Reviewed, UniProtKB/Swiss-Prot O15350 (P73_HUMAN)

Names and origin

Protein names

Recommended name:
Tumor protein p73

Alternative name(s):
p53-like transcription factor
p53-related protein

Gene names

Name:	TP73
Synonyms:	P73

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	636 AA.
Sequence status	Complete.
Protein existence	Evidence 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
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 ABL 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. Ref.16 Ref.17 Ref.18 Ref.19
Subcellular location	Nucleus. Note: Accumulates in the nucleus in response to DNA damage. Ref.19
Tissue specificity	Brain, kidney, placenta, colon, heart, liver, spleen, skeletal muscle, prostate, thymus and pancreas. Highly expressed in fetal tissue. Ref.6
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 ABL tyrosine kinase SH3 domain. Ref.18 The WW-binding motif mediates interaction with WWOX. Ref.18
Post-translational modification	Isoform alpha (but not isoform beta) is sumoylated on Lys-627, which potentiates proteasomal degradation but does not affect transcriptional activity. Ref.15
Involvement in disease	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. Hemizygosity is observed in neuroblastoma and oligodendroglioma.
Miscellaneous	Activated and stabilized by interaction with RANBP9.
Sequence similarities	Belongs to the p53 family. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative promoter usage Alternative splicing
Disease	Tumor suppressor
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction resulting in induction of apoptosis Ref.12 Traceable author statement. Source: ProtInc cellular transcription Inferred from electronic annotation. Source: UniProtKB-KW mismatch repair Traceable author statement. Source: ProtInc negative regulation of cell growth Inferred from electronic annotation. Source: InterPro positive regulation of cellular transcription, DNA-dependent Inferred from direct assay. Source: MGI response to tumor cell Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	transcription factor activity Inferred from direct assay. Source: MGI zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cables1	Q9ESJ1	1	EBI-389606,EBI-604411	From a different organism.
E6	P03126	1	EBI-389619,EBI-1177242	From a different organism.
E6	P03126	1	EBI-389623,EBI-1177242	From a different organism.
HMGB1	P09429	1	EBI-389606,EBI-389432

Alternative products

This entry describes 9 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 636

636

Tumor protein p73

PRO_0000185728

Regions

Domain

485 – 551

67

SAM

Region

1 – 46

46

Transactivation By similarity

Region

131 – 310

180

DNA-binding Potential

Region

345 – 386

42

Oligomerization Potential

Region

345 – 380

36

Interaction with HIPK2

Motif

483 – 487

5

WW-binding

Compositional bias

1 – 55

55

Asp/Glu-rich (acidic)

Compositional bias

168 – 171

4

Poly-Pro

Compositional bias

391 – 394

4

Poly-Gln

Compositional bias

483 – 486

4

Poly-Pro

Sites

Metal binding

194

1

Zinc By similarity

Metal binding

197

1

Zinc By similarity

Metal binding

258

1

Zinc By similarity

Metal binding

262

1

Zinc By similarity

Amino acid modifications

Modified residue

99

1

Phosphotyrosine; by ABL; in isoform Beta

Cross-link

627

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); in isoform Alpha Ref.15

Natural variations

Alternative sequence

1 – 62

62

MAQST…TTSVM → MLYVGDPARHLAT in isoform dN-Alpha, isoform dN-Beta and isoform dN-Gamma.

VSP_014368

Alternative sequence

400 – 495

96

Missing in isoform Zeta.

VSP_006546

Alternative sequence

400 – 476

77

SHLQP…AQSMV → PRDAQQPWPRSASQQRRDEQ QPQRPVHGLGVPLHSATPLP RRPQPRQFFNRIGVSKLHRV FHLPRVTEHLPPAEPDH in isoform Gamma and isoform dN-Gamma.

VSP_006540

Alternative sequence

400 – 445

46

SHLQP…ATPNL → PRDAQQPWPRSASQQRRDEQ QPQRPVHGLGVPLHSATPLP RRPQPR in isoform Epsilon.

VSP_006544

Alternative sequence

400 – 403

4

SHLQ → TWGP in isoform Delta.

VSP_006542

Alternative sequence

404 – 636

233

Missing in isoform Delta.

VSP_006543

Alternative sequence

446 – 526

81

Missing in isoform Epsilon.

VSP_006545

Alternative sequence

477 – 636

160

Missing in isoform Gamma and isoform dN-Gamma.

VSP_006541

Alternative sequence

495 – 636

142

SFLTG…EAEIH → RTWGP in isoform Beta and isoform dN-Beta.

VSP_006539

Experimental info

Mutagenesis

487

1

Y → A: Loss of interaction with WWOX. Ref.18

Mutagenesis

627

1

K → R: Strongly diminishes sumoylation but does not affect transcriptional activity. Ref.15

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

636

Helix Strand Turn

Details...

Helix

493 – 499

7

Helix

506 – 510

5

Turn

511 – 513

3

Helix

517 – 521

5

Helix

525 – 530

6

Turn

535 – 537

3

Helix

538 – 547

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified January 1, 1998. Version 1. Checksum: A467493C5D93EEE0	FASTA	636	69,623
	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
	Isoform Beta. Checksum: 0FDC0546E29D683E	FASTA	499	54,322
	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 CTPPPPYHAD PSLVRTWGP
	Isoform Gamma. Checksum: 78D99E725DCEFD5F	FASTA	476	53,026
	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 QQQQLLQRPP RDAQQPWPRS ASQQRRDEQQ 430 440 450 460 470 PQRPVHGLGV PLHSATPLPR RPQPRQFFNR IGVSKLHRVF HLPRVTEHLP PAEPDH
	Isoform Delta. Checksum: 72F1A3518940D832	FASTA	403	44,517
	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 GRENFEILMK LKESLELMEL VPQPLVDSYR QQQQLLQRPT WGP
	Isoform Epsilon. Checksum: 4C821E6FB836EC32	FASTA	555	61,694
	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 QQQQLLQRPP RDAQQPWPRS ASQQRRDEQQ 430 440 450 460 470 480 PQRPVHGLGV PLHSATPLPR RPQPRDLGAL KIPEQYRMTI WRGLQDLKQG HDYSTAQQLL 490 500 510 520 530 540 RSSNAATISI GGSGELQRQR VMEAVHFRVR HTITIPNRGG PGGGPDEWAD FGFDLPDCKA 550 RKQPIKEEFT EAEIH
	Isoform Zeta. Checksum: A996F9FEB731ABD1	FASTA	540	59,887
	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 QQQQLLQRPF LTGLGCPNCI EYFTSQGLQS 430 440 450 460 470 480 IYHLQNLTIE DLGALKIPEQ YRMTIWRGLQ DLKQGHDYST AQQLLRSSNA ATISIGGSGE 490 500 510 520 530 540 LQRQRVMEAV HFRVRHTITI PNRGGPGGGP DEWADFGFDL PDCKARKQPI KEEFTEAEIH
	Isoform dN-Alpha. Checksum: E8F1CAE88CED4EBC	FASTA	587	64,422
	10 20 30 40 50 60 MLYVGDPARH LATAQFNLLS STMDQMSSRA ASASPYTPEH AASVPTHSPY AQPSSTFDTM 70 80 90 100 110 120 SPAPVIPSNT DYPGPHHFEV TFQQSSTAKS ATWTYSPLLK KLYCQIAKTC PIQIKVSTPP 130 140 150 160 170 180 PPGTAIRAMP VYKKAEHVTD VVKRCPNHEL GRDFNEGQSA PASHLIRVEG NNLSQYVDDP 190 200 210 220 230 240 VTGRQSVVVP YEPPQVGTEF TTILYNFMCN SSCVGGMNRR PILIIITLEM RDGQVLGRRS 250 260 270 280 290 300 FEGRICACPG RDRKADEDHY REQQALNESS AKNGAASKRA FKQSPPAVPA LGAGVKKRRH 310 320 330 340 350 360 GDEDTYYLQV RGRENFEILM KLKESLELME LVPQPLVDSY RQQQQLLQRP SHLQPPSYGP 370 380 390 400 410 420 VLSPMNKVHG GMNKLPSVNQ LVGQPPPHSS AATPNLGPVG PGMLNNHGHA VPANGEMSSS 430 440 450 460 470 480 HSAQSMVSGS HCTPPPPYHA DPSLVSFLTG LGCPNCIEYF TSQGLQSIYH LQNLTIEDLG 490 500 510 520 530 540 ALKIPEQYRM TIWRGLQDLK QGHDYSTAQQ LLRSSNAATI SIGGSGELQR QRVMEAVHFR 550 560 570 580 VRHTITIPNR GGPGGGPDEW ADFGFDLPDC KARKQPIKEE FTEAEIH
	Isoform dN-Beta. Checksum: F1950AE8628B3863	FASTA	450	49,121
	10 20 30 40 50 60 MLYVGDPARH LATAQFNLLS STMDQMSSRA ASASPYTPEH AASVPTHSPY AQPSSTFDTM 70 80 90 100 110 120 SPAPVIPSNT DYPGPHHFEV TFQQSSTAKS ATWTYSPLLK KLYCQIAKTC PIQIKVSTPP 130 140 150 160 170 180 PPGTAIRAMP VYKKAEHVTD VVKRCPNHEL GRDFNEGQSA PASHLIRVEG NNLSQYVDDP 190 200 210 220 230 240 VTGRQSVVVP YEPPQVGTEF TTILYNFMCN SSCVGGMNRR PILIIITLEM RDGQVLGRRS 250 260 270 280 290 300 FEGRICACPG RDRKADEDHY REQQALNESS AKNGAASKRA FKQSPPAVPA LGAGVKKRRH 310 320 330 340 350 360 GDEDTYYLQV RGRENFEILM KLKESLELME LVPQPLVDSY RQQQQLLQRP SHLQPPSYGP 370 380 390 400 410 420 VLSPMNKVHG GMNKLPSVNQ LVGQPPPHSS AATPNLGPVG PGMLNNHGHA VPANGEMSSS 430 440 450 HSAQSMVSGS HCTPPPPYHA DPSLVRTWGP
	Isoform dN-Gamma. Checksum: 9D140E5D48BFB56E	FASTA	427	47,824
	10 20 30 40 50 60 MLYVGDPARH LATAQFNLLS STMDQMSSRA ASASPYTPEH AASVPTHSPY AQPSSTFDTM 70 80 90 100 110 120 SPAPVIPSNT DYPGPHHFEV TFQQSSTAKS ATWTYSPLLK KLYCQIAKTC PIQIKVSTPP 130 140 150 160 170 180 PPGTAIRAMP VYKKAEHVTD VVKRCPNHEL GRDFNEGQSA PASHLIRVEG NNLSQYVDDP 190 200 210 220 230 240 VTGRQSVVVP YEPPQVGTEF TTILYNFMCN SSCVGGMNRR PILIIITLEM RDGQVLGRRS 250 260 270 280 290 300 FEGRICACPG RDRKADEDHY REQQALNESS AKNGAASKRA FKQSPPAVPA LGAGVKKRRH 310 320 330 340 350 360 GDEDTYYLQV RGRENFEILM KLKESLELME LVPQPLVDSY RQQQQLLQRP PRDAQQPWPR 370 380 390 400 410 420 SASQQRRDEQ QPQRPVHGLG VPLHSATPLP RRPQPRQFFN RIGVSKLHRV FHLPRVTEHL PPAEPDH

References

	« Hide 'large scale' referencesShow '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: 9288759] [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: 9721206] [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: 9802988] [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: 10381648] [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: 10362363] [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: 11753569] [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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DN-ALPHA). Tissue: 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: 16710414] [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. , 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: 15489334] [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: 10391251] [Abstract] Cited for: PHOSPHORYLATION (ISOFORMS ALPHA AND BETA).
[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: 10203277] [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: 10961991] [Abstract] Cited for: SUMOYLATION AT LYS-627, MUTAGENESIS OF LYS-627.
[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: 11925430] [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: 12890487] [Abstract] Cited for: INTERACTION WITH HECW2.
[18]	"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: 15070730] [Abstract] 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: 15558019] [Abstract] Cited for: INTERACTION WITH RANBP9, SUBCELLULAR LOCATION.
[20]	"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: 11706030] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH CABLES1 AND TP53.
[21]	"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: 10449409] [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 , 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.
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.

IPI

IPI00006160.
IPI00215708.
IPI00215709.
IPI00215710.
IPI00215711.
IPI00215712.
IPI00607588.
IPI00607833.
IPI00607886.

RefSeq

NP_001119712.1.
NP_001119713.1.
NP_001119714.1.
NP_005418.1.

UniGene

Hs.697294

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

SMR

O15350. Positions 121-306.

DisProt

DP00319.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24202N.
DIP-46294N.

IntAct

O15350. 6 interactions.

STRING

O15350.

PTM databases

PhosphoSite

O15350.

Proteomic databases

PRIDE

O15350.

Genome annotation databases

Ensembl

ENST00000378295; ENSP00000367545; ENSG00000078900; Homo sapiens. [Genome view]

GeneID

7161.

KEGG

hsa:7161.

UCSC

uc001akp.2. human.
uc001akq.1. human.
uc001akr.2. human.
uc001aks.2. human.
uc009vlk.1. human.

Organism-specific databases

CTD

7161.

GeneCards

GC01P003592.

H-InvDB

HIX0028501.

HGNC

HGNC:12003. TP73.

HPA

CAB002514.
CAB003022.

MIM

601990. gene.

PharmGKB

PA36684.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06224.

HOVERGEN

HBG005201.

InParanoid

O15350.

OMA

VGQPPPH.

OrthoDB

EOG9KH5DG.

Gene expression databases

ArrayExpress

O15350.

Bgee

O15350.

Genevestigator

O15350.

GermOnline

ENSG00000078900. Homo sapiens.

Family and domain databases

InterPro

IPR008967. p53-like_TF_DNA-bd.
IPR012346. p53/RUNT-type_TF_DNA_bd.
IPR011615. p53_DNA_bd.
IPR010991. p53_tetrameristn.
IPR002117. p53_tumour_Ag.
IPR001660. SAM.
IPR011510. SAM_2.
IPR010993. SAM_homology.
IPR013761. SAM_type.
IPR015551. Trp53.
[Graphical view]

Gene3D

G3DSA:2.60.40.720. p53_RUNT_DNA_bd. 1 hit.
G3DSA:1.10.150.50. SAM_type. 1 hit.

PANTHER

PTHR11447. Trp53. 1 hit.

Pfam

PF00870. P53. 1 hit.
PF07710. P53_tetramer. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]

PRINTS

PR00386. P53SUPPRESSR.

SMART

SM00454. SAM. 1 hit.
[Graphical view]

SUPFAM

SSF49417. P53_like_DNA_bnd. 1 hit.
SSF47719. p53_tetrameristn. 1 hit.
SSF47769. SAM_homology. 1 hit.

PROSITE

PS00348. P53. 1 hit.
PS50105. SAM_DOMAIN. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

28022.

PMAP-CutDB

O15350.

SOURCE

Search...

Entry information

Entry name

P73_HUMAN

Accession

Primary (citable) accession number: O15350
Secondary accession number(s): B7Z9C1 , 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:	March 2, 2010
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.