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Search results 201 to 300 out of 458 for Ptpn14

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Hits by Strain

Type Details Score
Interaction Experiment
Fu B (2020)
Description: PTPN14 aggravates inflammation through promoting proteasomal degradation of SOCS7 in acute liver failure.
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Strain
MGI:6429448 | C57BL/6JSmoc-Ptpn14<em1Smoc>/Smoc
Attribute String: coisogenic, mutant strain, endonuclease-mediated mutation
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Publication
29017051 | J:245524
First Author: Aylon Y
Year: 2017
Journal: Cancer Cell
Title: Tumor Suppression by p53: Bring in the Hippo!
Volume: 32
Issue: 4
Pages: 397-399
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Publication
29017057 | J:243744
First Author: Mello SS
Year: 2017
Journal: Cancer Cell
Title: A p53 Super-tumor Suppressor Reveals a Tumor Suppressive p53-Ptpn14-Yap Axis in Pancreatic Cancer.
Volume: 32
Issue: 4
Pages: 460-473.e6
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Publication
32716083 | J:299883
First Author: Nishio M
Year: 2020
Journal: Cancer Sci
Title: Endogenous YAP1 activation drives immediate onset of cervical carcinoma in situ in mice.
Volume: 111
Issue: 10
Pages: 3576-3587
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Publication
18677119 | -
First Author: Wyatt L
Year: 2008
Journal: Cell Cycle
Title: PTP-Pez: a novel regulator of TGFbeta signaling.
Volume: 7
Issue: 15
Pages: 2290-5
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Protein Domain
IPR041782 | PTPN14/21_FERM_C
Type: Domain
Description: This entry represents the C-lobe of FERM domain found in protein-tyrosine phosphatases non-receptor type-14 (PTPN14, also known as Pez) and type-21 (PTPN21). A number of mutations in Pez/PTPN14 have been shown to be associated with breast and colorectal cancer []. PTPN14 and PTPN21 contain an N-terminal FERM domain and a C-terminal PTP catalytic domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites [, ].
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Protein
Q6NXW5
Organism: Mus musculus/domesticus
Length: 443  
Fragment?: false
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Protein
Q9JLJ9
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
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Protein
A0A1Y7VNX8
Organism: Mus musculus/domesticus
Length: 374  
Fragment?: false
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Protein
A0A1Y7VKP4
Organism: Mus musculus/domesticus
Length: 450  
Fragment?: false
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Protein
A0A286YD94
Organism: Mus musculus/domesticus
Length: 29  
Fragment?: true
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Publication
10970839 | -
First Author: Hamada K
Year: 2000
Journal: EMBO J
Title: Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain.
Volume: 19
Issue: 17
Pages: 4449-62
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Protein
Q8BHD4
Organism: Mus musculus/domesticus
Length: 595  
Fragment?: false
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Protein
Q6P5H6
Organism: Mus musculus/domesticus
Length: 517  
Fragment?: false
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Protein
B0R0D5
Organism: Mus musculus/domesticus
Length: 500  
Fragment?: true
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Protein
B0R0D4
Organism: Mus musculus/domesticus
Length: 509  
Fragment?: true
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Protein
Q8C3A0
Organism: Mus musculus/domesticus
Length: 310  
Fragment?: false
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Protein
A2AR56
Organism: Mus musculus/domesticus
Length: 570  
Fragment?: false
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Publication
9757824 | -
First Author: Chishti AH
Year: 1998
Journal: Trends Biochem Sci
Title: The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane.
Volume: 23
Issue: 8
Pages: 281-2
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Publication
10847681 | -
First Author: Pearson MA
Year: 2000
Journal: Cell
Title: Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.
Volume: 101
Issue: 3
Pages: 259-70
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Protein
Q78VI1
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: false
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Protein
Q9JLJ7
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: false
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Protein
A0A2I3BRG7
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
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Protein
H3BKK8
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: true
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Protein
F6U7Q0
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: true
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Protein
D3Z5B2
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: true
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Protein
Q3UFK8
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
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Protein
F6ZWR8
Organism: Mus musculus/domesticus
Length: 40  
Fragment?: true
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Protein
A0A1L1SVI6
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
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Protein
Q8R1I5
Organism: Mus musculus/domesticus
Length: 417  
Fragment?: true
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Protein
Q80X40
Organism: Mus musculus/domesticus
Length: 507  
Fragment?: true
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Protein
F6Y6G7
Organism: Mus musculus/domesticus
Length: 511  
Fragment?: false
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Protein
F7CWQ9
Organism: Mus musculus/domesticus
Length: 36  
Fragment?: true
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Protein
Q8CFX4
Organism: Mus musculus/domesticus
Length: 338  
Fragment?: true
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Protein
Q3UZ30
Organism: Mus musculus/domesticus
Length: 333  
Fragment?: true
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Protein
M0QWE8
Organism: Mus musculus/domesticus
Length: 320  
Fragment?: true
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Protein
A0A2I3BQ85
Organism: Mus musculus/domesticus
Length: 126  
Fragment?: true
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Protein Domain
IPR018979 | FERM_N
Type: Domain
Description: The FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane []. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus of the majority of FERM-containing proteins [, ], which includes: Band 4.1, which links the spectrin-actin cytoskeleton of erythrocytes to the plasma membrane.Ezrin, a component of the undercoat of the microvilli plasma membrane.Moesin, which is probably involved in binding major cytoskeletal structures to the plasma membrane.Radixin, which is involved in the binding of the barbed end of actin filaments to the plasma membrane in the undercoat of the cell- to-cell adherens junction.Talin, a cytoskeletal protein concentrated in regions of cell-substratum contact and, in lymphocytes, of cell-cell contacts.Filopodin, a slime mold protein that binds actin and which is involved in the control of cell motility and chemotaxis.Merlin (or schwannomin).Protein NBL4.Unconventional myosins X, VIIa and XV, which are mutated in congenital deafness.Focal-adhesion kinases (FAKs), cytoplasmic protein tyrosine kinases involved in signalling through integrins.Janus tyrosine kinases (JAKs), cytoplasmic tyrosine kinases that are non-covalently associated with the cytoplasmic tails of receptors for cytokines or polypeptidic hormones.Non-receptor tyrosine-protein kinase TYK2.Protein-tyrosine phosphatases PTPN3 and PTPN4, enzyme that appear to act at junctions between the membrane and the cytoskeleton.Protein-tyrosine phosphatases PTPN14 and PTP-D1, PTP-RL10 and PTP2E.Caenorhabditis elegans protein phosphatase ptp-1.Ezrin, moesin, and radixin are highly related proteins (ERM protein family), but the other proteins in which the FERM domain is found do not share any region of similarity outside of this domain. ERM proteins are made of three domains, the FERM domain, a central helical domain and a C-terminal tail domain, which binds F-actin. The amino-acid sequence of the FERM domain is highly conserved among ERM proteins and is responsible for membrane association by direct binding to the cytoplasmic domain or tail of integral membrane proteins. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail domains that masks their binding sites for other molecules. For cytoskeleton-membrane cross-linking, the dormant molecules becomes activated and the FERM domain attaches to the membrane by binding specific membrane proteins, while the last 34 residues of the tail bind actin filaments. Aside from binding to membranes, the activated FERM domain of ERM proteins can also bind the guanine nucleotide dissociation inhibitor of Rho GTPase (RhoDGI), which suggests that in addition to functioning as a cross-linker, ERM proteins may influence Rho signalling pathways. The crystal structure of the FERM domain reveals that it is composed of three structural modules (F1, F2, and F3) that together form a compact clover-shaped structure [].The FERM domain has also been called the amino-terminal domain, the 30kDa domain, 4.1N30, the membrane-cytoskeletal-linking domain, the ERM-like domain, the ezrin-like domain of the band 4.1 superfamily, the conserved N-terminal region, and the membrane attachment domain [].This domain is the N-terminal ubiquitin-like structural domain of the FERM domain.
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Protein Domain
IPR018980 | FERM_PH-like_C
Type: Domain
Description: The FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane []. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus of the majority of FERM-containing proteins [, ], which includes: Band 4.1, which links the spectrin-actin cytoskeleton of erythrocytes to the plasma membrane.Ezrin, a component of the undercoat of the microvilli plasma membrane.Moesin, which is probably involved in binding major cytoskeletal structures to the plasma membrane.Radixin, which is involved in the binding of the barbed end of actin filaments to the plasma membrane in the undercoat of the cell- to-cell adherens junction.Talin, a cytoskeletal protein concentrated in regions of cell-substratum contact and, in lymphocytes, of cell-cell contacts.Filopodin, a slime mold protein that binds actin and which is involved in the control of cell motility and chemotaxis.Merlin (or schwannomin).Protein NBL4.Unconventional myosins X, VIIa and XV, which are mutated in congenital deafness.Focal-adhesion kinases (FAKs), cytoplasmic protein tyrosine kinases involved in signalling through integrins.Janus tyrosine kinases (JAKs), cytoplasmic tyrosine kinases that are non-covalently associated with the cytoplasmic tails of receptors for cytokines or polypeptidic hormones.Non-receptor tyrosine-protein kinase TYK2.Protein-tyrosine phosphatases PTPN3 and PTPN4, enzyme that appear to act at junctions between the membrane and the cytoskeleton.Protein-tyrosine phosphatases PTPN14 and PTP-D1, PTP-RL10 and PTP2E.Caenorhabditis elegans protein phosphatase ptp-1.Ezrin, moesin, and radixin are highly related proteins (ERM protein family), but the other proteins in which the FERM domain is found do not share any region of similarity outside of this domain. ERM proteins are made of three domains, the FERM domain, a central helical domain and a C-terminal tail domain, which binds F-actin. The amino-acid sequence of the FERM domain is highly conserved among ERM proteins and is responsible for membrane association by direct binding to the cytoplasmic domain or tail of integral membrane proteins. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail domains that masks their binding sites for other molecules. For cytoskeleton-membrane cross-linking, the dormant molecules becomes activated and the FERM domain attaches to the membrane by binding specific membrane proteins, while the last 34 residues of the tail bind actin filaments. Aside from binding to membranes, the activated FERM domain of ERM proteins can also bind the guanine nucleotide dissociation inhibitor of Rho GTPase (RhoDGI), which suggests that in addition to functioning as a cross-linker, ERM proteins may influence Rho signalling pathways. The crystal structure of the FERM domain reveals that it is composed of three structural modules (F1, F2, and F3) that together form a compact clover-shaped structure [].The FERM domain has also been called the amino-terminal domain, the 30kDa domain, 4.1N30, the membrane-cytoskeletal-linking domain, the ERM-like domain, the ezrin-like domain of the band 4.1 superfamily, the conserved N-terminal region, and the membrane attachment domain [].This entry represents the PH-like domain found at the C terminus of the FERM domain.
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Protein Domain
IPR000299 | FERM_domain
Type: Domain
Description: The FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane []. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus of the majority of FERM-containing proteins [, ], which includes: Band 4.1, which links the spectrin-actin cytoskeleton of erythrocytes to the plasma membrane.Ezrin, a component of the undercoat of the microvilli plasma membrane.Moesin, which is probably involved in binding major cytoskeletal structures to the plasma membrane.Radixin, which is involved in the binding of the barbed end of actin filaments to the plasma membrane in the undercoat of the cell- to-cell adherens junction.Talin, a cytoskeletal protein concentrated in regions of cell-substratum contact and, in lymphocytes, of cell-cell contacts.Filopodin, a slime mold protein that binds actin and which is involved in the control of cell motility and chemotaxis.Merlin (or schwannomin).Protein NBL4.Unconventional myosins X, VIIa and XV, which are mutated in congenital deafness.Focal-adhesion kinases (FAKs), cytoplasmic protein tyrosine kinases involved in signalling through integrins.Janus tyrosine kinases (JAKs), cytoplasmic tyrosine kinases that are non-covalently associated with the cytoplasmic tails of receptors for cytokines or polypeptidic hormones.Non-receptor tyrosine-protein kinase TYK2.Protein-tyrosine phosphatases PTPN3 and PTPN4, enzyme that appear to act at junctions between the membrane and the cytoskeleton.Protein-tyrosine phosphatases PTPN14 and PTP-D1, PTP-RL10 and PTP2E.Caenorhabditis elegans protein phosphatase ptp-1.Ezrin, moesin, and radixin are highly related proteins (ERM protein family), but the other proteins in which the FERM domain is found do not share any region of similarity outside of this domain. ERM proteins are made of three domains, the FERM domain, a central helical domain and a C-terminal tail domain, which binds F-actin. The amino-acid sequence of the FERM domain is highly conserved among ERM proteins and is responsible for membrane association by direct binding to the cytoplasmic domain or tail of integral membrane proteins. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail domains that masks their binding sites for other molecules. For cytoskeleton-membrane cross-linking, the dormant molecules becomes activated and the FERM domain attaches to the membrane by binding specific membrane proteins, while the last 34 residues of the tail bind actin filaments. Aside from binding to membranes, the activated FERM domain of ERM proteins can also bind the guanine nucleotide dissociation inhibitor of Rho GTPase (RhoDGI), which suggests that in addition to functioning as a cross-linker, ERM proteins may influence Rho signalling pathways. The crystal structure of the FERM domain reveals that it is composed of three structural modules (F1, F2, and F3) that together form a compact clover-shaped structure [].The FERM domain has also been called the amino-terminal domain, the 30kDa domain, 4.1N30, the membrane-cytoskeletal-linking domain, the ERM-like domain, the ezrin-like domain of the band 4.1 superfamily, the conserved N-terminal region, and the membrane attachment domain [].
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Protein Domain
IPR019748 | FERM_central
Type: Domain
Description: The FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane []. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus of the majority of FERM-containing proteins [, ], which includes: Band 4.1, which links the spectrin-actin cytoskeleton of erythrocytes to the plasma membrane.Ezrin, a component of the undercoat of the microvilli plasma membrane.Moesin, which is probably involved in binding major cytoskeletal structures to the plasma membrane.Radixin, which is involved in the binding of the barbed end of actin filaments to the plasma membrane in the undercoat of the cell- to-cell adherens junction.Talin, a cytoskeletal protein concentrated in regions of cell-substratum contact and, in lymphocytes, of cell-cell contacts.Filopodin, a slime mold protein that binds actin and which is involved in the control of cell motility and chemotaxis.Merlin (or schwannomin).Protein NBL4.Unconventional myosins X, VIIa and XV, which are mutated in congenital deafness.Focal-adhesion kinases (FAKs), cytoplasmic protein tyrosine kinases involved in signalling through integrins.Janus tyrosine kinases (JAKs), cytoplasmic tyrosine kinases that are non-covalently associated with the cytoplasmic tails of receptors for cytokines or polypeptidic hormones.Non-receptor tyrosine-protein kinase TYK2.Protein-tyrosine phosphatases PTPN3 and PTPN4, enzyme that appear to act at junctions between the membrane and the cytoskeleton.Protein-tyrosine phosphatases PTPN14 and PTP-D1, PTP-RL10 and PTP2E.Caenorhabditis elegans protein phosphatase ptp-1.Ezrin, moesin, and radixin are highly related proteins (ERM protein family), but the other proteins in which the FERM domain is found do not share any region of similarity outside of this domain. ERM proteins are made of three domains, the FERM domain, a central helical domain and a C-terminal tail domain, which binds F-actin. The amino-acid sequence of the FERM domain is highly conserved among ERM proteins and is responsible for membrane association by direct binding to the cytoplasmic domain or tail of integral membrane proteins. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail domains that masks their binding sites for other molecules. For cytoskeleton-membrane cross-linking, the dormant molecules becomes activated and the FERM domain attaches to the membrane by binding specific membrane proteins, while the last 34 residues of the tail bind actin filaments. Aside from binding to membranes, the activated FERM domain of ERM proteins can also bind the guanine nucleotide dissociation inhibitor of Rho GTPase (RhoDGI), which suggests that in addition to functioning as a cross-linker, ERM proteins may influence Rho signalling pathways. The crystal structure of the FERM domain reveals that it is composed of three structural modules (F1, F2, and F3) that together form a compact clover-shaped structure [].The FERM domain has also been called the amino-terminal domain, the 30kDa domain, 4.1N30, the membrane-cytoskeletal-linking domain, the ERM-like domain, the ezrin-like domain of the band 4.1 superfamily, the conserved N-terminal region, and the membrane attachment domain [].
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Protein Domain
IPR019749 | Band_41_domain
Type: Domain
Description: The FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane []. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus of the majority of FERM-containing proteins [, ], which includes: Band 4.1, which links the spectrin-actin cytoskeleton of erythrocytes to the plasma membrane.Ezrin, a component of the undercoat of the microvilli plasma membrane.Moesin, which is probably involved in binding major cytoskeletal structures to the plasma membrane.Radixin, which is involved in the binding of the barbed end of actin filaments to the plasma membrane in the undercoat of the cell- to-cell adherens junction.Talin, a cytoskeletal protein concentrated in regions of cell-substratum contact and, in lymphocytes, of cell-cell contacts.Filopodin, a slime mold protein that binds actin and which is involved in the control of cell motility and chemotaxis.Merlin (or schwannomin).Protein NBL4.Unconventional myosins X, VIIa and XV, which are mutated in congenital deafness.Focal-adhesion kinases (FAKs), cytoplasmic protein tyrosine kinases involved in signalling through integrins.Janus tyrosine kinases (JAKs), cytoplasmic tyrosine kinases that are non-covalently associated with the cytoplasmic tails of receptors for cytokines or polypeptidic hormones.Non-receptor tyrosine-protein kinase TYK2.Protein-tyrosine phosphatases PTPN3 and PTPN4, enzyme that appear to act at junctions between the membrane and the cytoskeleton.Protein-tyrosine phosphatases PTPN14 and PTP-D1, PTP-RL10 and PTP2E.Caenorhabditis elegans protein phosphatase ptp-1.Ezrin, moesin, and radixin are highly related proteins (ERM protein family), but the other proteins in which the FERM domain is found do not share any region of similarity outside of this domain. ERM proteins are made of three domains, the FERM domain, a central helical domain and a C-terminal tail domain, which binds F-actin. The amino-acid sequence of the FERM domain is highly conserved among ERM proteins and is responsible for membrane association by direct binding to the cytoplasmic domain or tail of integral membrane proteins. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail domains that masks their binding sites for other molecules. For cytoskeleton-membrane cross-linking, the dormant molecules becomes activated and the FERM domain attaches to the membrane by binding specific membrane proteins, while the last 34 residues of the tail bind actin filaments. Aside from binding to membranes, the activated FERM domain of ERM proteins can also bind the guanine nucleotide dissociation inhibitor of Rho GTPase (RhoDGI), which suggests that in addition to functioning as a cross-linker, ERM proteins may influence Rho signalling pathways. The crystal structure of the FERM domain reveals that it is composed of three structural modules (F1, F2, and F3) that together form a compact clover-shaped structure [].The FERM domain has also been called the amino-terminal domain, the 30kDa domain, 4.1N30, the membrane-cytoskeletal-linking domain, the ERM-like domain, the ezrin-like domain of the band 4.1 superfamily, the conserved N-terminal region, and the membrane attachment domain [].
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Protein Domain
IPR019747 | FERM_CS
Type: Conserved_site
Description: The FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane []. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus of the majority of FERM-containing proteins [, ], which includes: Band 4.1, which links the spectrin-actin cytoskeleton of erythrocytes to the plasma membrane.Ezrin, a component of the undercoat of the microvilli plasma membrane.Moesin, which is probably involved in binding major cytoskeletal structures to the plasma membrane.Radixin, which is involved in the binding of the barbed end of actin filaments to the plasma membrane in the undercoat of the cell- to-cell adherens junction.Talin, a cytoskeletal protein concentrated in regions of cell-substratum contact and, in lymphocytes, of cell-cell contacts.Filopodin, a slime mold protein that binds actin and which is involved in the control of cell motility and chemotaxis.Merlin (or schwannomin).Protein NBL4.Unconventional myosins X, VIIa and XV, which are mutated in congenital deafness.Focal-adhesion kinases (FAKs), cytoplasmic protein tyrosine kinases involved in signalling through integrins.Janus tyrosine kinases (JAKs), cytoplasmic tyrosine kinases that are non-covalently associated with the cytoplasmic tails of receptorsfor cytokines or polypeptidic hormones.Non-receptor tyrosine-protein kinase TYK2.Protein-tyrosine phosphatases PTPN3 and PTPN4, enzyme that appear to act at junctions between the membrane and the cytoskeleton.Protein-tyrosine phosphatases PTPN14 and PTP-D1, PTP-RL10 and PTP2E.Caenorhabditis elegans protein phosphatase ptp-1.Ezrin, moesin, and radixin are highly related proteins (ERM protein family), but the other proteins in which the FERM domain is found do not share any region of similarity outside of this domain. ERM proteins are made of three domains, the FERM domain, a central helical domain and a C-terminal tail domain, which binds F-actin. The amino-acid sequence of the FERM domain is highly conserved among ERM proteins and is responsible for membrane association by direct binding to the cytoplasmic domain or tail of integral membrane proteins. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail domains that masks their binding sites for other molecules. For cytoskeleton-membrane cross-linking, the dormant molecules becomes activated and the FERM domain attaches to the membrane by binding specific membrane proteins, while the last 34 residues of the tail bind actin filaments. Aside from binding to membranes, the activated FERM domain of ERM proteins can also bind the guanine nucleotide dissociation inhibitor of Rho GTPase (RhoDGI), which suggests that in addition to functioning as a cross-linker, ERM proteins may influence Rho signalling pathways. The crystal structure of the FERM domain reveals that it is composed of three structural modules (F1, F2, and F3) that together form a compact clover-shaped structure [].The FERM domain has also been called the amino-terminal domain, the 30kDa domain, 4.1N30, the membrane-cytoskeletal-linking domain, the ERM-like domain, the ezrin-like domain of the band 4.1 superfamily, the conserved N-terminal region, and the membrane attachment domain [].This entry represents the conserved sites of the FERM domain.
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Protein Domain
IPR035963 | FERM_2
Type: Homologous_superfamily
Description: The FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane []. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface between the plasma membrane and the cytoskeleton. The FERM domain is located at the N terminus of the majority of FERM-containing proteins [, ], which includes: Band 4.1, which links the spectrin-actin cytoskeleton of erythrocytes to the plasma membrane.Ezrin, a component of the undercoat of the microvilli plasma membrane.Moesin, which is probably involved in binding major cytoskeletal structures to the plasma membrane.Radixin, which is involved in the binding of the barbed end of actin filaments to the plasma membrane in the undercoat of the cell- to-cell adherens junction.Talin, a cytoskeletal protein concentrated in regions of cell-substratum contact and, in lymphocytes, of cell-cell contacts.Filopodin, a slime mold protein that binds actin and which is involved in the control of cell motility and chemotaxis.Merlin (or schwannomin).Protein NBL4.Unconventional myosins X, VIIa and XV, which are mutated in congenital deafness.Focal-adhesion kinases (FAKs), cytoplasmic protein tyrosine kinases involved in signalling through integrins.Janus tyrosine kinases (JAKs), cytoplasmic tyrosine kinases that are non-covalently associated with the cytoplasmic tails of receptors for cytokines or polypeptidic hormones.Non-receptor tyrosine-protein kinase TYK2.Protein-tyrosine phosphatases PTPN3 and PTPN4, enzyme that appear to act at junctions between the membrane and the cytoskeleton.Protein-tyrosine phosphatases PTPN14 and PTP-D1, PTP-RL10 and PTP2E.Caenorhabditis elegans protein phosphatase ptp-1.Ezrin, moesin, and radixin are highly related proteins (ERM protein family), but the other proteins in which the FERM domain is found do not share any region of similarity outside of this domain. ERM proteins are made of three domains, the FERM domain, a central helical domain and a C-terminal tail domain, which binds F-actin. The amino-acid sequence of the FERM domain is highly conserved among ERM proteins and is responsible for membrane association by direct binding to the cytoplasmic domain or tail of integral membrane proteins. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail domains that masks their binding sites for other molecules. For cytoskeleton-membrane cross-linking, the dormant molecules becomes activated and the FERM domain attaches to the membrane by binding specific membrane proteins, while the last 34 residues of the tail bind actin filaments. Aside from binding to membranes, the activated FERM domain of ERM proteins can also bind the guanine nucleotide dissociation inhibitor of Rho GTPase (RhoDGI), which suggests that in addition to functioning as a cross-linker, ERM proteins may influence Rho signallingpathways. The crystal structure of the FERM domain reveals that it is composed of three structural modules (F1, F2, and F3) that together form a compact clover-shaped structure [].The FERM domain has also been called the amino-terminal domain, the 30kDa domain, 4.1N30, the membrane-cytoskeletal-linking domain, the ERM-like domain, the ezrin-like domain of the band 4.1 superfamily, the conserved N-terminal region, and the membrane attachment domain [].
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Protein
Q8C780
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: true
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Protein
A0A286YDD0
Organism: Mus musculus/domesticus
Length: 53  
Fragment?: true
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Protein
Q8CGJ2
Organism: Mus musculus/domesticus
Length: 639  
Fragment?: true
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Protein
Q8BT29
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: true
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Protein
A6X941
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: true
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Protein
E9PXK8
Organism: Mus musculus/domesticus
Length: 85  
Fragment?: false
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Protein
A0A0N4SVT9
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
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Protein
Q8CE88
Organism: Mus musculus/domesticus
Length: 876  
Fragment?: false
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Protein
Q8CAV9
Organism: Mus musculus/domesticus
Length: 957  
Fragment?: true
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Protein
E9PUU9
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
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Protein
Q05DI4
Organism: Mus musculus/domesticus
Length: 852  
Fragment?: true
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Protein
A0A087WP93
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: true
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Protein
E9QA59
Organism: Mus musculus/domesticus
Length: 88  
Fragment?: false
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Protein
A0A1Y7VNU2
Organism: Mus musculus/domesticus
Length: 850  
Fragment?: true
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Protein
A0A1L1SVA8
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: true
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Protein
E9Q210
Organism: Mus musculus/domesticus
Length: 89  
Fragment?: false
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Protein
A0A2R8VHB6
Organism: Mus musculus/domesticus
Length: 213  
Fragment?: true
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Protein
Q8C0V9
Organism: Mus musculus/domesticus
Length: 622  
Fragment?: false
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Protein
Q3TKJ2
Organism: Mus musculus/domesticus
Length: 321  
Fragment?: true
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Protein
Q8BV94
Organism: Mus musculus/domesticus
Length: 250  
Fragment?: false
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Protein
A0A1D5RLV1
Organism: Mus musculus/domesticus
Length: 476  
Fragment?: true
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Protein
E9Q805
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: true
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Protein
A0A286YDY4
Organism: Mus musculus/domesticus
Length: 852  
Fragment?: true
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Protein
Q8BX61
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: false
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Protein
Q6PG62
Organism: Mus musculus/domesticus
Length: 1015  
Fragment?: false
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Protein
Q8BW31
Organism: Mus musculus/domesticus
Length: 261  
Fragment?: true
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Protein
F2Z484
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
Q3UY58
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: true
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Protein
A2ALK9
Organism: Mus musculus/domesticus
Length: 229  
Fragment?: true
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Protein
F7CDA2
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: true
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Protein
Q8BV52
Organism: Mus musculus/domesticus
Length: 1113  
Fragment?: false
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Protein
A2A842
Organism: Mus musculus/domesticus
Length: 769  
Fragment?: false
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Protein
Q8BWC1
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: true
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Protein
E9PW99
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: true
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Protein
A0A286YCY8
Organism: Mus musculus/domesticus
Length: 287  
Fragment?: false
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Protein
A0A140LI67
Organism: Mus musculus/domesticus
Length: 1392  
Fragment?: false
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Protein
Q811C0
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: true
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Protein
A2AIM2
Organism: Mus musculus/domesticus
Length: 241  
Fragment?: true
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Protein
Q3UH12
Organism: Mus musculus/domesticus
Length: 476  
Fragment?: true
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Protein
P48193
Organism: Mus musculus/domesticus
Length: 858  
Fragment?: false
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Protein
P26043
Organism: Mus musculus/domesticus
Length: 583  
Fragment?: false
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Protein
Q8BGS1
Organism: Mus musculus/domesticus
Length: 731  
Fragment?: false
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Protein
Q91VS8
Organism: Mus musculus/domesticus
Length: 1065  
Fragment?: false
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Protein
P46662
Organism: Mus musculus/domesticus
Length: 596  
Fragment?: false
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Protein
Q8BIE6
Organism: Mus musculus/domesticus
Length: 1020  
Fragment?: false
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Protein
Q920B0
Organism: Mus musculus/domesticus
Length: 1035  
Fragment?: false
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Protein
Q9WV92
Organism: Mus musculus/domesticus
Length: 929  
Fragment?: false
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Protein
O70318
Organism: Mus musculus/domesticus
Length: 988  
Fragment?: false
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Protein
P52963
Organism: Mus musculus/domesticus
Length: 686  
Fragment?: false
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Protein
P26040
Organism: Mus musculus/domesticus
Length: 586  
Fragment?: false
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Protein
Q9JMC8
Organism: Mus musculus/domesticus
Length: 527  
Fragment?: false
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Protein
F8VPU2
Organism: Mus musculus/domesticus
Length: 1048  
Fragment?: false
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Protein
P26041
Organism: Mus musculus/domesticus
Length: 577  
Fragment?: false
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Protein
Q9Z2H5
Organism: Mus musculus/domesticus
Length: 879  
Fragment?: false
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Protein
A2AD83
Organism: Mus musculus/domesticus
Length: 703  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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