Ccun014691.2
Basic Information
- Insect
- Chouioia cunea
- Gene Symbol
- -
- Assembly
- GCA_030064505.1
- Location
- JAOPFQ010000006.1:9392257-9393169[-]
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 1 1.3e-37 7.1e-34 117.2 0.3 25 192 3 165 1 166 0.89
Sequence Information
- Coding Sequence
- ATGGCGACATTTGGTTACTCAAAGAAGCTAAACAAATActacataaaaagaaacgaagtgTTTCACGTGCAATTAAAGTGGTTGCCGACAGATCGAGCGCTATACTTACGTTCGGTGTTCGTCTACGCTGATGAGAAATATGAAGCGATACCTGTTAAACGATGTTTCGAACACATGGACTTAAAACTATCAAAGGAATACAAGGTCGAAGGCAGCCACATGGGTCACGTATTTCGAATAACAGATAATTCGAGTTATGAAATTGACGCGAATGGGTTTCTTAGTAGCAAGACAACGTTGTGGCCAGAGTCTGGTGCAATGTCCgttggttatttatttttctgtcaGAATAGTTGTGTTTCTGGTATGAATAGGAGGGCTACCAAGATGGTTTTTATGATTGAGGATGATAGAGCAGCGATAATTGCTACGACTTCTTTAAAGATACACATCTGCTGTAATCCAAAGCGTGACATGAAACGTGAGGAAGCTCGTACTTCGCCAAAtgtattagaaaatatatcgttCTCACTTTCGCCAATGCTAAACGAAAACATTCAGTACAACGAAGACGATCAGACAGCAGTGTACTCGCTAAACATTAATATTCTTGGCGAAGAAAACTACAAAGCTGTATGTAAGTACGCCTACGATTTAATGGCAGCTCAAGCATTTCGTACTGGTAATCATCAGCTTTACAAGCCGCACATGGATGCGCTTTTGAATAAAGAACCCTGTTACAACTGA
- Protein Sequence
- MATFGYSKKLNKYYIKRNEVFHVQLKWLPTDRALYLRSVFVYADEKYEAIPVKRCFEHMDLKLSKEYKVEGSHMGHVFRITDNSSYEIDANGFLSSKTTLWPESGAMSVGYLFFCQNSCVSGMNRRATKMVFMIEDDRAAIIATTSLKIHICCNPKRDMKREEARTSPNVLENISFSLSPMLNENIQYNEDDQTAVYSLNINILGEENYKAVCKYAYDLMAAQAFRTGNHQLYKPHMDALLNKEPCYN
Similar Transcription Factors
Sequence clustering based on sequence similarity using MMseqs2
- 100% Identity
- -
- 90% Identity
- -
- 80% Identity
- -