neuroblastoma suppressor of tumorigenicity 1 isoform 3 [Homo sapiens]
DAN domain-containing protein( domain architecture ID 10503509)
DAN domain-containing protein similar to neuroblastoma suppressor of tumorigenicity 1 that may play an important role in preventing cells from entering the final stage (G1/S) of the transformation process
List of domain hits
Name | Accession | Description | Interval | E-value | |||
DAN | pfam03045 | DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ... |
57-155 | 5.40e-30 | |||
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the cysteines may form disulphide bridges. This family of proteins has been termed the DAN family after the first member to be reported. This family includes DAN, Cerberus and Gremlin. The gremlin protein is an antagonist of bone morphogenetic protein signaling. It is postulated that all members of this family antagonize different TGF beta pfam00019 ligands. Recent work shows that the DAN protein is not an efficient antagonist of BMP-2/4 class signals, we found that DAN was able to interact with GDF-5 in a frog embryo assay, suggesting that DAN may regulate signaling by the GDF-5/6/7 class of BMPs in vivo. : Pssm-ID: 460786 Cd Length: 108 Bit Score: 106.99 E-value: 5.40e-30
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Name | Accession | Description | Interval | E-value | |||
DAN | pfam03045 | DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ... |
57-155 | 5.40e-30 | |||
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the cysteines may form disulphide bridges. This family of proteins has been termed the DAN family after the first member to be reported. This family includes DAN, Cerberus and Gremlin. The gremlin protein is an antagonist of bone morphogenetic protein signaling. It is postulated that all members of this family antagonize different TGF beta pfam00019 ligands. Recent work shows that the DAN protein is not an efficient antagonist of BMP-2/4 class signals, we found that DAN was able to interact with GDF-5 in a frog embryo assay, suggesting that DAN may regulate signaling by the GDF-5/6/7 class of BMPs in vivo. Pssm-ID: 460786 Cd Length: 108 Bit Score: 106.99 E-value: 5.40e-30
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CT | smart00041 | C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ... |
74-156 | 2.66e-04 | |||
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers. Pssm-ID: 214482 Cd Length: 82 Bit Score: 38.54 E-value: 2.66e-04
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Name | Accession | Description | Interval | E-value | |||
DAN | pfam03045 | DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ... |
57-155 | 5.40e-30 | |||
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the cysteines may form disulphide bridges. This family of proteins has been termed the DAN family after the first member to be reported. This family includes DAN, Cerberus and Gremlin. The gremlin protein is an antagonist of bone morphogenetic protein signaling. It is postulated that all members of this family antagonize different TGF beta pfam00019 ligands. Recent work shows that the DAN protein is not an efficient antagonist of BMP-2/4 class signals, we found that DAN was able to interact with GDF-5 in a frog embryo assay, suggesting that DAN may regulate signaling by the GDF-5/6/7 class of BMPs in vivo. Pssm-ID: 460786 Cd Length: 108 Bit Score: 106.99 E-value: 5.40e-30
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CT | smart00041 | C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ... |
74-156 | 2.66e-04 | |||
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers. Pssm-ID: 214482 Cd Length: 82 Bit Score: 38.54 E-value: 2.66e-04
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Blast search parameters | ||||
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