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Conserved domains on  [gi|1907129169|ref|XP_036016940|]
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microtubule-associated protein RP/EB family member 2 isoform X1 [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 ...
16-270 2.35e-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: 145.52  E-value: 2.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129169  16 SRHDIIAWVNDIVSLNYTKVEQLCSGAAYCQFMDMLFpGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEK 95
Cdd:COG5217     8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129169  96 LVKGRFQDNLDFIQWFKKFYDANYDGKEYDPVEARQGQDAIpppdpgeQIFNLPKKSHHANSPTagAAKSSPASKPGSTP 175
Cdd:COG5217    87 LVRCKLQDNLEFLQWLKDHWVRNLGHISYDRNARRLGRTPK-------STRELIEWIRSLGIPI--SAIRELSKGVASCK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129169 176 SR-------PSSAKRASSSGSASRSDKDLETQVI-QLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQE--------- 238
Cdd:COG5217   158 SLstihssfPQNFVKNTAGTHDYLRAMQACQEFIgSLNIKLYFPVDTLVKLEMERAFYFNKLRSIEILVETlkregpras 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907129169 239 ----------HGQEN----DDLVQRLMEVLYASDEQEGQTEEPEAE 270
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 ...
16-270 2.35e-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: 145.52  E-value: 2.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129169  16 SRHDIIAWVNDIVSLNYTKVEQLCSGAAYCQFMDMLFpGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEK 95
Cdd:COG5217     8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129169  96 LVKGRFQDNLDFIQWFKKFYDANYDGKEYDPVEARQGQDAIpppdpgeQIFNLPKKSHHANSPTagAAKSSPASKPGSTP 175
Cdd:COG5217    87 LVRCKLQDNLEFLQWLKDHWVRNLGHISYDRNARRLGRTPK-------STRELIEWIRSLGIPI--SAIRELSKGVASCK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129169 176 SR-------PSSAKRASSSGSASRSDKDLETQVI-QLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQE--------- 238
Cdd:COG5217   158 SLstihssfPQNFVKNTAGTHDYLRAMQACQEFIgSLNIKLYFPVDTLVKLEMERAFYFNKLRSIEILVETlkregpras 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907129169 239 ----------HGQEN----DDLVQRLMEVLYASDEQEGQTEEPEAE 270
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 ...
218-256 7.28e-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: 7.28e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907129169 218 VEKERDFYFGKLREIELLCQEHGQ--ENDDLVQRLMEVLYA 256
Cdd:pfam03271   1 LEKERDFYFNKLRDIEILCQEEEEdeEEDPLIKKIQDILYA 41
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
18-109 2.46e-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: 36.52  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129169   18 HDIIAWVNDIVSLNY-TKVEQ----LCSGAAYCQFMDMLFPGCISLKKV--KFQAKLEHEYIHNFklLQASFKRMNVDKV 90
Cdd:smart00033   1 KTLLRWVNSLLAEYDkPPVTNfssdLKDGVALCALLNSLSPGLVDKKKVaaSLSRFKKIENINLA--LSFAEKLGGKVVL 78
                           90
                   ....*....|....*....
gi 1907129169   91 IPVEKLVKGRfQDNLDFIQ 109
Cdd:smart00033  79 FEPEDLVEGP-KLILGVIW 96
 
Name Accession Description Interval E-value
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
16-270 2.35e-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: 145.52  E-value: 2.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129169  16 SRHDIIAWVNDIVSLNYTKVEQLCSGAAYCQFMDMLFpGCISLKKVKFQAKLEHEYIHNFKLLQASFKRMNVDKVIPVEK 95
Cdd:COG5217     8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129169  96 LVKGRFQDNLDFIQWFKKFYDANYDGKEYDPVEARQGQDAIpppdpgeQIFNLPKKSHHANSPTagAAKSSPASKPGSTP 175
Cdd:COG5217    87 LVRCKLQDNLEFLQWLKDHWVRNLGHISYDRNARRLGRTPK-------STRELIEWIRSLGIPI--SAIRELSKGVASCK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129169 176 SR-------PSSAKRASSSGSASRSDKDLETQVI-QLNEQVHSLKLALEGVEKERDFYFGKLREIELLCQE--------- 238
Cdd:COG5217   158 SLstihssfPQNFVKNTAGTHDYLRAMQACQEFIgSLNIKLYFPVDTLVKLEMERAFYFNKLRSIEILVETlkregpras 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907129169 239 ----------HGQEN----DDLVQRLMEVLYASDEQEGQTEEPEAE 270
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 ...
218-256 7.28e-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: 7.28e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1907129169 218 VEKERDFYFGKLREIELLCQEHGQ--ENDDLVQRLMEVLYA 256
Cdd:pfam03271   1 LEKERDFYFNKLRDIEILCQEEEEdeEEDPLIKKIQDILYA 41
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
16-119 4.62e-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: 4.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129169  16 SRHDIIAWVNDIVSLNYTKV------EQLCSGAAYCQFMDMLFPGCISLKKVKFQaklEHEYIHNFKL-LQASFKRMNVD 88
Cdd:pfam00307   3 LEKELLRWINSHLAEYGPGVrvtnftTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLaLDVAEKKLGVP 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1907129169  89 KV-IPVEKLVKGrfqDNLDFIQWFKKFYDANY 119
Cdd:pfam00307  80 KVlIEPEDLVEG---DNKSVLTYLASLFRRFQ 108
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
18-109 2.46e-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: 36.52  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129169   18 HDIIAWVNDIVSLNY-TKVEQ----LCSGAAYCQFMDMLFPGCISLKKV--KFQAKLEHEYIHNFklLQASFKRMNVDKV 90
Cdd:smart00033   1 KTLLRWVNSLLAEYDkPPVTNfssdLKDGVALCALLNSLSPGLVDKKKVaaSLSRFKKIENINLA--LSFAEKLGGKVVL 78
                           90
                   ....*....|....*....
gi 1907129169   91 IPVEKLVKGRfQDNLDFIQ 109
Cdd:smart00033  79 FEPEDLVEGP-KLILGVIW 96
 
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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