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the 16th letter of the Roman alphabet (同)p

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parking
phosphorusの化学記号

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/06/19 13:11:42」(JST)

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p53遺伝子（ピー53いでんし）とは、一つ一つの細胞内でDNA修復や細胞増殖停止、アポトーシスなどの細胞増殖サイクルの抑制を制御する機能を持ち、細胞ががん化したときアポトーシスを起させるとされる。この遺伝子による機能が不全となるとがんが起こると考えられている、いわゆる癌抑制遺伝子の一つ。

p53のpはタンパク質（protein）、53は分子量53,000を意味しタンパクは393個のアミノ酸から構成されている。この遺伝子は進化的に保存されており、昆虫や軟体動物にも存在している。ただしそれらのアミノ酸一次配列はかなり多様化している。またパラログとしてp63やp73もある。RB遺伝子とともによく知られている。

細胞が、がん化するためには複数の癌遺伝子と癌抑制遺伝子の変化が必要らしいことが分かっているが、p53遺伝子は悪性腫瘍（癌）において最も高頻度に異常が認められている。p53は、細胞の恒常性の維持やアポトーシス誘導といった重要な役割を持つことからゲノムの守護者（The Guardian of the genome）とも表現されるが、染色体構造が変化する機構と、それらの細胞内での働き、そしてそれらが生物にとってどのように大切なのかについてはよくわかっていない。

遺伝子座

ヒトのp53遺伝子は、第17番染色体短腕上（17p13.1）に存在する。

歴史

遺伝子産物であるp53は、1979年に腫瘍ウイルスSV40の大型T抗原と結合するタンパク質として発見された。その後の研究によりp53遺伝子が癌抑制遺伝子であることが証明され脚光を浴びることになった。

p53遺伝子は単に癌の抑制にのみ関与しているのではないことが示唆されている。2002年、Tynerらは通常のマウス（p53+/+）とp53が通常よりも活性化している変異マウス（p53+/m）を比較したところ、変異マウスでは癌の発生率は低かったものの組織の老化が早く寿命が短かったことを報告した^[2]。

機能

p53タンパク質は転写因子として働き、GADD45（英語版）、PPM1D、MDM2、p21CIP1/WAF1、BAX（英語版）、14-3-3δ（英語版）など多くの遺伝子群の発現に関与し多彩な生理機能を持つ。

損傷を受けたDNAの修復タンパク質の活性化
細胞周期の制御
DNAが修復不可能な損傷を受けた場合に、細胞の自殺であるアポトーシスを誘導

変異

半数以上の悪性腫瘍においてp53遺伝子の変異や欠失が認められる。変異の多くは点変異である。何らかの原因でp53遺伝子が損傷を受けると、細胞にアポトーシスが誘導されにくくなる。例えば、肺癌ではタバコに含まれるベンゾピレンという発癌物質によりp53遺伝子の変異が起こっている。また、肝細胞癌の原因の1つであるピーナッツに生えるカビが産生するアフラトキシンという物質は、p53遺伝子の249番目の塩基に点変異を多く引き起こす。

p53遺伝子の変異は抗p53抗体の出現と相関がみられる。日本では抗p53抗体測定は食道癌、大腸癌および乳癌が疑われる際に2007年11月より保険適応が認められた。

遺伝子治療

p53遺伝子の多彩な機能を利用して、癌の治療に応用しようとする試みがなされている。特によく研究がなされているのは、アデノウイルスなどのベクターを用いて癌細胞へp53遺伝子を導入する治療である。p53遺伝子に変異がある場合には、通常ではアポトーシスが起こるようなDNA障害が生じても細胞死が起こりにくい。このため、一般的にはp53遺伝子に変異を持つ癌では薬剤や放射線などの治療に抵抗性が存在する。遺伝子治療による癌細胞へのアポトーシスの誘導や、化学療法や放射線治療の効果の増強が期待されている。

Li-Fraumeni症候群

Li-Fraumeni症候群（リ・フラウメニ症候群）は家系内に脳腫瘍、乳癌、白血病や肉腫などの様々な癌が多発する稀な遺伝疾患である。p53遺伝子の変異が原因で起こる。病名は発見者Frederick P. LiとJoseph F. Fraumeni, Jrに因む。

脚注

^ Cho Y, Gorina S, Jeffrey PD, Pavletich NP (1994). "Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations". Science 265 (5170): 346–355. doi:10.1126/science.8023157. PMID 8023157.
^ Tyner SD, Venkatachalam S, Choi J, Jones S, Ghebranious N, Igelmann H, Lu X, Soron G, Cooper B, Brayton C, Park SH, Thompson T, Karsenty G, Bradley A, Donehower LA (2002). "p53 mutant mice that display early ageing-associated phenotypes". Nature 415 (6867): 45–53. doi:10.1038/415045a. PMID 11780111.

外部リンク

ウィキメディア・コモンズには、P53遺伝子に関連するカテゴリがあります。

がん抑制遺伝子ｐ５３の新しい制御機構を発見(九州大学ホームページ)
The p53 web site

wiki en

[Wiki en表示]

Tumor protein p53, also known as p53, cellular tumor antigen p53 (UniProt name), phosphoprotein p53, tumor suppressor p53, antigen NY-CO-13, or transformation-related protein 53 (TRP53), is any isoform of a protein encoded by homologous genes in various organisms, such as TP53 (humans) and Trp53 (mice). This homolog (originally thought to be, and often spoken of as, a single protein) is crucial in multicellular organisms, where it prevents cancer formation, thus, functions as a tumor suppressor.^[2] As such, p53 has been described as "the guardian of the genome" because of its role in conserving stability by preventing genome mutation.^[3] Hence TP53 is classified as a tumor suppressor gene.^[4]^[5]^[6]^[7]^[8] The name p53 was given in 1979 describing the apparent molecular mass; SDS-PAGE analysis indicates that it is a 53-kilodalton (kDa) protein. However, the actual mass of the full length p53 protein (p53α) based on the sum of masses of the amino acid residues is 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.^[9] In addition to the full length protein, the human TP53 gene encodes at least 15 protein isoforms, ranging in size from 3.5 to 43.7 kDa. All these p53 proteins are called the p53 isoforms.^[2] The International Cancer Genome Consortium has established that the TP53 gene is the most frequently mutated gene (>50%) in human cancer, indicating that the TP53 gene plays a crucial role in preventing cancer formation.^[2] TP53 gene encodes proteins that bind to DNA and regulate gene expression to prevent mutations of the genome.^[10]

Gene

In humans, the TP53 gene is located on the short arm of chromosome 17 (17p13.1).^[4]^[5]^[6]^[7] 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.^[11] TP53 orthologs^[12] have been identified in most mammals for which complete genome data are available.

In humans, a common polymorphism involves the substitution of an arginine for a proline at codon position 72. Many studies have investigated a genetic link between this variation and cancer susceptibility; however, the results have been controversial. For instance, a meta-analysis from 2009 failed to show a link for cervical cancer.^[13] A 2011 study found that the TP53 proline mutation did have a profound effect on pancreatic cancer risk among males.^[14] A study of Arab women found that proline homozygosity at TP53 codon 72 is associated with a decreased risk for breast cancer.^[15] One study suggested that TP53 codon 72 polymorphisms, MDM2 SNP309, and A2164G may collectively be associated with non-oropharyngeal cancer susceptibility and that MDM2 SNP309 in combination with TP53 codon 72 may accelerate the development of non-oropharyngeal cancer in women.^[16] A 2011 study found that TP53 codon 72 polymorphism was associated with an increased risk of lung cancer.^[17]

Meta-analyses from 2011 found no significant associations between TP53 codon 72 polymorphisms and both colorectal cancer risk^[18] and endometrial cancer risk.^[19] A 2011 study of a Brazilian birth cohort found an association between the non mutant arginine TP53 and individuals without a family history of cancer.^[20] Another 2011 study found that the p53 homozygous (Pro/Pro) genotype was associated with a significantly increased risk for renal cell carcinoma.^[21]

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

Structure

A schematic of the known protein domains in p53. (NLS = Nuclear Localization Signal).

Crystal structure of four p53 DNA binding domains (as found in the bioactive homo-tetramer) attand has seven domains:

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.^[22]
activation domain 2 (AD2) important for apoptotic activity: residues 43-63.
Proline rich domain important for the apoptotic activity of p53 by nuclear exportation via MAPK: residues 64-92.
central DNA-binding core domain (DBD). Contains one zinc atom and several arginine amino acids: residues 102-292. This region is responsible for binding the p53 co-repressor LMO3.^[23]
nuclear localization signaling domain, residues 316-325.
homo-oligomerisation domain (OD): residues 307-355. Tetramerization is essential for the activity of p53 in vivo.
C-terminal involved in downregulation of DNA binding of the central domain: residues 356-393.^[24]

A tandem of nine-amino-acid transactivation domains (9aaTAD) was identified in the AD1 and AD2 regions of transcription factor p53.^[25] KO mutations and position for p53 interaction with TFIID are listed below:^[26]

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).^[27]^[28]

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.^[29]

Function

p53 has many mechanisms of anticancer function, and plays a role in apoptosis, genomic 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. Thus, it may be an important factor in aging.^[30]
It can arrest growth 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 – 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 microRNA miR-34a,^[31] WAF1/CIP1 encoding for p21 and hundreds of other down-stream genes. p21 (WAF1) binds to the G1-S/CDK (CDK4/CDK6, CDK2, and CDK1) 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.^[32] Studies of human embryonic stem cells (hESCs) commonly describe the nonfunctional p53-p21 axis of the G1/S checkpoint pathway with subsequent relevance for cell cycle regulation and the DNA damage response (DDR). Importantly, p21 mRNA is clearly present and upregulated after the DDR in hESCs, but p21 protein is not detectable. In this cell type, p53 activates numerous microRNAs (like miR-302a, miR-302b, miR-302c, and miR-302d) that directly inhibit the p21 expression in hESCs.^[33]

Recent research has also linked the p53 and RB1 pathways, via p14ARF, raising the possibility that the pathways may regulate each other.^[34]

p53 by regulating LIF has been shown to facilitate implantation in the mouse model and possibly in humans.^[35]

p53 expression can be stimulated by UV light, which also causes DNA damage. In this case, p53 can initiate events leading to tanning.^[36]^[37]

Regulation

p53 becomes activated in response to myriad stressors, including but not limited to DNA damage (induced by either UV, IR, or chemical agents such as hydrogen peroxide), oxidative stress,^[38] 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, TP53RK) 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.

The novel molecule MI-63 binds to MDM2 making the action of p53 again possible in situations were p53's function has become inhibited.^[39]

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. USP42 has also been shown to deubiquitinate p53 and may be required for the ability of p53 to respond to stress.^[40]

Recent research has shown that HAUSP is mainly localized in the nucleus, though a fraction of it can be found in the cytoplasm and mitochondria. Overexpression of HAUSP results in p53 stabilization. However, depletion of HAUSP does not result to a decrease in p53 levels but rather increases p53 levels due to the fact that HAUSP binds and deubiquitinates Mdm2. It has been shown that HAUSP is a better binding partner to Mdm2 than p53 in unstressed cells.

USP10 however has been shown to be located in the cytoplasm in unstressed cells and deubiquitinates cyptoplasmic p53, reversing Mdm2 ubiquitination. Following DNA damage, USP10 translocates to the nucleus and contributes to p53 stability. Also USP10 does not interact with Mdm2.^[41]

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 and 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.^[42] Some oncogenes can also stimulate the transcription of proteins that bind to MDM2 and inhibit its activity.

Role in disease

Overview of signal transduction pathways involved in apoptosis.

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

If the TP53 gene is damaged, tumor suppression is severely compromised. People who inherit only one functional copy of the TP53 gene will most likely develop tumors in early adulthood, a disorder known as Li-Fraumeni syndrome.

The TP53 gene can also be modified by mutagens (chemicals, radiation, or viruses), increasing the likelihood for uncontrolled cell division. More than 50 percent of human tumors contain a mutation or deletion of the TP53 gene.^[43] Loss of p53 creates genomic instability that most often results in an aneuploidy phenotype.^[44]

Increasing the amount of p53 may seem a solution for treatment of tumors or prevention of their spreading. This, however, is not a usable method of treatment, since it can cause premature aging.^[45] Restoring endogenous normal p53 function holds some promise. Research has showed that this restoration can lead to regression of certain cancer cells without damaging other cells in the process. The ways by which tumor regression occurs depends mainly on the tumor type. For example, restoration of endogenous p53 function in lymphomas may induce apoptosis, while cell growth may be reduced to normal levels. Thus, pharmacological reactivation of p53 presents itself as a viable cancer treatment option.^[46]^[46]^[47] The first commercial gene therapy, Gendicine, was approved in China in 2003 for the treatment of head and neck squamous cell carcinoma. It delivers a functional copy of the p53 gene using an engineered adenovirus.^[48]

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 to the p53 protein and inactivates it. This mechanism, in synergy with the inactivation of the cell cycle regulator pRb by the HPV protein E7, allows for repeated cell division manifested clinically as 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.^[49]

The p53 protein is continually produced and degraded in cells of healthy people, resulting in damped oscillation. The degradation of the p53 protein is associated with binding of MDM2. In a negative feedback loop, MDM2 itself is induced by the p53 protein. Mutant p53 proteins often fail to induce MDM2, causing p53 to accumulate at very high levels. Moreover, the mutant p53 protein itself can inhibit normal p53 protein levels. In some cases, single missense mutations in p53 have been shown to disrupt p53 stability and function.^[50]

Experimental analysis of p53 mutations

Most p53 mutations are detected by DNA sequencing. However, it is known that single missense mutations can have a large spectrum from rather mild to very severe functional affects.^[50]

The large spectrum of cancer phenotypes due to mutations in the TP53 gene is also supported by the fact that different isoforms of p53 proteins have different cellular mechanisms for prevention against cancer. Mutations in TP53 can give rise to different isoforms, preventing their overall functionality in different cellular mechanisms and thereby extending the cancer phenotype from mild to severe. Recents studies show that p53 isoforms are differentially expressed in different human tissues, and the loss-of-function or gain-of-function mutations within the isoforms can cause tissue-specific cancer or provides cancer stem cell potential in different tissues.^[51]^[52]^[53]^[54]

The dynamics of p53 proteins, along with its antagonist Mdm2, indicate that the levels of p53, in units of concentration, oscillate as a function of time. This "damped" oscillation is both clinically documented ^[55] and mathematically modelled.^[56]^[57] Mathematical models also indicate that the p53 concentration oscillates much faster once teratogens, such as double-stranded breaks (DSB) or UV radiation, are introduced to the system. This supports and models the current understanding of p53 dynamics, where DNA damage induces p53 activation (see p53 regulation for more information). Current models can also be useful for modelling the mutations in p53 isoforms and their effects on p53 oscillation, thereby promoting de novo tissue-specific pharmacological drug discovery.

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 Memorial Sloan-Kettering Cancer Center, respectively. Independently, by Michel Kress and Pierre May, José A. Melero and Varda Rotter. 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,^[58] and independently in 1983 by Moshe Oren in collaboration with David Givol (Weizmann Institute of Science).^[59]^[60] The human TP53 gene was cloned in 1984^[4] and the full length clone in 1985.^[61]

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 at the Johns Hopkins School of Medicine.^[62]

Warren Maltzman, of the Waksman Institute of Rutgers University first demonstrated that TP53 was responsive to DNA damage in the form of ultraviolet radiation.^[63] 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.^[64]

In 1993, p53 was voted molecule of the year by Science magazine.^[65]

The p21 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 protein.

Isoforms

As 95% of human genes, TP53 encodes more than one protein. In 2005 several isoforms were discovered and until now, 12 human p53 isoforms were identified (p53α, p53β, p53γ, ∆40p53α, ∆40p53β, ∆40p53γ, ∆133p53α, ∆133p53β, ∆133p53γ, ∆160p53α, ∆160p53β, ∆160p53γ). Furthermore p53 isoforms are expressed in a tissue dependent manner and p53α is never expressed alone.^[8]

The full length p53 isoform proteins can be subdivided into different protein domains. Starting from the N-terminus, there are first the amino-terminal transactivation domains (TAD 1, TAD 2), which are needed to induce a subset of p53 target genes. This domain is followed by the Prolin rich domain (PXXP), whereby the motif PXXP is repeated (P is a Prolin and X can be any amino acid). It is required among others for p53 mediated apoptosis.^[66] Some isoforms lack the Proline rich domain, such as Δ133p53β,γ and Δ160p53α,β,γ; hence some isoforms of p53 are not mediating apoptosis, emphasizing the diversifying roles of the TP53 gene.^[67] Afterwards there is the DNA binding domain (DBD), which enables the proteins to sequence specific binding. The carboxyl terminal domain completes the protein. It includes the nuclear localization signal (NLS), the nuclear export signal (NES) and the oligomerisation domain (OD). The NLS and NES are responsible for the subcellular regulation of p53. Through the OD, p53 can form a tetramer and though bind to DNA. Among the isoforms, some domains can be missing, but all of them share most of the highly conserved DNA-binding domain.

The isoforms are formed by different mechanisms. The beta and the gamma isoforms are generated by multiple splicing of intron 9, which leads to a different C-terminus. Furthermore, the usage of an internal promoter in intron 4 causes the ∆133 and ∆160 isoforms, which leak the TAD domain and a part of the DBD. Moreover, alternative initiation of translation at codon 40 or 160 bear the ∆40p53 and ∆160p53 isoforms.^[8]

Due to the isoformic nature of p53 proteins, there has been several evidences showing that mutations within the TP53 gene giving rise to mutated isoforms are causative agents of various cancer phenotypes, from mild to severe, due to single mutation in the TP53 gene (refer to section Experimental Analysis of p53 mutations for more details).

Interactions

p53 has been shown to interact with:

AIMP2,^[68]
ANKRD2,^[69]
APTX,^[70]
ATM,^[71]^[72]^[73]^[74]^[75]
ATR,^[71]^[72]
ATF3,^[76]^[77]
AURKA,^[78]
BAK1,^[79]
BARD1,^[80]
BLM,^[81]^[82]^[83]^[84]
BRCA1,^[80]^[85]^[86]^[87]^[88]
BRCA2,^[80]^[89]
BRCC3,^[80]
BRE,^[80]
CEBPZ,^[90]
CDC14A,^[91]
Cdk1,^[92]^[93]
CFLAR,^[94]
CHEK1,^[81]^[95]^[96]
CCNG1,^[97]
CREBBP,^[98]^[99]^[100]
CREB1,^[100]
Cyclin H,^[101]
CDK7,^[101]^[102]
DNA-PKcs,^[72]^[95]^[103]
E4F1,^[104]^[105]
EFEMP2,^[106]
EIF2AK2,^[107]
ELL,^[108]
EP300,^[99]^[109]^[110]^[111]
ERCC6,^[112]^[113]
GNL3,^[114]
GPS2,^[115]
GSK3B,^[116]
HSP90AA1,^[117]^[118]^[119]
HIF1A,^[120]^[121]^[122]^[123]
HIPK1,^[124]
HIPK2,^[125]^[126]
HMGB1,^[127]^[128]
HSPA9,^[129]
Huntingtin,^[130]
ING1,^[131]^[132]
ING4,^[133]^[134]
ING5,^[133]
IκBα,^[135]
KPNB1,^[117]
LMO3,^[23]
Mdm2,^[98]^[136]^[137]^[138]
MDM4,^[139]^[140]
MED1,^[141]^[142]
MAPK9,^[143]^[144]
MNAT1,^[102]
NDN,^[145]
NCL,^[146]
NUMB,^[147]
NF-κB,^[148]
P16,^[104]^[138]^[149]
PARC,^[150]
PARP1,^[70]^[151]
PIAS1,^[106]^[152]
CDC14B,^[91]
PIN1,^[153]^[154]
PLAGL1,^[155]
PLK3,^[156]^[157]
PRKRA,^[158]
PHB,^[159]
PML,^[136]^[160]^[161]
PSME3,^[162]
PTEN,^[137]
PTK2,^[163]
PTTG1,^[164]
RAD51,^[80]^[165]^[166]
RCHY1,^[167]^[168]
RELA,^[148]
Reprimo
RPA1,^[169]^[170]
RPL11,^[149]
S100B,^[171]
SUMO1,^[172]^[173]
SMARCA4,^[174]
SMARCB1,^[174]
SMN1,^[175]
STAT3,^[148]
TBP,^[176]^[177]
TFAP2A,^[178]
TFDP1,^[179]
TIGAR,^[180]
TOP1,^[181]^[182]
TOP2A,^[183]
TP53BP1,^[81]^[184]^[185]^[186]^[187]^[188]^[189]
TP53BP2,^[189]^[190]
TOP2B,^[183]
TP53INP1,^[191]^[192]
TSG101,^[193]
UBE2A,^[194]
UBE2I,^[106]^[172]^[195]^[196]
UBC,^[68]^[162]^[173]^[197]^[198]^[199]^[200]^[201]
USP7,^[202]
WRN,^[84]^[203]
WWOX,^[204]
XPB,^[112]
YBX1,^[69]^[205]
YPEL3,^[206]
YWHAZ,^[207]
Zif268,^[208] and
ZNF148.^[209]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. ^{[§ 1]}

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|{{{bSize}}}px|alt=Fluorouracil (5-FU) Activity edit]]

File:FluoropyrimidineActivity_WP1601.png

Fluorouracil (5-FU) Activity edit

^ The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601".

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^ Gobert C, Skladanowski A, Larsen AK (Aug 1999). "The interaction between p53 and DNA topoisomerase I is regulated differently in cells with wild-type and mutant p53". Proceedings of the National Academy of Sciences of the United States of America 96 (18): 10355–60. doi:10.1073/pnas.96.18.10355. PMC 17892. PMID 10468612.
^ Mao Y, Mehl IR, Muller MT (Feb 2002). "Subnuclear distribution of topoisomerase I is linked to ongoing transcription and p53 status". Proceedings of the National Academy of Sciences of the United States of America 99 (3): 1235–40. doi:10.1073/pnas.022631899. PMC 122173. PMID 11805286.
^ ^a ^b Cowell IG, Okorokov AL, Cutts SA, Padget K, Bell M, Milner J et al. (Feb 2000). "Human topoisomerase IIalpha and IIbeta interact with the C-terminal region of p53". Experimental Cell Research 255 (1): 86–94. doi:10.1006/excr.1999.4772. PMID 10666337.
^ Derbyshire DJ, Basu BP, Serpell LC, Joo WS, Date T, Iwabuchi K et al. (Jul 2002). "Crystal structure of human 53BP1 BRCT domains bound to p53 tumour suppressor". The EMBO Journal 21 (14): 3863–72. doi:10.1093/emboj/cdf383. PMC 126127. PMID 12110597.
^ Ekblad CM, Friedler A, Veprintsev D, Weinberg RL, Itzhaki LS (Mar 2004). "Comparison of BRCT domains of BRCA1 and 53BP1: a biophysical analysis". Protein Science 13 (3): 617–25. doi:10.1110/ps.03461404. PMC 2286730. PMID 14978302.
^ Lo KW, Kan HM, Chan LN, Xu WG, Wang KP, Wu Z et al. (Mar 2005). "The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation". The Journal of Biological Chemistry 280 (9): 8172–9. doi:10.1074/jbc.M411408200. PMID 15611139.
^ Joo WS, Jeffrey PD, Cantor SB, Finnin MS, Livingston DM, Pavletich NP (Mar 2002). "Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure". Genes & Development 16 (5): 583–93. doi:10.1101/gad.959202. PMC 155350. PMID 11877378.
^ Derbyshire DJ, Basu BP, Date T, Iwabuchi K, Doherty AJ (Oct 2002). "Purification, crystallization and preliminary X-ray analysis of the BRCT domains of human 53BP1 bound to the p53 tumour suppressor". Acta Crystallographica. Section D, Biological Crystallography 58 (Pt 10 Pt 2): 1826–9. doi:10.1107/S0907444902010910. PMID 12351827.
^ ^a ^b Iwabuchi K, Bartel PL, Li B, Marraccino R, Fields S (Jun 1994). "Two cellular proteins that bind to wild-type but not mutant p53". Proceedings of the National Academy of Sciences of the United States of America 91 (13): 6098–102. doi:10.1073/pnas.91.13.6098. PMC 44145. PMID 8016121.
^ Naumovski L, Cleary ML (Jul 1996). "The p53-binding protein 53BP2 also interacts with Bc12 and impedes cell cycle progression at G2/M". Molecular and Cellular Biology 16 (7): 3884–92. PMC 231385. PMID 8668206.
^ Tomasini R, Samir AA, Carrier A, Isnardon D, Cecchinelli B, Soddu S et al. (Sep 2003). "TP53INP1s and homeodomain-interacting protein kinase-2 (HIPK2) are partners in regulating p53 activity". The Journal of Biological Chemistry 278 (39): 37722–9. doi:10.1074/jbc.M301979200. PMID 12851404.
^ Okamura S, Arakawa H, Tanaka T, Nakanishi H, Ng CC, Taya Y et al. (Jul 2001). "p53DINP1, a p53-inducible gene, regulates p53-dependent apoptosis". Molecular Cell 8 (1): 85–94. doi:10.1016/S1097-2765(01)00284-2. PMID 11511362.
^ Li L, Liao J, Ruland J, Mak TW, Cohen SN (Feb 2001). "A TSG101/MDM2 regulatory loop modulates MDM2 degradation and MDM2/p53 feedback control". Proceedings of the National Academy of Sciences of the United States of America 98 (4): 1619–24. doi:10.1073/pnas.98.4.1619. PMC 29306. PMID 11172000.
^ Lyakhovich A, Shekhar MP (Apr 2003). "Supramolecular complex formation between Rad6 and proteins of the p53 pathway during DNA damage-induced response". Molecular and Cellular Biology 23 (7): 2463–75. doi:10.1128/MCB.23.7.2463-2475.2003. PMC 150718. PMID 12640129.
^ Shen Z, Pardington-Purtymun PE, Comeaux JC, Moyzis RK, Chen DJ (Oct 1996). "Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system". Genomics 37 (2): 183–6. doi:10.1006/geno.1996.0540. PMID 8921390.
^ Bernier-Villamor V, Sampson DA, Matunis MJ, Lima CD (Feb 2002). "Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1". Cell 108 (3): 345–56. doi:10.1016/S0092-8674(02)00630-X. PMID 11853669.
^ Sehat B, Andersson S, Girnita L, Larsson O (Jul 2008). "Identification of c-Cbl as a new ligase for insulin-like growth factor-I receptor with distinct roles from Mdm2 in receptor ubiquitination and endocytosis". Cancer Research 68 (14): 5669–77. doi:10.1158/0008-5472.CAN-07-6364. PMID 18632619.
^ Song MS, Song SJ, Kim SY, Oh HJ, Lim DS (Jul 2008). "The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex". The EMBO Journal 27 (13): 1863–74. doi:10.1038/emboj.2008.115. PMC 2486425. PMID 18566590.
^ Yang W, Dicker DT, Chen J, El-Deiry WS (Mar 2008). "CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing MDM2". Cell Cycle 7 (5): 670–82. doi:10.4161/cc.7.5.5701. PMID 18382127.
^ Abe Y, Oda-Sato E, Tobiume K, Kawauchi K, Taya Y, Okamoto K et al. (Mar 2008). "Hedgehog signaling overrides p53-mediated tumor suppression by activating Mdm2". Proceedings of the National Academy of Sciences of the United States of America 105 (12): 4838–43. doi:10.1073/pnas.0712216105. PMC 2290789. PMID 18359851.
^ Dohmesen C, Koeppel M, Dobbelstein M (Jan 2008). "Specific inhibition of Mdm2-mediated neddylation by Tip60". Cell Cycle 7 (2): 222–31. doi:10.4161/cc.7.2.5185. PMID 18264029.
^ Li M, Chen D, Shiloh A, Luo J, Nikolaev AY, Qin J et al. (Apr 2002). "Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization". Nature 416 (6881): 648–53. doi:10.1038/nature737. PMID 11923872.
^ Brosh RM, Karmakar P, Sommers JA, Yang Q, Wang XW, Spillare EA et al. (Sep 2001). "p53 Modulates the exonuclease activity of Werner syndrome protein". The Journal of Biological Chemistry 276 (37): 35093–102. doi:10.1074/jbc.M103332200. PMID 11427532.
^ Chang NS, Pratt N, Heath J, Schultz L, Sleve D, Carey GB et al. (Feb 2001). "Hyaluronidase induction of a WW domain-containing oxidoreductase that enhances tumor necrosis factor cytotoxicity". The Journal of Biological Chemistry 276 (5): 3361–70. doi:10.1074/jbc.M007140200. PMID 11058590.
^ Okamoto T, Izumi H, Imamura T, Takano H, Ise T, Uchiumi T et al. (Dec 2000). "Direct interaction of p53 with the Y-box binding protein, YB-1: a mechanism for regulation of human gene expression". Oncogene 19 (54): 6194–202. doi:10.1038/sj.onc.1204029. PMID 11175333.
^ Kelley KD, Miller KR, Todd A, Kelley AR, Tuttle R, Berberich SJ (May 2010). "YPEL3, a p53-regulated gene that induces cellular senescence". Cancer Research 70 (9): 3566–75. doi:10.1158/0008-5472.CAN-09-3219. PMC 2862112. PMID 20388804.
^ Waterman MJ, Stavridi ES, Waterman JL, Halazonetis TD (Jun 1998). "ATM-dependent activation of p53 involves dephosphorylation and association with 14-3-3 proteins". Nature Genetics 19 (2): 175–8. doi:10.1038/542. PMID 9620776.
^ Liu J, Grogan L, Nau MM, Allegra CJ, Chu E, Wright JJ (Apr 2001). "Physical interaction between p53 and primary response gene Egr-1". International Journal of Oncology 18 (4): 863–70. doi:10.3892/ijo.18.4.863. PMID 11251186.
^ Bai L, Merchant JL (Jul 2001). "ZBP-89 promotes growth arrest through stabilization of p53". Molecular and Cellular Biology 21 (14): 4670–83. doi:10.1128/MCB.21.14.4670-4683.2001. PMC 87140. PMID 11416144.

External links

Lane Group at the Institute of Molecular and Cell Biology (IMCB), Singapore. p53 Knowledgebase [Retrieved 2008-04-06].
GeneReviews/NCBI/NIH/UW entry on Li-Fraumeni Syndrome
TUMOR PROTEIN p53 @ OMIM
p53 restoration of function
p53 @ The Atlas of Genetics and Cytogenetics in Oncology and Haematology
TP53 Gene @ GeneCards
p53 News provided by insciences organisation
David S. Goodsell. RCSB Protein Data Bank. p53 Tumor Suppressor; 2002-07-01 [Retrieved 2008-04-06].
Thierry Soussi. p53 Web Site [Retrieved 2008-04-06].
The George Pantziarka TP53 Trust A support group from the UK for sufferers of Li-Fraumeni Syndrome or other TP53-related disorders
IARC TP53 Somatic Mutations database maintained at IARC, Lyon, by Magali Olivier

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. リ・フラウメニ症候群 li fraumeni syndrome
2. 大腸癌の分子遺伝学 molecular genetics of colorectal cancer
3. 乳癌における予後因子の評価 measurement of prognostic factors in breast cancer
4. ヒトパピローマウイルス（HPV）感染のウイルス学および癌との関連 virology of human papillomavirus infections and the link to cancer
5. 症候性または進行した慢性リンパ性白血病に対する初期治療の選択 selection of initial therapy for symptomatic or advanced chronic lymphocytic leukemia

English Journal

Intelligent DNA machine for the ultrasensitive colorimetric detection of nucleic acids.

Xu J1, Qian J1, Li H1, Wu ZS2, Shen W1, Jia L3.
Biosensors & bioelectronics.Biosens Bioelectron.2016 Jan 15;75:41-7. doi: 10.1016/j.bios.2015.08.015. Epub 2015 Aug 10.
As DNA is employed to serve as a smart building block, an increasing interest has been devoted to the development of different DNA-based machines for the specific purpose, for example, the exploration of inter- or intramolecular interaction. In the current contribution, we developed an intelligent D
PMID 26291961

Targeting inhibitor of apoptosis proteins by Smac mimetic elicits cell death in poor prognostic subgroups of chronic lymphocytic leukemia.

Opel D1, Schnaiter A1, Dodier D1, Jovanovic M1, Gerhardinger A1, Idler I1, Mertens D1, Bullinger L1, Stilgenbauer S1, Fulda S2,3,4.
International journal of cancer. Journal international du cancer.Int J Cancer.2015 Dec 15;137(12):2959-70. doi: 10.1002/ijc.29650. Epub 2015 Jul 31.
Inhibitor of apoptosis (IAP) proteins are highly expressed in chronic lymphocytic leukemia (CLL) cells and contribute to evasion of cell death and poor therapeutic response. Here, we report that Smac mimetic BV6 dose-dependently induces cell death in 28 of 51 (54%) investigated CLL samples, while B-
PMID 26096065

Regulation of nonsmall-cell lung cancer stem cell like cells by neurotransmitters and opioid peptides.

Banerjee J1, Papu John AM1, Schuller HM1.
International journal of cancer. Journal international du cancer.Int J Cancer.2015 Dec 15;137(12):2815-24. doi: 10.1002/ijc.29646. Epub 2015 Jul 2.
Nonsmall-cell lung cancer (NSCLC) is the leading type of lung cancer and has a poor prognosis. We have shown that chronic stress promoted NSCLC xenografts in mice via stress neurotransmitter-activated cAMP signaling downstream of beta-adrenergic receptors and incidental beta-blocker therapy was repo
PMID 26088878

Japanese Journal

癌関連自己抗体の産生機序と腫瘍マーカーとしての意義 (AYUMI 自己抗体産生機序の新展開)

医学のあゆみ 256(12), 1229-1234, 2016-03-19
NAID 40020764603

Serum p53 Antibody is a Useful Biomarker for Long-Term Monitoring of Breast Cancer : Report of a Recurrent Case After Surgery

Toho journal of medicine 2(1), 22-25, 2016-03
NAID 40020776667

早期舌扁平上皮癌における頸部リンパ節後発転移・局所再発に関連する因子の臨床病理学的検討

北海道歯学雑誌 36(2), 110-119, 2016-03
NAID 120005725174

Related Pictures

Science Types: p53: The gene that cracked the cancer code - a review BioDiscovery Modulation of immune responses by the tumor suppressor p53 p53 - Simple English Wikipedia, the free encyclopedia Role of p53 gene p53 | MDM2 | Tocris Bioscience Frontiers | p53 Family and Cellular Stress Responses in Cancer | Oncology The MDM2-p53 Interaction | Molecular Cancer Research The p53 gene and cancer development

★リンクテーブル★

リンク元	「結腸癌」
拡張検索	「TP53遺伝子」「TP53 gene」
関連記事	「p53」「P」

「結腸癌」

Tumor protein p53
	; PDB rendering based on 1TUP: P53 complexed with DNA
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1A1U, 1AIE, 1C26, 1DT7, 1GZH, 1H26, 1HS5, 1JSP, 1KZY, 1MA3, 1OLG, 1OLH, 1PES, 1PET, 1SAE, 1SAF, 1SAK, 1SAL, 1TSR, 1TUP, 1UOL, 1XQH, 1YC5, 1YCQ, 1YCR, 1YCS, 2AC0, 2ADY, 2AHI, 2ATA, 2B3G, 2BIM, 2BIN, 2BIO, 2BIP, 2BIQ, 2F1X, 2FEJ, 2FOJ, 2FOO, 2GS0, 2H1L, 2H2D, 2H2F, 2H4F, 2H4H, 2H4J, 2H59, 2J0Z, 2J10, 2J11, 2J1W, 2J1X, 2J1Y, 2J1Z, 2J20, 2J21, 2K8F, 2L14, 2LY4, 2MEJ, 2OCJ, 2PCX, 2VUK, 2WGX, 2X0U, 2X0V, 2X0W, 2XWR, 2YBG, 2YDR, 2Z5S, 2Z5T, 3D05, 3D06, 3D07, 3D08, 3D09, 3D0A, 3DAB, 3DAC, 3IGK, 3IGL, 3KMD, 3KZ8, 3LW1, 3OQ5, 3PDH, 3Q01, 3Q05, 3Q06, 3SAK, 3TG5, 3TS8, 3ZME, 4AGL, 4AGM, 4AGN, 4AGO, 4AGP, 4AGQ, 4BUZ, 4BV2, 4HFZ, 4HJE, 4IBQ, 4IBS, 4IBT, 4IBU, 4IBV, 4IBW, 4IBY, 4IBZ, 4IJT, 4KVP, 4LO9, 4LOE, 4LOF, 4MZI, 4MZR
Identifiers
Symbols	TP53 ; BCC7; LFS1; P53; TRP53
External IDs	OMIM: 191170 MGI: 98834 HomoloGene: 460 ChEMBL: 4096 GeneCards: TP53 Gene
Gene ontology
Molecular function	• RNA polymerase II core promoter sequence-specific DNA binding; • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; • RNA polymerase II transcription factor binding; • RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; • protease binding; • p53 binding; • DNA binding; • chromatin binding; • damaged DNA binding; • sequence-specific DNA binding transcription factor activity; • copper ion binding; • protein binding; • ATP binding; • transcription factor binding; • zinc ion binding; • enzyme binding; • protein kinase binding; • protein phosphatase binding; • receptor tyrosine kinase binding; • ubiquitin protein ligase binding; • histone deacetylase regulator activity; • histone acetyltransferase binding; • identical protein binding; • transcription regulatory region DNA binding; • protein heterodimerization activity; • protein N-terminus binding; • chaperone binding; • protein phosphatase 2A binding; • MDM2/MDM4 family protein binding;
Cellular component	• chromatin; • nuclear chromatin; • nucleus; • nucleoplasm; • replication fork; • transcription factor TFIID complex; • nucleolus; • cytoplasm; • mitochondrion; • mitochondrial matrix; • endoplasmic reticulum; • cytosol; • nuclear matrix; • nuclear body; • PML body; • protein complex;
Biological process	• protein import into nucleus, translocation; • negative regulation of transcription from RNA polymerase II promoter; • DNA strand renaturation; • in utero embryonic development; • somitogenesis; • release of cytochrome c from mitochondria; • T cell proliferation involved in immune response; • B cell lineage commitment; • T cell lineage commitment; • response to ischemia; • base-excision repair; • nucleotide-excision repair; • double-strand break repair; • regulation of transcription, DNA-templated; • protein complex assembly; • apoptotic process; • cellular response to DNA damage stimulus; • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; • DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; • ER overload response; • cell cycle arrest; • transforming growth factor beta receptor signaling pathway; • Notch signaling pathway; • Ras protein signal transduction; • multicellular organismal development; • gastrulation; • negative regulation of neuroblast proliferation; • central nervous system development; • cell aging; • blood coagulation; • protein localization; • negative regulation of DNA replication; • cell proliferation; • negative regulation of cell proliferation; • determination of adult lifespan; • rRNA transcription; • response to salt stress; • response to X-ray; • response to gamma radiation; • positive regulation of cardiac muscle cell apoptotic process; • viral process; • cell differentiation; • negative regulation of cell growth; • DNA damage response, signal transduction by p53 class mediator; • negative regulation of transforming growth factor beta receptor signaling pathway; • positive regulation of histone deacetylation; • chromatin assembly; • mitotic G1 DNA damage checkpoint; • positive regulation of protein oligomerization; • T cell differentiation in thymus; • regulation of tissue remodeling; • cellular protein localization; • cellular response to UV; • multicellular organism growth; • cellular response to drug; • cellular response to glucose starvation; • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; • regulation of apoptotic process; • positive regulation of apoptotic process; • negative regulation of apoptotic process; • positive regulation of neuron apoptotic process; • negative regulation of transcription, DNA-templated; • positive regulation of transcription, DNA-templated; • positive regulation of transcription from RNA polymerase II promoter; • response to antibiotic; • regulation of mitochondrial membrane permeability; • negative regulation of fibroblast proliferation; • embryonic organ development; • positive regulation of peptidyl-tyrosine phosphorylation; • negative regulation of helicase activity; • protein tetramerization; • neuron apoptotic process; • positive regulation of thymocyte apoptotic process; • positive regulation of cell cycle arrest; • cellular response to hypoxia; • cellular response to ionizing radiation; • mitotic cell cycle arrest; • intrinsic apoptotic signaling pathway by p53 class mediator; • positive regulation of release of cytochrome c from mitochondria; • positive regulation of cell aging; • replicative senescence; • oxidative stress-induced premature senescence; • intrinsic apoptotic signaling pathway; • oligodendrocyte apoptotic process; • positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; • negative regulation of macromitophagy; • regulation of mitochondrial membrane permeability involved in apoptotic process; • negative regulation of reactive oxygen species metabolic process; • positive regulation of reactive oxygen species metabolic process; • positive regulation of intrinsic apoptotic signaling pathway;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

Tumor protein p53
	; PDB rendering based on 1TUP: P53 complexed with DNA
PDBに登録されている構造
PDB	Ortholog search: PDBe, RCSB, PDBj
PDBのIDコード一覧
	1A1U, 1AIE, 1C26, 1DT7, 1GZH, 1H26, 1HS5, 1JSP, 1KZY, 1MA3, 1OLG, 1OLH, 1PES, 1PET, 1SAE, 1SAF, 1SAK, 1SAL, 1TSR, 1TUP, 1UOL, 1XQH, 1YC5, 1YCQ, 1YCR, 1YCS, 2AC0, 2ADY, 2AHI, 2ATA, 2B3G, 2BIM, 2BIN, 2BIO, 2BIP, 2BIQ, 2FEJ, 2FOJ, 2FOO, 2GS0, 2H1L, 2H2D, 2H2F, 2H4F, 2H4H, 2H4J, 2H59, 2J0Z, 2J10, 2J11, 2J1W, 2J1X, 2J1Y, 2J1Z, 2J20, 2J21, 2K8F, 2L14, 2OCJ, 2PCX, 2QVQ, 2QXA, 2QXB, 2QXC, 2VUK, 2WGX, 2X0U, 2X0V, 2X0W, 2XWR, 2YBG, 2Z5S, 2Z5T, 3D05, 3D06, 3D07, 3D08, 3D09, 3D0A, 3DAB, 3DAC, 3IGK, 3IGL, 3KMD, 3KZ8, 3LW1, 3PDH, 3Q01, 3Q05, 3Q06, 3SAK, 3TG5, 3TS8, 4AGL, 4AGM, 4AGN, 4AGO, 4AGP, 4AGQ
識別記号
記号（英語版）	TP53; LFS1; P53; TRP53
その他ID	OMIM（英語版）: 191170 MGI（英語版）: 98834 HomoloGene（英語版）: 460 ChEMBL: 4096 GeneCards: TP53 Gene
遺伝子オントロジー
分子機能	• DNA strand annealing activity; • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; • RNA polymerase II transcription factor binding; • protease binding; • p53 binding; • DNA binding; • chromatin binding; • damaged DNA binding; • sequence-specific DNA binding transcription factor activity; • copper ion binding; • protein binding; • ATP binding; • transcription factor binding; • zinc ion binding; • enzyme binding; • protein kinase binding; • ubiquitin protein ligase binding; • histone deacetylase regulator activity; • histone acetyltransferase binding; • identical protein binding; • transcription regulatory region DNA binding; • metal ion binding; • protein heterodimerization activity; • protein N-terminus binding; • chaperone binding; • protein phosphatase 2A binding; • MDM2 binding;
細胞の構成要素	• chromatin; • nuclear chromatin; • insoluble fraction; • nucleus; • nucleoplasm; • nucleoplasm; • replication fork; • transcription factor TFIID complex; • chromatin assembly complex; • nucleolus; • cytoplasm; • mitochondrion; • endoplasmic reticulum; • cytosol; • cytosol; • nuclear matrix; • nuclear body; • PML body; • protein complex;
生物学的プロセス	• protein import into nucleus, translocation; • cell cycle checkpoint; • negative regulation of transcription from RNA polymerase II promoter; • negative regulation of transcription from RNA polymerase II promoter; • negative regulation of transcription from RNA polymerase II promoter; • DNA strand renaturation; • in utero embryonic development; • somitogenesis; • T cell proliferation involved in immune response; • B cell lineage commitment; • T cell lineage commitment; • base-excision repair; • nucleotide-excision repair; • double-strand break repair; • regulation of transcription, DNA-dependent; • protein complex assembly; • apoptotic process; • apoptotic process; • response to DNA damage stimulus; • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; • DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; • ER overload response; • cell cycle arrest; • cell cycle arrest; • Ras protein signal transduction; • multicellular organismal development; • gastrulation; • negative regulation of neuroblast proliferation; • central nervous system development; • cell aging; • blood coagulation; • protein localization; • negative regulation of DNA replication; • cell proliferation; • negative regulation of cell proliferation; • determination of adult lifespan; • induction of apoptosis by intracellular signals; • rRNA transcription; • response to salt stress; • embryo development ending in birth or egg hatching; • response to X-ray; • response to gamma radiation; • cell differentiation; • negative regulation of cell growth; • DNA damage response, signal transduction by p53 class mediator; • DNA damage response, signal transduction by p53 class mediator; • negative regulation of transforming growth factor beta receptor signaling pathway; • positive regulation of histone deacetylation; • mitotic cell cycle G1/S transition DNA damage checkpoint; • positive regulation of protein oligomerization; • T cell differentiation in thymus; • cellular protein localization; • cellular response to UV; • multicellular organism growth; • cellular response to drug; • cellular response to glucose starvation; • DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis; • regulation of apoptotic process; • positive regulation of apoptotic process; • negative regulation of apoptotic process; • negative regulation of apoptotic process; • positive regulation of neuron apoptosis; • interspecies interaction between organisms; • negative regulation of transcription, DNA-dependent; • positive regulation of transcription, DNA-dependent; • positive regulation of transcription, DNA-dependent; • positive regulation of transcription from RNA polymerase II promoter; • positive regulation of transcription from RNA polymerase II promoter; • response to antibiotic; • regulation of mitochondrial membrane permeability; • negative regulation of fibroblast proliferation; • positive regulation of peptidyl-tyrosine phosphorylation; • regulation of catalytic activity; • negative regulation of helicase activity; • protein tetramerization; • chromosome organization; • regulation of cell cycle; • positive regulation of thymocyte apoptosis; • positive regulation of cell cycle arrest; • cellular response to hypoxia; • cellular response to ionizing radiation; • signal transduction by p53 class mediator resulting in induction of apoptosis; • positive regulation of release of cytochrome c from mitochondria; • positive regulation of cell aging; • replicative senescence; • oxidative stress-induced premature senescence; • positive regulation of reactive oxygen species metabolic process; • positive regulation of intrinsic apoptotic signaling pathway;
	出典: Amigo / EGO
RNA発現パターン
	その他参照発現データ
オルソログ
	このテンプレートを: 表示・ノート・編集・履歴

　　[★]

英: colon cancer, colonic cancer, colon carcinoma, colonic carcinoma
関: 大腸癌

結腸癌の発生に関わる体細胞の遺伝子変異

normal →→→→→ carcinoma
APC	K-RAS	SMAD4	P53
β-catenin	BRAF	TGFβII

国試

097C013：2型結腸癌[show details]

「TP53遺伝子」

　　[★]

英: TP53 gene
関: p53遺伝子

「TP53 gene」

　　[★]

TP53遺伝子

関: p53 gene

「p53」

　　[★]

同: (遺伝子)p53 gene p53遺伝子; (蛋白質)p53 protein p53蛋白質

p53遺伝子

癌抑制遺伝子

MDM2はp53と結合して安定化し、ユビキチン化を介してP53の分解に導く
活性化ATM(DNA損傷などが引き金となる)はp53をリン酸化する
リン酸化されたp53は次の経路を活性化する

→Bax→アポトーシス

→p21^WAP1/CII1→細胞周期停止

→GADD45

---

p53(蛋白質)=

「P」

　　[★]

[1] Cho Y, Gorina S, Jeffrey PD, Pavletich NP (1994). "Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations". Science 265 (5170): 346–355. doi:10.1126/science.8023157. PMID 8023157.

[2] Tyner SD, Venkatachalam S, Choi J, Jones S, Ghebranious N, Igelmann H, Lu X, Soron G, Cooper B, Brayton C, Park SH, Thompson T, Karsenty G, Bradley A, Donehower LA (2002). "p53 mutant mice that display early ageing-associated phenotypes". Nature 415 (6867): 45–53. doi:10.1038/415045a. PMID 11780111.

[WikiPathways-210] The interactive pathway map can be edited at WikiPathways: "FluoropyrimidineActivity_WP1601".

[pmid8023157-1] Cho Y, Gorina S, Jeffrey PD, Pavletich NP (1994). "Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations". Science 265 (5170): 346–55. doi:10.1126/science.8023157. PMID 8023157.

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P53