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Search results 101 to 132 out of 132 for Hook3

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Type Details Score
Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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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
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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
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Publication
11238449 | -
First Author: Walenta JH
Year: 2001
Journal: J Cell Biol
Title: The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins.
Volume: 152
Issue: 5
Pages: 923-34
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Publication
12950921 | -
First Author: Shotland Y
Year: 2003
Journal: Mol Microbiol
Title: The Salmonella SpiC protein targets the mammalian Hook3 protein function to alter cellular trafficking.
Volume: 49
Issue: 6
Pages: 1565-76
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Protein
F6W1A2
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: true
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Protein
Q3UUZ6
Organism: Mus musculus/domesticus
Length: 366  
Fragment?: true
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Protein Domain
IPR008636 | Hook_C
Type: Domain
Description: The Hook family consists of several proteins from different eukaryotic organisms, first identified in Drosophila melanogaster in which play a role in endocytic cargo sorting []. In Drosophila and fungi there is a single Hook gene, whereas mammals have three Hook genes, Hook1, Hook2 and Hook3. Endogenous Hook3 binds to Golgi membranes while both Hook1 and Hook2 are localised to discrete but unidentified cellular structures [, ]. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubule structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head []. They are a widely expressed class of dynein-associated cargo adaptor proteins which include different domains. The N-terminal partof these proteins is sufficient to form a stable complex with dynein-dynactin and includes the most conserved region within the first 160 amino acids, termed the Hook domain. This domain is followed by three coiled-coil domains, important for dimerization and activation of dynein-dynactin complex motility, and then a C-terminal domain that binds a variety of proteins specific for each Hook isoform, involved in binding to specific organelles (organelle-binding domains). All mammalian Hook isoforms form a complex with Fused Toes and the Fused Toes- and Hook-interacting protein; fungal homologues of these proteins are important for dynein-mediated early endosome transport by linking Hook to the cargo [].This entry represents the central coiled-coiled region and the divergent C-terminal domain from Hook proteins.
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Publication
12075009 | J:77010
First Author: Mendoza-Lujambio I
Year: 2002
Journal: Hum Mol Genet
Title: The Hook1 gene is non-functional in the abnormal spermatozoon head shape (azh) mutant mouse.
Volume: 11
Issue: 14
Pages: 1647-58
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Publication
27482052 | -
First Author: Schroeder CM
Year: 2016
Journal: J Cell Biol
Title: Assembly and activation of dynein-dynactin by the cargo adaptor protein Hook3.
Volume: 214
Issue: 3
Pages: 309-18
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Publication
11018772 | -
First Author: Narayanan R
Year: 2000
Journal: J Neurobiol
Title: Drosophila endosomal proteins hook and deep orange regulate synapse size but not synaptic vesicle recycling.
Volume: 45
Issue: 2
Pages: 105-19
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Publication
30948426 | -
First Author: Marivin A
Year: 2019
Journal: J Cell Biol
Title: GPCR-independent activation of G proteins promotes apical cell constriction in vivo.
Volume: 218
Issue: 5
Pages: 1743-1763
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Publication
27623382 | -
First Author: Nechipurenko IV
Year: 2016
Journal: Dev Cell
Title: A Conserved Role for Girdin in Basal Body Positioning and Ciliogenesis.
Volume: 38
Issue: 5
Pages: 493-506
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Protein Domain
IPR043936 | HOOK_N
Type: Domain
Description: The Hook family consists of several proteins from different eukaryotic organisms, first identified in Drosophila melanogaster in which play a role in endocytic cargo sorting []. In Drosophila and fungi there is a single Hook gene, whereas mammals have three Hook genes, Hook1, Hook2 and Hook3. Endogenous Hook3 binds to Golgi membranes while both Hook1 and Hook2 are localised to discrete but unidentified cellular structures [, ]. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubule structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head []. They are a widely expressed class of dynein-associated cargo adaptor proteins which include different domains. The N-terminal part of these proteins is sufficient to form a stable complex with dynein-dynactin and includes the most conserved region within the first 160 amino acids, termed the Hook domain. This domain is followed by three coiled-coil domains, important for dimerization and activation of dynein-dynactin complex motility, and then a C-terminal domain that binds a variety of proteins specific for each Hook isoform, involved in binding to specific organelles (organelle-binding domains). All mammalian Hook isoforms form a complex with Fused Toes and the Fused Toes- and Hook-interacting protein; fungal homologues of these proteins are important for dynein-mediated early endosome transport by linking Hook to the cargo [].This entry includes residues in the first 160 amino acids at the N-terminal of Hook, which is the most conserved region and necessary for dynein-dynactin interaction. It interacts with dynein light intermediate chain 1 (LIC1) []. This domain is also found in protein Daple []and Girdin []which are G-protein modulators involved in ciliogenesis and cilium morphology, integrity of the actin cytoskeleton, formation of actin stress fibres and lamellipodia and membrane sorting in the early endosome.
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Protein
Q8BUK6
Organism: Mus musculus/domesticus
Length: 718  
Fragment?: false
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Protein
Q7TMK6
Organism: Mus musculus/domesticus
Length: 716  
Fragment?: false
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Protein
Q8BIL5
Organism: Mus musculus/domesticus
Length: 728  
Fragment?: false
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Protein
A0A1B0GSU8
Organism: Mus musculus/domesticus
Length: 611  
Fragment?: false
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Protein
Q5BKS5
Organism: Mus musculus/domesticus
Length: 720  
Fragment?: false
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Protein
Q3UWV9
Organism: Mus musculus/domesticus
Length: 692  
Fragment?: false
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Protein
Q3TKK8
Organism: Mus musculus/domesticus
Length: 715  
Fragment?: false
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Protein
A0A1B0GT78
Organism: Mus musculus/domesticus
Length: 692  
Fragment?: false
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Protein
Q4QRL3
Organism: Mus musculus/domesticus
Length: 1481  
Fragment?: false
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Protein
B2RXR1
Organism: Mus musculus/domesticus
Length: 1481  
Fragment?: false
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Protein
Q5SNZ0
Organism: Mus musculus/domesticus
Length: 1873  
Fragment?: false
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Protein
Q6VGS5
Organism: Mus musculus/domesticus
Length: 2009  
Fragment?: false
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Protein
Q8BJ23
Organism: Mus musculus/domesticus
Length: 221  
Fragment?: false
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Protein
Z4YKY0
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: false
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Protein
A0A6I8MX08
Organism: Mus musculus/domesticus
Length: 2016  
Fragment?: false
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Protein
Q80XQ1
Organism: Mus musculus/domesticus
Length: 1427  
Fragment?: false
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Protein
Q9DCU8
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: false
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