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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
5N74_H        20 LEKERDFYFGKLRNIELICQE--NEGENDPVLQRIVDILYA 58
Cdd:pfam03271  1 LEKERDFYFNKLRDIEILCQEeeEDEEEDPLIKKIQDILYA 41

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
5N74_H        20 LEKERDFYFGKLRNIELICQE--NEGENDPVLQRIVDILYA 58
Cdd:pfam03271  1 LEKERDFYFNKLRDIEILCQEeeEDEEEDPLIKKIQDILYA 41

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
5N74_H        20 LEKERDFYFGKLRNIELICQE--NEGENDPVLQRIVDILYA 58
Cdd:pfam03271  1 LEKERDFYFNKLRDIEILCQEeeEDEEEDPLIKKIQDILYA 41