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Conserved domains on  [gi|176866329|ref|NP_001116516|]
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bridging integrator 3 [Danio rerio]

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, ...
 12-236 8.52e-104

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: 300.44  E-value: 8.52e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  12 RKQIVSKTVERDFEREYEKLQKLEEQTKKLHKDMKKSTEADLAMSKAAVKISGDLLSNPLCEQDQHFLDSMNALDTAMKR 91
Cdd:cd07590    1 KKPILSKTVDRELEREVQKLQQLESTTKKLYKDMKKYIEAVLALSKAEQRLSQDLASGPLCEDNDELRNLVEALDSVTTQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  92 MDAFNQEKVNQIQKTVIDPLKKYGSVFPSLNMAVKRREQALQDYKRLQSKVEKYEEKEKTGPIMVKLHQAREELKPVRED 171
Cdd:cd07590   81 LDKTVQELVNLIQKTFIEPLKRLRSVFPSVNAAIKRREQSLQEYERLQAKVEKLAEKEKTGPNLAKLEQAEKALAAARAD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 176866329 172 FEAKNKQLLDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHKIFTELNDQIDQSALTDEQRKQE 236
Cdd:cd07590  161 FEKQNIKLLEELPKFYNGRTDYFQPCFEALIKSQVLYYSQSTKIFTQLAPNLDNPIEQLTISEQE 225
 
Name Accession Description Interval E-value
BAR_Bin3 cd07590
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ...
 12-236 8.52e-104

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: 300.44  E-value: 8.52e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  12 RKQIVSKTVERDFEREYEKLQKLEEQTKKLHKDMKKSTEADLAMSKAAVKISGDLLSNPLCEQDQHFLDSMNALDTAMKR 91
Cdd:cd07590    1 KKPILSKTVDRELEREVQKLQQLESTTKKLYKDMKKYIEAVLALSKAEQRLSQDLASGPLCEDNDELRNLVEALDSVTTQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  92 MDAFNQEKVNQIQKTVIDPLKKYGSVFPSLNMAVKRREQALQDYKRLQSKVEKYEEKEKTGPIMVKLHQAREELKPVRED 171
Cdd:cd07590   81 LDKTVQELVNLIQKTFIEPLKRLRSVFPSVNAAIKRREQSLQEYERLQAKVEKLAEKEKTGPNLAKLEQAEKALAAARAD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 176866329 172 FEAKNKQLLDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHKIFTELNDQIDQSALTDEQRKQE 236
Cdd:cd07590  161 FEKQNIKLLEELPKFYNGRTDYFQPCFEALIKSQVLYYSQSTKIFTQLAPNLDNPIEQLTISEQE 225
BAR smart00721
BAR domain;
19-225 1.01e-32

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 119.41  E-value: 1.01e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329    19 TVERDFEREYEKLQKLEEQTKKLHKDMKK------STEADLAMSKAAVKISGDLLSNPL----CEQDQHFLDSMNALDTA 88
Cdd:smart00721  24 KLDEDFEELERRFDTTEAEIEKLQKDTKLylqpnpAVRAKLASQKKLSKSLGEVYEGGDdgegLGADSSYGKALDKLGEA 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329    89 MKRMDAFNQEKVNQIQKTVIDPLKKYGSVFPSLNMAVKRREQALQDYKRLQSKVEKYEEKEKTgPIMVKLHQAREELKPV 168
Cdd:smart00721 104 LKKLLQVEESLSQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKAKKSKEK-KKDEKLAKAEEELRKA 182

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 176866329   169 REDFEAKNKQLLDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHKIFTELNDQIDQ 225
Cdd:smart00721 183 KQEFEESNAQLVEELPQLVASRVDFFVNCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 19-225 1.99e-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: 73.14  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329   19 TVERDFEREYEKLQKLEEQTKKLHKDMKKSTEADLAM--SKAAVKISGDLLSNPLCE------QDQHFLDSMNALDTAMK 90
Cdd:pfam03114  23 KLDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGAraKQTVLEQPEELLAESMIEagkdlgEDSSFGKALEDYGEALK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329   91 RMDAFNQEKVNQIQKTVIDPLKKYGSVFPSLNMAVKRREQALQDYKRLQSKVEKYEEKEKtgPIMVKLHQAREELKPVRE 170
Cdd:pfam03114 103 RLAQLLEQLDDRVETNFLDPLRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKKKS--SKAKDESQAEEELRKAQA 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 176866329  171 DFEAKNKQLLDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHKIFTELNDQIDQ 225
Cdd:pfam03114 181 KFEESNEQLKALLPNLLSLEVEFVVNQLVAFVEAQLDFHRQCYQLLEQLQQQLGK 235
 
Name Accession Description Interval E-value
BAR_Bin3 cd07590
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 3; BAR domains are dimerization, ...
 12-236 8.52e-104

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: 300.44  E-value: 8.52e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  12 RKQIVSKTVERDFEREYEKLQKLEEQTKKLHKDMKKSTEADLAMSKAAVKISGDLLSNPLCEQDQHFLDSMNALDTAMKR 91
Cdd:cd07590    1 KKPILSKTVDRELEREVQKLQQLESTTKKLYKDMKKYIEAVLALSKAEQRLSQDLASGPLCEDNDELRNLVEALDSVTTQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  92 MDAFNQEKVNQIQKTVIDPLKKYGSVFPSLNMAVKRREQALQDYKRLQSKVEKYEEKEKTGPIMVKLHQAREELKPVRED 171
Cdd:cd07590   81 LDKTVQELVNLIQKTFIEPLKRLRSVFPSVNAAIKRREQSLQEYERLQAKVEKLAEKEKTGPNLAKLEQAEKALAAARAD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 176866329 172 FEAKNKQLLDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHKIFTELNDQIDQSALTDEQRKQE 236
Cdd:cd07590  161 FEKQNIKLLEELPKFYNGRTDYFQPCFEALIKSQVLYYSQSTKIFTQLAPNLDNPIEQLTISEQE 225
BAR smart00721
BAR domain;
19-225 1.01e-32

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 119.41  E-value: 1.01e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329    19 TVERDFEREYEKLQKLEEQTKKLHKDMKK------STEADLAMSKAAVKISGDLLSNPL----CEQDQHFLDSMNALDTA 88
Cdd:smart00721  24 KLDEDFEELERRFDTTEAEIEKLQKDTKLylqpnpAVRAKLASQKKLSKSLGEVYEGGDdgegLGADSSYGKALDKLGEA 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329    89 MKRMDAFNQEKVNQIQKTVIDPLKKYGSVFPSLNMAVKRREQALQDYKRLQSKVEKYEEKEKTgPIMVKLHQAREELKPV 168
Cdd:smart00721 104 LKKLLQVEESLSQVKRTFILPLLNFLLGEFKEIKKARKKLERKLLDYDSARHKLKKAKKSKEK-KKDEKLAKAEEELRKA 182

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 176866329   169 REDFEAKNKQLLDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHKIFTELNDQIDQ 225
Cdd:smart00721 183 KQEFEESNAQLVEELPQLVASRVDFFVNCLQALIEAQLNFHRESYKLLQQLQQQLDK 239
BAR_Rvs161p cd07591
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 7-230 1.33e-27

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: 105.50  E-value: 1.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329   7 KIGQprkqiVSKTVERDFEREYEKLQKLEEQTKKLHKDMKKSTEADLAMSKAAVKIS-------GDLLSNPLCEQDQHFL 79
Cdd:cd07591    1 KTGQ-----VERTVDREFEFEERRYRTMEKASTKLQKEAKGYLDSLRALTSSQARIAetissfyGDAGDKDGAMLSQEYK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  80 DSMNALDT-AMKRMDA-FNQekvnqiqkTVIDPLKKYGSVFPSLNMAVKRREQALQDYKRLQSKVEKYEEKEKTGPimVK 157
Cdd:cd07591   76 QAVEELDAeTVKELDGpYRQ--------TVLDPIGRFNSYFPEINEAIKKRNHKLLDYDAARAKVRKLIDKPSEDP--TK 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 176866329 158 LHQAREELKPVREDFEAKNKQLLDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHKIFTELNDQIDQSALTD 230
Cdd:cd07591  146 LPRAEKELDEAKEVYETLNDQLKTELPQLVDLRIPYLDPSFEAFVKIQLRFFTEGYERLAQVQRYLDAQTRED 218
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 23-222 1.88e-17

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: 77.87  E-value: 1.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  23 DFEREYEKLQKLEEQTKKLHKDMKKSTEADLAMSKAAVKISGDLLSNPlceqDQHFLDSMNALDTAMKRMDAFNQEKVNQ 102
Cdd:cd07307    1 KLDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLS----NTDLGEALEKFGKIQKELEEFRDQLEQK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329 103 IQKTVIDPLKKYGSV-FPSLNMAVKRREQALQDYKRLQSKVEKYEEKEKTGpimVKLHQAREELKPVREDFEAKNKQLLD 181
Cdd:cd07307   77 LENKVIEPLKEYLKKdLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKKDS---SKLAEAEEELQEAKEKYEELREELIE 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 176866329 182 EMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHKIFTELNDQ 222
Cdd:cd07307  154 DLNKLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLPY 194
BAR pfam03114
BAR domain; BAR domains are dimerization, lipid binding and curvature sensing modules found in ...
 19-225 1.99e-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: 73.14  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329   19 TVERDFEREYEKLQKLEEQTKKLHKDMKKSTEADLAM--SKAAVKISGDLLSNPLCE------QDQHFLDSMNALDTAMK 90
Cdd:pfam03114  23 KLDEDFEELERRFDTTEKEIKKLQKDTKGYLQPNPGAraKQTVLEQPEELLAESMIEagkdlgEDSSFGKALEDYGEALK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329   91 RMDAFNQEKVNQIQKTVIDPLKKYGSVFPSLNMAVKRREQALQDYKRLQSKVEKYEEKEKtgPIMVKLHQAREELKPVRE 170
Cdd:pfam03114 103 RLAQLLEQLDDRVETNFLDPLRNLLKEFKEIQKHRKKLERKRLDYDAAKTRVKKAKKKKS--SKAKDESQAEEELRKAQA 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 176866329  171 DFEAKNKQLLDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHKIFTELNDQIDQ 225
Cdd:pfam03114 181 KFEESNEQLKALLPNLLSLEVEFVVNQLVAFVEAQLDFHRQCYQLLEQLQQQLGK 235
BAR_Amphiphysin cd07588
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysins; BAR domains are dimerization, lipid ...
 24-225 9.32e-13

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: 65.45  E-value: 9.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  24 FEREYEKLQKLEEQTKKLHKDMKKSTEADLAMSKAAVKISGDLLSnpLCEQDQHFLDSMNALdtaMKRMDAFNQEKVNQI 103
Cdd:cd07588   14 FDEHVNNFNKQQASANRLQKDLKNYLNSVRAMKQASKTLSETLKE--LYEPDWPGREHLASI---FEQLDLLWNDLEEKL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329 104 QKTVIDPLKKYGSVFPSLNMAVKRREQALQDYKR----LQSKVEKYEEKEktgpimVKLHQAREELKPVREDFEAKNKQL 179
Cdd:cd07588   89 SDQVLGPLTAYQSQFPEVKKRIAKRGRKLVDYDSarhnLEALKAKKKVDD------QKLTKAEEELQQAKKVYEELNTEL 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 176866329 180 LDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHKIFTELNDQIDQ 225
Cdd:cd07588  163 HEELPALYDSRIAFYVDTLQSIFAAESVFHKEIGKVNTKLNDVMDG 208
BAR_Amphiphysin_I_II cd07611
The Bin/Amphiphysin/Rvs (BAR) domain of Amphiphysin I and II; BAR domains are dimerization, ...
 18-221 2.36e-07

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: 49.94  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  18 KTVERDFEREYEKLQKLEEQTKKLHKDMKKSTEADLAMSKAAVKISGDLlsNPLCEQDQHFLDSMNaldTAMKRMDAFNQ 97
Cdd:cd07611    8 ETKDEQFEEYVQNFKRQETEGTRLQRELRAYLAAIKGMQEASKKLTESL--HEVYEPDWYGRDDVK---TIGEKCDLLWE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  98 EKVNQIQKTVIDPLKKYGSVFPSLNMAVKRREQALQDY-------KRLQSKVEKYEEkektgpimvKLHQAREELKPVRE 170
Cdd:cd07611   83 DFHQKLVDGALLTLDTYLGQFPDIKNRIAKRSRKLVDYdsarhhlEALQTSKRKDEG---------RIAKAEEEFQKAQK 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 176866329 171 DFEAKNKQLLDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHKIFTELND 221
Cdd:cd07611  154 VFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEISVLCHKLYE 204
BAR_DNMBP cd07589
The Bin/Amphiphysin/Rvs (BAR) domain of Dynamin Binding Protein; BAR domains are dimerization, ...
 18-214 3.38e-07

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: 49.24  E-value: 3.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  18 KTVERDFEREYEKLQKLEEQTKKLHKDMKKST----EADLAMSKAAVKISGdllsnpLCEQDQHFLDSMNALDTAMKR-- 91
Cdd:cd07589    1 QTKDKEFDELEKKFGSLEKQVQLVVRNVELYLqhvqESVLVKVLALEVVLD------LYPSNHPRLESKWERFRRVVRgi 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  92 MDAFNQEKVNQIQKTVIDPLKKYGSVFPSLNMAVKRREQALQDYKRLQSkvekyeekektgpIMVKLHQAREELKPVRED 171
Cdd:cd07589   75 SSKALPEFKSRVRKLVIEPLSSLLKLFSGPQKLIQKRYDKLLDYERYKE-------------KKERGGKVDEELEEAANQ 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 176866329 172 FEAKNKQLLDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHK 214
Cdd:cd07589  142 YEALNAQLKEELPKFNQLTAQLLETCLKSFVELQRDLYDTLLK 184
BAR_Bin2 cd07612
The Bin/Amphiphysin/Rvs (BAR) domain of Bridging integrator 2; BAR domains are dimerization, ...
 14-215 2.63e-06

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: 46.77  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  14 QIVSKTVE---RDFEREYEKLQKLEEQTKKLHKDMKKSTEADLAMSKAAVKISGDLLSNPLCEQDQHfldsmNALDTAMK 90
Cdd:cd07612    1 QKLGKTVEtkdEQFEQCAMNLNMQQSDGNRLYKDLKAYLNAVKVMHESSKRLSQTLQDIYEPDWDGH-----EDLGAIVE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  91 RMDAFNQEKVNQIQKTVIDPLKKYGSVFPSLNMAVKRREQALQDYKRLQSKVEKYEEKEKTGPImvKLHQAREELKPVRE 170
Cdd:cd07612   76 GEDLLWNDYEAKLHDQALRTMESYMAQFPDVKERVAKRGRKLVDYDSARHHLEALQNAKKKDDA--KIAKAEEEFNRAQV 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 176866329 171 DFEAKNKQLLDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHKI 215
Cdd:cd07612  154 VFEDINRELREELPILYDSRIGCYVTVFQNISNLRDTFYKEMSKL 198
BAR_Rvs167p cd07599
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Reduced viability upon ...
 22-213 7.91e-05

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: 42.63  E-value: 7.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  22 RDFEREYEKLQKLEEQTKKLHKDMKKSTEADLAM---SKAAVK--------ISGDLLSNPLCEQDQHFLDSMNALDTAMK 90
Cdd:cd07599    2 EQFEELEKDFKSLEKSLKKLIEQSKAFRDSWRSIlthQIAFAKefaelydpIVGPKESVGSHPAPESTLARLSRYVKALE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  91 RMDAFNQEKVNQIQKTVIDPLKKYGSVFPSLNMAVKRREQALQDYKRLQSKVEKYEEKEKTGPIM--VKLHQAREELKPV 168
Cdd:cd07599   82 ELKKELLEELEFFEERVILPAKELKKYIKKIRKTIKKRDHKKLDYDKLQNKLNKLLQKKKELSLKdeKQLAKLERKLEEA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 176866329 169 REDFEAKNKQLLDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMH 213
Cdd:cd07599  162 KEEYEALNELLKSELPKLLALADEFLPPLFKSFYYIQLNIYYTLH 206
BAR_3 pfam16746
BAR domain of APPL family; BAR_12 is the BAR coiled-coil domain at the N-terminus of APPL or ...
 22-113 4.69e-03

BAR domain of APPL family; BAR_12 is the BAR coiled-coil domain at the N-terminus of APPL or adaptor protein containing PH domain, PTB domain, and leucine zipper motif proteins in higher eukaryotes. This BAR domain contains four helices whereas the other classical BAR domains contain only three helices. The first three helices form an antiparallel coiled-coil, while the fourth helix, is unique to APPL1. BAR domains take part in many varied biological processes such as fission of synaptic vesicles, endocytosis, regulation of the actin cytoskeleton, transcriptional repression, cell-cell fusion, apoptosis, secretory vesicle fusion, and tissue differentiation.


Pssm-ID: 465256  Cd Length: 235  Bit Score: 37.54  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329   22 RDFEREyekLQKLEEQTKKLHKDMKKSTEADLAMSKAavkisGDLLSNPLCEQDQHFLD------SMNALDTAMKRMDAF 95
Cdd:pfam16746  18 EEHEAE---LDELEKKLKKLLKLCKRMIEAGKEYSAA-----QRLFANSLLDFKFEFIGdeetdeSLKKFSQLLQEMENF 89

                          90
                  ....*....|....*...
gi 176866329   96 NQEKVNQIQKTVIDPLKK 113
Cdd:pfam16746  90 HTILLDQAQRTIIKPLEN 107
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 21-222 8.15e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 36.56  E-value: 8.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  21 ERDFEREYEKLQKLEEQTKKLHKD----MKKSTEADLAMSK--AAVKISGDLLSNPLCEQDQHFLDSMNALDTAMKRMda 94
Cdd:cd07596    3 DQEFEEAKDYILKLEEQLKKLSKQaqrlVKRRRELGSALGEfgKALIKLAKCEEEVGGELGEALSKLGKAAEELSSLS-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329  95 fnQEKVNQIQKTVIDPLKKYGSVFPSLNMAVKRREQALQDY----KRLQSKVEKYEEKEKTGPIMVK--------LHQAR 162
Cdd:cd07596   81 --EAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLqslkKDLASKKAQLEKLKAAPGIKPAkveeleeeLEEAE 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866329 163 EELKPVREDFEAKNKQLLDEMPKFYNSRIDYFQPSFEALIRAQVVYFTEMHKIFTELNDQ 222
Cdd:cd07596  159 SALEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLLPE 218
 
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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