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Conserved domains on  [gi|2462548786|ref|XP_054236191|]
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CBY1-interacting BAR domain-containing protein 2 isoform X2 [Homo sapiens]

Protein Classification

BAR domain-containing protein( domain architecture ID 10166148)

BAR (Bin/Amphiphysin/Rvs) domain-containing protein, similar to human protein FAM92

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR_FAM92 cd07598
The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); BAR ...
 6-216 8.92e-103

The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); 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. This group is composed of proteins from the family with sequence similarity 92 (FAM92), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, FAM92A and FAM92B, which may exist in many variants. The Xenopus homolog of FAM92A1, xVAP019, is essential for embryo survival and cell differentiation. FAM92A1 may be involved in regulating cell proliferation and apoptosis. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


:

Pssm-ID: 153282  Cd Length: 211  Bit Score: 298.07  E-value: 8.92e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786   6 SRDSQVRVMENTVANTEKYFGQFCSLLAAYTRKTARLRDKADQLVKQLIDFANSENPELRATMRGFAEDLAKVQDYRQAQ 85
Cdd:cd07598     1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786  86 VERLETKVVNPLKLYGAQIKQTRAEIKKFKHVQNHEIKQLEKLEKLRQKSPSDQQMISQAETRVQRAAVDSSRTTLQLEE 165
Cdd:cd07598    81 VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQIISQAESELQKASVDANRSTKELEE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462548786 166 TVDGFQRQKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTLEKYDLERDL 216
Cdd:cd07598   161 QMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211
 
Name Accession Description Interval E-value
BAR_FAM92 cd07598
The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); BAR ...
 6-216 8.92e-103

The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); 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. This group is composed of proteins from the family with sequence similarity 92 (FAM92), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, FAM92A and FAM92B, which may exist in many variants. The Xenopus homolog of FAM92A1, xVAP019, is essential for embryo survival and cell differentiation. FAM92A1 may be involved in regulating cell proliferation and apoptosis. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153282  Cd Length: 211  Bit Score: 298.07  E-value: 8.92e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786   6 SRDSQVRVMENTVANTEKYFGQFCSLLAAYTRKTARLRDKADQLVKQLIDFANSENPELRATMRGFAEDLAKVQDYRQAQ 85
Cdd:cd07598     1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786  86 VERLETKVVNPLKLYGAQIKQTRAEIKKFKHVQNHEIKQLEKLEKLRQKSPSDQQMISQAETRVQRAAVDSSRTTLQLEE 165
Cdd:cd07598    81 VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQIISQAESELQKASVDANRSTKELEE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462548786 166 TVDGFQRQKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTLEKYDLERDL 216
Cdd:cd07598   161 QMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211
FAM92 pfam06730
FAM92 protein; This family of proteins has a role in embryogenesis. During embryogenesis it is ...
 6-216 3.06e-65

FAM92 protein; This family of proteins has a role in embryogenesis. During embryogenesis it is essential for ectoderm and axial mesoderm development. It may regulate cell proliferation and apoptosis.


Pssm-ID: 284207  Cd Length: 225  Bit Score: 203.37  E-value: 3.06e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786   6 SRDSQVRVMENTVANTEKYFGQFCSLLAAYTRKTARLRDKADQLVKQLIDFANSENP--ELRATMRGFAEDLAKVQDYRQ 83
Cdd:pfam06730  12 NKDAQTKIINEAINITEKHFGELCQIFAAVTRKMAKLRDKADELAKEIKAYAADEEIheKLCQGLKNFADAFAILGDYMD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786  84 AQVERLETKVVNPLKLYGAQIKQTRAEIKKFKHVQNHEIKQLEKLEKLRQKSPSDQQMISQAETRVQRAAVDSSRTTLQL 163
Cdd:pfam06730  92 AEVERLEAKIVEELAQFEQICKMKRDDLKAALIARDKEAKQLRQLEELKQKFPADNHVISAADSELFKAAMDAQRTNKEI 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462548786 164 EETVDGFQRQKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTLEKYDLERDL 216
Cdd:pfam06730 172 DDIIGNFEQQKLKDIKQIFSDFILIAMKFHGKALEILSAAYQDIGNIDEDDDF 224
BAR smart00721
BAR domain;
71-207 3.16e-04

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 41.22  E-value: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786   71 FAEDLAKVQDYRQAQVERLETKVVNPLKLYGAQIKQTRAEIKKFKH-VQNHEIK--QLEKLEKLRQKSPSDQQMISQAET 147
Cdd:smart00721 100 LGEALKKLLQVEESLSQVKRTFILPLLNFLLGEFKEIKKARKKLERkLLDYDSArhKLKKAKKSKEKKKDEKLAKAEEEL 179

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786  148 RVQRAAVDSSRTTLqLEETVDGFQRqKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTL 207
Cdd:smart00721 180 RKAKQEFEESNAQL-VEELPQLVAS-RVDFFVNCLQALIEAQLNFHRESYKLLQQLQQQL 237
 
Name Accession Description Interval E-value
BAR_FAM92 cd07598
The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); BAR ...
 6-216 8.92e-103

The Bin/Amphiphysin/Rvs (BAR) domain of Family with sequence similarity 92 (FAM92); 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. This group is composed of proteins from the family with sequence similarity 92 (FAM92), which were originally identified by the presence of the unknown domain DUF1208. This domain shows similarity to the BAR domains of sorting nexins. Mammals contain at least two member types, FAM92A and FAM92B, which may exist in many variants. The Xenopus homolog of FAM92A1, xVAP019, is essential for embryo survival and cell differentiation. FAM92A1 may be involved in regulating cell proliferation and apoptosis. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153282  Cd Length: 211  Bit Score: 298.07  E-value: 8.92e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786   6 SRDSQVRVMENTVANTEKYFGQFCSLLAAYTRKTARLRDKADQLVKQLIDFANSENPELRATMRGFAEDLAKVQDYRQAQ 85
Cdd:cd07598     1 ARDNQTKFIQERITNVEKHFGELCQDFAAYTRKTARLRDKGDELAKSINAYADTENPSLKQGLKNFAECLAALQDYRQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786  86 VERLETKVVNPLKLYGAQIKQTRAEIKKFKHVQNHEIKQLEKLEKLRQKSPSDQQMISQAETRVQRAAVDSSRTTLQLEE 165
Cdd:cd07598    81 VERLEAKVVQPLALYGTICKHARDDLKNTFTARNKELKQLKQLEKLRQKNPSDRQIISQAESELQKASVDANRSTKELEE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462548786 166 TVDGFQRQKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTLEKYDLERDL 216
Cdd:cd07598   161 QMDNFEKQKIRDIKTIFSDFVLIEMLFHAKALEVYTAAYQDIQNIDEEEDL 211
FAM92 pfam06730
FAM92 protein; This family of proteins has a role in embryogenesis. During embryogenesis it is ...
 6-216 3.06e-65

FAM92 protein; This family of proteins has a role in embryogenesis. During embryogenesis it is essential for ectoderm and axial mesoderm development. It may regulate cell proliferation and apoptosis.


Pssm-ID: 284207  Cd Length: 225  Bit Score: 203.37  E-value: 3.06e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786   6 SRDSQVRVMENTVANTEKYFGQFCSLLAAYTRKTARLRDKADQLVKQLIDFANSENP--ELRATMRGFAEDLAKVQDYRQ 83
Cdd:pfam06730  12 NKDAQTKIINEAINITEKHFGELCQIFAAVTRKMAKLRDKADELAKEIKAYAADEEIheKLCQGLKNFADAFAILGDYMD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786  84 AQVERLETKVVNPLKLYGAQIKQTRAEIKKFKHVQNHEIKQLEKLEKLRQKSPSDQQMISQAETRVQRAAVDSSRTTLQL 163
Cdd:pfam06730  92 AEVERLEAKIVEELAQFEQICKMKRDDLKAALIARDKEAKQLRQLEELKQKFPADNHVISAADSELFKAAMDAQRTNKEI 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462548786 164 EETVDGFQRQKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTLEKYDLERDL 216
Cdd:pfam06730 172 DDIIGNFEQQKLKDIKQIFSDFILIAMKFHGKALEILSAAYQDIGNIDEDDDF 224
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 18-199 6.27e-11

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: 60.15  E-value: 6.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786  18 VANTEKYFGQFCSLLAAYTRKTARLRDKADQLVKQLIDFA----NSENPELRATMRGFAEDLAKVQDYRQAQVERLETKV 93
Cdd:cd07307     2 LDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGkelpDLSNTDLGEALEKFGKIQKELEEFRDQLEQKLENKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786  94 VNPLKLYG-AQIKQTRAEIKKFKHVQNHEIKQLEKLEKLRQKSPsDQQMISQAETRVQRAAVDSSRTTLQLEETVDGFQR 172
Cdd:cd07307    82 IEPLKEYLkKDLKEIKKRRKKLDKARLDYDAAREKLKKLRKKKK-DSSKLAEAEEELQEAKEKYEELREELIEDLNKLEE 160

                         170       180
                  ....*....|....*....|....*..
gi 2462548786 173 QKLKDLQKFFCDFVTIEMVFHAKAVEV 199
Cdd:cd07307   161 KRKELFLSLLLSFIEAQSEFFKEVLKI 187
BAR smart00721
BAR domain;
71-207 3.16e-04

BAR domain;


Pssm-ID: 214787 [Multi-domain]  Cd Length: 239  Bit Score: 41.22  E-value: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786   71 FAEDLAKVQDYRQAQVERLETKVVNPLKLYGAQIKQTRAEIKKFKH-VQNHEIK--QLEKLEKLRQKSPSDQQMISQAET 147
Cdd:smart00721 100 LGEALKKLLQVEESLSQVKRTFILPLLNFLLGEFKEIKKARKKLERkLLDYDSArhKLKKAKKSKEKKKDEKLAKAEEEL 179

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786  148 RVQRAAVDSSRTTLqLEETVDGFQRqKLKDLQKFFCDFVTIEMVFHAKAVEVYSSAFQTL 207
Cdd:smart00721 180 RKAKQEFEESNAQL-VEELPQLVAS-RVDFFVNCLQALIEAQLNFHRESYKLLQQLQQQL 237
BAR_SNX4 cd07622
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 4; BAR domains are dimerization, lipid ...
 117-208 8.91e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 4; 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. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It is also implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and leptin. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153306  Cd Length: 201  Bit Score: 36.59  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462548786 117 VQNHEIKQLEkLEKLRQKSPSDQQmisQAETRVQRAAVDSSRTTLQLEETVDGFQRQKLKDLQKFFCDFVTIEMVFHAKA 196
Cdd:cd07622   114 CKKHELLQYD-LEKAEDALANKKQ---QGEEAVKEAKDELNEFVKKALEDVERFKKQKVRDLKEILISYAKLQIKLAKKG 189

                          90
                  ....*....|..
gi 2462548786 197 VEVYSSAFQTLE 208
Cdd:cd07622   190 LQTWTNIKECLQ 201
 
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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