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Conserved domains on  [gi|19387961|gb|AAH25804|]
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Microtubule-associated protein, RP/EB family, member 2 [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

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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 ...
 58-312 5.57e-41

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: 145.91  E-value: 5.57e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19387961  58 SRHDIIAWVNDIVSLNYTKVEQLCSGAAYCQFMDMLFpGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEK 137
Cdd:COG5217   8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19387961 138 LVKGRFQDNLDFIQWFKKFYDANYDGKEYDPVEARQGQDAIpppdpgeQIFNLPKKSHHANSPTagAAKSSPASKPGSTP 217
Cdd:COG5217  87 LVRCKLQDNLEFLQWLKDHWVRNLGHISYDRNARRLGRTPK-------STRELIEWIRSLGIPI--SAIRELSKGVASCK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19387961 218 SR-------PSSAKRASSSGSASRSDKDLETQVI-QLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQE--------- 280
Cdd:COG5217 158 SLstihssfPQNFVKNTAGTHDYLRAMQACQEFIgSLNIKLYFPVDTLVKLEMERAFYFNKLRSIEILVETlkregpras 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 19387961 281 ----------HGQEN----DDLVQRLMEVLYASDEQEGQTEEPEAE 312
Cdd:COG5217 238 ilpgtslqcpHCKNTreimDAKDNRIKEILYMTASGFERIMDMEAD 283
 
Name Accession Description Interval E-value
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 58-312 5.57e-41

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


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 145.91  E-value: 5.57e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19387961  58 SRHDIIAWVNDIVSLNYTKVEQLCSGAAYCQFMDMLFpGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEK 137
Cdd:COG5217   8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19387961 138 LVKGRFQDNLDFIQWFKKFYDANYDGKEYDPVEARQGQDAIpppdpgeQIFNLPKKSHHANSPTagAAKSSPASKPGSTP 217
Cdd:COG5217  87 LVRCKLQDNLEFLQWLKDHWVRNLGHISYDRNARRLGRTPK-------STRELIEWIRSLGIPI--SAIRELSKGVASCK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19387961 218 SR-------PSSAKRASSSGSASRSDKDLETQVI-QLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQE--------- 280
Cdd:COG5217 158 SLstihssfPQNFVKNTAGTHDYLRAMQACQEFIgSLNIKLYFPVDTLVKLEMERAFYFNKLRSIEILVETlkregpras 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 19387961 281 ----------HGQEN----DDLVQRLMEVLYASDEQEGQTEEPEAE 312
Cdd:COG5217 238 ilpgtslqcpHCKNTreimDAKDNRIKEILYMTASGFERIMDMEAD 283
EB1 pfam03271
EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ...
 260-298 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: 68.69  E-value: 2.52e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 19387961   260 VEKERDFYFGKLREIELLCQEHGQ--ENDDLVQRLMEVLYA 298
Cdd:pfam03271   1 LEKERDFYFNKLRDIEILCQEEEEdeEEDPLIKKIQDILYA 41
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 60-151 1.93e-03

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 37.30  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19387961     60 HDIIAWVNDIVSLNY-TKVEQ----LCSGAAYCQFMDMLFPGCISLKKV--KFQAKLEHEYIHNFklLQASFKRMNVDKV 132
Cdd:smart00033   1 KTLLRWVNSLLAEYDkPPVTNfssdLKDGVALCALLNSLSPGLVDKKKVaaSLSRFKKIENINLA--LSFAEKLGGKVVL 78

                           90
                   ....*....|....*....
gi 19387961    133 IPVEKLVKGRfQDNLDFIQ 151
Cdd:smart00033  79 FEPEDLVEGP-KLILGVIW 96
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 59-132 9.17e-03

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 35.39  E-value: 9.17e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19387961  59 RHDIIAWVNDIVSLNYTKV-----EQLCSGAAYCQFMDMLFPGCIslKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKV 132
Cdd:cd00014   1 EEELLKWINEVLGEELPVSitdlfESLRDGVLLCKLINKLSPGSI--PKINKKPKSPFKKRENINLFLNACKKLGLPEL 77
 
Name Accession Description Interval E-value
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 58-312 5.57e-41

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


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 145.91  E-value: 5.57e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19387961  58 SRHDIIAWVNDIVSLNYTKVEQLCSGAAYCQFMDMLFpGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEK 137
Cdd:COG5217   8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19387961 138 LVKGRFQDNLDFIQWFKKFYDANYDGKEYDPVEARQGQDAIpppdpgeQIFNLPKKSHHANSPTagAAKSSPASKPGSTP 217
Cdd:COG5217  87 LVRCKLQDNLEFLQWLKDHWVRNLGHISYDRNARRLGRTPK-------STRELIEWIRSLGIPI--SAIRELSKGVASCK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19387961 218 SR-------PSSAKRASSSGSASRSDKDLETQVI-QLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQE--------- 280
Cdd:COG5217 158 SLstihssfPQNFVKNTAGTHDYLRAMQACQEFIgSLNIKLYFPVDTLVKLEMERAFYFNKLRSIEILVETlkregpras 237

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 19387961 281 ----------HGQEN----DDLVQRLMEVLYASDEQEGQTEEPEAE 312
Cdd:COG5217 238 ilpgtslqcpHCKNTreimDAKDNRIKEILYMTASGFERIMDMEAD 283
EB1 pfam03271
EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ...
 260-298 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: 68.69  E-value: 2.52e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 19387961   260 VEKERDFYFGKLREIELLCQEHGQ--ENDDLVQRLMEVLYA 298
Cdd:pfam03271   1 LEKERDFYFNKLRDIEILCQEEEEdeEEDPLIKKIQDILYA 41
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 58-161 2.74e-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: 65.39  E-value: 2.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19387961    58 SRHDIIAWVNDIVSLNYTKV------EQLCSGAAYCQFMDMLFPGCISLKKVKFQaklEHEYIHNFKL-LQASFKRMNVD 130
Cdd:pfam00307   3 LEKELLRWINSHLAEYGPGVrvtnftTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLaLDVAEKKLGVP 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 19387961   131 KV-IPVEKLVKGrfqDNLDFIQWFKKFYDANY 161
Cdd:pfam00307  80 KVlIEPEDLVEG---DNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 60-151 1.93e-03

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 37.30  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19387961     60 HDIIAWVNDIVSLNY-TKVEQ----LCSGAAYCQFMDMLFPGCISLKKV--KFQAKLEHEYIHNFklLQASFKRMNVDKV 132
Cdd:smart00033   1 KTLLRWVNSLLAEYDkPPVTNfssdLKDGVALCALLNSLSPGLVDKKKVaaSLSRFKKIENINLA--LSFAEKLGGKVVL 78

                           90
                   ....*....|....*....
gi 19387961    133 IPVEKLVKGRfQDNLDFIQ 151
Cdd:smart00033  79 FEPEDLVEGP-KLILGVIW 96
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 59-132 9.17e-03

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 35.39  E-value: 9.17e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19387961  59 RHDIIAWVNDIVSLNYTKV-----EQLCSGAAYCQFMDMLFPGCIslKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKV 132
Cdd:cd00014   1 EEELLKWINEVLGEELPVSitdlfESLRDGVLLCKLINKLSPGSI--PKINKKPKSPFKKRENINLFLNACKKLGLPEL 77
 
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.
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