microtubule-associated protein RP/EB family member 2 isoform 4 [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
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 ... |
30-260 | 4.63e-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: 120.87 E-value: 4.63e-32
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| BIM1 | COG5217 | Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ... |
30-260 | 4.63e-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: 120.87 E-value: 4.63e-32
|
|||||||||
| EB1 | pfam03271 | EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ... |
208-246 | 2.80e-16 | |||||
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: 70.62 E-value: 2.80e-16
|
|||||||||
| PBP2_Lactococcal_OppA_like | cd08510 | The substrate binding component of an ABC-type lactococcal OppA-like transport system contains; ... |
64-121 | 9.19e-03 | |||||
The substrate binding component of an ABC-type lactococcal OppA-like transport system contains; This family represents the substrate binding domain of an ATP-binding cassette (ABC)-type oligopeptide import system from Lactococcus lactis and other gram-positive bacteria, as well as its closet homologs from gram-negative bacteria. Oligopeptide-binding protein (OppA) from Lactococcus lactis can bind peptides of length from 4 to at least 35 residues without sequence preference. The oligopeptide import system OppABCDEF is consisting of five subunits: two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and also is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction. Pssm-ID: 173875 [Multi-domain] Cd Length: 516 Bit Score: 37.25 E-value: 9.19e-03
|
|||||||||
| Name | Accession | Description | Interval | E-value | |||||
| BIM1 | COG5217 | Microtubule-binding protein involved in cell cycle control [Cell division and chromosome ... |
30-260 | 4.63e-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: 120.87 E-value: 4.63e-32
|
|||||||||
| EB1 | pfam03271 | EB1-like C-terminal motif; This motif is found at the C-terminus of proteins that are related ... |
208-246 | 2.80e-16 | |||||
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: 70.62 E-value: 2.80e-16
|
|||||||||
| CH | pfam00307 | Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
30-109 | 9.35e-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: 9.35e-09
|
|||||||||
| PBP2_Lactococcal_OppA_like | cd08510 | The substrate binding component of an ABC-type lactococcal OppA-like transport system contains; ... |
64-121 | 9.19e-03 | |||||
The substrate binding component of an ABC-type lactococcal OppA-like transport system contains; This family represents the substrate binding domain of an ATP-binding cassette (ABC)-type oligopeptide import system from Lactococcus lactis and other gram-positive bacteria, as well as its closet homologs from gram-negative bacteria. Oligopeptide-binding protein (OppA) from Lactococcus lactis can bind peptides of length from 4 to at least 35 residues without sequence preference. The oligopeptide import system OppABCDEF is consisting of five subunits: two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and also is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction. Pssm-ID: 173875 [Multi-domain] Cd Length: 516 Bit Score: 37.25 E-value: 9.19e-03
|
|||||||||
| Blast search parameters | ||||
|
