microtubule-associated protein RP/EB family member 3a isoform X2 [Pseudochaenichthys georgianus]
Protein Classification
RP/EB family microtubule-associated protein( domain architecture ID 1000504)
RP/EB family microtubule-associated protein may play important roles in microtubule dynamic regulation, cytokinesis, mitotic spindle positioning, and episome segregation
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| BIM1 super family | cl34944 | Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ... |
16-252 | 1.66e-42 | |||||
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton]; The actual alignment was detected with superfamily member COG5217: Pssm-ID: 227542 [Multi-domain] Cd Length: 342 Bit Score: 147.84 E-value: 1.66e-42
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| Name | Accession | Description | Interval | E-value | |||||
| BIM1 | COG5217 | Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ... |
16-252 | 1.66e-42 | |||||
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton]; Pssm-ID: 227542 [Multi-domain] Cd Length: 342 Bit Score: 147.84 E-value: 1.66e-42
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| EB1 | pfam03271 | EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ... |
200-238 | 5.75e-15 | |||||
EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related to the EB1 protein. The EB1 proteins contain an N-terminal CH domain pfam00307. The human EB1 protein was originally discovered as a protein interacting with the C-terminus of the APC protein. This interaction is often disrupted in colon cancer, due to deletions affecting the APC C-terminus. Several EB1 orthologues are also included in this family. The interaction between EB1 and APC has been shown to have a potent synergistic effect on microtubule polymerization. Neither of EB1 or APC alone has this effect. It is thought that EB1 targets APC to the + ends of microtubules, where APC promotes microtubule polymerization. This process is regulated by APC phosphorylation by Cdc2, which disrupts APC-EB1 binding. Human EB1 protein can functionally substitute for the yeast EB1 homolog Mal3. In addition, Mal3 can substitute for human EB1 in promoting microtubule polymerization with APC. Pssm-ID: 460870 Cd Length: 41 Bit Score: 67.15 E-value: 5.75e-15
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| Name | Accession | Description | Interval | E-value | |||||
| BIM1 | COG5217 | Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ... |
16-252 | 1.66e-42 | |||||
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton]; Pssm-ID: 227542 [Multi-domain] Cd Length: 342 Bit Score: 147.84 E-value: 1.66e-42
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| EB1 | pfam03271 | EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ... |
200-238 | 5.75e-15 | |||||
EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related to the EB1 protein. The EB1 proteins contain an N-terminal CH domain pfam00307. The human EB1 protein was originally discovered as a protein interacting with the C-terminus of the APC protein. This interaction is often disrupted in colon cancer, due to deletions affecting the APC C-terminus. Several EB1 orthologues are also included in this family. The interaction between EB1 and APC has been shown to have a potent synergistic effect on microtubule polymerization. Neither of EB1 or APC alone has this effect. It is thought that EB1 targets APC to the + ends of microtubules, where APC promotes microtubule polymerization. This process is regulated by APC phosphorylation by Cdc2, which disrupts APC-EB1 binding. Human EB1 protein can functionally substitute for the yeast EB1 homolog Mal3. In addition, Mal3 can substitute for human EB1 in promoting microtubule polymerization with APC. Pssm-ID: 460870 Cd Length: 41 Bit Score: 67.15 E-value: 5.75e-15
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| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
16-119 | 3.03e-13 | |||||
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy. Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 64.23 E-value: 3.03e-13
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