tumor protein p73 isoform c [Mus musculus]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
P53 | cd08367 | P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ... |
78-257 | 2.22e-99 | ||||
P53 DNA-binding domain; 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. : Pssm-ID: 176262 Cd Length: 179 Bit Score: 296.49 E-value: 2.22e-99
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SAM_superfamily super family | cl15755 | SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
353-408 | 2.60e-35 | ||||
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases. The actual alignment was detected with superfamily member cd09571: Pssm-ID: 472832 Cd Length: 65 Bit Score: 125.85 E-value: 2.60e-35
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P53_tetramer | pfam07710 | P53 tetramerization motif; |
296-335 | 1.67e-15 | ||||
P53 tetramerization motif; : Pssm-ID: 462238 Cd Length: 42 Bit Score: 70.00 E-value: 1.67e-15
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Gp37 super family | cl09862 | Gp37 protein; This protein of 154 residues consists of a unit of helices and beta sheets that ... |
403-490 | 1.84e-03 | ||||
Gp37 protein; This protein of 154 residues consists of a unit of helices and beta sheets that crystallizes into a beautiful asymmetrical dodecameric barrel-structure, of two six-membered rings one on top of the other. It is expressed in bacteria but is of viral origin as it is found in phage BcepMu and is probably a pathogenesis factor. The actual alignment was detected with superfamily member pfam09646: Pssm-ID: 430731 Cd Length: 134 Bit Score: 38.46 E-value: 1.84e-03
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Name | Accession | Description | Interval | E-value | ||||
P53 | cd08367 | P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ... |
78-257 | 2.22e-99 | ||||
P53 DNA-binding domain; 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. Pssm-ID: 176262 Cd Length: 179 Bit Score: 296.49 E-value: 2.22e-99
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P53 | pfam00870 | P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ... |
68-260 | 2.57e-91 | ||||
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). This sequence is identical to human P53 and would appear to be a a human contaminant within the Zea mays sampling effort. Pssm-ID: 459972 [Multi-domain] Cd Length: 191 Bit Score: 276.09 E-value: 2.57e-91
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SAM_tumor-p73 | cd09571 | SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a ... |
353-408 | 2.60e-35 | ||||
SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a putative protein-protein interaction and lipid-binding domain. p73 is a homolog to the tumor suppressor p53. p73 has a C-terminal SAM domain in the longest spliced alpha form, while p53 doesn't have it. p73 knockout mouse shows significant developmental abnormalities but no increased cancer susceptibility, suggesting that p73 plays a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for the p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain. Pssm-ID: 188970 Cd Length: 65 Bit Score: 125.85 E-value: 2.60e-35
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P53_tetramer | pfam07710 | P53 tetramerization motif; |
296-335 | 1.67e-15 | ||||
P53 tetramerization motif; Pssm-ID: 462238 Cd Length: 42 Bit Score: 70.00 E-value: 1.67e-15
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SAM_2 | pfam07647 | SAM domain (Sterile alpha motif); |
353-406 | 2.01e-08 | ||||
SAM domain (Sterile alpha motif); Pssm-ID: 429573 Cd Length: 66 Bit Score: 50.73 E-value: 2.01e-08
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SAM | smart00454 | Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
353-408 | 1.56e-04 | ||||
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation. Pssm-ID: 197735 Cd Length: 68 Bit Score: 39.97 E-value: 1.56e-04
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Gp37 | pfam09646 | Gp37 protein; This protein of 154 residues consists of a unit of helices and beta sheets that ... |
403-490 | 1.84e-03 | ||||
Gp37 protein; This protein of 154 residues consists of a unit of helices and beta sheets that crystallizes into a beautiful asymmetrical dodecameric barrel-structure, of two six-membered rings one on top of the other. It is expressed in bacteria but is of viral origin as it is found in phage BcepMu and is probably a pathogenesis factor. Pssm-ID: 430731 Cd Length: 134 Bit Score: 38.46 E-value: 1.84e-03
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Name | Accession | Description | Interval | E-value | ||||
P53 | cd08367 | P53 DNA-binding domain; P53 is a tumor suppressor gene product; mutations in p53 or lack of ... |
78-257 | 2.22e-99 | ||||
P53 DNA-binding domain; 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. Pssm-ID: 176262 Cd Length: 179 Bit Score: 296.49 E-value: 2.22e-99
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P53 | pfam00870 | P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). ... |
68-260 | 2.57e-91 | ||||
P53 DNA-binding domain; This family contains one anomalous member, viz: Zea mays (Q6JAD8). This sequence is identical to human P53 and would appear to be a a human contaminant within the Zea mays sampling effort. Pssm-ID: 459972 [Multi-domain] Cd Length: 191 Bit Score: 276.09 E-value: 2.57e-91
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SAM_tumor-p73 | cd09571 | SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a ... |
353-408 | 2.60e-35 | ||||
SAM domain of tumor-p73 proteins; SAM (sterile alpha motif) domain of p73 proteins is a putative protein-protein interaction and lipid-binding domain. p73 is a homolog to the tumor suppressor p53. p73 has a C-terminal SAM domain in the longest spliced alpha form, while p53 doesn't have it. p73 knockout mouse shows significant developmental abnormalities but no increased cancer susceptibility, suggesting that p73 plays a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for the p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain. Pssm-ID: 188970 Cd Length: 65 Bit Score: 125.85 E-value: 2.60e-35
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SAM_tumor-p63,p73 | cd09503 | SAM domain of tumor-p63,p73 proteins; SAM (sterile alpha motif) domain of p63, p73 ... |
353-407 | 8.59e-25 | ||||
SAM domain of tumor-p63,p73 proteins; SAM (sterile alpha motif) domain of p63, p73 transcriptional factors is a putative protein-protein interaction domain and lipid-binding domain. p63 and p73 are homologs to the tumor suppressor p53. They have a C-terminal SAM domain in their longest spliced alpha forms, while p53 doesn't have it. p63 or p73 knockout mice show significant developmental abnormalities but no increased cancer susceptibility, suggesting that p63 and p73 play a role in regulation of normal development. It was shown that SAM domain of p73 is able to bind some membrane lipids. The structural rearrangements in SAM are necessary to accomplish the binding. No evidence for homooligomerization through SAM domains was found for p63/p73 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain. Pssm-ID: 188902 Cd Length: 65 Bit Score: 97.00 E-value: 8.59e-25
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SAM_tumor-p63 | cd09572 | SAM domain of tumor-p63 proteins; SAM (sterile alpha motif) domain of p63 proteins is a ... |
353-407 | 1.65e-15 | ||||
SAM domain of tumor-p63 proteins; SAM (sterile alpha motif) domain of p63 proteins is a putative protein-protein interaction domain. p63 is homolog to the tumor suppressor p53. p63 has a C-terminal SAM domain in the longest spliced alpha form, while p53 doesn't have it. p63 knockout mice show significant developmental abnormalities but no increased cancer susceptibility, suggesting that p63 plays a role in regulation of normal development. No evidence for homooligomerization through SAM domains was found for the p63 subfamily. It was suggested that the partner proteins should be either more distantly related SAM-containing domain proteins or proteins without the SAM domain. Mutations in the SAM domain of p63 are found in AEC syndrome patients. Pssm-ID: 188971 Cd Length: 65 Bit Score: 70.77 E-value: 1.65e-15
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P53_tetramer | pfam07710 | P53 tetramerization motif; |
296-335 | 1.67e-15 | ||||
P53 tetramerization motif; Pssm-ID: 462238 Cd Length: 42 Bit Score: 70.00 E-value: 1.67e-15
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SAM_2 | pfam07647 | SAM domain (Sterile alpha motif); |
353-406 | 2.01e-08 | ||||
SAM domain (Sterile alpha motif); Pssm-ID: 429573 Cd Length: 66 Bit Score: 50.73 E-value: 2.01e-08
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SAM | smart00454 | Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related ... |
353-408 | 1.56e-04 | ||||
Sterile alpha motif; Widespread domain in signalling and nuclear proteins. In EPH-related tyrosine kinases, appears to mediate cell-cell initiated signal transduction via the binding of SH2-containing proteins to a conserved tyrosine that is phosphorylated. In many cases mediates homodimerisation. Pssm-ID: 197735 Cd Length: 68 Bit Score: 39.97 E-value: 1.56e-04
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Gp37 | pfam09646 | Gp37 protein; This protein of 154 residues consists of a unit of helices and beta sheets that ... |
403-490 | 1.84e-03 | ||||
Gp37 protein; This protein of 154 residues consists of a unit of helices and beta sheets that crystallizes into a beautiful asymmetrical dodecameric barrel-structure, of two six-membered rings one on top of the other. It is expressed in bacteria but is of viral origin as it is found in phage BcepMu and is probably a pathogenesis factor. Pssm-ID: 430731 Cd Length: 134 Bit Score: 38.46 E-value: 1.84e-03
|
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SAM_superfamily | cd09487 | SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ... |
353-404 | 2.01e-03 | ||||
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases. Pssm-ID: 188886 [Multi-domain] Cd Length: 56 Bit Score: 36.45 E-value: 2.01e-03
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Blast search parameters | ||||
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