Basic Information

Gene Symbol
tp53
Assembly
GCA_947579665.1
Location
OX388344.1:77516217-77523023[+]

Transcription Factor Domain

TF Family
P53
Domain
P53 domain
PFAM
PF00870
TF Group
Beta-Scaffold Factors
Description
P53 is a tumor suppressor gene product; mutations in p53 or lack of expression are found associated with a large fraction of all human cancers. P53 is activated by DNA damage and acts as a regulator of gene expression that ultimatively blocks progression through the cell cycle. P53 binds to DNA as a tetrameric transcription factor. In its inactive form, p53 is bound to the ring finger protein Mdm2, which promotes its ubiquitinylation and subsequent proteosomal degradation. Phosphorylation of p53 disrupts the Mdm2-p53 complex, while the stable and active p53 binds to regulatory regions of its target genes, such as the cyclin-kinase inhibitor p21, which complexes and inactivates cdk2 and other cyclin complexes [PMID: 20066118, PMID: 12629332, PMID: 1397838, PMID: 6544917, PMID: 19826090, PMID: 19776744, PMID: 6278740, PMID: 221923, PMID: 6318442, PMID: 20030809].This domain is found in p53 transcription factors, where it is responsible for DNA-binding. The DNA-binding domain acts to clamp, or in the case of TonEBP, encircle the DNA target in order to stabilise the protein-DNA complex [PMID: 11780147]. Protein interactions may also serve to stabilise the protein-DNA complex, for example in the STAT-1 dimer the SH2 (Src homology 2) domain in each monomer is coupled to the DNA-binding domain to increase stability [PMID: 9630226]. The DNA-binding domain consists of a beta-sandwich formed of 9 strands in 2 sheets with a Greek-key topology. This structure is found in many transcription factors, often within the DNA-binding domain.
Hmmscan Out
# of c-Evalue i-Evalue score bias hmm coord from hmm coord to ali coord from ali coord to env coord from env coord to acc
1 2 1.1e-62 1.3e-57 197.5 1.2 2 192 74 260 73 261 0.96
2 2 0.063 7.6e+03 -0.7 0.0 19 43 278 302 270 329 0.77

Sequence Information

Coding Sequence
ATGATTGATATTCTTTTATCCTTTTCTAAAGTTTGTCGGAAAACCGACACAATGGTTACCAAAGGAGAAGAATTCCTGTGTAGCCAGGAACCGTCACTTAGTGAAAGTGATCTTCAAGCAGTGCTCGGCATGTACGATGTATTCGATATGGATCAGTTATCGGAAGAGGAGAAGTTTAAGGTGACATTGCCACCATCTCCGACTTGCCCCCTGCCGTCAACAGAGGATTGGTCTGGATCATATGATTTTGAACTCAAAGTCAATACTGTTAATGCGAACAAGAAAACATGGCTATTTTCGAGTTCATTGAATAAGATATTCATTGATGTGCACAAAAGCATTCCACTGCAGTTCAAGATTAACTGCCCTGATGATGGGGAAGCCTTCTCCATCAGAGCACTACCCGTTTATAGTATATCTCAGCACATGACTTTTCCCGTCAACCGATGCCCTTTACACCTGAAAGAAGACGAGAATAAAGGAGTAACTAAACGGAATCATGTGGTTCAGTGTGAAGACCTCCGTGCCCTATATGAATATGACGAGGAAAGTAAGCGCTACAGTGTACTCACTACCTTAGGATGCCCACAGCCTGGCTCCGACTTGGTGACACGCATGTATTCATTTTCCTGCAAGAGCAGTTGCTGCGGGGGGATGAATCGCAGACCCATAATGGTCATTTTCACTCTAGAGAGAGACCAGCATGTGGTTGGGAGAAAAACATTGAACTTCAGAGTCTGCAGTTGTCCTAAAAGAGACAAGGATAAAGAAGAGAAGGCTGCAATGGAAGAAAAACTACGAGAAGAACCTCAGAACCATCCTGGAAAGATTAAGAAGGAAAAGGAGAGCAGCATGAATCCCTCTAAAAAAAGGAAGTCCTTGTTTGCTTCAAATGAAGAAAATGCTTCCTCTAGCAAGATCCATGGTACTGCTCATTATCGTGAAATACTGCGGCATCTAATTATGCTGAAGTGTGCTGAGTTTGATGAAACAGGATCACAAGAAGCCTTAGCTAGCAAAGCAGAATACGAAGATTTGTGGTAA
Protein Sequence
MIDILLSFSKVCRKTDTMVTKGEEFLCSQEPSLSESDLQAVLGMYDVFDMDQLSEEEKFKVTLPPSPTCPLPSTEDWSGSYDFELKVNTVNANKKTWLFSSSLNKIFIDVHKSIPLQFKINCPDDGEAFSIRALPVYSISQHMTFPVNRCPLHLKEDENKGVTKRNHVVQCEDLRALYEYDEESKRYSVLTTLGCPQPGSDLVTRMYSFSCKSSCCGGMNRRPIMVIFTLERDQHVVGRKTLNFRVCSCPKRDKDKEEKAAMEEKLREEPQNHPGKIKKEKESSMNPSKKRKSLFASNEENASSSKIHGTAHYREILRHLIMLKCAEFDETGSQEALASKAEYEDLW

Similar Transcription Factors

Sequence clustering based on sequence similarity using MMseqs2

100% Identity
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90% Identity
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80% Identity
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