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O15350

- P73_HUMAN

UniProt

O15350 - P73_HUMAN

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Protein
Tumor protein p73
Gene
TP73, P73
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 1941Zinc By similarity
Metal bindingi197 – 1971Zinc By similarity
Metal bindingi258 – 2581Zinc By similarity
Metal bindingi262 – 2621Zinc By 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
Complete GO annotation...

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Source: RefGenome
  2. activation of MAPK activity Source: Ensembl
  3. cell cycle arrest Source: Ensembl
  4. cellular response to DNA damage stimulus Source: UniProtKB
  5. cellular response to UV Source: RefGenome
  6. cerebrospinal fluid secretion Source: Ensembl
  7. digestive tract morphogenesis Source: Ensembl
  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 from RNA polymerase II promoter Source: UniProtKB
  25. positive regulation of transcription, DNA-templated 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 X-ray Source: RefGenome
  30. response to gamma radiation Source: RefGenome
  31. response to organonitrogen compound Source: Ensembl
  32. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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.2 Publications

GO - Cellular componenti

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

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 p73
PRO_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 Alpha1 Publication

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.

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

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.

Miscellaneous databases

EvolutionaryTraceiO15350.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4646Transactivation By similarity
Add
BLAST
Regioni131 – 310180DNA-binding Reviewed prediction
Add
BLAST
Regioni345 – 38642Oligomerization Reviewed prediction
Add
BLAST
Regioni345 – 38036Interaction with HIPK2
Add
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.

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.
VSP_045082Add
BLAST
Alternative sequencei1 – 6262MAQST…TTSVM → MLYVGDPARHLAT in isoform dN-Alpha, isoform dN-Beta, isoform dN-Gamma and isoform 11.
VSP_014368Add
BLAST
Alternative sequencei400 – 636237Missing in isoform 11.
VSP_053809Add
BLAST
Alternative sequencei400 – 526127SHLQP…NLTIE → PRDAQQPWPRSASQRRDEQQ PQRPVHGLGVPLHSATPLPR RPQPRQ in isoform 12.
VSP_053810Add
BLAST
Alternative sequencei400 – 49596Missing in isoform Zeta.
VSP_006546Add
BLAST
Alternative sequencei400 – 47677SHLQP…AQSMV → PRDAQQPWPRSASQQRRDEQ QPQRPVHGLGVPLHSATPLP RRPQPRQFFNRIGVSKLHRV FHLPRVTEHLPPAEPDH in isoform Gamma and isoform dN-Gamma.
VSP_006540Add
BLAST
Alternative sequencei400 – 44546SHLQP…ATPNL → PRDAQQPWPRSASQQRRDEQ QPQRPVHGLGVPLHSATPLP RRPQPR in isoform Epsilon.
VSP_006544Add
BLAST
Alternative sequencei400 – 4034SHLQ → TWGP in isoform Delta.
VSP_006542
Alternative sequencei404 – 636233Missing in isoform Delta.
VSP_006543Add
BLAST
Alternative sequencei446 – 52681Missing in isoform Epsilon.
VSP_006545Add
BLAST
Alternative sequencei477 – 636160Missing in isoform Gamma and isoform dN-Gamma.
VSP_006541Add
BLAST
Alternative sequencei495 – 636142SFLTG…EAEIH → RTWGP in isoform Beta and isoform dN-Beta.
VSP_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.
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]
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...

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 .
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 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 167 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

Similar proteinsi