P41685

SS
Gene name
TP53 (TRP53)
Protein name
Cellular tumor antigen p53
Names
Tumor suppressor p53
Species
Felis catus (Cat) (Felis silvestris catus)
KEGG Pathway
fca:493847
EC number
Protein Class

Descriptions

The p53 protein contains several functional domains: N-terminal transactivation domains (TAD), a proline-rich domain (PRD), a DNA-binding domain (DBD), a nuclear localization signal, a tetramerization domain (TET), and a C-terminal regulatory domain.<br>Phosphorylation within TAD2 domain inhibits DNA-binding of p53 by enhancing competitive interactions between the transactivation domain 2 (TAD2) and DBD. Deletion of the PRD strengthens the TAD2–DBD interaction and leads to autoinhibition of DNA binding even withouth the phosphorylation within TAD2 domain. In addition, the C-terminal regulatory domain of p53 interacts with the core DNA-binding domain and locks the DNA-binding domain into an inactive conformation. p300-mediated acetylation of specific lysine residues in the C-terminus of p53 disrupts the interaction between the C-terminal domain and the DNA-binding domain, thus allowing the DNA-binding domain to adopt an active conformation. Additionally, acetylation of specific lysine residues within the C-terminus of p53 can disrupt the autoinhibition and activate p53, allowing it to function as a transcription factor and regulate genes involved in cell cycle control and DNA repair.

Autoinhibitory domains (AIDs)

47-55 (TAD2 domain) SS

Target domain

83-285 (DBD domain)

Relief mechanism

PTM

Assay

61-82 (Proline-rich domain) SS

Target domain

83-285 (DBD domain)

Relief mechanism

PTM

Assay

356-386 (C-terminal regulatory domain) SS

Target domain

83-285 (DBD domain)

Relief mechanism

PTM

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P41685

Entry ID Method Resolution Chain Position Source
AF-P41685-F1 Predicted AlphaFoldDB

No variants for P41685

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P41685

1 associated diseases with P41685

Without disease ID

3 regional properties for P41685

Type Name Position InterPro Accession
domain p53, tetramerisation domain 312 - 350 IPR010991
domain p53, DNA-binding domain 92 - 282 IPR011615
domain p53 transactivation domain 6 - 30 IPR013872

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Nucleus
  • Nucleus, PML body
  • Endoplasmic reticulum
  • Mitochondrion matrix
  • Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
  • Interaction with BANP promotes nuclear localization
  • Recruited into PML bodies together with CHEK2
  • Translocates to mitochondria upon oxidative stress (By similarity)
  • Translocates to mitochondria in response to mitomycin C treatment (By similarity)
  • Competitive inhibition of TP53 interaction with HSPA9/MOT-2 by UBXN2A results in increased protein abundance and subsequent translocation of TP53 to the nucleus (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

8 GO annotations of cellular component

Name Definition
centrosome A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
PML body A class of nuclear body; they react against SP100 auto-antibodies (PML, promyelocytic leukemia); cells typically contain 10-30 PML bodies per nucleus; alterations in the localization of PML bodies occurs after viral infection.

6 GO annotations of molecular function

Name Definition
ATP-dependent DNA/DNA annealing activity An ATP-dependent activity that facilitates the formation of a complementary double-stranded DNA molecule.
copper ion binding Binding to a copper (Cu) ion.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA-binding transcription factor activity, RNA polymerase II-specific A DNA-binding transcription factor activity that modulates the transcription of specific gene sets transcribed by RNA polymerase II.
promoter-specific chromatin binding Binding to a section of chromatin that is associated with gene promoter sequences of DNA.
RNA polymerase II cis-regulatory region sequence-specific DNA binding Binding to a specific upstream regulatory DNA sequence (transcription factor recognition sequence or binding site) located in cis relative to the transcription start site (i.e., on the same strand of DNA) of a gene transcribed by RNA polymerase II.

14 GO annotations of biological process

Name Definition
cell cycle The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division.
cellular senescence A cell aging process stimulated in response to cellular stress, whereby normal cells lose the ability to divide through irreversible cell cycle arrest.
circadian behavior The specific behavior of an organism that recurs with a regularity of approximately 24 hours.
DNA damage response Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
entrainment of circadian clock by photoperiod The synchronization of a circadian rhythm to photoperiod, the intermittent cycle of light (day) and dark (night).
negative regulation of cell growth Any process that stops, prevents, or reduces the frequency, rate, extent or direction of cell growth.
negative regulation of DNA-templated transcription Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription.
nucleotide-excision repair A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
oligodendrocyte apoptotic process Any apoptotic process in an oligodendrocyte. Oligodendrocytes belong to a class of large neuroglial (macroglial) cells in the central nervous system, where they form the insulating myelin sheath of axons.
positive regulation of apoptotic process Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
positive regulation of intrinsic apoptotic signaling pathway Any process that activates or increases the frequency, rate or extent of intrinsic apoptotic signaling pathway.
positive regulation of transcription by RNA polymerase II Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter.
protein tetramerization The formation of a protein tetramer, a macromolecular structure consisting of four noncovalently associated identical or nonidentical subunits.
regulation of transcription by RNA polymerase II Any process that modulates the frequency, rate or extent of transcription mediated by RNA polymerase II.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P04637 TP53 Cellular tumor antigen p53 Homo sapiens (Human) EV
P10361 Tp53 Cellular tumor antigen p53 Rattus norvegicus (Rat) PR
P56424 TP53 Cellular tumor antigen p53 Macaca mulatta (Rhesus macaque) SS
10 20 30 40 50 60
MQEPPLELTI EPPLSQETFS ELWNLLPENN VLSSELSSAM NELPLSEDVA NWLDEAPDDA
70 80 90 100 110 120
SGMSAVPAPA APAPATPAPA ISWPLSSFVP SQKTYPGAYG FHLGFLQSGT AKSVTCTYSP
130 140 150 160 170 180
PLNKLFCQLA KTCPVQLWVR SPPPPGTCVR AMAIYKKSEF MTEVVRRCPH HERCPDSSDG
190 200 210 220 230 240
LAPPQHLIRV EGNLHAKYLD DRNTFRHSVV VPYEPPEVGS DCTTIHYNFM CNSSCMGGMN
250 260 270 280 290 300
RRPIITIITL EDSNGKLLGR NSFEVRVCAC PGRDRRTEEE NFRKKGEPCP EPPPGSTKRA
310 320 330 340 350 360
LPPSTSSTPP QKKKPLDGEY FTLQIRGRER FEMFRELNEA LELKDAQSGK EPGGSRAHSS
370 380
HLKAKKGQST SRHKKPMLKR EGLDSD