protein cordon-bleu isoform 3 [Mus musculus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Cobl | pfam09469 | Cordon-bleu ubiquitin-like domain; The Cordon-bleu protein domain is highly conserved among ... |
145-222 | 8.12e-42 | ||
Cordon-bleu ubiquitin-like domain; The Cordon-bleu protein domain is highly conserved among vertebrates. The sequence contains three repeated lysine, arginine, and proline-rich regions, the KKRAP motif. The exact function of the protein is unknown but it is thought to be involved in mid-brain neural tube closure. It is expressed specifically in the node. This domain has a ubiquitin-like fold. : Pssm-ID: 462810 Cd Length: 79 Bit Score: 147.73 E-value: 8.12e-42
|
||||||
| WH2_Wb_Cobl | cd21800 | second Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wb) found in ... |
1214-1257 | 3.07e-16 | ||
second Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wb) found in protein Cordon-Bleu (Cobl) and similar proteins; This family contains the second tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2), called Wb, found in protein Cordon-Bleu (Cobl), a potent actin filament nucleator that plays an important role in the reorganization of the actin cytoskeleton. It regulates neuron morphogenesis and increases branching of axons and dendrites. It also modulates dendrite branching in Purkinje cells. Cobl binds to and sequesters actin monomers (G-actin). Cobl contains three tandem WH2 or W domains consisting of an N-terminal alpha helix and a C-terminal LRKV motif. The first two WH2 domains have the highest binding affinity for actin. They are functionally active in actin nucleation and polymerization. The model corresponds to the second WH2 domain. : Pssm-ID: 409198 [Multi-domain] Cd Length: 44 Bit Score: 73.42 E-value: 3.07e-16
|
||||||
| WH2_Wa_Cobl | cd21799 | first Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wa) found in ... |
1168-1200 | 7.96e-12 | ||
first Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wa) found in protein Cordon-Bleu (Cobl) and similar proteins; This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2), called Wa, found in protein Cordon-Bleu (Cobl), a potent actin filament nucleator that plays an important role in the reorganization of the actin cytoskeleton. It regulates neuron morphogenesis and increases branching of axons and dendrites. It also modulates dendrite branching in Purkinje cells. Cobl binds to and sequesters actin monomers (G-actin). Cobl contains three tandem WH2 (or W) domains consisting of an N-terminal alpha helix and a C-terminal LRKV motif. The first two WH2 domains have the highest binding affinity for actin. They are functionally active in actin nucleation and polymerization. The model corresponds to the first WH2 domain. : Pssm-ID: 409197 [Multi-domain] Cd Length: 33 Bit Score: 60.92 E-value: 7.96e-12
|
||||||
| WH2_Wc_Cobl | cd21801 | third Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wc) found in ... |
1302-1327 | 3.40e-11 | ||
third Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wc) found in protein Cordon-Bleu (Cobl) and similar proteins; This family contains the third tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2), called Wc, found in protein Cordon-Bleu (Cobl), a potent actin filament nucleator that plays an important role in the reorganization of the actin cytoskeleton. It regulates neuron morphogenesis and increases branching of axons and dendrites. It also modulates dendrite branching in Purkinje cells. Cobl binds to and sequesters actin monomers (G-actin). Cobl contains three tandem WH2 (or W) domains consisting of an N-terminal alpha helix and a C-terminal LRKV motif. The first two WH2 domains have the highest binding affinity for actin. They are functionally active in actin nucleation and polymerization. The model corresponds to the first WH2 domain. : Pssm-ID: 409199 Cd Length: 26 Bit Score: 58.85 E-value: 3.40e-11
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| Cobl | pfam09469 | Cordon-bleu ubiquitin-like domain; The Cordon-bleu protein domain is highly conserved among ... |
145-222 | 8.12e-42 | ||
Cordon-bleu ubiquitin-like domain; The Cordon-bleu protein domain is highly conserved among vertebrates. The sequence contains three repeated lysine, arginine, and proline-rich regions, the KKRAP motif. The exact function of the protein is unknown but it is thought to be involved in mid-brain neural tube closure. It is expressed specifically in the node. This domain has a ubiquitin-like fold. Pssm-ID: 462810 Cd Length: 79 Bit Score: 147.73 E-value: 8.12e-42
|
||||||
| WH2_Wb_Cobl | cd21800 | second Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wb) found in ... |
1214-1257 | 3.07e-16 | ||
second Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wb) found in protein Cordon-Bleu (Cobl) and similar proteins; This family contains the second tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2), called Wb, found in protein Cordon-Bleu (Cobl), a potent actin filament nucleator that plays an important role in the reorganization of the actin cytoskeleton. It regulates neuron morphogenesis and increases branching of axons and dendrites. It also modulates dendrite branching in Purkinje cells. Cobl binds to and sequesters actin monomers (G-actin). Cobl contains three tandem WH2 or W domains consisting of an N-terminal alpha helix and a C-terminal LRKV motif. The first two WH2 domains have the highest binding affinity for actin. They are functionally active in actin nucleation and polymerization. The model corresponds to the second WH2 domain. Pssm-ID: 409198 [Multi-domain] Cd Length: 44 Bit Score: 73.42 E-value: 3.07e-16
|
||||||
| WH2_Wa_Cobl | cd21799 | first Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wa) found in ... |
1168-1200 | 7.96e-12 | ||
first Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wa) found in protein Cordon-Bleu (Cobl) and similar proteins; This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2), called Wa, found in protein Cordon-Bleu (Cobl), a potent actin filament nucleator that plays an important role in the reorganization of the actin cytoskeleton. It regulates neuron morphogenesis and increases branching of axons and dendrites. It also modulates dendrite branching in Purkinje cells. Cobl binds to and sequesters actin monomers (G-actin). Cobl contains three tandem WH2 (or W) domains consisting of an N-terminal alpha helix and a C-terminal LRKV motif. The first two WH2 domains have the highest binding affinity for actin. They are functionally active in actin nucleation and polymerization. The model corresponds to the first WH2 domain. Pssm-ID: 409197 [Multi-domain] Cd Length: 33 Bit Score: 60.92 E-value: 7.96e-12
|
||||||
| WH2_Wc_Cobl | cd21801 | third Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wc) found in ... |
1302-1327 | 3.40e-11 | ||
third Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wc) found in protein Cordon-Bleu (Cobl) and similar proteins; This family contains the third tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2), called Wc, found in protein Cordon-Bleu (Cobl), a potent actin filament nucleator that plays an important role in the reorganization of the actin cytoskeleton. It regulates neuron morphogenesis and increases branching of axons and dendrites. It also modulates dendrite branching in Purkinje cells. Cobl binds to and sequesters actin monomers (G-actin). Cobl contains three tandem WH2 (or W) domains consisting of an N-terminal alpha helix and a C-terminal LRKV motif. The first two WH2 domains have the highest binding affinity for actin. They are functionally active in actin nucleation and polymerization. The model corresponds to the first WH2 domain. Pssm-ID: 409199 Cd Length: 26 Bit Score: 58.85 E-value: 3.40e-11
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| Cobl | pfam09469 | Cordon-bleu ubiquitin-like domain; The Cordon-bleu protein domain is highly conserved among ... |
145-222 | 8.12e-42 | ||
Cordon-bleu ubiquitin-like domain; The Cordon-bleu protein domain is highly conserved among vertebrates. The sequence contains three repeated lysine, arginine, and proline-rich regions, the KKRAP motif. The exact function of the protein is unknown but it is thought to be involved in mid-brain neural tube closure. It is expressed specifically in the node. This domain has a ubiquitin-like fold. Pssm-ID: 462810 Cd Length: 79 Bit Score: 147.73 E-value: 8.12e-42
|
||||||
| WH2_Wb_Cobl | cd21800 | second Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wb) found in ... |
1214-1257 | 3.07e-16 | ||
second Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wb) found in protein Cordon-Bleu (Cobl) and similar proteins; This family contains the second tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2), called Wb, found in protein Cordon-Bleu (Cobl), a potent actin filament nucleator that plays an important role in the reorganization of the actin cytoskeleton. It regulates neuron morphogenesis and increases branching of axons and dendrites. It also modulates dendrite branching in Purkinje cells. Cobl binds to and sequesters actin monomers (G-actin). Cobl contains three tandem WH2 or W domains consisting of an N-terminal alpha helix and a C-terminal LRKV motif. The first two WH2 domains have the highest binding affinity for actin. They are functionally active in actin nucleation and polymerization. The model corresponds to the second WH2 domain. Pssm-ID: 409198 [Multi-domain] Cd Length: 44 Bit Score: 73.42 E-value: 3.07e-16
|
||||||
| WH2_Wa_Cobl | cd21799 | first Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wa) found in ... |
1168-1200 | 7.96e-12 | ||
first Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wa) found in protein Cordon-Bleu (Cobl) and similar proteins; This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2), called Wa, found in protein Cordon-Bleu (Cobl), a potent actin filament nucleator that plays an important role in the reorganization of the actin cytoskeleton. It regulates neuron morphogenesis and increases branching of axons and dendrites. It also modulates dendrite branching in Purkinje cells. Cobl binds to and sequesters actin monomers (G-actin). Cobl contains three tandem WH2 (or W) domains consisting of an N-terminal alpha helix and a C-terminal LRKV motif. The first two WH2 domains have the highest binding affinity for actin. They are functionally active in actin nucleation and polymerization. The model corresponds to the first WH2 domain. Pssm-ID: 409197 [Multi-domain] Cd Length: 33 Bit Score: 60.92 E-value: 7.96e-12
|
||||||
| WH2_Wc_Cobl | cd21801 | third Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wc) found in ... |
1302-1327 | 3.40e-11 | ||
third Wiskott Aldrich syndrome homology region 2 (WH2 motif) repeat (called Wc) found in protein Cordon-Bleu (Cobl) and similar proteins; This family contains the third tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2), called Wc, found in protein Cordon-Bleu (Cobl), a potent actin filament nucleator that plays an important role in the reorganization of the actin cytoskeleton. It regulates neuron morphogenesis and increases branching of axons and dendrites. It also modulates dendrite branching in Purkinje cells. Cobl binds to and sequesters actin monomers (G-actin). Cobl contains three tandem WH2 (or W) domains consisting of an N-terminal alpha helix and a C-terminal LRKV motif. The first two WH2 domains have the highest binding affinity for actin. They are functionally active in actin nucleation and polymerization. The model corresponds to the first WH2 domain. Pssm-ID: 409199 Cd Length: 26 Bit Score: 58.85 E-value: 3.40e-11
|
||||||
| Blast search parameters | ||||
|
