354 – 3607
    Helixi362 – 37716
    Helixi378 – 3803
    Helixi383 – 39513
    Helixi493 – 4997
    Turni503 – 5053
    Helixi506 – 5105
    Turni511 – 5133
    Helixi517 – 5215
    Helixi525 – 5306
    Turni535 – 5373
    Helixi538 – 54710

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1COKNMR-A487-554[»]
    1DXSX-ray2.54A487-564[»]
    2KBYNMR-A/B/C/D351-398[»]
    2WQIX-ray1.70A/B/C/D351-399[»]
    2WQJX-ray2.001/2/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z351-383[»]
    2WTTX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P351-399[»]
    2XWCX-ray1.82A112-311[»]
    3VD0X-ray2.95A/B/C/D/I/J/K/L115-312[»]
    3VD1X-ray2.95A/B/C/D/I/J/K/L115-312[»]
    3VD2X-ray4.00A/B/C/D/I/J115-312[»]
    4A63X-ray2.27A/C/E/G/I/K112-311[»]
    4G82X-ray3.10A/B115-312[»]
    4G83X-ray4.00A/B115-312[»]
    4GUOX-ray3.19A/B/C/D/I/J/K/L115-312[»]
    4GUQX-ray3.70A/B115-312[»]
    DisProtiDP00319.
    ProteinModelPortaliO15350.
    SMRiO15350. Positions 115-396, 487-554.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15350.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini485 – 55167SAMAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 4646TransactivationBy similarityAdd
    BLAST
    Regioni131 – 310180DNA-bindingSequence AnalysisAdd
    BLAST
    Regioni345 – 38642OligomerizationSequence AnalysisAdd
    BLAST
    Regioni345 – 38036Interaction with HIPK2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi483 – 4875WW-binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1 – 5555Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi168 – 1714Poly-Pro
    Compositional biasi391 – 3944Poly-Gln
    Compositional biasi483 – 4864Poly-Pro

    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.1 Publication
    The WW-binding motif mediates interaction with WWOX.1 Publication

    Sequence similaritiesi

    Belongs to the p53 family.Curated

    Phylogenomic databases

    eggNOGiNOG80479.
    HOVERGENiHBG005201.
    InParanoidiO15350.
    KOiK10148.
    OMAiNEGQSAP.
    OrthoDBiEOG7JQBNW.
    PhylomeDBiO15350.
    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 (12)i

    Sequence statusi: Complete.

    This entry describes 12 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform Alpha (identifier: O15350-1) [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

    MAQSTATSPD GGTTFEHLWS SLEPDSTYFD LPQSSRGNNE VVGGTDSSMD    50
    VFHLEGMTTS VMAQFNLLSS TMDQMSSRAA SASPYTPEHA ASVPTHSPYA 100
    QPSSTFDTMS PAPVIPSNTD YPGPHHFEVT FQQSSTAKSA TWTYSPLLKK 150
    LYCQIAKTCP IQIKVSTPPP PGTAIRAMPV YKKAEHVTDV VKRCPNHELG 200
    RDFNEGQSAP ASHLIRVEGN NLSQYVDDPV TGRQSVVVPY EPPQVGTEFT 250
    TILYNFMCNS SCVGGMNRRP ILIIITLEMR DGQVLGRRSF EGRICACPGR 300
    DRKADEDHYR EQQALNESSA KNGAASKRAF KQSPPAVPAL GAGVKKRRHG 350
    DEDTYYLQVR GRENFEILMK LKESLELMEL VPQPLVDSYR QQQQLLQRPS 400
    HLQPPSYGPV LSPMNKVHGG MNKLPSVNQL VGQPPPHSSA ATPNLGPVGP 450
    GMLNNHGHAV PANGEMSSSH SAQSMVSGSH CTPPPPYHAD PSLVSFLTGL 500
    GCPNCIEYFT SQGLQSIYHL QNLTIEDLGA LKIPEQYRMT IWRGLQDLKQ 550
    GHDYSTAQQL LRSSNAATIS IGGSGELQRQ RVMEAVHFRV RHTITIPNRG 600
    GPGGGPDEWA DFGFDLPDCK ARKQPIKEEF TEAEIH 636
    Length:636
    Mass (Da):69,623
    Last modified:January 1, 1998 - v1
    Checksum:iA467493C5D93EEE0
    GO
    Isoform Beta (identifier: O15350-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         495-636: SFLTGLGCPN...KEEFTEAEIH → RTWGP

    Note: Produced by alternative splicing of isoform Alpha.

    Show »
    Length:499
    Mass (Da):54,322
    Checksum:i0FDC0546E29D683E
    GO
    Isoform Gamma (identifier: O15350-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         400-476: SHLQPPSYGP...SSSHSAQSMV → PRDAQQPWPR...EHLPPAEPDH
         477-636: Missing.

    Note: Produced by alternative splicing of isoform Alpha. The splicing of exon 11 results in a frameshift from the original reading frame.

    Show »
    Length:476
    Mass (Da):53,026
    Checksum:i78D99E725DCEFD5F
    GO
    Isoform Delta (identifier: O15350-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         400-403: SHLQ → TWGP
         404-636: Missing.

    Note: Produced by alternative splicing of isoform Alpha.

    Show »
    Length:403
    Mass (Da):44,517
    Checksum:i72F1A3518940D832
    GO
    Isoform Epsilon (identifier: O15350-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         400-445: SHLQPPSYGP...PHSSAATPNL → PRDAQQPWPR...TPLPRRPQPR
         446-526: Missing.

    Note: Produced by alternative splicing of isoform Alpha. The splicing of exon 11 results in a frameshift from the original reading frame. The splicing of exon 13 reverts the reading frame to the sequence of isoform Alpha.

    Show »
    Length:555
    Mass (Da):61,694
    Checksum:i4C821E6FB836EC32
    GO
    Isoform Zeta (identifier: O15350-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         400-495: Missing.

    Note: Produced by alternative splicing of isoform Alpha.

    Show »
    Length:540
    Mass (Da):59,887
    Checksum:iA996F9FEB731ABD1
    GO
    Isoform dN-Alpha (identifier: O15350-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-62: MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVM → MLYVGDPARHLAT

    Note: Produced by alternative promoter usage.

    Show »
    Length:587
    Mass (Da):64,422
    Checksum:iE8F1CAE88CED4EBC
    GO
    Isoform dN-Beta (identifier: O15350-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-62: MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVM → MLYVGDPARHLAT
         495-636: SFLTGLGCPN...KEEFTEAEIH → RTWGP

    Note: Produced by alternative splicing of isoform dN-Alpha.

    Show »
    Length:450
    Mass (Da):49,121
    Checksum:iF1950AE8628B3863
    GO
    Isoform dN-Gamma (identifier: O15350-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-62: MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVM → MLYVGDPARHLAT
         400-476: SHLQPPSYGP...SSSHSAQSMV → PRDAQQPWPR...EHLPPAEPDH
         477-636: Missing.

    Note: Produced by alternative splicing of isoform dN-Alpha.

    Show »
    Length:427
    Mass (Da):47,824
    Checksum:i9D140E5D48BFB56E
    GO
    Isoform 10 (identifier: O15350-11) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-71: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:565
    Mass (Da):62,034
    Checksum:i3D989435C093E515
    GO
    Isoform 11 (identifier: O15350-12) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-62: MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVM → MLYVGDPARHLAT
         400-636: Missing.

    Show »
    Length:350
    Mass (Da):38,874
    Checksum:i4BA732383EFE92A0
    GO
    Isoform 12 (identifier: O15350-13) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         400-526: SHLQPPSYGP...IYHLQNLTIE → PRDAQQPWPR...PLPRRPQPRQ

    Note: No experimental confirmation available.

    Show »
    Length:555
    Mass (Da):61,694
    Checksum:i40CC002014B124C7
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7171Missing in isoform 10. 1 PublicationVSP_045082Add
    BLAST
    Alternative sequencei1 – 6262MAQST…TTSVM → MLYVGDPARHLAT in isoform dN-Alpha, isoform dN-Beta, isoform dN-Gamma and isoform 11. 3 PublicationsVSP_014368Add
    BLAST
    Alternative sequencei400 – 636237Missing in isoform 11. 1 PublicationVSP_053809Add
    BLAST
    Alternative sequencei400 – 526127SHLQP…NLTIE → PRDAQQPWPRSASQRRDEQQ PQRPVHGLGVPLHSATPLPR RPQPRQ in isoform 12. CuratedVSP_053810Add
    BLAST
    Alternative sequencei400 – 49596Missing in isoform Zeta. 1 PublicationVSP_006546Add
    BLAST
    Alternative sequencei400 – 47677SHLQP…AQSMV → PRDAQQPWPRSASQQRRDEQ QPQRPVHGLGVPLHSATPLP RRPQPRQFFNRIGVSKLHRV FHLPRVTEHLPPAEPDH in isoform Gamma and isoform dN-Gamma. 2 PublicationsVSP_006540Add
    BLAST
    Alternative sequencei400 – 44546SHLQP…ATPNL → PRDAQQPWPRSASQQRRDEQ QPQRPVHGLGVPLHSATPLP RRPQPR in isoform Epsilon. 1 PublicationVSP_006544Add
    BLAST
    Alternative sequencei400 – 4034SHLQ → TWGP in isoform Delta. 1 PublicationVSP_006542
    Alternative sequencei404 – 636233Missing in isoform Delta. 1 PublicationVSP_006543Add
    BLAST
    Alternative sequencei446 – 52681Missing in isoform Epsilon. 1 PublicationVSP_006545Add
    BLAST
    Alternative sequencei477 – 636160Missing in isoform Gamma and isoform dN-Gamma. 2 PublicationsVSP_006541Add
    BLAST
    Alternative sequencei495 – 636142SFLTG…EAEIH → RTWGP in isoform Beta and isoform dN-Beta. 3 PublicationsVSP_006539Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11416 mRNA. Translation: CAA72220.1.
    Y11416 mRNA. Translation: CAA72221.1.
    Y11416 mRNA. Translation: CAA72219.1.
    AF079094
    , AF079082, AF079083, AF079084, AF079085, AF079086, AF079087, AF079088, AF079089, AF079090, AF079091, AF079092, AF079093 Genomic DNA. Translation: AAD39696.1.
    AF077628
    , AF077616, AF077617, AF077618, AF077619, AF077620, AF077621, AF077624, AF077625, AF077626, AF077627 Genomic DNA. Translation: AAC61887.1.
    AY040827 mRNA. Translation: AAK81884.1.
    AY040828 mRNA. Translation: AAK81885.1.
    AY040829 mRNA. Translation: AAK81886.1.
    AB055065 mRNA. Translation: BAB87244.1.
    AB055066 mRNA. Translation: BAB87245.1.
    AK302118 mRNA. Translation: BAH13630.1.
    AK304177 mRNA. Translation: BAH14127.1.
    AK304784 mRNA. Translation: BAH14257.1.
    AL136528 Genomic DNA. Translation: CAI19123.1.
    AL136528 Genomic DNA. Translation: CAI19124.1.
    AL136528 Genomic DNA. Translation: CAI19125.1.
    AL136528 Genomic DNA. Translation: CAI19126.1.
    AL136528 Genomic DNA. Translation: CAI19127.1.
    CH471130 Genomic DNA. Translation: EAW71464.1.
    BC117251 mRNA. Translation: AAI17252.1.
    BC117253 mRNA. Translation: AAI17254.1.
    CCDSiCCDS44049.1. [O15350-8]
    CCDS44050.1. [O15350-9]
    CCDS49.1. [O15350-1]
    CCDS55566.1. [O15350-2]
    CCDS55567.1. [O15350-13]
    CCDS55568.1. [O15350-6]
    CCDS55569.1. [O15350-11]
    CCDS59965.1. [O15350-4]
    RefSeqiNP_001119712.1. NM_001126240.2. [O15350-8]
    NP_001119713.1. NM_001126241.2. [O15350-9]
    NP_001119714.1. NM_001126242.2.
    NP_001191113.1. NM_001204184.1. [O15350-2]
    NP_001191114.1. NM_001204185.1.
    NP_001191115.1. NM_001204186.1. [O15350-4]
    NP_001191116.1. NM_001204187.1. [O15350-13]
    NP_001191117.1. NM_001204188.1. [O15350-6]
    NP_001191118.1. NM_001204189.1.
    NP_001191119.1. NM_001204190.1.
    NP_001191120.1. NM_001204191.1.
    NP_001191121.1. NM_001204192.1. [O15350-11]
    NP_005418.1. NM_005427.3. [O15350-1]
    UniGeneiHs.192132.

    Genome annotation databases

    EnsembliENST00000346387; ENSP00000340740; ENSG00000078900. [O15350-6]
    ENST00000354437; ENSP00000346423; ENSG00000078900. [O15350-2]
    ENST00000357733; ENSP00000350366; ENSG00000078900. [O15350-13]
    ENST00000378280; ENSP00000367529; ENSG00000078900.
    ENST00000378285; ENSP00000367534; ENSG00000078900. [O15350-9]
    ENST00000378288; ENSP00000367537; ENSG00000078900. [O15350-8]
    ENST00000378290; ENSP00000367539; ENSG00000078900. [O15350-11]
    ENST00000378295; ENSP00000367545; ENSG00000078900. [O15350-1]
    ENST00000603362; ENSP00000474626; ENSG00000078900. [O15350-13]
    ENST00000604074; ENSP00000475143; ENSG00000078900. [O15350-4]
    ENST00000604479; ENSP00000474322; ENSG00000078900. [O15350-6]
    GeneIDi7161.
    KEGGihsa:7161.
    UCSCiuc001akp.3. human. [O15350-1]
    uc001akr.3. human. [O15350-8]
    uc001aks.3. human. [O15350-9]
    uc009vlk.2. human. [O15350-10]
    uc021ofb.1. human. [O15350-4]
    uc021ofd.1. human. [O15350-2]
    uc021ofe.1. human. [O15350-6]

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11416 mRNA. Translation: CAA72220.1 .
    Y11416 mRNA. Translation: CAA72221.1 .
    Y11416 mRNA. Translation: CAA72219.1 .
    AF079094
    , AF079082 , AF079083 , AF079084 , AF079085 , AF079086 , AF079087 , AF079088 , AF079089 , AF079090 , AF079091 , AF079092 , AF079093 Genomic DNA. Translation: AAD39696.1 .
    AF077628
    , AF077616 , AF077617 , AF077618 , AF077619 , AF077620 , AF077621 , AF077624 , AF077625 , AF077626 , AF077627 Genomic DNA. Translation: AAC61887.1 .
    AY040827 mRNA. Translation: AAK81884.1 .
    AY040828 mRNA. Translation: AAK81885.1 .
    AY040829 mRNA. Translation: AAK81886.1 .
    AB055065 mRNA. Translation: BAB87244.1 .
    AB055066 mRNA. Translation: BAB87245.1 .
    AK302118 mRNA. Translation: BAH13630.1 .
    AK304177 mRNA. Translation: BAH14127.1 .
    AK304784 mRNA. Translation: BAH14257.1 .
    AL136528 Genomic DNA. Translation: CAI19123.1 .
    AL136528 Genomic DNA. Translation: CAI19124.1 .
    AL136528 Genomic DNA. Translation: CAI19125.1 .
    AL136528 Genomic DNA. Translation: CAI19126.1 .
    AL136528 Genomic DNA. Translation: CAI19127.1 .
    CH471130 Genomic DNA. Translation: EAW71464.1 .
    BC117251 mRNA. Translation: AAI17252.1 .
    BC117253 mRNA. Translation: AAI17254.1 .
    CCDSi CCDS44049.1. [O15350-8 ]
    CCDS44050.1. [O15350-9 ]
    CCDS49.1. [O15350-1 ]
    CCDS55566.1. [O15350-2 ]
    CCDS55567.1. [O15350-13 ]
    CCDS55568.1. [O15350-6 ]
    CCDS55569.1. [O15350-11 ]
    CCDS59965.1. [O15350-4 ]
    RefSeqi NP_001119712.1. NM_001126240.2. [O15350-8 ]
    NP_001119713.1. NM_001126241.2. [O15350-9 ]
    NP_001119714.1. NM_001126242.2.
    NP_001191113.1. NM_001204184.1. [O15350-2 ]
    NP_001191114.1. NM_001204185.1.
    NP_001191115.1. NM_001204186.1. [O15350-4 ]
    NP_001191116.1. NM_001204187.1. [O15350-13 ]
    NP_001191117.1. NM_001204188.1. [O15350-6 ]
    NP_001191118.1. NM_001204189.1.
    NP_001191119.1. NM_001204190.1.
    NP_001191120.1. NM_001204191.1.
    NP_001191121.1. NM_001204192.1. [O15350-11 ]
    NP_005418.1. NM_005427.3. [O15350-1 ]
    UniGenei Hs.192132.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1COK NMR - A 487-554 [» ]
    1DXS X-ray 2.54 A 487-564 [» ]
    2KBY NMR - A/B/C/D 351-398 [» ]
    2WQI X-ray 1.70 A/B/C/D 351-399 [» ]
    2WQJ X-ray 2.00 1/2/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z 351-383 [» ]
    2WTT X-ray 2.30 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P 351-399 [» ]
    2XWC X-ray 1.82 A 112-311 [» ]
    3VD0 X-ray 2.95 A/B/C/D/I/J/K/L 115-312 [» ]
    3VD1 X-ray 2.95 A/B/C/D/I/J/K/L 115-312 [» ]
    3VD2 X-ray 4.00 A/B/C/D/I/J 115-312 [» ]
    4A63 X-ray 2.27 A/C/E/G/I/K 112-311 [» ]
    4G82 X-ray 3.10 A/B 115-312 [» ]
    4G83 X-ray 4.00 A/B 115-312 [» ]
    4GUO X-ray 3.19 A/B/C/D/I/J/K/L 115-312 [» ]
    4GUQ X-ray 3.70 A/B 115-312 [» ]
    DisProti DP00319.
    ProteinModelPortali O15350.
    SMRi O15350. Positions 115-396, 487-554.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113014. 99 interactions.
    DIPi DIP-24202N.
    IntActi O15350. 18 interactions.
    MINTi MINT-97729.

    PTM databases

    PhosphoSitei O15350.

    Proteomic databases

    MaxQBi O15350.
    PaxDbi O15350.
    PRIDEi O15350.

    Protocols and materials databases

    DNASUi 7161.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000346387 ; ENSP00000340740 ; ENSG00000078900 . [O15350-6 ]
    ENST00000354437 ; ENSP00000346423 ; ENSG00000078900 . [O15350-2 ]
    ENST00000357733 ; ENSP00000350366 ; ENSG00000078900 . [O15350-13 ]
    ENST00000378280 ; ENSP00000367529 ; ENSG00000078900 .
    ENST00000378285 ; ENSP00000367534 ; ENSG00000078900 . [O15350-9 ]
    ENST00000378288 ; ENSP00000367537 ; ENSG00000078900 . [O15350-8 ]
    ENST00000378290 ; ENSP00000367539 ; ENSG00000078900 . [O15350-11 ]
    ENST00000378295 ; ENSP00000367545 ; ENSG00000078900 . [O15350-1 ]
    ENST00000603362 ; ENSP00000474626 ; ENSG00000078900 . [O15350-13 ]
    ENST00000604074 ; ENSP00000475143 ; ENSG00000078900 . [O15350-4 ]
    ENST00000604479 ; ENSP00000474322 ; ENSG00000078900 . [O15350-6 ]
    GeneIDi 7161.
    KEGGi hsa:7161.
    UCSCi uc001akp.3. human. [O15350-1 ]
    uc001akr.3. human. [O15350-8 ]
    uc001aks.3. human. [O15350-9 ]
    uc009vlk.2. human. [O15350-10 ]
    uc021ofb.1. human. [O15350-4 ]
    uc021ofd.1. human. [O15350-2 ]
    uc021ofe.1. human. [O15350-6 ]

    Organism-specific databases

    CTDi 7161.
    GeneCardsi GC01P003592.
    HGNCi HGNC:12003. TP73.
    HPAi CAB002514.
    CAB003022.
    MIMi 601990. gene.
    neXtProti NX_O15350.
    PharmGKBi PA36684.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG80479.
    HOVERGENi HBG005201.
    InParanoidi O15350.
    KOi K10148.
    OMAi NEGQSAP.
    OrthoDBi EOG7JQBNW.
    PhylomeDBi O15350.
    TreeFami TF106101.

    Enzyme and pathway databases

    SignaLinki O15350.

    Miscellaneous databases

    ChiTaRSi TP73. human.
    EvolutionaryTracei O15350.
    GeneWikii P73.
    GenomeRNAii 7161.
    NextBioi 28022.
    PMAP-CutDB O15350.
    PROi O15350.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15350.
    Bgeei O15350.
    Genevestigatori O15350.

    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. "Monoallelically expressed gene related to p53 at 1p36, a region frequently deleted in neuroblastoma and other human cancers."
      Kaghad M., Bonnet H., Yang A., Creancier L., Biscan J.-C., Valent A., Minty A., Chalon P., Lelias J.-M., Dumont X., Ferrara P., McKeon F., Caput D.
      Cell 90:809-819(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
      Tissue: Colon.
    2. "Genomic organization and mutation analysis of p73 in oligodendrogliomas with chromosome 1 p-arm deletions."
      Mai M., Huang H., Reed C., Qian C., Smith J.S., Alderete B., Jenkins R., Smith D.I., Liu W.
      Genomics 51:359-363(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA).
    3. "Two new p73 splice variants, gamma and delta, with different transcriptional activity."
      De Laurenzi V., Costanzo A., Barcaroli D., Terrinoni A., Falco M., Annicchiarico-Petruzzelli M., Levrero M., Melino G.
      J. Exp. Med. 188:1763-1768(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GAMMA AND DELTA).
      Tissue: Neuroblastoma.
    4. "Additional complexity in p73: induction by mitogens in lymphoid cells and identification of two new splicing variants epsilon and zeta."
      De Laurenzi V., Catani M.V., Terrinoni A., Corazzari M., Melino G., Costanzo A., Levrero M., Knight R.A.
      Cell Death Differ. 6:389-390(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS EPSILON AND ZETA).
      Tissue: Hepatoma, Lymphocyte, Mammary cancer and Skin.
    5. "Mutational analysis of p73 and p53 in human cancer cell lines."
      Yoshikawa H., Nagashima M., Khan M.A., McMenamin M.G., Hagiwara K., Harris C.C.
      Oncogene 18:3415-3421(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA).
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DN-ALPHA; DN-BETA AND DN-GAMMA), FUNCTION, TISSUE SPECIFICITY, INDUCTION.
    7. "Identification of the p73-specific target sequence present in the deltaNp73 proper promoter."
      Nakagawa T., Takahashi M., Ozaki T., Watanabe K., Nakagawara A.
      Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DN-ALPHA AND DN-BETA).
    8. "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] (ISOFORMS DN-ALPHA; 10 AND 11).
      Tissue: Testis and Uterus.
    9. "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].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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 ALPHA).
      Tissue: Colon.
    12. "p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage."
      Yuan Z.-M., Shioya H., Ishiko T., Sun X., Gu J., Huang Y., Lu H., Kharbanda S., Weichselbaum R., Kufe D.
      Nature 399:814-817(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ABL1, PHOSPHORYLATION AT TYR-99 BY ABL1, MUTAGENESIS OF TYR-99.
    13. Cited for: FUNCTION.
    14. "Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif."
      Minty A., Dumont X., Kaghad M., Caput D.
      J. Biol. Chem. 275:36316-36323(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-627, MUTAGENESIS OF LYS-627.
    15. "Differential effect of ik3-1/cables on p53- and p73-induced cell death."
      Tsuji K., Mizumoto K., Yamochi T., Nishimoto I., Matsuoka M.
      J. Biol. Chem. 277:2951-2957(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CABLES1 AND TP53.
    16. "Identification and characterization of HIPK2 interacting with p73 and modulating functions of the p53 family in vivo."
      Kim E.-J., Park J.-S., Um S.-J.
      J. Biol. Chem. 277:32020-32028(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIPK2.
    17. "A novel HECT-type E3 ubiquitin ligase, NEDL2, stabilizes p73 and enhances its transcriptional activity."
      Miyazaki K., Ozaki T., Kato C., Hanamoto T., Fujita T., Irino S., Watanabe K., Nakagawa T., Nakagawara A.
      Biochem. Biophys. Res. Commun. 308:106-113(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HECW2.
    18. Cited for: INTERACTION WITH WWOX, DOMAIN, MUTAGENESIS OF TYR-487.
    19. "Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells."
      Kramer S., Ozaki T., Miyazaki K., Kato C., Hanamoto T., Nakagawara A.
      Oncogene 24:938-944(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RANBP9, SUBCELLULAR LOCATION.
    20. "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.
    21. "p73-mediated transcriptional activity is negatively regulated by polo-like kinase 1."
      Soond S.M., Barry S.P., Melino G., Knight R.A., Latchman D.S., Stephanou A.
      Cell Cycle 7:1214-1223(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-27.
    22. "Inhibitory role of Plk1 in the regulation of p73-dependent apoptosis through physical interaction and phosphorylation."
      Koida N., Ozaki T., Yamamoto H., Ono S., Koda T., Ando K., Okoshi R., Kamijo T., Omura K., Nakagawara A.
      J. Biol. Chem. 283:8555-8563(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-27, MUTAGENESIS OF THR-27.
    23. "Regulation of p73 by Hck through kinase-dependent and independent mechanisms."
      Paliwal P., Radha V., Swarup G.
      BMC Mol. Biol. 8:45-45(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-28, SUBCELLULAR LOCATION, INTERACTION WITH HCK.
    24. "Yap1 phosphorylation by c-Abl is a critical step in selective activation of proapoptotic genes in response to DNA damage."
      Levy D., Adamovich Y., Reuven N., Shaul Y.
      Mol. Cell 29:350-361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YAP1.
    25. "Plk3 inhibits pro-apoptotic activity of p73 through physical interaction and phosphorylation."
      Sang M., Ando K., Okoshi R., Koida N., Li Y., Zhu Y., Shimozato O., Geng C., Shan B., Nakagawara A., Ozaki T.
      Genes Cells 14:775-788(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY PLK3.
    26. "The F-box protein FBXO45 promotes the proteasome-dependent degradation of p73."
      Peschiaroli A., Scialpi F., Bernassola F., Pagano M., Melino G.
      Oncogene 28:3157-3166(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FBXO45, UBIQUITINATION.
    27. "Pirh2, a ubiquitin E3 ligase, inhibits p73 transcriptional activity by promoting its ubiquitination."
      Wu H., Zeinab R.A., Flores E.R., Leng R.P.
      Mol. Cancer Res. 9:1780-1790(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY RCHY1/PIRH2.
    28. "Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain."
      Chi S.W., Ayed A., Arrowsmith C.H.
      EMBO J. 18:4438-4445(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 487-554.

    Entry informationi

    Entry nameiP73_HUMAN
    AccessioniPrimary (citable) accession number: O15350
    Secondary accession number(s): B7Z7J4
    , B7Z8Z1, B7Z9C1, C9J521, O15351, Q17RN8, Q5TBV5, Q5TBV6, Q8NHW9, Q8TDY5, Q8TDY6, Q9NTK8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 168 of the entry and version 1 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

    Miscellaneous

    Maps to a chromosome region frequently mutated in diverse cell lines of human cancer. Appears not to be frequently mutated in human cancers, in contrast to p53/TP53. Hemizygosity is observed in neuroblastoma and oligodendroglioma.
    Activated and stabilized by interaction with RANBP9.

    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