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Search results 101 to 137 out of 137 for Fgd3

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0.02s

Type

Details

Score

Publication

- | J:60000

First Author:	UniProt-GOA
Year:	2012

Title:	Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping

•

Publication

12466851 | J:80000

First Author:	Okazaki Y
Year:	2002
Journal:	Nature
Title:	Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume:	420
Issue:	6915
Pages:	563-73

•

Publication

21267068 | J:153498

First Author:	Diez-Roux G
Year:	2011
Journal:	PLoS Biol
Title:	A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume:	9
Issue:	1
Pages:	e1000582

•

Publication

- | J:75000

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2002

Title:	Mouse Genome Informatics Computational Sequence to Gene Associations

•

Publication

- | J:157972

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2010
Journal:	Database Download
Title:	Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).

•

Publication

- | J:161428

First Author:	Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year:	2010

Title:	Annotation inferences using phylogenetic trees

•

Publication

- | J:63103

First Author:	Mouse Genome Database and National Center for Biotechnology Information
Year:	2000
Journal:	Database Release
Title:	Entrez Gene Load

•

Publication

- | J:262123

First Author:	Allen Institute for Brain Science
Year:	2004
Journal:	Allen Institute
Title:	Allen Brain Atlas: mouse riboprobes

•

Publication

- | J:144086

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2009
Journal:	Database Download
Title:	Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform

•

Publication

- | J:155721

First Author:	Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year:	2010
Journal:	Database Download
Title:	Consensus CDS project

•

Publication

- | J:85324

First Author:	Mouse Genome Informatics Group
Year:	2003
Journal:	Database Procedure
Title:	Automatic Encodes (AutoE) Reference

•

Publication

- | J:53168

First Author:	Bairoch A
Year:	1999
Journal:	Database Release
Title:	SWISS-PROT Annotated protein sequence database

•

Publication

- | J:91388

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2005

Title:	Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations

•

Publication

- | J:155221

First Author:	Mouse Genome Informatics
Year:	2010
Journal:	Database Release
Title:	Protein Ontology Association Load.

•

Publication

- | J:90438

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2005

Title:	Obtaining and loading genome assembly coordinates from NCBI annotations

•

Publication

- | J:144087

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2009
Journal:	Database Download
Title:	Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform

•

Publication

26306008 | J:228925

First Author:	Takasuga A
Year:	2015
Journal:	PLoS Genet
Title:	Non-synonymous FGD3 Variant as Positional Candidate for Disproportional Tall Stature Accounting for a Carcass Weight QTL (CW-3) and Skeletal Dysplasia in Japanese Black Cattle.
Volume:	11
Issue:	8
Pages:	e1005433

•

Protein Domain

IPR035939 | FGD1_PH1

Type:

Domain

Description:

This entry represents the N-terminal PH domain of FGD1.In general, FGDs (including FGD1, FGD2, FGD3 and FGD4/Frabin) have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain []. Mutations in the FGD1 gene are responsible for the X-linked disorder known as faciogenital dysplasia (FGDY) []. Both FGD1 and FGD3 are targeted by the ubiquitin ligase SCF(FWD1/beta-TrCP) upon phosphorylation of two serine residues in its DSGIDS motif and subsequently degraded by the proteasome. However, FGD1 and FGD3 induced significantly different morphological changes in HeLa Tet-Off cells and while FGD1 induced long finger-like protrusions, FGD3 induced broad sheet-like protrusions when the level of GTP-bound Cdc42 was significantly increased by the inducible expression of FGD3. They also reciprocally regulated cell motility in inducibly expressed in HeLa Tet-Off cells, FGD1 stimulated cell migration while FGD3 inhibited it. FGD1 and FGD3 therefore play different roles to regulate cellular functions, even though their intracellular levels are tightly controlled by the same destruction pathway through SCF(FWD1/beta-TrCP) [, ].PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner []. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity []. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane []. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes [].

•

Protein Domain

IPR035941 | FGD1-4_PH2

Type:

Domain

Description:

This entry represents the C-terminal PH domain of FGD1-4.In general, FGDs (including FGD1, FGD2, FGD3 and FGD4/Frabin) have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulatorof membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain []. Mutations in the FGD1 gene are responsible for the X-linked disorder known as faciogenital dysplasia (FGDY) []. Both FGD1 and FGD3 are targeted by the ubiquitin ligase SCF(FWD1/beta-TrCP) upon phosphorylation of two serine residues in its DSGIDS motif and subsequently degraded by the proteasome. However, FGD1 and FGD3 induced significantly different morphological changes in HeLa Tet-Off cells and while FGD1 induced long finger-like protrusions, FGD3 induced broad sheet-like protrusions when the level of GTP-bound Cdc42 was significantly increased by the inducible expression of FGD3. They also reciprocally regulated cell motility in inducibly expressed in HeLa Tet-Off cells, FGD1 stimulated cell migration while FGD3 inhibited it. FGD1 and FGD3 therefore play different roles to regulate cellular functions, even though their intracellular levels are tightly controlled by the same destruction pathway through SCF(FWD1/beta-TrCP) [, ].PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner []. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity []. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane []. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes [].

•

Publication

18410521 | -

First Author:	Nakanishi H
Year:	2008
Journal:	J Cell Mol Med
Title:	Frabin and other related Cdc42-specific guanine nucleotide exchange factors couple the actin cytoskeleton with the plasma membrane.
Volume:	12
Issue:	4
Pages:	1169-76

•

Publication

19261807 | -

First Author:	Egorov MV
Year:	2009
Journal:	Mol Biol Cell
Title:	Faciogenital dysplasia protein (FGD1) regulates export of cargo proteins from the golgi complex via Cdc42 activation.
Volume:	20
Issue:	9
Pages:	2413-27

•

Publication

21212517 | -

First Author:	Oshima T
Year:	2011
Journal:	Biol Pharm Bull
Title:	Role of FGD1, a Cdc42 guanine nucleotide exchange factor, in epidermal growth factor-stimulated c-Jun NH2-terminal kinase activation and cell migration.
Volume:	34
Issue:	1
Pages:	54-60

•

Publication

18838382 | J:143609

First Author:	Huber C
Year:	2008
Journal:	J Biol Chem
Title:	FGD2, a CDC42-specific exchange factor expressed by antigen-presenting cells, localizes to early endosomes and active membrane ruffles.
Volume:	283
Issue:	49
Pages:	34002-12

•

Protein Domain

IPR037797 | FGD2_PH1

Type:

Domain

Description:

In general, FGDs (including FGD1, FGD2, FGD3 and FGD4/Frabin) have a RhoGEF (DH) domain, followed by an N-terminal PH domain, a FYVE domain and a C-terminal PH domain. All FGDs are guanine nucleotide exchange factors that activates the Rho GTPase Cdc42, an important regulator of membrane trafficking. The RhoGEF domain is responsible for GEF catalytic activity, while the N-terminal PH domain is involved in intracellular targeting of the DH domain []. FGD2 is expressed by antigen-presenting cells where it may be involved in leukocyte signaling and vesicle trafficking [].This entry represents the N-terminal PH domain of FGD2.

•

Protein

P52734

Organism:	Mus musculus/domesticus
Length:	960
Fragment?:	false

•

Protein

A2ALP5

Organism:	Mus musculus/domesticus
Length:	791
Fragment?:	false

•

Protein

Q3UG32

Organism:	Mus musculus/domesticus
Length:	960
Fragment?:	false

•

Publication

15493994 | -

First Author:	Lemmon MA
Year:	2004
Journal:	Biochem Soc Trans
Title:	Pleckstrin homology domains: not just for phosphoinositides.
Volume:	32
Issue:	Pt 5
Pages:	707-11

•

Protein

Q91ZT5

Organism:	Mus musculus/domesticus
Length:	766
Fragment?:	false

•

Protein

F8WGX0

Organism:	Mus musculus/domesticus
Length:	754
Fragment?:	true

•

Protein

Q99K79

Organism:	Mus musculus/domesticus
Length:	397
Fragment?:	false

•

Protein

A0A3Q4EH50

Organism:	Mus musculus/domesticus
Length:	316
Fragment?:	false

•

Publication

14594214 | -

First Author:	Cozier GE
Year:	2004
Journal:	Curr Top Microbiol Immunol
Title:	Membrane targeting by pleckstrin homology domains.
Volume:	282

Pages:	49-88

•

Publication

22728242 | -

First Author:	Scheffzek K
Year:	2012
Journal:	FEBS Lett
Title:	Pleckstrin homology (PH) like domains - versatile modules in protein-protein interaction platforms.
Volume:	586
Issue:	17
Pages:	2662-73

•

Protein

Q8BY35

Organism:	Mus musculus/domesticus
Length:	655
Fragment?:	false

•

Protein

O88842

Organism:	Mus musculus/domesticus
Length:	733
Fragment?:	false

•

Protein

Q3TNB8

Organism:	Mus musculus/domesticus
Length:	733
Fragment?:	false

•

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Search results 101 to 137 out of 137 for Fgd3

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