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Conserved domains on  [gi|6912494|ref|NP_036457|]
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microtubule-associated protein RP/EB family member 1 [Homo sapiens]

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 ...
 16-257 1.39e-45

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: 156.31  E-value: 1.39e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912494   16 SRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFpGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDK 95
Cdd:COG5217   8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912494   96 LVKGKFQDNFEFVQWFKKFFDANYDGKDYDPVAARQGQetavAPSLVAPALNKPKK---PLT----SSSAAPQRPISTQR 168
Cdd:COG5217  87 LVRCKLQDNLEFLQWLKDHWVRNLGHISYDRNARRLGR----TPKSTRELIEWIRSlgiPISaireLSKGVASCKSLSTI 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912494  169 TAAAPKAGPgvvrKNPGVGNGDDEAAELMQQ--------VNVLKLTVEDLEKERDFYFGKLRNIELI------------- 227
Cdd:COG5217 163 HSSFPQNFV----KNTAGTHDYLRAMQACQEfigslnikLYFPVDTLVKLEMERAFYFNKLRSIEILvetlkregprasi 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 6912494  228 ----------CQENEGENDPVLQRIVDILYATDEGF-VIPD 257
Cdd:COG5217 239 lpgtslqcphCKNTREIMDAKDNRIKEILYMTASGFeRIMD 279
 
Name Accession Description Interval E-value
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 16-257 1.39e-45

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


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 156.31  E-value: 1.39e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912494   16 SRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFpGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDK 95
Cdd:COG5217   8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912494   96 LVKGKFQDNFEFVQWFKKFFDANYDGKDYDPVAARQGQetavAPSLVAPALNKPKK---PLT----SSSAAPQRPISTQR 168
Cdd:COG5217  87 LVRCKLQDNLEFLQWLKDHWVRNLGHISYDRNARRLGR----TPKSTRELIEWIRSlgiPISaireLSKGVASCKSLSTI 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912494  169 TAAAPKAGPgvvrKNPGVGNGDDEAAELMQQ--------VNVLKLTVEDLEKERDFYFGKLRNIELI------------- 227
Cdd:COG5217 163 HSSFPQNFV----KNTAGTHDYLRAMQACQEfigslnikLYFPVDTLVKLEMERAFYFNKLRSIEILvetlkregprasi 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 6912494  228 ----------CQENEGENDPVLQRIVDILYATDEGF-VIPD 257
Cdd:COG5217 239 lpgtslqcphCKNTREIMDAKDNRIKEILYMTASGFeRIMD 279
EB1 pfam03271
EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ...
 210-248 4.35e-17

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: 72.93  E-value: 4.35e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 6912494    210 LEKERDFYFGKLRNIELICQE--NEGENDPVLQRIVDILYA 248
Cdd:pfam03271   1 LEKERDFYFNKLRDIEILCQEeeEDEEEDPLIKKIQDILYA 41
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 17-90 5.76e-05

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: 41.17  E-value: 5.76e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6912494   17 RHDMLAWINESLQLNLTK-----IEQLCSGAAYCQFMDMLFPGSIalKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKI 90
Cdd:cd00014   1 EEELLKWINEVLGEELPVsitdlFESLRDGVLLCKLINKLSPGSI--PKINKKPKSPFKKRENINLFLNACKKLGLPEL 77
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 18-100 2.10e-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: 36.91  E-value: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912494      18 HDMLAWINESLQLNL-TKIEQ----LCSGAAYCQFMDMLFPGSIALKKV--KFQAKLEHEYIQNFkiLQAGFKRMGVDKI 90
Cdd:smart00033   1 KTLLRWVNSLLAEYDkPPVTNfssdLKDGVALCALLNSLSPGLVDKKKVaaSLSRFKKIENINLA--LSFAEKLGGKVVL 78

                           90
                   ....*....|
gi 6912494      91 IPVDKLVKGK 100
Cdd:smart00033  79 FEPEDLVEGP 88
 
Name Accession Description Interval E-value
BIM1 COG5217
Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ...
 16-257 1.39e-45

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


Pssm-ID: 227542 [Multi-domain]  Cd Length: 342  Bit Score: 156.31  E-value: 1.39e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912494   16 SRHDMLAWINESLQLNLTKIEQLCSGAAYCQFMDMLFpGSIALKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKIIPVDK 95
Cdd:COG5217   8 SREELLFWENVVVRLDLQRIEDCGEGFAMQQIHDSIY-VDLPDSLVRFPWIAEYKHPGNGKILQLLFSDYGIDKAVLVLV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912494   96 LVKGKFQDNFEFVQWFKKFFDANYDGKDYDPVAARQGQetavAPSLVAPALNKPKK---PLT----SSSAAPQRPISTQR 168
Cdd:COG5217  87 LVRCKLQDNLEFLQWLKDHWVRNLGHISYDRNARRLGR----TPKSTRELIEWIRSlgiPISaireLSKGVASCKSLSTI 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912494  169 TAAAPKAGPgvvrKNPGVGNGDDEAAELMQQ--------VNVLKLTVEDLEKERDFYFGKLRNIELI------------- 227
Cdd:COG5217 163 HSSFPQNFV----KNTAGTHDYLRAMQACQEfigslnikLYFPVDTLVKLEMERAFYFNKLRSIEILvetlkregprasi 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 6912494  228 ----------CQENEGENDPVLQRIVDILYATDEGF-VIPD 257
Cdd:COG5217 239 lpgtslqcphCKNTREIMDAKDNRIKEILYMTASGFeRIMD 279
EB1 pfam03271
EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ...
 210-248 4.35e-17

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: 72.93  E-value: 4.35e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 6912494    210 LEKERDFYFGKLRNIELICQE--NEGENDPVLQRIVDILYA 248
Cdd:pfam03271   1 LEKERDFYFNKLRDIEILCQEeeEDEEEDPLIKKIQDILYA 41
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
 16-119 7.17e-15

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: 68.85  E-value: 7.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912494     16 SRHDMLAWINESLQLNLTKI------EQLCSGAAYCQFMDMLFPGSIALKKVKFQaklEHEYIQNFKI-LQAGFKRMGVD 88
Cdd:pfam00307   3 LEKELLRWINSHLAEYGPGVrvtnftTDLRDGLALCALLNKLAPGLVDKKKLNKS---EFDKLENINLaLDVAEKKLGVP 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 6912494     89 KI-IPVDKLVKGkfqDNFEFVQWFKKFFDANY 119
Cdd:pfam00307  80 KVlIEPEDLVEG---DNKSVLTYLASLFRRFQ 108
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
 17-90 5.76e-05

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: 41.17  E-value: 5.76e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6912494   17 RHDMLAWINESLQLNLTK-----IEQLCSGAAYCQFMDMLFPGSIalKKVKFQAKLEHEYIQNFKILQAGFKRMGVDKI 90
Cdd:cd00014   1 EEELLKWINEVLGEELPVsitdlFESLRDGVLLCKLINKLSPGSI--PKINKKPKSPFKKRENINLFLNACKKLGLPEL 77
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
 18-100 2.10e-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: 36.91  E-value: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6912494      18 HDMLAWINESLQLNL-TKIEQ----LCSGAAYCQFMDMLFPGSIALKKV--KFQAKLEHEYIQNFkiLQAGFKRMGVDKI 90
Cdd:smart00033   1 KTLLRWVNSLLAEYDkPPVTNfssdLKDGVALCALLNSLSPGLVDKKKVaaSLSRFKKIENINLA--LSFAEKLGGKVVL 78

                           90
                   ....*....|
gi 6912494      91 IPVDKLVKGK 100
Cdd:smart00033  79 FEPEDLVEGP 88
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 192-222 6.42e-03

Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, and neural retina leucine zipper or NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. MafA and MafB also play crucial roles in islet beta cells; they regulate genes essential for glucose sensing and insulin secretion cooperatively and sequentially. Large Mafs are also implicated in oncogenesis; MafB and c-Maf chromosomal translocations result in multiple myelomas. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269866  Cd Length: 70  Bit Score: 34.56  E-value: 6.42e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 6912494  192 EAAELMQQVNVLKLTVEDLEKERDFY---FGKLR 222
Cdd:cd14718  37 EKCQLQQQVEQLKQEVSRLARERDAYkekYEKLA 70
 
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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