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Protein

Tumor protein p73

Gene

TP73

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi194ZincBy similarity1
Metal bindingi197ZincBy similarity1
Metal bindingi258ZincBy similarity1
Metal bindingi262ZincBy similarity1

GO - Molecular functioni

  • chromatin binding Source: GO_Central
  • damaged DNA binding Source: GO_Central
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • p53 binding Source: GO_Central
  • protein kinase binding Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcription factor activity, sequence-specific DNA binding Source: MGI
  • transcription factor binding Source: ParkinsonsUK-UCL
  • transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Cell cycle, Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000078900-MONOMER.
ReactomeiR-HSA-139915. Activation of PUMA and translocation to mitochondria.
R-HSA-6803204. TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
R-HSA-6803205. TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
R-HSA-6803207. TP53 Regulates Transcription of Caspase Activators and Caspases.
R-HSA-6803211. TP53 Regulates Transcription of Death Receptors and Ligands.
R-HSA-6804759. Regulation of TP53 Activity through Association with Co-factors.
SignaLinkiO15350.
SIGNORiO15350.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:12003. TP73.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi27T → A: Impaired phosphorylation. 1 Publication1
Mutagenesisi99Y → F: Impaired phosphorylation of isoform beta by ABL1. 1 Publication1
Mutagenesisi487Y → A: Loss of interaction with WWOX. 1 Publication1
Mutagenesisi627K → R: Strongly diminishes sumoylation but does not affect transcriptional activity. 1 Publication1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNETi7161.
MalaCardsiTP73.
OpenTargetsiENSG00000078900.
PharmGKBiPA36684.

Polymorphism and mutation databases

BioMutaiTP73.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001857281 – 636Tumor protein p73Add BLAST636

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27Phosphothreonine; by PLK12 Publications1
Modified residuei28Phosphotyrosine; by SRC and HCK1 Publication1
Modified residuei99Phosphotyrosine; by ABL11 Publication1
Cross-linki627Glycyl 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.2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO15350.
PaxDbiO15350.
PeptideAtlasiO15350.
PRIDEiO15350.

PTM databases

iPTMnetiO15350.
PhosphoSitePlusiO15350.

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

BgeeiENSG00000078900.
ExpressionAtlasiO15350. baseline and differential.
GenevisibleiO15350. HS.

Organism-specific databases

HPAiCAB002514.
CAB003022.
HPA027314.
HPA044516.

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. Interacts with Epstein-Barr virus protein EBNA6; this interaction inhibits TP73-mediated apoptotic pathway.10 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
RUNX2Q139503EBI-389606,EBI-976402
SIRT1Q96EB64EBI-389606,EBI-1802965
YAP1P469377EBI-389619,EBI-1044059

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • p53 binding Source: GO_Central
  • protein kinase binding Source: UniProtKB
  • transcription factor binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi113014. 117 interactors.
DIPiDIP-24202N.
IntActiO15350. 21 interactors.
MINTiMINT-97729.
STRINGi9606.ENSP00000367545.

Structurei

Secondary structure

1636
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 20Combined sources6
Turni123 – 126Combined sources4
Beta strandi128 – 130Combined sources3
Beta strandi136 – 138Combined sources3
Beta strandi141 – 145Combined sources5
Turni146 – 149Combined sources4
Beta strandi150 – 153Combined sources4
Beta strandi157 – 164Combined sources8
Beta strandi174 – 181Combined sources8
Turni184 – 188Combined sources5
Helixi195 – 199Combined sources5
Turni202 – 206Combined sources5
Beta strandi214 – 219Combined sources6
Beta strandi224 – 227Combined sources4
Turni229 – 231Combined sources3
Beta strandi234 – 239Combined sources6
Beta strandi250 – 256Combined sources7
Helixi260 – 262Combined sources3
Turni263 – 268Combined sources6
Beta strandi271 – 278Combined sources8
Beta strandi280 – 282Combined sources3
Beta strandi284 – 294Combined sources11
Helixi298 – 311Combined sources14
Beta strandi354 – 360Combined sources7
Helixi362 – 377Combined sources16
Helixi378 – 380Combined sources3
Helixi383 – 395Combined sources13
Helixi493 – 499Combined sources7
Turni503 – 505Combined sources3
Helixi506 – 510Combined sources5
Turni511 – 513Combined sources3
Helixi517 – 521Combined sources5
Helixi525 – 530Combined sources6
Turni535 – 537Combined sources3
Helixi538 – 547Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1COKNMR-A487-554[»]
1DXSX-ray2.54A487-564[»]
2KBYNMR-A/B/C/D351-398[»]
2MPSNMR-B10-25[»]
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[»]
5HOBX-ray1.22A/B/C/D/E/F/G/H351-398[»]
5HOCX-ray1.36A/B351-398[»]
5KBDX-ray2.80A/B115-312[»]
DisProtiDP00319.
ProteinModelPortaliO15350.
SMRiO15350.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15350.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini485 – 551SAMAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 46TransactivationBy similarityAdd BLAST46
Regioni131 – 310DNA-bindingSequence analysisAdd BLAST180
Regioni345 – 386OligomerizationSequence analysisAdd BLAST42
Regioni345 – 380Interaction with HIPK21 PublicationAdd BLAST36

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi483 – 487WW-binding5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 55Asp/Glu-rich (acidic)Add BLAST55
Compositional biasi168 – 171Poly-Pro4
Compositional biasi391 – 394Poly-Gln4
Compositional biasi483 – 486Poly-Pro4

Domaini

Possesses an acidic transactivation domain, a central DNA binding domain and a C-terminal oligomerization domain that binds to the ABL1 tyrosine kinase SH3 domain.1 Publication
The WW-binding motif mediates interaction with WWOX.1 Publication

Sequence similaritiesi

Belongs to the p53 family.Curated

Phylogenomic databases

eggNOGiENOG410IGE4. Eukaryota.
ENOG410XV9W. LUCA.
GeneTreeiENSGT00390000015092.
HOGENOMiHOG000039956.
HOVERGENiHBG005201.
InParanoidiO15350.
KOiK10148.
OMAiNEGQSAP.
OrthoDBiEOG091G0XY5.
PhylomeDBiO15350.
TreeFamiTF106101.

Family and domain databases

CDDicd08367. P53. 1 hit.
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.
IPR032646. Tp73.
[Graphical view]
PANTHERiPTHR11447. PTHR11447. 2 hits.
PTHR11447:SF21. PTHR11447:SF21. 2 hits.
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. AlignAdd to basket

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

        10         20         30         40         50
MAQSTATSPD GGTTFEHLWS SLEPDSTYFD LPQSSRGNNE VVGGTDSSMD
60 70 80 90 100
VFHLEGMTTS VMAQFNLLSS TMDQMSSRAA SASPYTPEHA ASVPTHSPYA
110 120 130 140 150
QPSSTFDTMS PAPVIPSNTD YPGPHHFEVT FQQSSTAKSA TWTYSPLLKK
160 170 180 190 200
LYCQIAKTCP IQIKVSTPPP PGTAIRAMPV YKKAEHVTDV VKRCPNHELG
210 220 230 240 250
RDFNEGQSAP ASHLIRVEGN NLSQYVDDPV TGRQSVVVPY EPPQVGTEFT
260 270 280 290 300
TILYNFMCNS SCVGGMNRRP ILIIITLEMR DGQVLGRRSF EGRICACPGR
310 320 330 340 350
DRKADEDHYR EQQALNESSA KNGAASKRAF KQSPPAVPAL GAGVKKRRHG
360 370 380 390 400
DEDTYYLQVR GRENFEILMK LKESLELMEL VPQPLVDSYR QQQQLLQRPS
410 420 430 440 450
HLQPPSYGPV LSPMNKVHGG MNKLPSVNQL VGQPPPHSSA ATPNLGPVGP
460 470 480 490 500
GMLNNHGHAV PANGEMSSSH SAQSMVSGSH CTPPPPYHAD PSLVSFLTGL
510 520 530 540 550
GCPNCIEYFT SQGLQSIYHL QNLTIEDLGA LKIPEQYRMT IWRGLQDLKQ
560 570 580 590 600
GHDYSTAQQL LRSSNAATIS IGGSGELQRQ RVMEAVHFRV RHTITIPNRG
610 620 630
GPGGGPDEWA DFGFDLPDCK ARKQPIKEEF TEAEIH
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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0450821 – 71Missing in isoform 10. 1 PublicationAdd BLAST71
Alternative sequenceiVSP_0143681 – 62MAQST…TTSVM → MLYVGDPARHLAT in isoform dN-Alpha, isoform dN-Beta, isoform dN-Gamma and isoform 11. 3 PublicationsAdd BLAST62
Alternative sequenceiVSP_053809400 – 636Missing in isoform 11. 1 PublicationAdd BLAST237
Alternative sequenceiVSP_053810400 – 526SHLQP…NLTIE → PRDAQQPWPRSASQRRDEQQ PQRPVHGLGVPLHSATPLPR RPQPRQ in isoform 12. CuratedAdd BLAST127
Alternative sequenceiVSP_006546400 – 495Missing in isoform Zeta. 1 PublicationAdd BLAST96
Alternative sequenceiVSP_006540400 – 476SHLQP…AQSMV → PRDAQQPWPRSASQQRRDEQ QPQRPVHGLGVPLHSATPLP RRPQPRQFFNRIGVSKLHRV FHLPRVTEHLPPAEPDH in isoform Gamma and isoform dN-Gamma. 2 PublicationsAdd BLAST77
Alternative sequenceiVSP_006544400 – 445SHLQP…ATPNL → PRDAQQPWPRSASQQRRDEQ QPQRPVHGLGVPLHSATPLP RRPQPR in isoform Epsilon. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_006542400 – 403SHLQ → TWGP in isoform Delta. 1 Publication4
Alternative sequenceiVSP_006543404 – 636Missing in isoform Delta. 1 PublicationAdd BLAST233
Alternative sequenceiVSP_006545446 – 526Missing in isoform Epsilon. 1 PublicationAdd BLAST81
Alternative sequenceiVSP_006541477 – 636Missing in isoform Gamma and isoform dN-Gamma. 2 PublicationsAdd BLAST160
Alternative sequenceiVSP_006539495 – 636SFLTG…EAEIH → RTWGP in isoform Beta and isoform dN-Beta. 3 PublicationsAdd BLAST142

Sequence databases

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1COKNMR-A487-554[»]
1DXSX-ray2.54A487-564[»]
2KBYNMR-A/B/C/D351-398[»]
2MPSNMR-B10-25[»]
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[»]
5HOBX-ray1.22A/B/C/D/E/F/G/H351-398[»]
5HOCX-ray1.36A/B351-398[»]
5KBDX-ray2.80A/B115-312[»]
DisProtiDP00319.
ProteinModelPortaliO15350.
SMRiO15350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113014. 117 interactors.
DIPiDIP-24202N.
IntActiO15350. 21 interactors.
MINTiMINT-97729.
STRINGi9606.ENSP00000367545.

PTM databases

iPTMnetiO15350.
PhosphoSitePlusiO15350.

Polymorphism and mutation databases

BioMutaiTP73.

Proteomic databases

MaxQBiO15350.
PaxDbiO15350.
PeptideAtlasiO15350.
PRIDEiO15350.

Protocols and materials databases

DNASUi7161.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7161.
DisGeNETi7161.
GeneCardsiTP73.
HGNCiHGNC:12003. TP73.
HPAiCAB002514.
CAB003022.
HPA027314.
HPA044516.
MalaCardsiTP73.
MIMi601990. gene.
neXtProtiNX_O15350.
OpenTargetsiENSG00000078900.
PharmGKBiPA36684.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGE4. Eukaryota.
ENOG410XV9W. LUCA.
GeneTreeiENSGT00390000015092.
HOGENOMiHOG000039956.
HOVERGENiHBG005201.
InParanoidiO15350.
KOiK10148.
OMAiNEGQSAP.
OrthoDBiEOG091G0XY5.
PhylomeDBiO15350.
TreeFamiTF106101.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000078900-MONOMER.
ReactomeiR-HSA-139915. Activation of PUMA and translocation to mitochondria.
R-HSA-6803204. TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
R-HSA-6803205. TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
R-HSA-6803207. TP53 Regulates Transcription of Caspase Activators and Caspases.
R-HSA-6803211. TP53 Regulates Transcription of Death Receptors and Ligands.
R-HSA-6804759. Regulation of TP53 Activity through Association with Co-factors.
SignaLinkiO15350.
SIGNORiO15350.

Miscellaneous databases

ChiTaRSiTP73. human.
EvolutionaryTraceiO15350.
GeneWikiiP73.
GenomeRNAii7161.
PMAP-CutDBO15350.
PROiO15350.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000078900.
ExpressionAtlasiO15350. baseline and differential.
GenevisibleiO15350. HS.

Family and domain databases

CDDicd08367. P53. 1 hit.
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.
IPR032646. Tp73.
[Graphical view]
PANTHERiPTHR11447. PTHR11447. 2 hits.
PTHR11447:SF21. PTHR11447:SF21. 2 hits.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 193 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.