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O15350 (P73_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor protein p73
Alternative name(s):
p53-like transcription factor
p53-related protein
Gene names
Name:TP73
Synonyms:P73
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length636 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.14 Ref.23

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

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. Ref.12 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.24 Ref.25 Ref.27

Subcellular location

Nucleus. Cytoplasm. Note: Accumulates in the nucleus in response to DNA damage. Ref.20 Ref.24

Tissue specificity

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. Ref.6 Ref.21

Induction

Not induced by DNA damage. Isoforms lacking the transactivation domain block gene induction. Ref.6

Domain

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. Ref.19

The WW-binding motif mediates interaction with WWOX. Ref.19

Post-translational modification

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. Ref.15

Higher levels of phosphorylation seen in the brain from patients with Huntington disease.

Polyubiquitinated by RCHY1/PIRH2; leading to its degradation by the proteasome.

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.

Sequence similarities

Belongs to the p53 family.

Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
   DiseaseTumor suppressor
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Inferred from Biological aspect of Ancestor. Source: RefGenome

activation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from direct assay Ref.23. Source: UniProtKB

cellular response to UV

Inferred from Biological aspect of Ancestor. Source: RefGenome

cerebrospinal fluid secretion

Inferred from electronic annotation. Source: Ensembl

digestive tract morphogenesis

Inferred from electronic annotation. Source: Ensembl

hippocampus development

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway in response to DNA damage

Traceable author statement Ref.12. Source: ProtInc

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from direct assay Ref.23Ref.26. Source: UniProtKB

kidney development

Inferred from electronic annotation. Source: Ensembl

mismatch repair

Traceable author statement PubMed 10391249. Source: ProtInc

mitotic G1 DNA damage checkpoint

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of JUN kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of neuron apoptotic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuron development

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell size

Inferred from electronic annotation. Source: Ensembl

positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

positive regulation of oligodendrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.23Ref.26. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16343436. Source: UniProtKB

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

protein tetramerization

Inferred from electronic annotation. Source: InterPro

release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

response to X-ray

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to gamma radiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromatin

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from direct assay Ref.26. Source: UniProtKB

transcription factor complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionchromatin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

damaged DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

double-stranded DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

identical protein binding

Inferred from physical interaction PubMed 22340593. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

p53 binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 15678106. Source: IntAct

protein kinase binding

Inferred from physical interaction Ref.23Ref.26. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 15678106. Source: MGI

transcription factor binding

Inferred from physical interaction PubMed 11748232. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 16343436. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 12 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform Alpha (identifier: O15350-1)

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.
Isoform Beta (identifier: O15350-2)

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.
Isoform Gamma (identifier: O15350-3)

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.
Isoform Delta (identifier: O15350-4)

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.
Isoform Epsilon (identifier: O15350-5)

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.
Isoform Zeta (identifier: O15350-6)

The sequence of this isoform differs from the canonical sequence as follows:
     400-495: Missing.
Note: Produced by alternative splicing of isoform Alpha.
Isoform dN-Alpha (identifier: O15350-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVM → MLYVGDPARHLAT
Note: Produced by alternative promoter usage.
Isoform dN-Beta (identifier: O15350-9)

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.
Isoform dN-Gamma (identifier: O15350-10)

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.
Isoform 10 (identifier: O15350-11)

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: Missing.
Note: No experimental confirmation available.
Isoform 11 (identifier: O15350-12)

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVM → MLYVGDPARHLAT
     400-636: Missing.
Isoform 12 (identifier: O15350-13)

The sequence of this isoform differs from the canonical sequence as follows:
     400-526: SHLQPPSYGP...IYHLQNLTIE → PRDAQQPWPR...PLPRRPQPRQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 636636Tumor protein p73
PRO_0000185728

Regions

Domain485 – 55167SAM
Region1 – 4646Transactivation By similarity
Region131 – 310180DNA-binding Potential
Region345 – 38642Oligomerization Potential
Region345 – 38036Interaction with HIPK2
Motif483 – 4875WW-binding
Compositional bias1 – 5555Asp/Glu-rich (acidic)
Compositional bias168 – 1714Poly-Pro
Compositional bias391 – 3944Poly-Gln
Compositional bias483 – 4864Poly-Pro

Sites

Metal binding1941Zinc By similarity
Metal binding1971Zinc By similarity
Metal binding2581Zinc By similarity
Metal binding2621Zinc By similarity

Amino acid modifications

Modified residue271Phosphothreonine; by PLK1 Ref.22 Ref.23
Modified residue281Phosphotyrosine; by SRC and HCK Ref.24
Modified residue991Phosphotyrosine; by ABL1 Ref.12
Cross-link627Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); in isoform Alpha Ref.15

Natural variations

Alternative sequence1 – 7171Missing in isoform 10.
VSP_045082
Alternative sequence1 – 6262MAQST…TTSVM → MLYVGDPARHLAT in isoform dN-Alpha, isoform dN-Beta, isoform dN-Gamma and isoform 11.
VSP_014368
Alternative sequence400 – 636237Missing in isoform 11.
VSP_053809
Alternative sequence400 – 526127SHLQP…NLTIE → PRDAQQPWPRSASQRRDEQQ PQRPVHGLGVPLHSATPLPR RPQPRQ in isoform 12.
VSP_053810
Alternative sequence400 – 49596Missing in isoform Zeta.
VSP_006546
Alternative sequence400 – 47677SHLQP…AQSMV → PRDAQQPWPRSASQQRRDEQ QPQRPVHGLGVPLHSATPLP RRPQPRQFFNRIGVSKLHRV FHLPRVTEHLPPAEPDH in isoform Gamma and isoform dN-Gamma.
VSP_006540
Alternative sequence400 – 44546SHLQP…ATPNL → PRDAQQPWPRSASQQRRDEQ QPQRPVHGLGVPLHSATPLP RRPQPR in isoform Epsilon.
VSP_006544
Alternative sequence400 – 4034SHLQ → TWGP in isoform Delta.
VSP_006542
Alternative sequence404 – 636233Missing in isoform Delta.
VSP_006543
Alternative sequence446 – 52681Missing in isoform Epsilon.
VSP_006545
Alternative sequence477 – 636160Missing in isoform Gamma and isoform dN-Gamma.
VSP_006541
Alternative sequence495 – 636142SFLTG…EAEIH → RTWGP in isoform Beta and isoform dN-Beta.
VSP_006539

Experimental info

Mutagenesis271T → A: Impaired phosphorylation. Ref.23
Mutagenesis991Y → F: Impaired phosphorylation of isoform beta by ABL1. Ref.12
Mutagenesis4871Y → A: Loss of interaction with WWOX. Ref.19
Mutagenesis6271K → R: Strongly diminishes sumoylation but does not affect transcriptional activity. Ref.15

Secondary structure

.............................................................. 636
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: A467493C5D93EEE0

FASTA63669,623
        10         20         30         40         50         60 
MAQSTATSPD GGTTFEHLWS SLEPDSTYFD LPQSSRGNNE VVGGTDSSMD VFHLEGMTTS 

        70         80         90        100        110        120 
VMAQFNLLSS TMDQMSSRAA SASPYTPEHA ASVPTHSPYA QPSSTFDTMS PAPVIPSNTD 

       130        140        150        160        170        180 
YPGPHHFEVT FQQSSTAKSA TWTYSPLLKK LYCQIAKTCP IQIKVSTPPP PGTAIRAMPV 

       190        200        210        220        230        240 
YKKAEHVTDV VKRCPNHELG RDFNEGQSAP ASHLIRVEGN NLSQYVDDPV TGRQSVVVPY 

       250        260        270        280        290        300 
EPPQVGTEFT TILYNFMCNS SCVGGMNRRP ILIIITLEMR DGQVLGRRSF EGRICACPGR 

       310        320        330        340        350        360 
DRKADEDHYR EQQALNESSA KNGAASKRAF KQSPPAVPAL GAGVKKRRHG DEDTYYLQVR 

       370        380        390        400        410        420 
GRENFEILMK LKESLELMEL VPQPLVDSYR QQQQLLQRPS HLQPPSYGPV LSPMNKVHGG 

       430        440        450        460        470        480 
MNKLPSVNQL VGQPPPHSSA ATPNLGPVGP GMLNNHGHAV PANGEMSSSH SAQSMVSGSH 

       490        500        510        520        530        540 
CTPPPPYHAD PSLVSFLTGL GCPNCIEYFT SQGLQSIYHL QNLTIEDLGA LKIPEQYRMT 

       550        560        570        580        590        600 
IWRGLQDLKQ GHDYSTAQQL LRSSNAATIS IGGSGELQRQ RVMEAVHFRV RHTITIPNRG 

       610        620        630 
GPGGGPDEWA DFGFDLPDCK ARKQPIKEEF TEAEIH 

« Hide

Isoform Beta [UniParc].

Checksum: 0FDC0546E29D683E
Show »

FASTA49954,322
Isoform Gamma [UniParc].

Checksum: 78D99E725DCEFD5F
Show »

FASTA47653,026
Isoform Delta [UniParc].

Checksum: 72F1A3518940D832
Show »

FASTA40344,517
Isoform Epsilon [UniParc].

Checksum: 4C821E6FB836EC32
Show »

FASTA55561,694
Isoform Zeta [UniParc].

Checksum: A996F9FEB731ABD1
Show »

FASTA54059,887
Isoform dN-Alpha [UniParc].

Checksum: E8F1CAE88CED4EBC
Show »

FASTA58764,422
Isoform dN-Beta [UniParc].

Checksum: F1950AE8628B3863
Show »

FASTA45049,121
Isoform dN-Gamma [UniParc].

Checksum: 9D140E5D48BFB56E
Show »

FASTA42747,824
Isoform 10 [UniParc].

Checksum: 3D989435C093E515
Show »

FASTA56562,034
Isoform 11 [UniParc].

Checksum: 4BA732383EFE92A0
Show »

FASTA35038,874
Isoform 12 [UniParc].

Checksum: 40CC002014B124C7
Show »

FASTA55561,694

References

« Hide 'large scale' references
[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]"Human DeltaNp73 regulates a dominant negative feedback loop for TAp73 and p53."
Grob T.J., Novak U., Maisse C., Barcaroli D., Luthi A.U., Pirnia F., Hugli B., Graber H.U., De Laurenzi V., Fey M.F., Melino G., Tobler A.
Cell Death Differ. 8:1213-1223(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]Erratum
Yuan Z.-M., Shioya H., Ishiko T., Sun X., Gu J., Huang Y., Lu H., Kharbanda S., Weichselbaum R., Kufe D.
Nature 400:792-792(1999)
[14]"The emerging p53 gene family."
Kaelin W.G. Jr.
J. Natl. Cancer Inst. 91:594-598(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"Functional association between Wwox tumor suppressor protein and p73, a p53 homolog."
Aqeilan R.I., Pekarsky Y., Herrero J.J., Palamarchuk A., Letofsky J., Druck T., Trapasso F., Han S.-Y., Melino G., Huebner K., Croce C.M.
Proc. Natl. Acad. Sci. U.S.A. 101:4401-4406(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WWOX, DOMAIN, MUTAGENESIS OF TYR-487.
[20]"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.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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.
[26]"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.
[27]"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.
[28]"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.
[29]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y11416 mRNA. Translation: CAA72220.1.
Y11416 mRNA. Translation: CAA72221.1.
Y11416 mRNA. Translation: CAA72219.1.
AF079094 expand/collapse EMBL AC list , AF079082, AF079083, AF079084, AF079085, AF079086, AF079087, AF079088, AF079089, AF079090, AF079091, AF079092, AF079093 Genomic DNA. Translation: AAD39696.1.
AF077628 expand/collapse EMBL AC list , 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.
CCDSCCDS44049.1. [O15350-8]
CCDS44050.1. [O15350-9]
CCDS49.1. [O15350-1]
CCDS55566.1. [O15350-2]
CCDS55568.1. [O15350-6]
CCDS55569.1. [O15350-11]
CCDS59965.1. [O15350-4]
RefSeqNP_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]
UniGeneHs.192132.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00319.
ProteinModelPortalO15350.
SMRO15350. Positions 115-396, 487-554.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113014. 99 interactions.
DIPDIP-24202N.
IntActO15350. 18 interactions.
MINTMINT-97729.

PTM databases

PhosphoSiteO15350.

Proteomic databases

MaxQBO15350.
PaxDbO15350.
PRIDEO15350.

Protocols and materials databases

DNASU7161.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346387; ENSP00000340740; ENSG00000078900. [O15350-6]
ENST00000354437; ENSP00000346423; ENSG00000078900. [O15350-2]
ENST00000357733; ENSP00000350366; ENSG00000078900.
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.
ENST00000604074; ENSP00000475143; ENSG00000078900. [O15350-4]
ENST00000604479; ENSP00000474322; ENSG00000078900. [O15350-6]
GeneID7161.
KEGGhsa:7161.
UCSCuc001akp.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

CTD7161.
GeneCardsGC01P003592.
HGNCHGNC:12003. TP73.
HPACAB002514.
CAB003022.
MIM601990. gene.
neXtProtNX_O15350.
PharmGKBPA36684.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG80479.
HOVERGENHBG005201.
InParanoidO15350.
KOK10148.
OMANEGQSAP.
OrthoDBEOG7JQBNW.
PhylomeDBO15350.
TreeFamTF106101.

Enzyme and pathway databases

SignaLinkO15350.

Gene expression databases

ArrayExpressO15350.
BgeeO15350.
GenevestigatorO15350.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.40.720. 1 hit.
4.10.170.10. 1 hit.
InterProIPR008967. 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]
PANTHERPTHR11447. PTHR11447. 1 hit.
PfamPF00870. P53. 1 hit.
PF07710. P53_tetramer. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PRINTSPR00386. P53SUPPRESSR.
SMARTSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47719. SSF47719. 1 hit.
SSF47769. SSF47769. 1 hit.
SSF49417. SSF49417. 1 hit.
PROSITEPS00348. P53. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTP73. human.
EvolutionaryTraceO15350.
GeneWikiP73.
GenomeRNAi7161.
NextBio28022.
PMAP-CutDBO15350.
PROO15350.
SOURCESearch...

Entry information

Entry nameP73_HUMAN
AccessionPrimary (citable) accession number: O15350
Secondary accession number(s): B7Z7J4 expand/collapse secondary AC list , B7Z8Z1, B7Z9C1, C9J521, O15351, Q17RN8, Q5TBV5, Q5TBV6, Q8NHW9, Q8TDY5, Q8TDY6, Q9NTK8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM