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Conserved domains on  [gi|568988330|ref|XP_006519393|]
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bridging integrator 3 isoform X1 [Mus musculus]

Protein Classification

bridging integrator 3( domain architecture ID 10166121)

bridging integrator 3 (BIN3) is involved in cytokinesis and septation where it has a role in the localization of F-actin; it contains a BAR (Bin/Amphiphysin/Rvs) domain

Gene Symbol:  BIN3
Gene Ontology:  GO:0140090|GO:0097753|GO:0005515
PubMed:  23872330|15649145|30456600|14993925

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR_Bin3 cd07590
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ...
 12-209 6.45e-97

The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 3 (Bin3) is widely expressed in many tissues except in the brain. It plays roles in regulating filamentous actin localization and in cell division. In humans, the Bin3 gene is located in chromosome 8p21.3, a region that is implicated in cancer suppression. Homozygous inactivation of the Bin3 gene in mice led to the development of cataracts and an increased likelihood of lymphomas during aging, suggesting a role for Bin3 in lens development and cancer suppression. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


:

Pssm-ID: 153274  Cd Length: 225  Bit Score: 281.95  E-value: 6.45e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  12 KKQIVSKTVERDFEREYGKLQQLEEQTKRLQKDMKKSTDADLAMSKSAVKISQDLLSNPLCEQDQDFLHMVTALDTAMKR 91
Cdd:cd07590    1 KKPILSKTVDRELEREVQKLQQLESTTKKLYKDMKKYIEAVLALSKAEQRLSQDLASGPLCEDNDELRNLVEALDSVTTQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  92 MDAFNQEKVNQIQKTVIEPLKKFSSIFPSLNMAVKRREQALQDYGRLQAKVEKYEEKEKTGPVLAKLHQAREELRPVRED 171
Cdd:cd07590   81 LDKTVQELVNLIQKTFIEPLKRLRSVFPSVNAAIKRREQSLQEYERLQAKVEKLAEKEKTGPNLAKLEQAEKALAAARAD 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568988330 172 FEAKNKQLLDEMPRFYGSRLDYFQPSFESLIRAQACSH 209
Cdd:cd07590  161 FEKQNIKLLEELPKFYNGRTDYFQPCFEALIKSQVLYY 198
 
Name Accession Description Interval E-value
BAR_Bin3 cd07590
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ...
 12-209 6.45e-97

The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 3 (Bin3) is widely expressed in many tissues except in the brain. It plays roles in regulating filamentous actin localization and in cell division. In humans, the Bin3 gene is located in chromosome 8p21.3, a region that is implicated in cancer suppression. Homozygous inactivation of the Bin3 gene in mice led to the development of cataracts and an increased likelihood of lymphomas during aging, suggesting a role for Bin3 in lens development and cancer suppression. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153274  Cd Length: 225  Bit Score: 281.95  E-value: 6.45e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  12 KKQIVSKTVERDFEREYGKLQQLEEQTKRLQKDMKKSTDADLAMSKSAVKISQDLLSNPLCEQDQDFLHMVTALDTAMKR 91
Cdd:cd07590    1 KKPILSKTVDRELEREVQKLQQLESTTKKLYKDMKKYIEAVLALSKAEQRLSQDLASGPLCEDNDELRNLVEALDSVTTQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  92 MDAFNQEKVNQIQKTVIEPLKKFSSIFPSLNMAVKRREQALQDYGRLQAKVEKYEEKEKTGPVLAKLHQAREELRPVRED 171
Cdd:cd07590   81 LDKTVQELVNLIQKTFIEPLKRLRSVFPSVNAAIKRREQSLQEYERLQAKVEKLAEKEKTGPNLAKLEQAEKALAAARAD 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568988330 172 FEAKNKQLLDEMPRFYGSRLDYFQPSFESLIRAQACSH 209
Cdd:cd07590  161 FEKQNIKLLEELPKFYNGRTDYFQPCFEALIKSQVLYY 198
BAR smart00721
BAR domain;
19-206 1.43e-32

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 118.26  E-value: 1.43e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330    19 TVERDFEREYGKLQQLEEQTKRLQKDMKK------STDADLAMSKSAVKISQDLLSNPL----CEQDQDFLHMVTALDTA 88
Cdd:smart00721  24 KLDEDFEELERRFDTTEAEIEKLQKDTKLylqpnpAVRAKLASQKKLSKSLGEVYEGGDdgegLGADSSYGKALDKLGEA 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330    89 MKRMdAFNQEKVNQIQKTVIEPLKKFS-SIFPSLNMAVKRREQALQDYGRLQAKVEKYEEKEKTgPVLAKLHQAREELRP 167
Cdd:smart00721 104 LKKL-LQVEESLSQVKRTFILPLLNFLlGEFKEIKKARKKLERKLLDYDSARHKLKKAKKSKEK-KKDEKLAKAEEELRK 181

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 568988330   168 VREDFEAKNKQLLDEMPRFYGSRLDYFQPSFESLIRAQA 206
Cdd:smart00721 182 AKQEFEESNAQLVEELPQLVASRVDFFVNCLQALIEAQL 220
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 19-210 1.77e-15

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 72.75  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330   19 TVERDFEREYGKLQQLEEQTKRLQKDMKKSTDADLAM--SKSAVKISQDLLSNPLCE------QDQDFLHMVTALDTAMK 90
Cdd:pfam03114  23 KLDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGAraKQTVLEQPEELLAESMIEagkdlgEDSSFGKALEDYGEALK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330   91 RMDAFNQEKVNQIQKTVIEPLKKFSSIFPSLNMAVKRREQALQDYGRLQAKVEKYEEKEKTGpvLAKLHQAREELRPVRE 170
Cdd:pfam03114 103 RLAQLLEQLDDRVETNFLDPLRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKKKSSK--AKDESQAEEELRKAQA 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568988330  171 DFEAKNKQLLDEMPRFYGSRLDYFQPSFESLIRAQACSHH 210
Cdd:pfam03114 181 KFEESNEQLKALLPNLLSLEVEFVVNQLVAFVEAQLDFHR 220
 
Name Accession Description Interval E-value
BAR_Bin3 cd07590
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ...
 12-209 6.45e-97

The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 3 (Bin3) is widely expressed in many tissues except in the brain. It plays roles in regulating filamentous actin localization and in cell division. In humans, the Bin3 gene is located in chromosome 8p21.3, a region that is implicated in cancer suppression. Homozygous inactivation of the Bin3 gene in mice led to the development of cataracts and an increased likelihood of lymphomas during aging, suggesting a role for Bin3 in lens development and cancer suppression. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153274  Cd Length: 225  Bit Score: 281.95  E-value: 6.45e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  12 KKQIVSKTVERDFEREYGKLQQLEEQTKRLQKDMKKSTDADLAMSKSAVKISQDLLSNPLCEQDQDFLHMVTALDTAMKR 91
Cdd:cd07590    1 KKPILSKTVDRELEREVQKLQQLESTTKKLYKDMKKYIEAVLALSKAEQRLSQDLASGPLCEDNDELRNLVEALDSVTTQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  92 MDAFNQEKVNQIQKTVIEPLKKFSSIFPSLNMAVKRREQALQDYGRLQAKVEKYEEKEKTGPVLAKLHQAREELRPVRED 171
Cdd:cd07590   81 LDKTVQELVNLIQKTFIEPLKRLRSVFPSVNAAIKRREQSLQEYERLQAKVEKLAEKEKTGPNLAKLEQAEKALAAARAD 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568988330 172 FEAKNKQLLDEMPRFYGSRLDYFQPSFESLIRAQACSH 209
Cdd:cd07590  161 FEKQNIKLLEELPKFYNGRTDYFQPCFEALIKSQVLYY 198
BAR smart00721
BAR domain;
19-206 1.43e-32

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 118.26  E-value: 1.43e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330    19 TVERDFEREYGKLQQLEEQTKRLQKDMKK------STDADLAMSKSAVKISQDLLSNPL----CEQDQDFLHMVTALDTA 88
Cdd:smart00721  24 KLDEDFEELERRFDTTEAEIEKLQKDTKLylqpnpAVRAKLASQKKLSKSLGEVYEGGDdgegLGADSSYGKALDKLGEA 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330    89 MKRMdAFNQEKVNQIQKTVIEPLKKFS-SIFPSLNMAVKRREQALQDYGRLQAKVEKYEEKEKTgPVLAKLHQAREELRP 167
Cdd:smart00721 104 LKKL-LQVEESLSQVKRTFILPLLNFLlGEFKEIKKARKKLERKLLDYDSARHKLKKAKKSKEK-KKDEKLAKAEEELRK 181

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 568988330   168 VREDFEAKNKQLLDEMPRFYGSRLDYFQPSFESLIRAQA 206
Cdd:smart00721 182 AKQEFEESNAQLVEELPQLVASRVDFFVNCLQALIEAQL 220
BAR_Rvs161p cd07591
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 7-205 5.71e-28

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 161 and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 161 (Rvs161p) and Schizosaccharomyces pombe Hob3 (homolog of Bin3). S. cerevisiae Rvs161p plays a role in regulating cell polarity, actin cytoskeleton polarization, vesicle trafficking, endocytosis, bud formation, and the mating response. It forms a heterodimer with another BAR domain protein Rvs167p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. S. pombe Hob3 is important in regulating filamentous actin localization and may be required in activating Cdc42 and recruiting it to cell division sites. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153275  Cd Length: 224  Bit Score: 105.89  E-value: 5.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330   7 KIGQpkkqiVSKTVERDFEREYGKLQQLEEQTKRLQKDMKKSTDADLAMSKSAVKISQDLLSNPLCEQDQDFLHMVTALD 86
Cdd:cd07591    1 KTGQ-----VERTVDREFEFEERRYRTMEKASTKLQKEAKGYLDSLRALTSSQARIAETISSFYGDAGDKDGAMLSQEYK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  87 TAMKRMDA-FNQEKVNQIQKTVIEPLKKFSSIFPSLNMAVKRREQALQDYGRLQAKVEKYEEKEKTGPvlAKLHQAREEL 165
Cdd:cd07591   76 QAVEELDAeTVKELDGPYRQTVLDPIGRFNSYFPEINEAIKKRNHKLLDYDAARAKVRKLIDKPSEDP--TKLPRAEKEL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568988330 166 RPVREDFEAKNKQLLDEMPRFYGSRLDYFQPSFESLIRAQ 205
Cdd:cd07591  154 DEAKEVYETLNDQLKTELPQLVDLRIPYLDPSFEAFVKIQ 193
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 30-210 3.62e-18

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 79.03  E-value: 3.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  30 KLQQLEEQTKRLQKDMKKSTDADLAMSKSAVKISQDL--LSNPLCEQDQDFLH-MVTALDTAMKRMDAFNQEKVNQIQKT 106
Cdd:cd07307    1 KLDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALqeLGKELPDLSNTDLGeALEKFGKIQKELEEFRDQLEQKLENK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330 107 VIEPLKKF-SSIFPSLNMAVKRREQALQDYGRLQAKVEKYEEKEKTgpvLAKLHQAREELRPVREDFEAKNKQLLDEMPR 185
Cdd:cd07307   81 VIEPLKEYlKKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKD---SSKLAEAEEELQEAKEKYEELREELIEDLNK 157

                        170       180
                 ....*....|....*....|....*
gi 568988330 186 FYGSRLDYFQPSFESLIRAQACSHH 210
Cdd:cd07307  158 LEEKRKELFLSLLLSFIEAQSEFFK 182
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 19-210 1.77e-15

BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different protein families. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysin, endophilin, BRAP and Nadrin. BAR domains are also frequently found alongside domains that determine lipid specificity, like pfam00169 and pfam00787 domains in beta centaurins and sorting nexins respectively.


Pssm-ID: 460810 [Multi-domain]  Cd Length: 235  Bit Score: 72.75  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330   19 TVERDFEREYGKLQQLEEQTKRLQKDMKKSTDADLAM--SKSAVKISQDLLSNPLCE------QDQDFLHMVTALDTAMK 90
Cdd:pfam03114  23 KLDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGAraKQTVLEQPEELLAESMIEagkdlgEDSSFGKALEDYGEALK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330   91 RMDAFNQEKVNQIQKTVIEPLKKFSSIFPSLNMAVKRREQALQDYGRLQAKVEKYEEKEKTGpvLAKLHQAREELRPVRE 170
Cdd:pfam03114 103 RLAQLLEQLDDRVETNFLDPLRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKKKSSK--AKDESQAEEELRKAQA 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568988330  171 DFEAKNKQLLDEMPRFYGSRLDYFQPSFESLIRAQACSHH 210
Cdd:pfam03114 181 KFEESNEQLKALLPNLLSLEVEFVVNQLVAFVEAQLDFHR 220
BAR_Amphiphysin cd07588
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysins; BAR domains are dimerization, lipid ...
 40-209 1.07e-09

The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Amphiphysins function primarily in endocytosis and other membrane remodeling events. They contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. This subfamily is composed of different isoforms of amphiphysin and Bridging integrator 2 (Bin2). Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin and synaptojanin. They function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. Bin2 is mainly expressed in hematopoietic cells and is upregulated during granulocyte differentiation. The N-BAR domains of amphiphysins form a curved dimer with a positively-charged concave face that can drive membrane bending and curvature.


Pssm-ID: 153272  Cd Length: 211  Bit Score: 56.21  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  40 RLQKDMKKSTDADLAMSKSAVKISQDLLSnpLCEQDQDFLHMVTALdtaMKRMDAFNQEKVNQIQKTVIEPLKKFSSIFP 119
Cdd:cd07588   30 RLQKDLKNYLNSVRAMKQASKTLSETLKE--LYEPDWPGREHLASI---FEQLDLLWNDLEEKLSDQVLGPLTAYQSQFP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330 120 SLNMAVKRREQALQDYGR----LQAKVEKYEEKEktgpvlAKLHQAREELRPVREDFEAKNKQLLDEMPRFYGSRLDYFQ 195
Cdd:cd07588  105 EVKKRIAKRGRKLVDYDSarhnLEALKAKKKVDD------QKLTKAEEELQQAKKVYEELNTELHEELPALYDSRIAFYV 178

                        170
                 ....*....|....
gi 568988330 196 PSFESLIRAQACSH 209
Cdd:cd07588  179 DTLQSIFAAESVFH 192
BAR_DNMBP cd07589
The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin Binding Protein; BAR domains are dimerization, ...
 18-206 5.53e-08

The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin Binding Protein; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. DyNamin Binding Protein (DNMBP), also called Tuba, is a Cdc42-specific Guanine nucleotide Exchange Factor (GEF) that binds dynamin and various actin regulatory proteins. It serves as a link between dynamin function, Rho GTPase signaling, and actin dynamics. It plays an important role in regulating cell junction configuration. DNMBP contains BAR and SH3 domains as well as a Dbl Homology domain (DH domain), which harbors GEF activity. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The BAR domain of DNMBP may be involved in binding to membranes. The gene encoding DNMBP is a candidate gene for late onset Alzheimer's disease.


Pssm-ID: 153273  Cd Length: 195  Bit Score: 51.16  E-value: 5.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  18 KTVERDFEREYGKLQQLEEQTKRLQKDMKKSTDA---DLAMSKSAVKISQDLLSnplcEQDQDFLHMVTALDTAMKR-MD 93
Cdd:cd07589    1 QTKDKEFDELEKKFGSLEKQVQLVVRNVELYLQHvqeSVLVKVLALEVVLDLYP----SNHPRLESKWERFRRVVRGiSS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  94 AFNQEKVNQIQKTVIEPLKKFSSIFPSLNMAVKRREQALQDYGRLQAkvekyeekektgpVLAKLHQAREELRPVREDFE 173
Cdd:cd07589   77 KALPEFKSRVRKLVIEPLSSLLKLFSGPQKLIQKRYDKLLDYERYKE-------------KKERGGKVDEELEEAANQYE 143

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568988330 174 AKNKQLLDEMPRFYGSRLDYFQPSFESLIRAQA 206
Cdd:cd07589  144 ALNAQLKEELPKFNQLTAQLLETCLKSFVELQR 176
BAR_Bin2 cd07612
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 2; BAR domains are dimerization, ...
 14-201 1.10e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Bridging integrator 2 (Bin2) is a BAR domain containing protein that is mainly expressed in hematopoietic cells. It is upregulated during granulocyte differentiation and is thought to function primarily in this lineage. The BAR domain of Bin2 is closely related to the BAR domains of amphiphysins, which function primarily in endocytosis and other membrane remodeling events. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. Unlike amphiphysins, Bin2 does not appear to contain a C-terminal SH3 domain. Amphiphysin I proteins, enriched in the brain and nervous system, function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), function in intracellular vessicle trafficking. Bin2 can form a stable complex with Bin1 in cells but cannot replace the function of Bin1, and thus, appears to harbor a nonredundant function. The N-BAR domain of amphiphysin forms a curved dimer with a positively-charged concave face that can drive membrane bending and curvature.


Pssm-ID: 153296  Cd Length: 211  Bit Score: 44.85  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  14 QIVSKTVE---RDFEREYGKLQQLEEQTKRLQKDMKKSTDADLAMSKSAVKISQDLLsnplcEQDQDFLHMVTALDTAMK 90
Cdd:cd07612    1 QKLGKTVEtkdEQFEQCAMNLNMQQSDGNRLYKDLKAYLNAVKVMHESSKRLSQTLQ-----DIYEPDWDGHEDLGAIVE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  91 RMDAFNQEKVNQIQKTVIEPLKKFSSIFPSLNMAVKRREQALQDYG----RLQAKVEKYEEKEktgpvlAKLHQAREELR 166
Cdd:cd07612   76 GEDLLWNDYEAKLHDQALRTMESYMAQFPDVKERVAKRGRKLVDYDsarhHLEALQNAKKKDD------AKIAKAEEEFN 149

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568988330 167 PVREDFEAKNKQLLDEMPRFYGSRLDYFQPSFESL 201
Cdd:cd07612  150 RAQVVFEDINRELREELPILYDSRIGCYVTVFQNI 184
BAR_Amphiphysin_I_II cd07611
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin I and II; BAR domains are dimerization, ...
 18-209 1.61e-05

The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin I and II; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Amphiphysins function primarily in endocytosis and other membrane remodeling events. They contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin and synaptojanin. They function in synaptic vesicle endocytosis. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. The N-BAR domain of amphiphysin forms a curved dimer with a positively-charged concave face that can drive membrane bending and curvature. Human autoantibodies to amphiphysin-1 hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Mutations in amphiphysin-2 (BIN1) are associated with autosomal recessive centronuclear myopathy.


Pssm-ID: 153295  Cd Length: 211  Bit Score: 44.54  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  18 KTVERDFEREYGKLQQLEEQTKRLQKDMKKSTDADLAMSKSAVKISQDLlsNPLCEQDqdfLHMVTALDTAMKRMDA--- 94
Cdd:cd07611    8 ETKDEQFEEYVQNFKRQETEGTRLQRELRAYLAAIKGMQEASKKLTESL--HEVYEPD---WYGRDDVKTIGEKCDLlwe 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  95 -FNQEKVNQIQKTviepLKKFSSIFPSLNMAVKRREQALQDYGrlQAKVEKYEEKEKTGPVLAKLHQAREELRPVREDFE 173
Cdd:cd07611   83 dFHQKLVDGALLT----LDTYLGQFPDIKNRIAKRSRKLVDYD--SARHHLEALQTSKRKDEGRIAKAEEEFQKAQKVFE 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568988330 174 AKNKQLLDEMPRFYGSRLDYFQPSFESLIRAQACSH 209
Cdd:cd07611  157 EFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFH 192
BAR_Rvs167p cd07599
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 30-202 4.77e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon starvation protein 167 and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. This subfamily is composed of fungal proteins with similarity to Saccharomyces cerevisiae Reduced viability upon starvation protein 167 (Rvs167p) and Schizosaccharomyces pombe Hob1 (homolog of Bin1). S. cerevisiae Rvs167p plays a role in regulation of the actin cytoskeleton, endocytosis, and sporulation. It forms a heterodimer with another BAR domain protein Rvs161p. Rvs161p and Rvs167p share common functions but are not interchangeable. Their BAR domains cannot be replaced with each other and the overexpression of one cannot suppress the mutant phenotypes of the other. Rvs167p also interacts with the GTPase activating protein (GAP) Gyp5p, which is involved in ER to Golgi vesicle trafficking. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153283 [Multi-domain]  Cd Length: 216  Bit Score: 39.93  E-value: 4.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  30 KLQQLEEQTKRLQKDMKKSTDADLAM--SKSAVKISQDLLSNPL---------CEQDQDFLHMVTALDTAMKRMDAFNQE 98
Cdd:cd07599   10 DFKSLEKSLKKLIEQSKAFRDSWRSIltHQIAFAKEFAELYDPIvgpkesvgsHPAPESTLARLSRYVKALEELKKELLE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568988330  99 KVNQIQKTVIEPLKKFSSIFPSLNMAVKRREQALQDYGRLQAKVEKYEEKEKTgPVL---AKLHQAREELRPVREDFEAK 175
Cdd:cd07599   90 ELEFFEERVILPAKELKKYIKKIRKTIKKRDHKKLDYDKLQNKLNKLLQKKKE-LSLkdeKQLAKLERKLEEAKEEYEAL 168

                        170       180
                 ....*....|....*....|....*..
gi 568988330 176 NKQLLDEMPRFYGSRLDYFQPSFESLI 202
Cdd:cd07599  169 NELLKSELPKLLALADEFLPPLFKSFY 195
 
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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