hypothetical protein CERSUDRAFT_104910 [Gelatoporia subvermispora B]
Protein Classification
cyclin-D1-binding protein 1( domain architecture ID 10594744)
cyclin-D1-binding protein 1 may negatively regulate cell cycle progression, and act at least in part via inhibition of the cyclin-D1/CDK4 complex, thereby preventing phosphorylation of RB1 and blocking E2F-dependent transcription
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| GCIP | pfam13324 | Grap2 and cyclin-D-interacting; GCIP, or Grap2 and cyclin-D-interacting protein, is found in ... |
62-299 | 7.99e-47 | |||||
Grap2 and cyclin-D-interacting; GCIP, or Grap2 and cyclin-D-interacting protein, is found in eukaryotes, and in the protein Swiss:O95273, residues 149-190 constitute a helix-loop-helix domain, residues 190-240 an acidic region, and 240-261 a leucine zipper domain. GCIP interacts with full-length Grap2 protein and with the COOH-terminal unique and SH3 domains (designated QC domain) of Grap2. It is potentially involved in the regulation of cell differentiation and proliferation through Grap2 and cyclin D-mediated signalling pathways. In mice, it is involved in G1/S-phase progression of hepatocytes, which in older animals is associated with the development of liver tumours. In vitro it acts as an inhibitory HLH protein, for example, blocking transcription of the HNF-4 promoter. In its function as a cyclin D1-binding protein it is able to reduce CDK4-mediated phosphorylation of the retinoblastoma protein and to inhibit E2F-mediated transcriptional activity. GCIP has also been shown to have interact physically with Rad (Ras associated with diabetes), Rad being important in regulating cellular senescence. : Pssm-ID: 463844 Cd Length: 261 Bit Score: 160.16 E-value: 7.99e-47
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| Name | Accession | Description | Interval | E-value | |||||
| GCIP | pfam13324 | Grap2 and cyclin-D-interacting; GCIP, or Grap2 and cyclin-D-interacting protein, is found in ... |
62-299 | 7.99e-47 | |||||
Grap2 and cyclin-D-interacting; GCIP, or Grap2 and cyclin-D-interacting protein, is found in eukaryotes, and in the protein Swiss:O95273, residues 149-190 constitute a helix-loop-helix domain, residues 190-240 an acidic region, and 240-261 a leucine zipper domain. GCIP interacts with full-length Grap2 protein and with the COOH-terminal unique and SH3 domains (designated QC domain) of Grap2. It is potentially involved in the regulation of cell differentiation and proliferation through Grap2 and cyclin D-mediated signalling pathways. In mice, it is involved in G1/S-phase progression of hepatocytes, which in older animals is associated with the development of liver tumours. In vitro it acts as an inhibitory HLH protein, for example, blocking transcription of the HNF-4 promoter. In its function as a cyclin D1-binding protein it is able to reduce CDK4-mediated phosphorylation of the retinoblastoma protein and to inhibit E2F-mediated transcriptional activity. GCIP has also been shown to have interact physically with Rad (Ras associated with diabetes), Rad being important in regulating cellular senescence. Pssm-ID: 463844 Cd Length: 261 Bit Score: 160.16 E-value: 7.99e-47
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| Name | Accession | Description | Interval | E-value | |||||
| GCIP | pfam13324 | Grap2 and cyclin-D-interacting; GCIP, or Grap2 and cyclin-D-interacting protein, is found in ... |
62-299 | 7.99e-47 | |||||
Grap2 and cyclin-D-interacting; GCIP, or Grap2 and cyclin-D-interacting protein, is found in eukaryotes, and in the protein Swiss:O95273, residues 149-190 constitute a helix-loop-helix domain, residues 190-240 an acidic region, and 240-261 a leucine zipper domain. GCIP interacts with full-length Grap2 protein and with the COOH-terminal unique and SH3 domains (designated QC domain) of Grap2. It is potentially involved in the regulation of cell differentiation and proliferation through Grap2 and cyclin D-mediated signalling pathways. In mice, it is involved in G1/S-phase progression of hepatocytes, which in older animals is associated with the development of liver tumours. In vitro it acts as an inhibitory HLH protein, for example, blocking transcription of the HNF-4 promoter. In its function as a cyclin D1-binding protein it is able to reduce CDK4-mediated phosphorylation of the retinoblastoma protein and to inhibit E2F-mediated transcriptional activity. GCIP has also been shown to have interact physically with Rad (Ras associated with diabetes), Rad being important in regulating cellular senescence. Pssm-ID: 463844 Cd Length: 261 Bit Score: 160.16 E-value: 7.99e-47
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