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Search results 301 to 381 out of 381 for Fh1

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Type Details Score
Publication
18815276 | J:265609
First Author: Young KG
Year: 2008
Journal: Mol Biol Cell
Title: INF1 is a novel microtubule-associated formin.
Volume: 19
Issue: 12
Pages: 5168-80
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Publication
12906795 | J:84868
First Author: Li F
Year: 2003
Journal: Curr Biol
Title: The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition.
Volume: 13
Issue: 15
Pages: 1335-40
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Publication
15138637 | J:93259
First Author: Katoh M
Year: 2004
Journal: Int J Mol Med
Title: Identification and characterization of human FHDC1, mouse Fhdc1 and zebrafish fhdc1 genes in silico.
Volume: 13
Issue: 6
Pages: 929-34
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Publication
17684061 | J:128373
First Author: Gopinath SD
Year: 2007
Journal: J Cell Sci
Title: The RhoA effector mDiaphanous regulates MyoD expression and cell cycle progression via SRF-dependent and SRF-independent pathways.
Volume: 120
Issue: Pt 17
Pages: 3086-98
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Publication
28566324 | J:247277
First Author: Quirós PM
Year: 2017
Journal: J Cell Biol
Title: Multi-omics analysis identifies ATF4 as a key regulator of the mitochondrial stress response in mammals.
Volume: 216
Issue: 7
Pages: 2027-2045
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Publication
19383632 | J:149484
First Author: Zhou F
Year: 2009
Journal: Hum Mol Genet
Title: Formin1 disruption confers oligodactylism and alters Bmp signaling.
Volume: 18
Issue: 13
Pages: 2472-82
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Publication
38387459 | J:347661
First Author: Nikalayevich E
Year: 2024
Journal: Dev Cell
Title: Aberrant cortex contractions impact mammalian oocyte quality.
Volume: 59
Issue: 7
Pages: 841-852.e7
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Protein
Q9JL04
Organism: Mus musculus/domesticus
Length: 1578  
Fragment?: false
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Publication
14992721 | J:88572
First Author: Shimada A
Year: 2004
Journal: Mol Cell
Title: The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization.
Volume: 13
Issue: 4
Pages: 511-22
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Protein
Q05860
Organism: Mus musculus/domesticus
Length: 1466  
Fragment?: false
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Protein
B9EHJ5
Organism: Mus musculus/domesticus
Length: 1334  
Fragment?: false
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Protein
B7ZW99
Organism: Mus musculus/domesticus
Length: 1332  
Fragment?: false
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Protein
E9Q7P6
Organism: Mus musculus/domesticus
Length: 1332  
Fragment?: false
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Protein
A0A5F8MPL0
Organism: Mus musculus/domesticus
Length: 850  
Fragment?: false
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Publication
17915251 | J:166349
First Author: Ramirez-Espain X
Year: 2007
Journal: J Mol Biol
Title: Structural characterization of a new binding motif and a novel binding mode in group 2 WW domains.
Volume: 373
Issue: 5
Pages: 1255-68
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Protein
Q3ULZ2
Organism: Mus musculus/domesticus
Length: 1149  
Fragment?: false
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Protein
A0A0A6YXK5
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
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Protein
Q3USM5
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: true
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Protein
A0A0A6YY57
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: true
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Protein
Q05BK1
Organism: Mus musculus/domesticus
Length: 235  
Fragment?: false
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Publication
15006353 | -
First Author: Xu Y
Year: 2004
Journal: Cell
Title: Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture.
Volume: 116
Issue: 5
Pages: 711-23
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Protein
Q62438
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: true
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Publication
19633175 | -
First Author: Liu R
Year: 2009
Journal: Development
Title: Wash functions downstream of Rho and links linear and branched actin nucleation factors.
Volume: 136
Issue: 16
Pages: 2849-60
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Publication
11171383 | -
First Author: Kato T
Year: 2001
Journal: J Cell Sci
Title: Localization of a mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells.
Volume: 114
Issue: Pt 4
Pages: 775-84
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Protein Domain
IPR010472 | FH3_dom
Type: Domain
Description: Formin homology (FH) proteins play a crucial role in the reorganisation of the actin cytoskeleton, which mediates various functions of the cell cortex including motility, adhesion, and cytokinesis []. Formins are multidomain proteins that interact with diverse signalling molecules and cytoskeletal proteins, although some formins have been assigned functions within the nucleus. Formins are characterised by the presence of three FH domains (FH1, FH2 and FH3), although members of the formin family do not necessarily contain all three domains []. The proline-rich FH1 domain mediates interactions with a variety of proteins, including the actin-binding protein profilin, SH3 (Src homology 3) domain proteins, and WW domain proteins. The FH2 domain () is required to inhibit actin polymerisation. The FH3 domain is less well conserved and is required for directing formins to the correct intracellular location, such the mitotic spindle [], or the projection tip during conjugation []. In addition, some formins can contain a GTPase-binding domain (GBD) () required for binding to Rho small GTPases, and a C-terminal conserved Dia-autoregulatory domain (DAD).This entry represents the FH3 domain.
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Protein Domain
IPR042201 | FH2_Formin_sf
Type: Homologous_superfamily
Description: Formin homology (FH) proteins play a crucial role in the reorganisation of the actin cytoskeleton, which mediates various functions of the cell cortex including motility, adhesion, and cytokinesis []. Formins are multidomain proteins that interact with diverse signalling molecules and cytoskeletal proteins, although some formins have been assigned functions within the nucleus. Formins are characterised by the presence of three FH domains (FH1, FH2 and FH3), although members of the formin family do not necessarily contain all three domains []. The proline-rich FH1 domain mediates interactions with a variety of proteins, including the actin-binding protein profilin, SH3 (Src homology 3) domain proteins, and WW domain proteins. The FH2 domain is required for the self-association of formin proteins through the ability of FH2 domains to directly bind each other [], and may also act to inhibit actin polymerisation []. The FH3 domain () is less well conserved and may be important for determining intracellular localisation of formin family proteins. In addition, some formins can contain a GTPase-binding domain (GBD) () required for binding to Rho small GTPases, and a C-terminal conserved Dia-autoregulatory domain (DAD).This superfamily represents the FH2 domain, which was shown by X-ray crystallography to have an elongated, crescent shape containing three helical subdomains [].
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Protein Domain
IPR015425 | FH2_Formin
Type: Domain
Description: Formin homology (FH) proteins play a crucial role in the reorganisation of the actin cytoskeleton, which mediates various functions of thecell cortex including motility, adhesion, and cytokinesis []. Formins are multidomain proteins that interact with diverse signalling molecules and cytoskeletal proteins, although some formins have been assigned functions within the nucleus. Formins are characterised by the presence of three FH domains (FH1, FH2 and FH3), although members of the formin family do not necessarily contain all three domains []. The proline-rich FH1 domain mediates interactions with a variety of proteins, including the actin-binding protein profilin, SH3 (Src homology 3) domain proteins, and WW domain proteins. The FH2 domain is required for the self-association of formin proteins through the ability of FH2 domains to directly bind each other [], and may also act to inhibit actin polymerisation []. The FH3 domain () is less well conserved and may be important for determining intracellular localisation of formin family proteins. In addition, some formins can contain a GTPase-binding domain (GBD) () required for binding to Rho small GTPases, and a C-terminal conserved Dia-autoregulatory domain (DAD).This entry represents the FH2 domain, which was shown by X-ray crystallography to have an elongated, crescent shape containing three helical subdomains [].
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Protein Domain
IPR001265 | Formin_Cappuccino_subfam
Type: Family
Description: Formins (formin homology proteins) proteins play a crucial role in the reorganisation of the actin cytoskeleton and associate with the fast-growing end (barbed end) of actin filaments [, ]. This entry represents the formin homologues from animals (and some fungi), including protein cappuccino from Drosophila melanogaster and formins from human and mouse. Protein cappuccino acts as an actin nucleation factor and promotes assembly of actin filaments together with spir. It may play a role in intracellular vesicle transport along actin fibres, providing a novel link between actin cytoskeleton dynamics and intracellular transport []. Formins are characterised by the presence of three FH domains (FH1, FH2 and FH3), although members of the formin family do not necessarily contain all three domains []. The proline-rich FH1 domain mediates interactions with a variety of proteins, including the actin-binding protein profilin, SH3 (Src homology 3) domain proteins, and WW domain proteins. The FH2 domain is required for the self-association of formin proteins through the ability of FH2 domains to directly bind each other [], and may also act to inhibit actin polymerisation []. The FH3 domain () is less well conserved and may be important for determining intracellular localisation of formin family proteins. In addition, some formins can contain a GTPase-binding domain (GBD) () required for binding to Rho small GTPases, and a C-terminal conserved Dia-autoregulatory domain (DAD).
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Publication
10631086 | -
First Author: Tanaka K
Year: 2000
Journal: Biochem Biophys Res Commun
Title: Formin family proteins in cytoskeletal control.
Volume: 267
Issue: 2
Pages: 479-81
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Protein
Q496P2
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
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Protein
Q6P9T5
Organism: Mus musculus/domesticus
Length: 743  
Fragment?: false
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Protein
Q8BI52
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: false
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Protein
G3UWI1
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: true
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Protein
O08548
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: true
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Protein
Q3U104
Organism: Mus musculus/domesticus
Length: 679  
Fragment?: false
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Protein
A0A1Y7VM80
Organism: Mus musculus/domesticus
Length: 720  
Fragment?: true
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Protein
Q3UX40
Organism: Mus musculus/domesticus
Length: 173  
Fragment?: true
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Protein
Q3UVP0
Organism: Mus musculus/domesticus
Length: 656  
Fragment?: true
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Publication
16292343 | -
First Author: Lammers M
Year: 2005
Journal: EMBO J
Title: The regulation of mDia1 by autoinhibition and its release by Rho*GTP.
Volume: 24
Issue: 23
Pages: 4176-87
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Protein
O08808
Organism: Mus musculus/domesticus
Length: 1255  
Fragment?: false
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Protein
O70566
Organism: Mus musculus/domesticus
Length: 1098  
Fragment?: false
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Protein
Q9Z207
Organism: Mus musculus/domesticus
Length: 1171  
Fragment?: false
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Protein
Q0GNC1
Organism: Mus musculus/domesticus
Length: 1273  
Fragment?: false
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Protein
E9QLA5
Organism: Mus musculus/domesticus
Length: 1271  
Fragment?: false
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Protein
K4PWM5
Organism: Mus musculus/domesticus
Length: 1109  
Fragment?: false
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Protein
Q3U4Y4
Organism: Mus musculus/domesticus
Length: 949  
Fragment?: false
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Protein
Q3UU77
Organism: Mus musculus/domesticus
Length: 1001  
Fragment?: true
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Protein
E9PXV7
Organism: Mus musculus/domesticus
Length: 1255  
Fragment?: false
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Protein
Q8K331
Organism: Mus musculus/domesticus
Length: 929  
Fragment?: false
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Protein
F6XC54
Organism: Mus musculus/domesticus
Length: 1220  
Fragment?: false
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Protein
E9Q4U7
Organism: Mus musculus/domesticus
Length: 1102  
Fragment?: false
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Protein
F8WIG5
Organism: Mus musculus/domesticus
Length: 1171  
Fragment?: false
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Protein
Q3TSX1
Organism: Mus musculus/domesticus
Length: 999  
Fragment?: true
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Protein
Q8C414
Organism: Mus musculus/domesticus
Length: 824  
Fragment?: true
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Protein
D3Z074
Organism: Mus musculus/domesticus
Length: 1220  
Fragment?: false
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Protein
Q5DTM7
Organism: Mus musculus/domesticus
Length: 1192  
Fragment?: true
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Protein
Q9CSJ1
Organism: Mus musculus/domesticus
Length: 129  
Fragment?: true
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Protein
Q0VGT1
Organism: Mus musculus/domesticus
Length: 1171  
Fragment?: false
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Protein
Q6W4W7
Organism: Mus musculus/domesticus
Length: 1102  
Fragment?: false
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Protein
E9PV41
Organism: Mus musculus/domesticus
Length: 1264  
Fragment?: false
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Protein
Q5DTQ4
Organism: Mus musculus/domesticus
Length: 1285  
Fragment?: true
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Protein
Q5PR81
Organism: Mus musculus/domesticus
Length: 1147  
Fragment?: true
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Protein
Q0QWG9
Organism: Mus musculus/domesticus
Length: 1203  
Fragment?: false
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Protein
Q3TY82
Organism: Mus musculus/domesticus
Length: 668  
Fragment?: false
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Protein
Q6P247
Organism: Mus musculus/domesticus
Length: 235  
Fragment?: true
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Protein
A2APV2
Organism: Mus musculus/domesticus
Length: 1086  
Fragment?: false
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Protein
Q9JL26
Organism: Mus musculus/domesticus
Length: 1094  
Fragment?: false
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Protein
Q80U19
Organism: Mus musculus/domesticus
Length: 1115  
Fragment?: false
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Protein
Q8BPM0
Organism: Mus musculus/domesticus
Length: 1077  
Fragment?: false
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Protein
Q6ZPF4
Organism: Mus musculus/domesticus
Length: 1028  
Fragment?: false
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Protein
A0A1W2P6X3
Organism: Mus musculus/domesticus
Length: 1100  
Fragment?: false
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Protein
E9PXE6
Organism: Mus musculus/domesticus
Length: 1034  
Fragment?: false
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Protein
D3Z7A7
Organism: Mus musculus/domesticus
Length: 1027  
Fragment?: false
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Protein
A2AQW2
Organism: Mus musculus/domesticus
Length: 1085  
Fragment?: false
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Protein
F8VPR2
Organism: Mus musculus/domesticus
Length: 1083  
Fragment?: false
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Protein
Q6ZQ74
Organism: Mus musculus/domesticus
Length: 1087  
Fragment?: true
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Protein
A2AB60
Organism: Mus musculus/domesticus
Length: 1090  
Fragment?: false
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Publication
9606213 | -
First Author: Petersen J
Year: 1998
Journal: J Cell Biol
Title: FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation.
Volume: 141
Issue: 5
Pages: 1217-28
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Protein
Q76LL6
Organism: Mus musculus/domesticus
Length: 1578  
Fragment?: false
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Protein
Q6P9Q4
Organism: Mus musculus/domesticus
Length: 1197  
Fragment?: false
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Protein
Q3US76
Organism: Mus musculus/domesticus
Length: 497  
Fragment?: true
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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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom