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Conserved domains on  [gi|165905601|ref|NP_077748|]
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proline-serine-threonine phosphatase-interacting protein 2 [Homo sapiens]

Protein Classification

proline-serine-threonine phosphatase-interacting protein 2( domain architecture ID 10166613)

proline-serine-threonine phosphatase-interacting protein 2 (PSTPIP2) binds to F-actin and may be involved in regulation of the actin cytoskeleton; PSTPIP2 contains an N-terminal F-BAR (FES-CIP4 homology and Bin/Amphiphysin/Rvs) domain but lacks the SH3 (Src homology 3) domain that is found in PSTPIP1

Gene Symbol:  PSTPIP2
Gene Ontology:  GO:0140090|GO:0097753|GO:0005515|GO:0003779
PubMed:  9804817|15649145|14993925

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-254 1.45e-154

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 2; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2), also known as Macrophage Actin-associated tYrosine Phosphorylated protein (MAYP), is mostly expressed in hematopoietic cells but is also expressed in the brain. It is involved in regulating cell adhesion and motility. Mutations in the gene encoding murine PSTPIP2 can cause autoinflammatory disorders such as chronic multifocal osteomyelitis and macrophage autoinflammatory disease. PSTPIP2 contains an N-terminal F-BAR domain and lacks the PEST motifs and SH3 domain that are found in PSTPIP1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


:

Pssm-ID: 153356 [Multi-domain]  Cd Length: 240  Bit Score: 432.84  E-value: 1.45e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  15 ILSTIGYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRKKPCGQSEINTLKRALEVFKQQVDNVAQCHIQL 94
Cdd:cd07672    1 LTSTGGYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGQTEINTLKRSLDVFKQQIDNVGQSHIQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  95 AQSLREEARKMEEFREKQKLQRKKTELIMDAIHKQKSLQFKKTMDAKKNYEQKCRDKDEAEQAVSRSANLVNPKQQEKLF 174
Cdd:cd07672   81 AQTLRDEAKKMEDFRERQKLARKKIELIMDAIHKQRAMQFKKTMESKKNYEQKCRDKDEAEQAVNRNANLVNVKQQEKLF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 175 VKLATSKTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNALWLHVNQLSQQCVTSDEMYEQVRK 254
Cdd:cd07672  161 AKLAQSKQNAEDADRLYMQNISVLDKIREDWQKEHVKACEFFEKQECERINFFRNAVWTHVNQLSQQCVTSDEMYEEVRK 240
 
Name Accession Description Interval E-value
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-254 1.45e-154

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 2; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2), also known as Macrophage Actin-associated tYrosine Phosphorylated protein (MAYP), is mostly expressed in hematopoietic cells but is also expressed in the brain. It is involved in regulating cell adhesion and motility. Mutations in the gene encoding murine PSTPIP2 can cause autoinflammatory disorders such as chronic multifocal osteomyelitis and macrophage autoinflammatory disease. PSTPIP2 contains an N-terminal F-BAR domain and lacks the PEST motifs and SH3 domain that are found in PSTPIP1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153356 [Multi-domain]  Cd Length: 240  Bit Score: 432.84  E-value: 1.45e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  15 ILSTIGYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRKKPCGQSEINTLKRALEVFKQQVDNVAQCHIQL 94
Cdd:cd07672    1 LTSTGGYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGQTEINTLKRSLDVFKQQIDNVGQSHIQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  95 AQSLREEARKMEEFREKQKLQRKKTELIMDAIHKQKSLQFKKTMDAKKNYEQKCRDKDEAEQAVSRSANLVNPKQQEKLF 174
Cdd:cd07672   81 AQTLRDEAKKMEDFRERQKLARKKIELIMDAIHKQRAMQFKKTMESKKNYEQKCRDKDEAEQAVNRNANLVNVKQQEKLF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 175 VKLATSKTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNALWLHVNQLSQQCVTSDEMYEQVRK 254
Cdd:cd07672  161 AKLAQSKQNAEDADRLYMQNISVLDKIREDWQKEHVKACEFFEKQECERINFFRNAVWTHVNQLSQQCVTSDEMYEEVRK 240
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 20-93 5.46e-16

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 71.92  E-value: 5.46e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 165905601   20 GYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRK----KPCGQSEINTLKRALEVFKQQVDNVAQCHIQ 93
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKflkkKKKPEDDGGTLKKAWDELLTETEQLAKQHLK 78
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 10-94 6.98e-13

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 63.51  E-value: 6.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601    10 FWSADilsTIGYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRKKPC---GQSEINTLKRALEVFKQQVDN 86
Cdd:smart00055   3 FWSEL---DDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAvrdTEPEYGSLSKAWEVLLSETDA 79


                   ....*...
gi 165905601    87 VAQCHIQL 94
Cdd:smart00055  80 LAKQHLEL 87
 
Name Accession Description Interval E-value
F-BAR_PSTPIP2 cd07672
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-254 1.45e-154

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 2; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2), also known as Macrophage Actin-associated tYrosine Phosphorylated protein (MAYP), is mostly expressed in hematopoietic cells but is also expressed in the brain. It is involved in regulating cell adhesion and motility. Mutations in the gene encoding murine PSTPIP2 can cause autoinflammatory disorders such as chronic multifocal osteomyelitis and macrophage autoinflammatory disease. PSTPIP2 contains an N-terminal F-BAR domain and lacks the PEST motifs and SH3 domain that are found in PSTPIP1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153356 [Multi-domain]  Cd Length: 240  Bit Score: 432.84  E-value: 1.45e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  15 ILSTIGYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRKKPCGQSEINTLKRALEVFKQQVDNVAQCHIQL 94
Cdd:cd07672    1 LTSTGGYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGQTEINTLKRSLDVFKQQIDNVGQSHIQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  95 AQSLREEARKMEEFREKQKLQRKKTELIMDAIHKQKSLQFKKTMDAKKNYEQKCRDKDEAEQAVSRSANLVNPKQQEKLF 174
Cdd:cd07672   81 AQTLRDEAKKMEDFRERQKLARKKIELIMDAIHKQRAMQFKKTMESKKNYEQKCRDKDEAEQAVNRNANLVNVKQQEKLF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 175 VKLATSKTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNALWLHVNQLSQQCVTSDEMYEQVRK 254
Cdd:cd07672  161 AKLAQSKQNAEDADRLYMQNISVLDKIREDWQKEHVKACEFFEKQECERINFFRNAVWTHVNQLSQQCVTSDEMYEEVRK 240
F-BAR_PSTPIP cd07647
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 15-254 6.74e-132

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153331 [Multi-domain]  Cd Length: 239  Bit Score: 375.28  E-value: 6.74e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  15 ILSTIGYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRKKPCGQsEINTLKRALEVFKQQVDNVAQCHIQL 94
Cdd:cd07647    1 FTSTTGFDTLLQRLKEGKKMCKELEDFLKQRAKAEEDYGKALLKLSKSAGPGD-EIGTLKSSWDSLRKETENVANAHIQL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  95 AQSLREEARKMEEFREKQKLQRKKTELIMDAIHKQKSLQFKKTMDAKKNYEQKCRDKDEAEQAVSRSANLVNPKQQEKLF 174
Cdd:cd07647   80 AQSLREEAEKLEEFREKQKEERKKTEDIMKRSQKNKKELYKKTMKAKKSYEQKCREKDKAEQAYEKSSSGAQPKEAEKLK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 175 VKLATSKTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNALWLHVNQLSQQCVTSDEMYEQVRK 254
Cdd:cd07647  160 KKAAQCKTSAEEADSAYKSSIGCLEDARVEWESEHATACQVFQNMEEERIKFLRNALWVHCNLGSMQCVKLDEMYEDVRK 239
F-BAR_PSTPIP1 cd07671
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ...
 20-257 4.43e-86

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 1 (PSTPIP1), also known as CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153355 [Multi-domain]  Cd Length: 242  Bit Score: 259.12  E-value: 4.43e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  20 GYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRKKPcGQSEINTLKRALEVFKQQVDNVAQCHIQLAQSLR 99
Cdd:cd07671    6 GYEILLQRLLDGRKMCKDVEELLKQRAQAEERYGKELVQIARKAG-GQTEINTLKASFDQLKQQIENIGNSHIQLAGMLR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 100 EEARKMEEFREKQKLQRKKTELIMDAIHKQKSLQFKKTMDAKKNYEQKCRDKDEAEQAVSRSANLVNPKQQEKLFVKLAT 179
Cdd:cd07671   85 EELKSLEEFRERQKEQRKKYEAVMERVQKSKVSLYKKTMESKKTYEQRCREADEAEQTFERSSSTGNPKQSEKSQNKAKQ 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 165905601 180 SKTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNALWLHVNQLSQQCVTSDEMYEQVRKSLE 257
Cdd:cd07671  165 CRDAATEAERVYKQNIEQLDKARTEWETEHILTCEVFQLQEDDRITILRNALWVHCNHFSMQCVKDDELYEEVRTTLE 242
F-BAR_PombeCdc15_like cd07651
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...
 20-254 3.41e-36

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153335 [Multi-domain]  Cd Length: 236  Bit Score: 130.50  E-value: 3.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  20 GYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRKKPcGQSEINTLKRALEVFKQQVDNVAQCHIQLAQSLR 99
Cdd:cd07651    6 GFDVIQTRIKDSLRTLEELRSFYKERASIEEEYAKRLEKLSRKSL-GGSEEGGLKNSLDTLRLETESMAKSHLKFAKQIR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 100 EEAR-KMEEFREKQKLQRKKTELIMDAIHKQKSLQFKKTMDAKKNYEQKCRDKdeaeQAVSRSANLVNPKQQEKLFVKLA 178
Cdd:cd07651   85 QDLEeKLAAFASSYTQKRKKIQSHMEKLLKKKQDQEKYLEKAREKYEADCSKI----NSYTLQSQLTWGKELEKNNAKLN 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 165905601 179 TSKTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNALWLHVNQLSQQCVTSDEMYEQVRK 254
Cdd:cd07651  161 KAQSSINSSRRDYQNAVKALRELNEIWNREWKAALDDFQDLEEERIQFLKSNCWTFANNISTLCVDDDESCERIRS 236
F-BAR_FCHO cd07648
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; ...
 20-285 1.63e-22

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proteins in this group have been named FCH domain Only (FCHO) proteins. Vertebrates have two members, FCHO1 and FCHO2. These proteins contain an F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153332 [Multi-domain]  Cd Length: 261  Bit Score: 94.72  E-value: 1.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  20 GYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKdLLNLSRKKPCGQSEINTLKRALEVFKQQVDNVAQCHIQLAQSLR 99
Cdd:cd07648    6 GFDVLYHNMKHGQIAVKELADFLRERATIEETYSK-ALNKLAKQASNSSQLGTFAPLWLVLRVSTEKLSELHLQLVQKLQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 100 EEARKMEEFREKQKLQRK--KTELI--MDAIH--KQKSLQFKKtmdAKKNYEQKCRDKDEAEQAVSrsanlvNPKQQEKL 173
Cdd:cd07648   85 ELIKDVQKYGEEQHKKHKkvKEEESgtAEAVQaiQTTTAALQK---AKEAYHARCLELERLRRENA------SPKEIEKA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 174 FVKLATSKtaveDSDKAYmlhigtLDK---VREEWQSEHIKACEAFEAQECERINFFRNALWLHVNQLSQQCVTSDEMYE 250
Cdd:cd07648  156 EAKLKKAQ----DEYKAL------VEKynnIRADFETKMTDSCKRFQEIEESHLRQMKEFLASYAEVLSENHSAVGQVHE 225

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 165905601 251 QVRKSLEMCSIQRDIEYFVNQRKTGQIPPAPIMYE 285
Cdd:cd07648  226 EFKRQVDELTVDKLLRQFVESKGTGTEKPELIEFE 260
F-BAR_FCHO2 cd07673
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; ...
 6-285 2.45e-20

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 2 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. The specific function of FCH domain Only 2 (FCHO2) is still unknown. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO1 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153357 [Multi-domain]  Cd Length: 269  Bit Score: 88.96  E-value: 2.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601   6 FKGNFWSAdilSTIGYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSrKKPCGQSEINTLKRALEVFKQQVD 85
Cdd:cd07673    2 FLENFWGE---KNSGFDVLYHNMKHGQISTKELSDFIRERATIEEAYSRSMTKLA-KSASNYSQLGTFAPVWDVFKTSTE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  86 NVAQCHIQLAQSLREEARKMEEFREKQKLQRKKTEL----IMDAIHKQKSLQfKKTMDAKKNYEQKCRDKDEAEQAVSRS 161
Cdd:cd07673   78 KLANCHLELVRKLQELIKEVQKYGEEQVKSHKKTKEevagTLEAVQNIQSIT-QALQKSKENYNAKCLEQERLKKEGATQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 162 ANLvnpkqqEKLFVKlatSKTAVEdsdkAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNALWLHVNQLSQQ 241
Cdd:cd07673  157 REI------EKAAVK---SKKATE----SYKLYVEKYALAKADFEQKMTETAQKFQDIEETHLIRIKEIIGSYSNSVKEI 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 165905601 242 CVTSDEMYEQVRKSLEMCSIQRDIEYFVNQRKTGQIPPAPIMYE 285
Cdd:cd07673  224 HIQIGQVHEEFINNMANTTVESLIQKFAESKGTGKERPGPIEFE 267
F-BAR_FCHO1 cd07674
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; ...
 20-285 6.12e-18

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of FCH domain Only 1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FCH domain Only 1 (FCHO1) may be involved in clathrin-coated vesicle formation. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCHO2 and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153358 [Multi-domain]  Cd Length: 261  Bit Score: 81.91  E-value: 6.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  20 GYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRKKPCGqSEINTLKRALEVFKQQVDNVAQCHIQLAQSLR 99
Cdd:cd07674    6 GFDVLYHNMKHGQISTKELADFVRERAAIEETYSKSMSKLSKMASNG-SPLGTFAPMWEVFRVSSDKLALCHLELMRKLN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 100 EEARKMEEFREKQ-KLQRKKTELIMDAIHKQKSLQFKKTM--DAKKNYEQKCRDKDEAEQAVSrsanlvnpKQQEKLFVK 176
Cdd:cd07674   85 DLIKDINRYGDEQvKIHKKTKEEAIGTLEAVQSLQVQSQHlqKSRENYHSKCVEQERLRREGV--------PQKELEKAE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 177 LATSKTAvedsdKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNALWLHVNQLSQQCVTSDEMYEQVRKSL 256
Cdd:cd07674  157 LKTKKAA-----ESLRGSVEKYNRARGDFEQKMLESAQKFQDIEETHLRHMKLLIKGYSHSVEDTHVQIGQVHEEFKQNV 231

                        250       260
                 ....*....|....*....|....*....
gi 165905601 257 EMCSIQRDIEYFVNQRKTGQIPPAPIMYE 285
Cdd:cd07674  232 ENVGVENLIRKFAESKGTGKERPGPVGFE 260
FCH_F-BAR cd07610
The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a ...
 20-254 1.17e-16

The Extended FES-CIP4 Homology (FCH) or F-BAR (FCH and Bin/Amphiphysin/Rvs) domain, a dimerization module that binds and bends membranes; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. F-BAR domain containing proteins, also known as Pombe Cdc15 homology (PCH) family proteins, include Fes and Fer tyrosine kinases, PACSINs/Syndapins, FCHO, PSTPIP, CIP4-like proteins and srGAPs. Many members also contain an SH3 domain and play roles in endocytosis. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. These tubules have diameters larger than those observed with N-BARs. The F-BAR domains of some members such as NOSTRIN and Rgd1 are important for the subcellular localization of the protein.


Pssm-ID: 153294 [Multi-domain]  Cd Length: 191  Bit Score: 76.99  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  20 GYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRKKPCG-QSEINTLKRALEVFKQQVDNVAQCHIQLAQSL 98
Cdd:cd07610    1 GFELLEKRTELGLDLLKDLREFLKKRAAIEEEYAKNLQKLAKKFSKKpESGKTSLGTSWNSLREETESAATVHEELSEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  99 REEARKMEEFREKQKLQRKKTELimdaihkqkslqfkktmdakknyeqkcrdkdeaeqavsrsanlvnpKQQEKLFVKLA 178
Cdd:cd07610   81 SQLIREPLEKVKEDKEQARKKEL----------------------------------------------AEGEKLKKKLQ 114

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 165905601 179 TS-KTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNALWLHVNQLSQQCVTSDEMYEQVRK 254
Cdd:cd07610  115 ELwAKLAKKADEEYREQVEKLNPAQSEYEEEKLNKIQAEQEREEERLEILKDNLKNYINAIKEIPQKIQQELEQSIN 191
FCH pfam00611
Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The ...
 20-93 5.46e-16

Fes/CIP4, and EFC/F-BAR homology domain; Alignment extended from. Highly alpha-helical. The cytosolic endocytic adaptor proteins in fungi carry this domain at the N-terminus; several of these have been referred to as muniscin proteins. These N-terminal BAR, N-BAR, and EFC/F-BAR domains are found in proteins that regulate membrane trafficking events by inducing membrane tubulation. The domain dimerizes into a curved structure that binds to liposomes and either senses or induces the curvature of the membrane bilayer to cause biophysical changes to the shape of the bilayer; it also thereby recruits other trafficking factors, such as the GTPase dynamin. Most EFC/F-BAR domain-family members localize to actin-rich structures.


Pssm-ID: 459868 [Multi-domain]  Cd Length: 78  Bit Score: 71.92  E-value: 5.46e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 165905601   20 GYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRK----KPCGQSEINTLKRALEVFKQQVDNVAQCHIQ 93
Cdd:pfam00611   1 GFKVLLKRLKQGIKLLEELASFLKERAEIEEEYAKKLQKLAKKflkkKKKPEDDGGTLKKAWDELLTETEQLAKQHLK 78
FCH smart00055
Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also ...
 10-94 6.98e-13

Fes/CIP4 homology domain; Alignment extended from original report. Highly alpha-helical. Also known as the RAEYL motif or the S. pombe Cdc15 N-terminal domain.


Pssm-ID: 214492 [Multi-domain]  Cd Length: 87  Bit Score: 63.51  E-value: 6.98e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601    10 FWSADilsTIGYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRKKPC---GQSEINTLKRALEVFKQQVDN 86
Cdd:smart00055   3 FWSEL---DDGFEALLSRLKNGLRLLEDLKKFMRERAKIEEEYAKKLQKLSKKLRAvrdTEPEYGSLSKAWEVLLSETDA 79


                   ....*...
gi 165905601    87 VAQCHIQL 94
Cdd:smart00055  80 LAKQHLEL 87
F-BAR_PACSIN2 cd07679
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 21-231 3.14e-12

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 2 (PACSIN2); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 2 or Syndapin II is expressed ubiquitously and is involved in the regulation of tubulin polymerization. It associates with Golgi membranes and forms a complex with dynamin II which is crucial in promoting vesicle formation from the trans-Golgi network. PACSIN 2 contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153363 [Multi-domain]  Cd Length: 258  Bit Score: 65.86  E-value: 3.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  21 YDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSR-------KKPcgqsEINTLKRALEVFKQQVDNVAQCHIQ 93
Cdd:cd07679    7 YKRTVKRIDDGHRLCNDLMNCLHERARIEKVYAQQLTEWAKrwrqlveKGP----QYGTVEKAWCALMSEAEKVSELHLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  94 LAQSLreearkMEEFREKQKLQRKktelimDAIHKQKSLQFKKTMDA---------------------KKNYEQKCRdkd 152
Cdd:cd07679   83 VKASL------MNEDFEKIKNWQK------EAFHKQMMGGFKETKEAedgfrkaqkpwakklkeveaaKKAYHTACK--- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 153 EAEQAVSRSAN-----LVNPKQQEKLFVKLATSKTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFF 227
Cdd:cd07679  148 EEKLATSREANskadpALNPEQLKKLQDKVEKCKQDVLKTKEKYEKSLKELDQTTPQYMENMEQVFEQCQQFEEKRLRFF 227


                 ....
gi 165905601 228 RNAL 231
Cdd:cd07679  228 REVL 231
F-BAR_GAS7 cd07649
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein ...
 20-231 5.38e-11

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Growth Arrest Specific protein 7; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Growth Arrest Specific protein 7 (GAS7) is mainly expressed in the brain and is required for neurite outgrowth. It may also play a role in the protection and migration of embryonic stem cells. Treatment-related acute myeloid leukemia (AML) has been reported resulting from mixed-lineage leukemia (MLL)-GAS7 translocations as a complication of primary cancer treatment. GAS7 contains an N-terminal SH3 domain, followed by a WW domain, and a central F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153333 [Multi-domain]  Cd Length: 233  Bit Score: 61.57  E-value: 5.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  20 GYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRKKPCGQSEiNTLKRALEVFKQQVDNVAQCHIQLAQSLR 99
Cdd:cd07649    6 GFEILLQKQLKGKQMQKEMAEFIRERIKIEEEYAKNLSKLSQSSLAAQEE-GTLGEAWAQVKKSLADEAEVHLKFSSKLQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 100 EEARK-MEEFREKQKLQRKKTELIMDAIHKQKSLQFKKTMDAKKNYEQKCRDKDEAEQAVSRSANLVNPKQQEKLFVKla 178
Cdd:cd07649   85 SEVEKpLLNFRENFKKDMKKLDHHIADLRKQLASRYAAVEKARKALLERQKDLEGKTQQLEIKLSNKTEEDIKKARRK-- 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 165905601 179 tSKTAVEDsdkaYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNAL 231
Cdd:cd07649  163 -STQAGDD----LMRCVDLYNQAQSKWFEEMVTTSLELERLEVERIEMIRQHL 210
F-BAR_PACSIN cd07655
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 30-231 1.46e-10

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153339 [Multi-domain]  Cd Length: 258  Bit Score: 60.79  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  30 NGRKNCKEFEDFLKERAAIEERYGKDLLNLSRK------KPCgqsEINTLKRALEVFKQQVDNVAQCHIQLAQSLREEAr 103
Cdd:cd07655   16 DGHKLCDDLMKMVQERAEIEKAYAKKLKEWAKKwrdlieKGP---EYGTLETAWKGLLSEAERLSELHLSIRDKLLNDV- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 104 kMEEFREKQK--------LQRKKTELIMDAIHK-QK--SLQFKKTMDAKKNYEQKCRDKDEAEQAV--SRSANLVNPKQQ 170
Cdd:cd07655   92 -VEEVKTWQKenyhksmmGGFKETKEAEDGFAKaQKpwAKLLKKVEKAKKAYHAACKAEKSAQKQEnnAKSDTSLSPDQV 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 165905601 171 EKLFVKLATSKTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNAL 231
Cdd:cd07655  171 KKLQDKVEKCKQEVSKTKDKYEKALEDLNKYNPRYMEDMEQVFDKCQEFEEKRLDFFKEIL 231
F-BAR_PACSIN1 cd07680
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 21-231 1.02e-09

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 1 or Syndapin I is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. It contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153364 [Multi-domain]  Cd Length: 258  Bit Score: 58.13  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  21 YDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSR-------KKPcgqsEINTLKRALEVFKQQVDNVAQCHIQ 93
Cdd:cd07680    7 YKRTVKRIDDGHRLCNDLMNCVQERAKIEKAYGQQLTDWAKrwrqlieKGP----QYGSLERAWGAIMTEADKVSELHQE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  94 LAQSLREEarKMEEFREKQKlqrkktelimDAIHKQKSLQFKKTMD---------------------AKKNYEQKCRDKD 152
Cdd:cd07680   83 VKNNLLNE--DLEKVKNWQK----------DAYHKQIMGGFKETKEaedgfrkaqkpwakkmkeleaAKKAYHLACKEEK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 153 EA--EQAVSRSANLVNPKQQEKLFVKLATSKTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNA 230
Cdd:cd07680  151 LAmtREANSKAEQSVTPEQQKKLQDKVDKCKQDVQKTQEKYEKVLDDVGKTTPQYMENMEQVFEQCQQFEEKRLVFLKEV 230


                 .
gi 165905601 231 L 231
Cdd:cd07680  231 L 231
F-BAR_CIP4-like cd07653
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ...
 21-157 6.38e-09

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Members of this subfamily typically contain an N-terminal F-BAR domain and a C-terminal SH3 domain. In addition, some members such as FNBP1L contain a central Cdc42-binding HR1 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153337 [Multi-domain]  Cd Length: 251  Bit Score: 55.72  E-value: 6.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  21 YDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLS-----RKKPCGQSEINTLKrALEVFKQQVDNVAQCHIQLA 95
Cdd:cd07653    7 FDNLEKHTQKGIDFLERYGKFVKERAAIEQEYAKKLRKLVkkylpKKKEEDEYSFSSVK-AFRSILNEVNDIAGQHELIA 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 165905601  96 QSLREEA-RKMEEFREKQKLQRKKteLIMDAIHKQKSL--QFKKTMDAKKNYEQKCRDKDEAEQA 157
Cdd:cd07653   86 ENLNSNVcKELKTLISELRQERKK--HLSEGSKLQQKLesSIKQLEKSKKAYEKAFKEAEKAKQK 148
F-BAR_NOSTRIN cd07658
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic ...
 20-231 2.12e-08

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Nitric Oxide Synthase TRaffic INducer (NOSTRIN); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Nitric Oxide Synthase TRaffic INducer (NOSTRIN) is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). NOSTRIN facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of NOSTRIN may be correlated to preeclampsia. NOSTRIN contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. The F-BAR domain of NOSTRIN is necessary and sufficient for its membrane association and is responsible for its subcellular localization.


Pssm-ID: 153342 [Multi-domain]  Cd Length: 239  Bit Score: 53.92  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  20 GYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRK--KPCgQSEINTLKRALEVFKQQVDNVAQCHIQLAQS 97
Cdd:cd07658    6 GFEELRRYVKQGGDFCKELATVLQERAELELNYAKGLSKLSGKlsKAS-KSVSGTLSSAWTCVAEEMESEADIHRNLGSA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  98 LREEA---------------RKMEEFREK--QKLQRKKTELImdAIHKQKSLQFK---KTMDAKKNYEQKCrDKDEAEQA 157
Cdd:cd07658   85 LTEEAikplrqvldeqhktrKPVENEVDKaaKLLTDWRSEQI--KVKKKLHGLAReneKLQDQVEDNKQSC-TKQKMLNK 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 165905601 158 VSRSANlVNPKQQEKLFVKLATSKTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECERINFFRNAL 231
Cdd:cd07658  162 LKKSAE-VQDKEDEKLEAKRKKGEESRLKAENEYYTCCVRLERLRLEWESALRKGLNQYESLEEERLQHLKHSL 234
F-BAR_FBP17 cd07676
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; ...
 21-210 9.26e-06

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 17; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Formin Binding Protein 17 (FBP17), also called FormiN Binding Protein 1 (FNBP1), is involved in dynamin-mediated endocytosis. It is recruited to clathrin-coated pits late in the endocytosis process and may play a role in the invagination and scission steps. FBP17 binds in vivo to tankyrase, a protein involved in telomere maintenance and mitogen activated protein kinase (MAPK) signaling. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153360 [Multi-domain]  Cd Length: 253  Bit Score: 46.19  E-value: 9.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  21 YDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRK---KPCGQSEIN---TLKRALEVFKQQVDNVAQCHIQL 94
Cdd:cd07676    7 FDNLEKHTQWGIEVLEKYIKFVKERTEIELSYAKQLRNLSKKyqpKKNSKEEEEykyTSCRAFLMTLNEMNDYAGQHEVI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  95 AQSLREEArKMEEFREKQKLQRKKTELIMDAIHKQKSLQ--FKKTMDAKKNYEQKCRDKDEAEQAVSR--------SANL 164
Cdd:cd07676   87 SENLASQI-IVELTRYVQELKQERKSHFHDGRKAQQHIEtcWKQLESSKRRFERDCKEADRAQQYFEKmdadinvtKADV 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 165905601 165 VNPKQQEKLFVKLAtsktavEDSDKAYMLHIGTLDKVREEWQSEHI 210
Cdd:cd07676  166 EKARQQAQIRHQMA------EDSKAEYSSYLQKFNKEQHEHYYTHI 205
F-BAR_Rgd1 cd07652
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ...
 34-232 1.15e-05

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153336 [Multi-domain]  Cd Length: 234  Bit Score: 45.80  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  34 NCKEFEDFLKERAAIEERYGKDLLNLSRkkpcgqSEINTLKRA---LEVFKQQVDNVAQCHIQLAQ-------------- 96
Cdd:cd07652   20 SAKEFATFLKKRAAIEEEHARGLKKLAR------TTLDTYKRPdhkQGSFSNAYHSSLEFHEKLADnglrfakalnemsd 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  97 SLREEARKMEEFREKQKLQRKKTEL-IMDAIHkqkslQFKKtmdAKKNYEQKCRDKDE---AEQAVSRSANLVNPK---Q 169
Cdd:cd07652   94 ELSSLAKTVEKSRKSIKETGKRAEKkVQDAEA-----AAEK---AKARYDSLADDLERvktGDPGKKLKFGLKGNKsaaQ 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 165905601 170 QEK-LFVKlatsktaVEDSDKAYMLHIGTLDKVREEWQSEH-----------IKACEAfeaqeCERINFFRNALW 232
Cdd:cd07652  166 HEDeLLRK-------VQAADQDYASKVNAAQALRQELLSRHrpeavkdlfdlILEIDA-----ALRLQYQKYALP 228
F-BAR_PACSIN3 cd07681
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein ...
 10-231 1.85e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSIN 3 or Syndapin III is expressed ubiquitously and regulates glucose uptake in adipocytes through its role in GLUT1 trafficking. It also modulates the subcellular localization and stimulus-specific function of the cation channel TRPV4. PACSIN 3 contains an N-terminal F-BAR domain and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153365 [Multi-domain]  Cd Length: 258  Bit Score: 42.23  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  10 FWSADilstiGYDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRKKPCG---QSEINTLKRALEVFKQQVDN 86
Cdd:cd07681    1 FWEAG-----NYRRTVKRIEDGYRLCNDLVSCFQERAKIEKGYAQQLSDWARKWRGIvekGPQYGTLEKAWHAFLTAAER 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  87 VAQCHIQLAQSLREEarKMEEFREKQKlqrkktelimDAIHKQKSLQFKKTMDA---------------------KKNYE 145
Cdd:cd07681   76 LSEIHLELRENLVGE--DSEKVRAWQK----------EAFHKQMIGGFRESKEAeegfrkaqkpwvkklkevessKKGYH 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 146 QKCRDKDEAE--QAVSRSANLVNPKQQEKLFVKLATSKTAVEDSDKAYMLHIGTLDKVREEWQSEHIKACEAFEAQECER 223
Cdd:cd07681  144 AARKDERTAQtrETHAKADSTVSQEQLRKLQDRVEKCTQEAEKAKEQYEKALEELNRYNPRYMEDMEQAFEICQEAERKR 223


                 ....*...
gi 165905601 224 INFFRNAL 231
Cdd:cd07681  224 LCFFKEML 231
F-BAR_FNBP1L cd07675
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 1-Like; ...
 21-171 2.07e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Formin Binding Protein 1-Like; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. FormiN Binding Protein 1-Like (FNBP1L), also known as Toca-1 (Transducer of Cdc42-dependent actin assembly), forms a complex with neural Wiskott-Aldrich syndrome protein (N-WASP). The FNBP1L/N-WASP complex induces the formation of filopodia and endocytic vesicles. FNBP1L is required for Cdc42-induced actin assembly and is essential for autophagy of intracellular pathogens. It contains an N-terminal F-BAR domain, a central Cdc42-binding HR1 domain, and a C-terminal SH3 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153359 [Multi-domain]  Cd Length: 252  Bit Score: 42.34  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  21 YDNIIQHLNNGRKNCKEFEDFLKERAAIEERYGKDLLNLSRK---KPCGQSEINTLKRALEVFK--QQVDNVAQCHIQLA 95
Cdd:cd07675    7 FDNLDKHTQWGIDFLERYAKFVKERLEIEQNYAKQLRNLVKKycpKRSSKDEEPRFTSCLSFYNilNELNDYAGQREVVA 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 165905601  96 QSLREEARKmEEFREKQKLQRKKTELIMDAIHKQKSL-QFKKTMD-AKKNYEQKCRDKDEAEQAVSRSANLVNPKQQE 171
Cdd:cd07675   87 EEMGHRVYG-ELMRYSHDLKGERKMHLQEGRKAQQYLdMCWKQMDnSKKKFERECREAEKAQQSYERLDNDTNATKSD 163
F-BAR_Syp1p_like cd07650
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of yeast Syp1 protein; F-BAR ...
 36-270 9.04e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of yeast Syp1 protein; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Syp1p is associated with septins, a family of GTP-binding proteins that serve as elements of septin filaments, which are required for cell morphogenesis and division. Syp1p regulates cell-cycle dependent septin cytoskeletal dynamics in yeast. It contains an N-terminal F-BAR domain and a C-terminal domain of unknown function named SAFF which is also present in FCH domain Only (FCHO) proteins and endophilin interacting protein 1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.


Pssm-ID: 153334 [Multi-domain]  Cd Length: 228  Bit Score: 40.00  E-value: 9.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601  36 KEFEDFLKERAAIEERYGKDLLNLSRKK-PCGQSEINTLKRALEVFKQQVDNVAQCHIQLAQSLREEARK-MEEFREKQK 113
Cdd:cd07650   22 TELADWLQERRRLERQYVQGLRKLARRNePLNKSLLGVFQNPWLTIESETEFIAASHGELAQRIETDVEEpLRDFATSTE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 114 LQRKKTELiMDAIHKQKSLqfkktmdakknyeqkcrdkDEAEQAVSRSanlvnpkqqEKLFVKLATSKTAVEDSDkayml 193
Cdd:cd07650  102 FMNTLDDD-QNLSNLAKEL-------------------DESQKKWDKL---------KKKHSKASSKAVSAAVSD----- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165905601 194 higtLDKVREEWQSEHIKACEAFEAQECERINFFRNALwlhvnqLSQQCVTSDeMYEQVRKSLEMC-------SIQRDIE 266
Cdd:cd07650  148 ----LEEARQQWDSQAPFLFELLQAIDEERLNHLKDVL------LQFQTHESD-YALRTTESAEECmnqllefDTEDEIQ 216


                 ....
gi 165905601 267 YFVN 270
Cdd:cd07650  217 RFAR 220
 
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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