p53

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For the band and album of the same name, see P53 (band) and P53 (album).

Tumor protein p53

PDB rendering based on 1TUP.

[show]Available structures
Identifiers
Symbols TP53; LFS1; TRP53; p53
External OMIM: 191170 MGI: 98834 HomoloGene: 460
IDs GeneCards: TP53 Gene
[show]Gene Ontology
RNA expression pattern
 More reference expression data
Orthologs
Species Human Mouse
Entrez 7157 22059
Ensembl ENSG00000141510 ENSMUSG00000059552
UniProt P04637 O70366
RefSeq
NM_000546 NM_011640
(mRNA)
RefSeq
NP_000537 NP_035770
(protein)
Location Chr 17: Chr 11:
(UCSC) 7.51 - 7.53 Mb 69.4 - 69.41 Mb
PubMed
[1] [2]
search

p53 (also known as protein 53 or tumor protein 53), is a tumor suppressor protein that in
humans is encoded by the TP53 gene.[1][2][3][4] p53 is important in multicellular organisms, where
it regulates the cell cycle and, thus, functions as a tumor suppressor that is involved in preventing
cancer. As such, p53 has been described as "the guardian of the genome", the "guardian angel
gene", and the "master watchman", referring to its role in conserving stability by preventing
genome mutation.[5]

The name p53 is in reference to its apparent molecular mass: It runs as a 53-kilodalton (kDa)
protein on SDS-PAGE. But, based on calculations from its amino acid residues, p53's mass is
actually only 43.7 kDa. This difference is due to the high number of proline residues in the
protein, which slow its migration on SDS-PAGE, thus making it appear heavier than it actually
is.[6] This effect is observed with p53 from a variety of species, including humans, rodents, frogs,
and fish.

Contents
[hide]
 • 1 Nomenclature
• 2 Gene
• 3 Structure
• 4 Function
• 5 Regulation
• 6 Role in disease
• 7 Discovery
• 8 Interactions
• 9 References
• 10 Additional images

• 11 External links

[edit] Nomenclature
p53 is also known as:

• UniProt name: Cellular tumor antigen p53

• Antigen NY-CO-13
• Phosphoprotein p53
• Transformation-related protein 53 (TRP53)
• Tumor suppressor p53

[edit] Gene
In humans, p53 is encoded by the TP53 gene located on the short arm of chromosome 17
(17p13.1).[1][2][3][4] The gene spans 20 kb, with a non-coding exon 1 and a very long first intron of
10 kb.The coding sequence contains five regions showing a high degree of conservation in
vertebrates, predominantly in exons 2, 5, 6, 7 and 8, but the sequences found in invertebrates
show only distant resemblance to mammalian TP53.[7] TP53 orthologs [8] have been identified in
most mammals for which complete genome data are available.

In humans, the two most common polymorphisms to occur involve the substitution of an
Arginine base for a Proline base. This polymorphism arises out of a SNP mutation on the 72
codon, where a guanine base is replaced by a cytosine.[9]

For these mammals, the gene is located on different chromosomes:

• Chimp and orangutan, chromosome 17

• Macaque, chromosome 16
• Mouse, chromosome 11
• Rat, chromosome 10
• Dog, chromosome 5
• Cow, chromosome 19
 • Pig, chromosome 12
• Horse, chromosome 11
• Opossum, chromosome 2

(Italics are used to denote the TP53 gene name and distinguish it from the protein it encodes.)

[edit] Structure
Human p53 is 393 amino acids long and has seven domains:

1. an acidic N-terminus transcription-activation domain (TAD), also known as activation

domain 1 (AD1), which activates transcription factors: residues 1-42. The N-terminus
contains two complementary transcriptional activation domains, with a major one at
residues 1–42 and a minor one at residues 55–75, specifically involved in the regulation
of several pro-apoptotic genes.[10]
2. activation domain 2 (AD2) important for apoptotic activity: residues 43-63.
3. Proline rich domain important for the apoptotic activity of p53: residues 64-92.
4. central DNA-binding core domain (DBD). Contains one zinc atom and several arginine
amino acids: residues 100-300.
5. nuclear localization signaling domain, residues 316-325.
6. homo-oligomerisation domain (OD): residues 307-355. Tetramerization is essential for
the activity of p53 in vivo.
7. C-terminal involved in downregulation of DNA binding of the central domain: residues
356-393.[11]

A tandem of nine-amino-acid transactivation domains (9aaTAD) was identified in the AD1 and
AD2 regions of transcription factor p53.[12] KO mutations and position for p53 interaction with
TFIID are listed below:[13]

9aaTADs mediate p53 interaction with general coactivators - TAF9, CBP/p300 (all four domains
KIX, TAZ1, TAZ2 and IBiD), GCN5 and PC4, regulatory protein MDM2 and replication protein
A (RPA).[14][15]
Mutations that deactivate p53 in cancer usually occur in the DBD. Most of these mutations
destroy the ability of the protein to bind to its target DNA sequences, and thus prevents
transcriptional activation of these genes. As such, mutations in the DBD are recessive loss-of-
function mutations. Molecules of p53 with mutations in the OD dimerise with wild-type p53, and
prevent them from activating transcription. Therefore OD mutations have a dominant negative
effect on the function of p53.

Wild-type p53 is a labile protein, comprising folded and unstructured regions that function in a
synergistic manner.[16]

[edit] Function
p53 has many anticancer mechanisms, and plays a role in apoptosis, genetic stability, and
inhibition of angiogenesis. In its anti-cancer role, p53 works through several mechanisms:

• It can activate DNA repair proteins when DNA has sustained damage.
• It can induce growth arrest by holding the cell cycle at the G1/S regulation point on DNA
damage recognition (if it holds the cell here for long enough, the DNA repair proteins
will have time to fix the damage and the cell will be allowed to continue the cell cycle).
• It can initiate apoptosis, the programmed cell death, if DNA damage proves to be
irreparable.
p53 pathway: In a normal cell p53 is inactivated by its negative regulator, mdm2. Upon DNA
damage or other stresses, various pathways will lead to the dissociation of the p53 and mdm2
complex. Once activated, p53 will induce a cell cycle arrest to allow either repair and survival of
the cell or apoptosis to discard the damaged cell. How p53 makes this choice is currently
unknown.

Activated p53 binds DNA and activates expression of several genes including WAF1/CIP1
encoding for p21. p21 (WAF1) binds to the G1-S/CDK (CDK2) and S/CDK complexes
(molecules important for the G1/S transition in the cell cycle) inhibiting their activity.

When p21(WAF1) is complexed with CDK2 the cell cannot continue to the next stage of cell
division. A mutant p53 will no longer bind DNA in an effective way, and, as a consequence, the
p21 protein will not be available to act as the "stop signal" for cell division. Thus, cells will
divide uncontrollably, and form tumors.[17]

Recent research has also linked the p53 and RB1 pathways, via p14ARF, raising the possibility
that the pathways may regulate each other.[18]

p53 by regulating LIF has been shown to facilitate implantation in the mouse model and possibly
in humans.[19]

p53 expression can be stimulated by UV light, which also causes DNA damage. In this case, p53
can initiate events leading to tanning.[20][21]

[edit] Regulation
p53 becomes activated in response to a myriad of stress types, which include but are not limited
to DNA damage (induced by either UV, IR, or chemical agents such as hydrogen peroxide),
oxidative stress,[22] osmotic shock, ribonucleotide depletion, and deregulated oncogene
expression. This activation is marked by two major events. First, the half-life of the p53 protein
is increased drastically, leading to a quick accumulation of p53 in stressed cells. Second, a
conformational change forces p53 to be activated as a transcription regulator in these cells. The
critical event leading to the activation of p53 is the phosphorylation of its N-terminal domain.
The N-terminal transcriptional activation domain contains a large number of phosphorylation
sites and can be considered as the primary target for protein kinases transducing stress signals.

The protein kinases that are known to target this transcriptional activation domain of p53 can be
roughly divided into two groups. A first group of protein kinases belongs to the MAPK family
(JNK1-3, ERK1-2, p38 MAPK), which is known to respond to several types of stress, such as
membrane damage, oxidative stress, osmotic shock, heat shock, etc. A second group of protein
kinases (ATR, ATM, CHK1 and CHK2, DNA-PK, CAK) is implicated in the genome integrity
checkpoint, a molecular cascade that detects and responds to several forms of DNA damage
caused by genotoxic stress. Oncogenes also stimulate p53 activation, mediated by the protein
p14ARF.

In unstressed cells, p53 levels are kept low through a continuous degradation of p53. A protein
called Mdm2 (also called HDM2 in humans), which is itself a product of p53, binds to p53,
preventing its action and transports it from the nucleus to the cytosol. Also Mdm2 acts as
ubiquitin ligase and covalently attaches ubiquitin to p53 and thus marks p53 for degradation by
the proteasome. However, ubiquitylation of p53 is reversible. A ubiquitin specific protease,
USP7 (or HAUSP), can cleave ubiquitin off p53, thereby protecting it from proteasome-
dependent degradation. This is one means by which p53 is stabilized in response to oncogenic
insults.

Phosphorylation of the N-terminal end of p53 by the above-mentioned protein kinases disrupts
Mdm2-binding. Other proteins, such as Pin1, are then recruited to p53 and induce a
conformational change in p53, which prevents Mdm2-binding even more. Phosphorylation also
allows for binding of transcriptional coactivators, like p300 or PCAF, which then acetylate the
carboxy-terminal end of p53, exposing the DNA binding domain of p53, allowing it to activate
or repress specific genes. Deacetylase enzymes, such as Sirt1 and Sirt7, can deacetylate p53,
leading to an inhibition of apoptosis.[23] Some oncogenes can also stimulate the transcription of
proteins that bind to MDM2 and inhibit its activity.

[edit] Role in disease

Overview of signal transduction pathways involved in apoptosis.

A micrograph showing cells with abnormal p53 expression (brown) in a brain tumour. p53
immunostain.

If the TP53 gene is damaged, tumor suppression is severely reduced. People who inherit only
one functional copy of the TP53 gene will most likely develop tumors in early adulthood, a
disease known as Li-Fraumeni syndrome. The TP53 gene can also be damaged in cells by
mutagens (chemicals, radiation, or viruses), increasing the likelihood that the cell will begin
decontrolled division. More than 50 percent of human tumors contain a mutation or deletion of
the TP53 gene.[24] Increasing the amount of p53, which may initially seem a good way to treat
tumors or prevent them from spreading, is in actuality not a usable method of treatment, since it
can cause premature aging.[25] However, restoring endogenous p53 function holds a lot of
promise.[26] Loss of p53 creates genomic instability that most often results in the aneuploidy
phenotype.[27]

Certain pathogens can also affect the p53 protein that the TP53 gene expresses. One such
example, human papillomavirus (HPV), encodes a protein, E6, which binds the p53 protein and
inactivates it. This, in synergy with the inactivation of another cell cycle regulator, pRb, by the
HPV protein E7, allows for repeated cell division manifested in the clinical disease of warts.
Certain HPV types, in particular types 16 and 18, can also lead to progression from a benign wart
to low or high-grade cervical dysplasia, which are reversible forms of precancerous lesions.
Persistent infection of the cervix over the years can cause irreversible changes leading to
carcinoma in situ and eventually invasive cervical cancer. This results from the effects of HPV
genes, particularly those encoding E6 and E7, which are the two viral oncoproteins that are
preferentially retained and expressed in cervical cancers by integration of the viral DNA into the
host genome.[28]

In healthy humans, the p53 protein is continually produced and degraded in the cell. The
degradation of the p53 protein is, as mentioned, associated with MDM2 binding. In a negative
feedback loop, MDM2 is itself induced by the p53 protein. However, mutant p53 proteins often
do not induce MDM2, and are thus able to accumulate at very high concentrations. Worse,
mutant p53 protein itself can inhibit normal p53 protein levels.

[edit] Discovery
p53 was identified in 1979 by Lionel Crawford, David P. Lane, Arnold Levine, and Lloyd Old,
working at Imperial Cancer Research Fund (UK) Princeton University/UMDNJ (Cancer Institute
of New Jersey), and Sloan-Kettering Memorial Hospital, respectively. It had been hypothesized
to exist before as the target of the SV40 virus, a strain that induced development of tumors. The
TP53 gene from the mouse was first cloned by Peter Chumakov of the Russian Academy of
Sciences in 1982,[29] and independently in 1983 by Moshe Oren in collaboration with David
Givol (Weizmann Institute of Science).[30][31] The human TP53 gene was cloned in 1984[1] and the
full length clone in 1985.[32]

It was initially presumed to be an oncogene due to the use of mutated cDNA following
purification of tumour cell mRNA. Its character as a tumor suppressor gene was finally revealed
in 1989 by Bert Vogelstein working at Johns Hopkins School of Medicine.[33]

Warren Maltzman, of the Waksman Institute of Rutgers University first demonstrated that TP53
was responsive to DNA damage in the form of ultraviolet radiation.[34] In a series of publications
in 1991-92, Michael Kastan, Johns Hopkins University, reported that TP53 was a critical part of
a signal transduction pathway that helped cells respond to DNA damage.[35]

In 1992, Wafik El-Deiry when he was working with Bert Vogelstein at Johns Hopkins
University identified the consensus sequence, to which human p53 could bind, by
immunoprecipitating human genomic DNA that could be bound by baculovirus-produced human
p53 protein. This sequence was published in the first issue of the journal Nature Genetics in 1992
in work that is highly cited. The consensus sequence is 5'-RRRCWWGYYY-N(0-13)-
RRRCWWGYYY-3' and is located in the regulatory regions of genes that are activated by the
p53 transcription factor. The presence of p53 response elements in or around genes (promoters,
upstream sequences, introns) is a powerful predictor of regulation and activation of a particular
gene by p53.

In 1993, p53 was voted molecule of the year by Science magazine.[36]

That same year, 1993, Wafik El-Deiry when he was working with Bert Vogelstein at Johns
Hopkins University discovered p21(WAF1) as a gene regulated directly by p53. This work was
reported in the most highly cited paper ever published in the journal Cell, and provided a
molecular mechanism by which mammalian cells undergo growth arrest when damaged. The
p21(WAF1) protein binds directly to cyclin-CDK complexes that drive forward the cell cycle
and inhibits their kinase activity thereby causing cell cycle arrest to allow repair to take place.
p21 can also mediate growth arrest associated with differentiation and a more permanent growth
arrest associated with cellular senescence. The p21 gene contains several p53 response elements
that mediate direct binding of the p53 protein, resulting in transcriptional activation of the gene
encoding the p21(WAF1) protein.

[edit] Interactions
p53 has been shown to interact with

• ANKRD2[37]
• Aprataxin[38]
• Ataxia telangiectasia and Rad3 related[39][40]
• Ataxia telangiectasia mutated[39][40][41][42][43]
• ATF3,[44][45]
• Aurora A kinase[46]
• BAK1[47]
• BARD1[48]
• Bloom syndrome protein[49][50][51][52]
• BRCA1[48][53][54][55][56]
• BRCA2[48][57]
• BRCC3[48]
• BRE[48]
• CCAAT/enhancer binding protein zeta[58]
• CDC14A[59]
• Cdk1[60][61]
• CFLAR[62]
• CHEK1[49][63][64] CCNG1,[65]
• CREB-binding protein[66][67][68]
• CREB1[68]
• Cyclin H[69]
• Cyclin-dependent kinase 7[69][70]
• DNA-PKcs[40][63][71]
• E4F1[72][73]
• EFEMP2[74]
• EP300[67][75][76][77]
• ERCC6[78][79]
• GNL3[80]
• GPS2[81]
• GSK3B[82]
• Heat shock protein 90kDa alpha (cytosolic), member A1[83][84][85]
• HIF1A[86][87][88][89]
• HIPK1[90]
• HIPK2[91][92]
• HMGB1[93][94]
• HSPA9[95]
• Huntingtin[96]
• ING1[97][98]
• ING4[99][100]
• ING5[99] ELL,[101]
• IκBα[102]
• KPNB1[83]
• Mdm2[66][103][104][105]
• MDM4[106][107]
• MED1[108][109]
• Mitogen-activated protein kinase 9[110][111]
• MNAT1[70]
• Multisynthetase complex auxiliary component p38[112]
• NDN[113]
• Nucleolin[114]
• NUMB[115]
• P16[72][116][105]
• PARC[117]
• PARP1[38][118]
• PIAS1[74][119] CDC14B[59]
• PIN1[120][121]
• PLAGL1[122]
• PLK3[123][124]
• PRKRA[125]
• Prohibitin[126]
• Promyelocytic leukemia protein[103][127][128]
• Protein kinase R[129]
• PSME3[130]
• PTEN[104]
• PTK2[131]
• PTTG1[132]
• RAD51[48][133][134]
• RCHY1[135][136]
• Replication protein A1[137][138]
• RPL11[116]
• S100B,[139]
• Small ubiquitin-related modifier 1[140][141]
• SMARCA4,[142]
• SMARCB1[142]
• SMN1[143]
• TATA binding protein[144][145]
• TFAP2A[146]
• TFDP1[147]
• TOP1[148][149]
• TOP2A[150]
• TP53BP1[49][151][152][153][154][155][156]
• TP53BP2,[156][157] TOP2B,[150]
 • TP53INP1[158][159]
• TSG101[160]
• UBE2A[161]
• UBE2I[74][140][162][163]
• Ubiquitin C[130][112][141][164][165][166][167][168]
• USP7[169]
• Werner syndrome ATP-dependent helicase[52][170]
• WWOX[171]
• XPB[78]
• Y box binding protein 1[37][172]
• YWHAZ[173]
• Zif268[174]
• ZNF148[175]

[edit] References
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