NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|569003472|ref|XP_006525808|]
View 

microtubule-associated protein RP/EB family member 2 isoform X2 [Mus musculus]

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

Gene Ontology:  GO:0008017|GO:0051301
PubMed:  10188731

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 29-259 1.70e-32

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: 122.03  E-value: 1.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003472  29 TGAAYCQFMDMLFpGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEKLVKGRFQDNLDFIQWFKKFYDANY 108
Cdd:COG5217   32 EGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLVLVRCKLQDNLEFLQWLKDHWVRNL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003472 109 DGKEYDPVEARQGQDAIpppdpgeQIFNLPKKSHHANSPTagAAKSSPASKPGSTPSR-------PSSAKRASSSGSASR 181
Cdd:COG5217  111 GHISYDRNARRLGRTPK-------STRELIEWIRSLGIPI--SAIRELSKGVASCKSLstihssfPQNFVKNTAGTHDYL 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003472 182 SDKDLETQVI-QLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQE-------------------HGQEN----DDLVQ 237
Cdd:COG5217  182 RAMQACQEFIgSLNIKLYFPVDTLVKLEMERAFYFNKLRSIEILVETlkregprasilpgtslqcpHCKNTreimDAKDN 261

                        250       260
                 ....*....|....*....|..
gi 569003472 238 RLMEVLYASDEQEGQTEEPEAE 259
Cdd:COG5217  262 RIKEILYMTASGFERIMDMEAD 283
 
Name Accession Description Interval E-value
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 29-259 1.70e-32

Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton];


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 122.03  E-value: 1.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003472  29 TGAAYCQFMDMLFpGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEKLVKGRFQDNLDFIQWFKKFYDANY 108
Cdd:COG5217   32 EGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLVLVRCKLQDNLEFLQWLKDHWVRNL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003472 109 DGKEYDPVEARQGQDAIpppdpgeQIFNLPKKSHHANSPTagAAKSSPASKPGSTPSR-------PSSAKRASSSGSASR 181
Cdd:COG5217  111 GHISYDRNARRLGRTPK-------STRELIEWIRSLGIPI--SAIRELSKGVASCKSLstihssfPQNFVKNTAGTHDYL 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003472 182 SDKDLETQVI-QLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQE-------------------HGQEN----DDLVQ 237
Cdd:COG5217  182 RAMQACQEFIgSLNIKLYFPVDTLVKLEMERAFYFNKLRSIEILVETlkregprasilpgtslqcpHCKNTreimDAKDN 261

                        250       260
                 ....*....|....*....|..
gi 569003472 238 RLMEVLYASDEQEGQTEEPEAE 259
Cdd:COG5217  262 RIKEILYMTASGFERIMDMEAD 283
EB1 pfam03271
EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ...
 207-245 2.52e-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: 67.92  E-value: 2.52e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 569003472  207 VEKERDFYFGKLREIELLCQEHGQ--ENDDLVQRLMEVLYA 245
Cdd:pfam03271   1 LEKERDFYFNKLRDIEILCQEEEEdeEEDPLIKKIQDILYA 41
 
Name Accession Description Interval E-value
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 29-259 1.70e-32

Microtubule-binding protein involved in cell cycle control [Cell division and chromosome partitioning / Cytoskeleton];


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 122.03  E-value: 1.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003472  29 TGAAYCQFMDMLFpGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEKLVKGRFQDNLDFIQWFKKFYDANY 108
Cdd:COG5217   32 EGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLVLVRCKLQDNLEFLQWLKDHWVRNL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003472 109 DGKEYDPVEARQGQDAIpppdpgeQIFNLPKKSHHANSPTagAAKSSPASKPGSTPSR-------PSSAKRASSSGSASR 181
Cdd:COG5217  111 GHISYDRNARRLGRTPK-------STRELIEWIRSLGIPI--SAIRELSKGVASCKSLstihssfPQNFVKNTAGTHDYL 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003472 182 SDKDLETQVI-QLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQE-------------------HGQEN----DDLVQ 237
Cdd:COG5217  182 RAMQACQEFIgSLNIKLYFPVDTLVKLEMERAFYFNKLRSIEILVETlkregprasilpgtslqcpHCKNTreimDAKDN 261

                        250       260
                 ....*....|....*....|..
gi 569003472 238 RLMEVLYASDEQEGQTEEPEAE 259
Cdd:COG5217  262 RIKEILYMTASGFERIMDMEAD 283
EB1 pfam03271
EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ...
 207-245 2.52e-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: 67.92  E-value: 2.52e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 569003472  207 VEKERDFYFGKLREIELLCQEHGQ--ENDDLVQRLMEVLYA 245
Cdd:pfam03271   1 LEKERDFYFNKLRDIEILCQEEEEdeEEDPLIKKIQDILYA 41
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 29-108 9.28e-09

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: 52.29  E-value: 9.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003472   29 TGAAYCQFMDMLFPGCISLKKVKFQaklEHEYIHNFKL-LQASFKRMNVDKV-IPVEKLVKGrfqDNLDFIQWFKKFYDA 106
Cdd:pfam00307  33 DGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLaLDVAEKKLGVPKVlIEPEDLVEG---DNKSVLTYLASLFRR 106


                  ..
gi 569003472  107 NY 108
Cdd:pfam00307 107 FQ 108
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH