UniProtKB - Q8SPZ3 (P53_DELLE)
Cellular tumor antigen p53
TP53
Functioni
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 169 | ZincBy similarity | 1 | |
Metal bindingi | 172 | ZincBy similarity | 1 | |
Metal bindingi | 232 | ZincBy similarity | 1 | |
Metal bindingi | 236 | ZincBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
DNA bindingi | 95 – 286 | By similarityAdd BLAST | 192 |
GO - Molecular functioni
- ATP binding Source: UniProtKB
- copper ion binding Source: UniProtKB
- DNA binding Source: UniProtKB
- DNA-binding transcription factor activity, RNA polymerase II-specific Source: UniProtKB
- promoter-specific chromatin binding Source: UniProtKB
- RNA polymerase II distal enhancer sequence-specific DNA binding Source: UniProtKB
GO - Biological processi
- cell aging Source: UniProtKB
- cell cycle Source: UniProtKB-KW
- cellular response to DNA damage stimulus Source: UniProtKB
- circadian behavior Source: UniProtKB
- DNA strand renaturation Source: UniProtKB
- entrainment of circadian clock by photoperiod Source: UniProtKB
- multicellular organism development Source: UniProtKB
- negative regulation of cell growth Source: UniProtKB
- negative regulation of transcription, DNA-templated Source: UniProtKB
- nucleotide-excision repair Source: UniProtKB
- oligodendrocyte apoptotic process Source: UniProtKB
- positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
- positive regulation of transcription by RNA polymerase II Source: UniProtKB
- protein tetramerization Source: InterPro
Keywordsi
Molecular function | Activator, DNA-binding, Repressor |
Biological process | Apoptosis, Biological rhythms, Cell cycle, Necrosis, Transcription, Transcription regulation |
Ligand | Metal-binding, Zinc |
Names & Taxonomyi
Protein namesi | Recommended name: Cellular tumor antigen p53Alternative name(s): Tumor suppressor p53 |
Gene namesi | Name:TP53 Synonyms:P53 |
Organismi | Delphinapterus leucas (Beluga whale) |
Taxonomic identifieri | 9749 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Cetacea › Odontoceti › Monodontidae › Delphinapterus |
Proteomesi |
|
Subcellular locationi
Mitochondrion
- Mitochondrion matrix By similarity
Endoplasmic reticulum
- Endoplasmic reticulum By similarity
Nucleus
Other locations
- Cytoplasm By similarity
Note: Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress. Translocates to mitochondria in response to mitomycin C treatment (By similarity).By similarity
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB-SubCell
Mitochondrion
- mitochondrial matrix Source: UniProtKB-SubCell
- mitochondrion Source: UniProtKB
Nucleus
Other locations
- cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, Endoplasmic reticulum, Mitochondrion, NucleusPathology & Biotechi
Involvement in diseasei
Keywords - Diseasei
Tumor suppressorPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000185699 | 1 – 387 | Cellular tumor antigen p53Add BLAST | 387 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 15 | Phosphoserine; by CDK5, PRPK, AMPK, NUAK1 and ATMBy similarity | 1 | |
Modified residuei | 18 | Phosphothreonine; by CK1, VRK1 and VRK2By similarity | 1 | |
Modified residuei | 20 | Phosphoserine; by CHEK2, CK1 and PLK3By similarity | 1 | |
Modified residuei | 33 | Phosphoserine; by CDK5 and CDK7By similarity | 1 | |
Modified residuei | 37 | Phosphoserine; by MAPKAPK5By similarity | 1 | |
Modified residuei | 46 | Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCGBy similarity | 1 | |
Modified residuei | 113 | N6-acetyllysine; by KAT6ABy similarity | 1 | |
Modified residuei | 176 | Phosphoserine; by AURKBBy similarity | 1 | |
Modified residuei | 263 | Phosphoserine; by AURKBBy similarity | 1 | |
Modified residuei | 278 | Phosphothreonine; by AURKBBy similarity | 1 | |
Cross-linki | 285 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Cross-linki | 286 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Modified residuei | 299 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 309 | Phosphoserine; by AURKA, CDK1 and CDK2By similarity | 1 | |
Modified residuei | 315 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 327 | Omega-N-methylarginineBy similarity | 1 | |
Modified residuei | 329 | Symmetric dimethylarginineBy similarity | 1 | |
Modified residuei | 331 | Symmetric dimethylarginineBy similarity | 1 | |
Modified residuei | 364 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 364 | N6-methyllysine; by SMYD2; alternateBy similarity | 1 | |
Modified residuei | 366 | N6-methyllysine; by SETD7By similarity | 1 | |
Modified residuei | 367 | N6,N6-dimethyllysine; by EHMT1 and EHMT2; alternateBy similarity | 1 | |
Modified residuei | 367 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 375 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 376 | N6,N6-dimethyllysine; alternateBy similarity | 1 | |
Modified residuei | 376 | N6-acetyllysine; by KAT6A; alternateBy similarity | 1 | |
Modified residuei | 376 | N6-methyllysine; by KMT5A; alternateBy similarity | 1 | |
Cross-linki | 380 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity | ||
Modified residuei | 386 | Phosphoserine; by CK2, CDK2 and NUAK1By similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
PRIDEi | Q8SPZ3 |
Interactioni
Subunit structurei
Forms homodimers and homotetramers (By similarity). Binds DNA as a homotetramer.
Interacts with AXIN1. Probably part of a complex consisting of TP53, HIPK2 and AXIN1.
Interacts with histone acetyltransferases EP300 and methyltransferases HRMT1L2 and CARM1, and recruits them to promoters.
Interacts (via C-terminus) with TAF1; when TAF1 is part of the TFIID complex.
Interacts with ING4; this interaction may be indirect.
Found in a complex with CABLES1 and TP73.
Interacts with HIPK1, HIPK2, and TP53INP1.
Interacts with WWOX.
Interacts with USP7 and SYVN1.
Interacts with HSP90AB1.
Interacts with CHD8; leading to recruit histone H1 and prevent transactivation activity.
Interacts with ARMC10, BANP, CDKN2AIP, NUAK1, STK11/LKB1, UHRF2 and E4F.
Interacts with YWHAZ; the interaction enhances TP53 transcriptional activity. Phosphorylation of YWHAZ on 'Ser-58' inhibits this interaction.
Interacts (via DNA-binding domain) with MAML1 (via N-terminus).
Interacts with MKRN1.
Interacts with PML (via C-terminus).
Interacts with MDM2; leading to ubiquitination and proteasomal degradation of TP53. Directly interacts with FBXO42; leading to ubiquitination and degradation of TP53.
Interacts (phosphorylated at Ser-15 by ATM) with the phosphatase PP2A-PPP2R5C holoenzyme; regulates stress-induced TP53-dependent inhibition of cell proliferation.
Interacts with PPP2R2A.
Interacts with AURKA, DAXX, BRD7 and TRIM24.
Interacts (when monomethylated at Lys-376) with L3MBTL1.
Interacts with GRK5. Binds to the CAK complex (CDK7, cyclin H and MAT1) in response to DNA damage.
Interacts with CDK5 in neurons.
Interacts with AURKB, SETD2, UHRF2 and NOC2L.
Interacts (via N-terminus) with PTK2/FAK1; this promotes ubiquitination by MDM2.
Interacts with PTK2B/PYK2; this promotes ubiquitination by MDM2.
Interacts with PRKCG.
Interacts with PPIF; the association implicates preferentially tetrameric TP53, is induced by oxidative stress and is impaired by cyclosporin A (CsA).
Interacts with SNAI1; the interaction induces SNAI1 degradation via MDM2-mediated ubiquitination and inhibits SNAI1-induced cell invasion.
Interacts with KAT6A.
Interacts with UBC9.
Interacts with ZNF385B; the interaction is direct.
Interacts (via DNA-binding domain) with ZNF385A; the interaction is direct and enhances p53/TP53 transactivation functions on cell-cycle arrest target genes, resulting in growth arrest (By similarity).
Interacts with ANKRD2.
Interacts with RFFL and RNF34; involved in p53/TP53 ubiquitination.
Interacts with MTA1 and COP1.
Interacts with CCAR2 (via N-terminus).
Interacts with MORC3.
Interacts (via C-terminus) with POU4F2 (via C-terminus).
Interacts (via oligomerization region) with NOP53; the interaction is direct and may prevent the MDM2-mediated proteasomal degradation of TP53.
Interacts with AFG1L; mediates mitochondrial translocation of TP53.
Interacts with UBD (By similarity).
Interacts with TAF6 (By similarity).
Interacts with C10orf90/FATS; the interaction inhibits binding of TP53 and MDM2 (By similarity).
Interacts with NUPR1; interaction is stress-dependent.
Forms a complex with EP300 and NUPR1; this complex binds CDKN1A promoter leading to transcriptional induction of CDKN1A (By similarity).
Interacts with PRMT5 in response to DNA damage; the interaction is STRAP dependent (By similarity).
Interacts with PPP1R13L (via SH3 domain and ANK repeats); the interaction inhibits pro-apoptotic activity of p53/TP53 (By similarity).
Interacts with PPP1R13B/ASPP1 and TP53BP2/ASPP2; the interactions promotes pro-apototic activity (By similarity).
By similaritySites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 113 | Interaction with DNABy similarity | 1 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 314 | Interaction with CCAR2By similarityAdd BLAST | 314 | |
Regioni | 1 – 45 | Transcription activation (acidic)By similarityAdd BLAST | 45 | |
Regioni | 59 – 103 | Interaction with WWOXBy similarityAdd BLAST | 45 | |
Regioni | 93 – 364 | Interaction with HIPK1By similarityAdd BLAST | 272 | |
Regioni | 93 – 294 | Required for interaction with ZNF385ABy similarityAdd BLAST | 202 | |
Regioni | 106 – 230 | Required for interaction with FBXO42By similarityAdd BLAST | 125 | |
Regioni | 109 – 286 | Interaction with AXIN1By similarityAdd BLAST | 178 | |
Regioni | 250 – 288 | Interaction with E4F1By similarityAdd BLAST | 39 | |
Regioni | 267 – 274 | Interaction with DNABy similarity | 8 | |
Regioni | 313 – 354 | Interaction with HIPK2By similarityAdd BLAST | 42 | |
Regioni | 319 – 350 | OligomerizationBy similarityAdd BLAST | 32 | |
Regioni | 353 – 357 | Interaction with USP7By similarity | 5 | |
Regioni | 362 – 381 | Basic (repression of DNA-binding)By similarityAdd BLAST | 20 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 299 – 315 | Bipartite nuclear localization signalBy similarityAdd BLAST | 17 | |
Motifi | 333 – 344 | Nuclear export signalBy similarityAdd BLAST | 12 | |
Motifi | 364 – 366 | [KR]-[STA]-K motif | 3 |
Domaini
Sequence similaritiesi
Family and domain databases
CDDi | cd08367 P53, 1 hit |
Gene3Di | 2.60.40.720, 1 hit 4.10.170.10, 1 hit |
InterProi | View protein in InterPro IPR008967 p53-like_TF_DNA-bd IPR012346 p53/RUNT-type_TF_DNA-bd_sf IPR011615 p53_DNA-bd IPR036674 p53_tetramer_sf IPR010991 p53_tetrameristn IPR013872 p53_transactivation_domain IPR002117 p53_tumour_suppressor |
PANTHERi | PTHR11447 PTHR11447, 1 hit |
Pfami | View protein in Pfam PF00870 P53, 1 hit PF08563 P53_TAD, 1 hit PF07710 P53_tetramer, 1 hit |
PRINTSi | PR00386 P53SUPPRESSR |
SUPFAMi | SSF47719 SSF47719, 1 hit SSF49417 SSF49417, 1 hit |
PROSITEi | View protein in PROSITE PS00348 P53, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
10 20 30 40 50
MEESQAELGV EPPLSQETFS DLWKLLPENN LLSSELSPAV DDLLLSPEDV
60 70 80 90 100
ANWLDERPDE APQMPEPPAP AAPTPAAPAP ATSWPLSSFV PSQKTYPGSY
110 120 130 140 150
GFHLGFLHSG TAKSVTCTYS PALNKLFCQL AKTCPVQLWV SSPPPPGTRV
160 170 180 190 200
RAMAIYKKSE YMTEVVRRCP HHERCSDYSD GLAPPQHLIR VEGNLRAEYL
210 220 230 240 250
DDRNTFRHSV VVPYEPPEVG SDCTTIHYNF MCNSSCMGGM NRRPILTIIT
260 270 280 290 300
LEDSNGNLLG RNSFEVRVCA CPGRDRRTEE ENFHKKGQSC PELPTGSAKR
310 320 330 340 350
ALPTGTSSSP PQKKKPLDGE YFTLQIRGRE RFEMFRELNE ALELKDAQAG
360 370 380
KEPGESRAHS SHLKSKKGQS PSRHKKLMFK REGPDSD
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A2Y9Q793 | A0A2Y9Q793_DELLE | Cellular tumor antigen p53 | TP53 | 387 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF475081 mRNA Translation: AAL83290.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF475081 mRNA Translation: AAL83290.1 |
3D structure databases
SMRi | Q8SPZ3 |
ModBasei | Search... |
Proteomic databases
PRIDEi | Q8SPZ3 |
Family and domain databases
CDDi | cd08367 P53, 1 hit |
Gene3Di | 2.60.40.720, 1 hit 4.10.170.10, 1 hit |
InterProi | View protein in InterPro IPR008967 p53-like_TF_DNA-bd IPR012346 p53/RUNT-type_TF_DNA-bd_sf IPR011615 p53_DNA-bd IPR036674 p53_tetramer_sf IPR010991 p53_tetrameristn IPR013872 p53_transactivation_domain IPR002117 p53_tumour_suppressor |
PANTHERi | PTHR11447 PTHR11447, 1 hit |
Pfami | View protein in Pfam PF00870 P53, 1 hit PF08563 P53_TAD, 1 hit PF07710 P53_tetramer, 1 hit |
PRINTSi | PR00386 P53SUPPRESSR |
SUPFAMi | SSF47719 SSF47719, 1 hit SSF49417 SSF49417, 1 hit |
PROSITEi | View protein in PROSITE PS00348 P53, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | P53_DELLE | |
Accessioni | Q8SPZ3Primary (citable) accession number: Q8SPZ3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 20, 2005 |
Last sequence update: | June 1, 2002 | |
Last modified: | October 16, 2019 | |
This is version 138 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families