four-jointed box protein 1 precursor [Rattus norvegicus]
Protein Classification
Four-jointed-like_C domain-containing protein( domain architecture ID 10180060)
Four-jointed-like_C domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Four-jointed-like_C | cd10468 | C-terminal kinase domain of Drosophila Four-jointed (Fj), mouse Fjx1, and related proteins; ... |
145-429 | 4.75e-165 | |||||
C-terminal kinase domain of Drosophila Four-jointed (Fj), mouse Fjx1, and related proteins; Drosophila Fj is a Golgi type II transmembrane protein that is partially secreted, and is a kinase that phosphorylates Ser or Thr residues within extracellular cadherin domains of a transmembrane receptor Fat and its ligand, Dachsous (Ds). Mutation of three conserved Asp residues at the Drosophila Fj putative active site abolished its ability to phosphorylate Ft and Ds cadherin domains. The Fat signaling pathway regulates growth, gene expression, and planar cell polarity (PCP). Defects from mutation in Drosophila Fj include loss of the intermediate leg joint, and a PCP defect in the eye. The expression of the Drospophila fj gene is modulated by Notch, Unpaired (JAK/STAT), and Wingless signals. Mouse Fjx1, has been shown to be involved in both the Fat and Hippo signaling pathways; these two pathways intersect at multiple points. The Hippo pathway is important in organ size control and in cancer. The expression of the mouse fjx1 gene is also Notch dependent; fjx1 is expressed in the brain, the peripheral nervous system, in epithelial structures of different organs, and during limb development. : Pssm-ID: 198459 Cd Length: 286 Bit Score: 466.18 E-value: 4.75e-165
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| Four-jointed-like_C | cd10468 | C-terminal kinase domain of Drosophila Four-jointed (Fj), mouse Fjx1, and related proteins; ... |
145-429 | 4.75e-165 | |||||
C-terminal kinase domain of Drosophila Four-jointed (Fj), mouse Fjx1, and related proteins; Drosophila Fj is a Golgi type II transmembrane protein that is partially secreted, and is a kinase that phosphorylates Ser or Thr residues within extracellular cadherin domains of a transmembrane receptor Fat and its ligand, Dachsous (Ds). Mutation of three conserved Asp residues at the Drosophila Fj putative active site abolished its ability to phosphorylate Ft and Ds cadherin domains. The Fat signaling pathway regulates growth, gene expression, and planar cell polarity (PCP). Defects from mutation in Drosophila Fj include loss of the intermediate leg joint, and a PCP defect in the eye. The expression of the Drospophila fj gene is modulated by Notch, Unpaired (JAK/STAT), and Wingless signals. Mouse Fjx1, has been shown to be involved in both the Fat and Hippo signaling pathways; these two pathways intersect at multiple points. The Hippo pathway is important in organ size control and in cancer. The expression of the mouse fjx1 gene is also Notch dependent; fjx1 is expressed in the brain, the peripheral nervous system, in epithelial structures of different organs, and during limb development. Pssm-ID: 198459 Cd Length: 286 Bit Score: 466.18 E-value: 4.75e-165
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| Four-jointed-like_C | cd10468 | C-terminal kinase domain of Drosophila Four-jointed (Fj), mouse Fjx1, and related proteins; ... |
145-429 | 4.75e-165 | |||||
C-terminal kinase domain of Drosophila Four-jointed (Fj), mouse Fjx1, and related proteins; Drosophila Fj is a Golgi type II transmembrane protein that is partially secreted, and is a kinase that phosphorylates Ser or Thr residues within extracellular cadherin domains of a transmembrane receptor Fat and its ligand, Dachsous (Ds). Mutation of three conserved Asp residues at the Drosophila Fj putative active site abolished its ability to phosphorylate Ft and Ds cadherin domains. The Fat signaling pathway regulates growth, gene expression, and planar cell polarity (PCP). Defects from mutation in Drosophila Fj include loss of the intermediate leg joint, and a PCP defect in the eye. The expression of the Drospophila fj gene is modulated by Notch, Unpaired (JAK/STAT), and Wingless signals. Mouse Fjx1, has been shown to be involved in both the Fat and Hippo signaling pathways; these two pathways intersect at multiple points. The Hippo pathway is important in organ size control and in cancer. The expression of the mouse fjx1 gene is also Notch dependent; fjx1 is expressed in the brain, the peripheral nervous system, in epithelial structures of different organs, and during limb development. Pssm-ID: 198459 Cd Length: 286 Bit Score: 466.18 E-value: 4.75e-165
|
|||||||||
| FAM20_C_like | cd10467 | C-terminal putative kinase domain of FAM20 (family with sequence similarity 20), Drosophila ... |
146-429 | 1.49e-60 | |||||
C-terminal putative kinase domain of FAM20 (family with sequence similarity 20), Drosophila Four-jointed (Fj), and related proteins; Drosophila Fj is a Golgi kinase that phosphorylates Ser or Thr residues within extracellular cadherin domains of a transmembrane receptor Fat and its ligand, Dachsous (Ds). The Fat signaling pathway regulates growth, gene expression, and planar cell polarity (PCP). Defects from mutation in the Drosophila fj gene include loss of the intermediate leg joint, and a PCP defect in the eye. Fjx1, the murine homologue of Fj, has been shown to be involved in both the Fat and Hippo signaling pathways, these two pathways intersect at multiple points. The Hippo pathway is important in organ size control and in cancer. FAM20B is a xylose kinase that may regulate the number of glycosaminoglycan chains by phosphorylating the xylose residue in the glycosaminoglycan-protein linkage region of proteoglycans. This domain has homology to a kinase-active site, mutation of three conserved Asp residues at the Drosophila Fj putative active site abolished its ability to phosphorylate Ft and Ds cadherin domains. FAM20A may participate in enamel development and gingival homeostasis, FAM20B in proteoglycan production, and FAM20C in bone development. FAM20C, also called Dentin Matrix Protein 4, is abundant in the dentin matrix, and may participate in the differentiation of mesenchymal precursor cells into functional odontoblast-like cells. Mutations in FAM20C are associated with lethal Osteosclerotic Bone Dysplasia (Raine Syndrome), and mutations in FAM20A with Amelogenesis imperfecta (AI) and Gingival Hyperplasia Syndrome. This model includes the FAM20_C domain family, previously known as DUF1193; FAM20_C appears to be homologous to the catalytic domain of the phosphoinositide 3-kinase (PI3K)-like family. Pssm-ID: 198458 Cd Length: 210 Bit Score: 196.32 E-value: 1.49e-60
|
|||||||||
| FAM20_C | cd10314 | C-terminal putative kinase domain of FAM20 (family with sequence similarity 20) proteins; This ... |
235-431 | 1.07e-04 | |||||
C-terminal putative kinase domain of FAM20 (family with sequence similarity 20) proteins; This family contains the C-terminal domain of FAM20A, -B, -C and related proteins. FAM20A may participate in enamel development and gingival homeostasis, FAM20B in proteoglycan production, and FAM20C in bone development. FAM20B is a xylose kinase that may regulate the number of glycosaminoglycan chains by phosphorylating the xylose residue in the glycosaminoglycan-protein linkage region of proteoglycans. FAM20C, also called Dentin Matrix Protein 4, is abundant in the dentin matrix, and may participate in the differentiation of mesenchymal precursor cells into functional odontoblast-like cells. Mutations in FAM20C are associated with lethal Osteosclerotic Bone Dysplasia (Raine Syndrome), and mutations in FAM20A with Amelogenesis imperfecta (AI) and Gingival Hyperplasia Syndrome. The C-terminal domains of members of this family are putative kinase domains, based on mutagenesis of the C-terminal domain of Drosophila Four-Jointed, a related Golgi kinase. This domain family is also known as DUF1193. Pssm-ID: 198457 Cd Length: 209 Bit Score: 43.41 E-value: 1.07e-04
|
|||||||||
| Blast search parameters | ||||
|
