5M97


Conserved Protein Domain Family
EB1

?
pfam03271: EB1 
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.
Statistics
?
PSSM-Id: 460870
Aligned: 141 rows
Threshold Bit Score: 32.4806
Created: 21-Mar-2022
Updated: 17-Oct-2022
Structure
?
Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
5M97_B        28 LERERDFYFNKLREIEILV---QThl--------tTSPMsMENML--ERIQAILYS 70  Schizosaccharomyces pombe 972h-
XP_004037254 201 sEIEKSFYFSKLKDIDFLVdvys---------elsQNDTkLHDLI--DKIRKILYt 245
EGW35246     232 LQIERNFYFNKLQDIEMIVqhileak--ehgksyeFADLdIFKLS--NKIQTILYA 283
CCE43260     384 LQVERNFYFNKCRDIEILIqnie---------hneTLMSeLDVLTllKKIEDTLYA 430
XP_001706073 181 gQLESQFYFDKLHEIEIYMdqmnelmtqveiaepeDSPFyIKSVV--KKIEDILYA 234
EDK42622     372 LQTERNFYFNKLRDIELLIqniQAdp-------siVEKLdVLTLT--AQVEKLLYK 418
EMG49735     248 MQSERNFYFNKLRAIEILV---QHake------mdGLSSdLLQFA--NEIEKIMYE 292
Q59W48       246 VESERDFYFNKLRAIEILV---QHake------meGLSGdVLQFA--NEIEKIMYE 290 Candida albicans
EOB12584      14 MEANRDFYFKKLVEIEKYLe---------------MNKEiCEDAK--TEIFEILYK 52 
EEQ82749     192 LEENRNFYFCILVEIEKYLt---------------ECDSiEENVK--NDIFNILYK 230
| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap