|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 101 to 179 out of 179 for Tom1

<< First    < Previous  |  Next >    Last >>
0.023s

Categories

Hits by Pathway

Hits by Strain

Hits by Category

Type Details Score
Publication
11751856 | -
First Author: Zhang G
Year: 2002
Journal: J Biol Chem
Title: Negative regulation of toll-like receptor-mediated signaling by Tollip.
Volume: 277
Issue: 9
Pages: 7059-65
•
•
•
•
•
Protein Domain
IPR041198 | GGA_N-GAT
Type: Domain
Description: This domain is found in the N-terminal region of the GGA and Tom1 (GAT) domain in Golgi-localizing gamma-adaptin ARF-binding protein 1 (GGA1). This domain can also be found in GGA2 and GGA3. The GAT domains is the key region in GGA that interacts with ARF. ARF plays a crucial role in docking adaptor proteins to membranes. This domain is referred to as N-GAT and it interacts extensively with ARF [].The GAT domain is a region of homology of ~130 residues, which is found in eukaryotic GGAs (for Golgi-localized, gamma ear-containing ADP ribosylation factor (ARF)-binding proteins) and vertebrate TOMs (for target of myb). The GAT domain is found in its entirety only in GGAs, although, at the C terminus it shares partial sequence similarity with a short region of TOMs. The GAT domain is found in association with other domains, such as VHS and GAE. The GAT domain of GGAs serves as a molecular anchor of GGA to trans-Golgi network (TGN) membranes via its interaction with the GTP-bound form of a member of the ARFfamily of small GTPases and can bind specifically to the Rab GTPase effector rabaptin5 and to ubiquitin [, , , ].The GGA-GAT domain possesses an all α-helical structure, composed of four helices arranged in a somewhat unusual topology, which has been called the helical paper clip. The overall structure shows that the GAT domain has an elongated shape, in which the longest helix participates in two small independent subdomains: an N-terminal helix-loop-helix hook and a C-terminal three-helix bundle. The hook subdomain has been shown to be both necessary and sufficient for ARF-GTP binding and Golgi targeting of GGAs. The N-terminal hook subdomain contains a hydrophobic patch, which is found to interact directly with ARF []. It has been proposed that this interaction might stabilise the hook subdomain []. The C-terminal three-helix bundle is involved in the binding with Rabaptin5 and ubiquitin [].
•
•
•
•
•
Protein
A2A9W5
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: true
•
•
•
•
•
Protein
B0R0N7
Organism: Mus musculus/domesticus
Length: 65  
Fragment?: true
•
•
•
•
•
Protein
A6PWP3
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: true
•
•
•
•
•
Protein
A0A1D5RM84
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: true
•
•
•
•
•
Protein
A0A1D5RM12
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: false
•
•
•
•
•
Protein
A0A0A6YVP6
Organism: Mus musculus/domesticus
Length: 50  
Fragment?: false
•
•
•
•
•
Publication
10693761 | J:60640
First Author: Mao Y
Year: 2000
Journal: Cell
Title: Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction.
Volume: 100
Issue: 4
Pages: 447-56
•
•
•
•
•
Publication
11859376 | -
First Author: Shiba T
Year: 2002
Journal: Nature
Title: Structural basis for recognition of acidic-cluster dileucine sequence by GGA1.
Volume: 415
Issue: 6874
Pages: 937-41
•
•
•
•
•
Publication
14973137 | -
First Author: Bai H
Year: 2004
Journal: J Biol Chem
Title: GGA1 interacts with the adaptor protein AP-1 through a WNSF sequence in its hinge region.
Volume: 279
Issue: 17
Pages: 17411-7
•
•
•
•
•
Publication
14745135 | -
First Author: Nakayama K
Year: 2003
Journal: Cell Struct Funct
Title: The structure and function of GGAs, the traffic controllers at the TGN sorting crossroads.
Volume: 28
Issue: 5
Pages: 431-42
•
•
•
•
•
Publication
16413283 | -
 
First Author: Nakayama K
Year: 2005
Journal: Methods Enzymol
Title: Analysis of Arf interaction with GGAs in vitro and in vivo.
Volume: 404
Pages: 367-77
•
•
•
•
•
Publication
15966896 | -
First Author: Kawasaki M
Year: 2005
Journal: Genes Cells
Title: Molecular mechanism of ubiquitin recognition by GGA3 GAT domain.
Volume: 10
Issue: 7
Pages: 639-54
•
•
•
•
•
Protein Domain
IPR008152 | Clathrin_a/b/g-adaptin_app_Ig
Type: Domain
Description: Proteins synthesized on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. These vesicles have specific coat proteins (such as clathrin or coatomer) that are important for cargo selection and direction of transport []. Clathrin coats contain both clathrin (acts as a scaffold) and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The two major types of clathrin adaptor complexes are the heterotetrameric adaptor protein (AP) complexes, and the monomeric GGA (Golgi-localising, Gamma-adaptin ear domain homology, ARF-binding proteins) adaptors [, ].AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and lipids to clathrin at vesicle budding sites, as well as binding accessory proteins that regulate coat assembly and disassembly (such as AP180, epsins and auxilin). There are different AP complexes in mammals. AP1 is responsible for the transport of lysosomal hydrolases between the TGN and endosomes []. AP2 associates with the plasma membrane and is responsible for endocytosis []. AP3 is responsible for protein trafficking to lysosomes and other related organelles []. AP4 is less well characterised. AP complexes are heterotetramers composed of two large subunits (adaptins), a medium subunit (mu) and a small subunit (sigma). For example, in AP1 these subunits are gamma-1-adaptin, beta-1-adaptin, mu-1 and sigma-1, while in AP2 they are alpha-adaptin, beta-2-adaptin, mu-2 and sigma-2. Each subunit has a specific function. Adaptins recognise and bind to clathrin through their hinge region (clathrinbox), and recruit accessory proteins that modulate AP function through their C-terminal ear (appendage) domains. Mu recognises tyrosine-based sorting signals within the cytoplasmic domains of transmembrane cargo proteins []. One function of clathrin and AP2 complex-mediated endocytosis is to regulate the number of GABA(A) receptors available at the cell surface []. GGAs (Golgi-localising, Gamma-adaptin ear domain homology, ARF-binding proteins) are a family of monomeric clathrin adaptor proteins that are conserved from yeasts to humans. GGAs regulate clathrin-mediated the transport of proteins (such as mannose 6-phosphate receptors) from the TGN to endosomes and lysosomes through interactions with TGN-sorting receptors, sometimes in conjunction with AP-1 [, ]. GGAs bind cargo, membranes, clathrin and accessory factors. GGA1, GGA2 and GGA3 all contain a domain homologous to the ear domain of gamma-adaptin. GGAs are composed of a single polypeptide with four domains: an N-terminal VHS (Vps27p/Hrs/Stam) domain, a GAT (GGA and Tom1) domain, a hinge region, and a C-terminal GAE (gamma-adaptin ear) domain. The VHS domain is responsible for endocytosis and signal transduction, recognising transmembrane cargo through the ACLL sequence in the cytoplasmic domains of sorting receptors []. The GAT domain (also found in Tom1 proteins) interacts with ARF (ADP-ribosylation factor) to regulate membrane trafficking [], and with ubiquitin for receptor sorting []. The hinge region contains a clathrin box for recognition and binding to clathrin, similar to that found in AP adaptins. The GAE domain is similar to the AP gamma-adaptin ear domain, and is responsible for the recruitment of accessory proteins that regulate clathrin-mediated endocytosis [].This entry represents a β-sandwich structural motif found in the appendage (ear) domain of alpha-, beta- and gamma-adaptin from AP clathrin adaptor complexes, and the GAE (gamma-adaptin ear) domain of GGA adaptor proteins. These domains have an immunoglobulin-like β-sandwich fold containing 7 or 8 strands in 2 β-sheets in a Greek key topology [, ]. Although these domains share a similar fold, there is little sequence identity between the alpha/beta-adaptins and gamma-adaptin/GAE.
•
•
•
•
•
Protein
Q3TB03
Organism: Mus musculus/domesticus
Length: 388  
Fragment?: true
•
•
•
•
•
Protein
A0A2R8VI72
Organism: Mus musculus/domesticus
Length: 363  
Fragment?: false
•
•
•
•
•
Protein
Q8R0H9
Organism: Mus musculus/domesticus
Length: 635  
Fragment?: false
•
•
•
•
•
Protein
Q6P5E6
Organism: Mus musculus/domesticus
Length: 603  
Fragment?: false
•
•
•
•
•
Protein
Q3UE19
Organism: Mus musculus/domesticus
Length: 603  
Fragment?: false
•
•
•
•
•
Protein
Q3TVV9
Organism: Mus musculus/domesticus
Length: 603  
Fragment?: false
•
•
•
•
•
Protein
S4R2D2
Organism: Mus musculus/domesticus
Length: 595  
Fragment?: false
•
•
•
•
•
Protein
Q9QZ06
Organism: Mus musculus/domesticus
Length: 274  
Fragment?: false
•
•
•
•
•
Protein
F7AT44
Organism: Mus musculus/domesticus
Length: 270  
Fragment?: false
•
•
•
•
•
Protein
A9JEI5
Organism: Mus musculus/domesticus
Length: 205  
Fragment?: false
•
•
•
•
•
Protein
A2ARJ0
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: true
•
•
•
•
•
Protein
Q8BQL7
Organism: Mus musculus/domesticus
Length: 274  
Fragment?: false
•
•
•
•
•
Publication
12679809 | J:116254
First Author: Shiba T
Year: 2003
Journal: Nat Struct Biol
Title: Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport.
Volume: 10
Issue: 5
Pages: 386-93
•
•
•
•
•
Publication
11301005 | -
First Author: Puertollano R
Year: 2001
Journal: Cell
Title: The GGAs promote ARF-dependent recruitment of clathrin to the TGN.
Volume: 105
Issue: 1
Pages: 93-102
•
•
•
•
•
Publication
12636914 | -
First Author: Collins BM
Year: 2003
Journal: Dev Cell
Title: The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs.
Volume: 4
Issue: 3
Pages: 321-32
•
•
•
•
•
Publication
15457209 | -
First Author: Zhu G
Year: 2004
Journal: EMBO J
Title: Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5.
Volume: 23
Issue: 20
Pages: 3909-17
•
•
•
•
•
Protein
Q8BMI3
Organism: Mus musculus/domesticus
Length: 718  
Fragment?: false
•
•
•
•
•
Protein
A2A9W7
Organism: Mus musculus/domesticus
Length: 640  
Fragment?: false
•
•
•
•
•
Publication
12808037 | -
First Author: Lui WW
Year: 2003
Journal: Mol Biol Cell
Title: Binding partners for the COOH-terminal appendage domains of the GGAs and gamma-adaptin.
Volume: 14
Issue: 6
Pages: 2385-98
•
•
•
•
•
Protein
O88811
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
•
•
•
•
•
Protein
P70297
Organism: Mus musculus/domesticus
Length: 548  
Fragment?: false
•
•
•
•
•
Protein
Q3TQ49
Organism: Mus musculus/domesticus
Length: 548  
Fragment?: false
•
•
•
•
•
Protein
Q3UGN9
Organism: Mus musculus/domesticus
Length: 462  
Fragment?: false
•
•
•
•
•
Protein
Q3UMC8
Organism: Mus musculus/domesticus
Length: 553  
Fragment?: false
•
•
•
•
•
Protein
Q3TGH8
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
•
•
•
•
•
Publication
12042876 | -
First Author: Nogi T
Year: 2002
Journal: Nat Struct Biol
Title: Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain.
Volume: 9
Issue: 7
Pages: 527-31
•
•
•
•
•
Protein
P22892
Organism: Mus musculus/domesticus
Length: 822  
Fragment?: false
•
•
•
•
•
Protein
O88512
Organism: Mus musculus/domesticus
Length: 791  
Fragment?: false
•
•
•
•
•
Protein
Q99LI8
Organism: Mus musculus/domesticus
Length: 775  
Fragment?: false
•
•
•
•
•
Protein
Q3UMA3
Organism: Mus musculus/domesticus
Length: 776  
Fragment?: false
•
•
•
•
•
Protein
Q8CBB7
Organism: Mus musculus/domesticus
Length: 825  
Fragment?: false
•
•
•
•
•
Protein
A0A140LIG7
Organism: Mus musculus/domesticus
Length: 317  
Fragment?: true
•
•
•
•
•
Protein
Q8CC03
Organism: Mus musculus/domesticus
Length: 695  
Fragment?: true
•
•
•
•
•
Protein
B1ATY9
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: true
•
•
•
•
•
Protein
Q3TLL4
Organism: Mus musculus/domesticus
Length: 771  
Fragment?: false
•
•
•
•
•
Protein
Q8BSZ7
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: true
•
•
•
•
•
Protein
Q3UHW6
Organism: Mus musculus/domesticus
Length: 791  
Fragment?: false
•
•
•
•
•
Protein
Q3U9D1
Organism: Mus musculus/domesticus
Length: 791  
Fragment?: false
•
•
•
•
•
Protein
Q3UKX8
Organism: Mus musculus/domesticus
Length: 825  
Fragment?: false
•
•
•
•
•
Publication
11080148 | -
First Author: Haucke V
Year: 2000
Journal: EMBO J
Title: Dual interaction of synaptotagmin with mu2- and alpha-adaptin facilitates clathrin-coated pit nucleation.
Volume: 19
Issue: 22
Pages: 6011-9
•
•
•
•
•
Publication
15107467 | -
First Author: Touz MC
Year: 2004
Journal: Mol Biol Cell
Title: Adaptor protein complex 1 mediates the transport of lysosomal proteins from a Golgi-like organelle to peripheral vacuoles in the primitive eukaryote Giardia lamblia.
Volume: 15
Issue: 7
Pages: 3053-60
•
•
•
•
•
Publication
12952931 | -
First Author: Conner SD
Year: 2003
Journal: J Cell Biol
Title: Differential requirements for AP-2 in clathrin-mediated endocytosis.
Volume: 162
Issue: 5
Pages: 773-9
•
•
•
•
•
Publication
16542748 | -
First Author: Gupta SN
Year: 2006
Journal: Eur J Cell Biol
Title: Re-routing of the invariant chain to the direct sorting pathway by introduction of an AP3-binding motif from LIMP II.
Volume: 85
Issue: 6
Pages: 457-67
•
•
•
•
•
Publication
17254016 | J:299556
First Author: Kanematsu T
Year: 2007
Journal: J Neurochem
Title: Phospholipase C-related inactive protein is implicated in the constitutive internalization of GABAA receptors mediated by clathrin and AP2 adaptor complex.
Volume: 101
Issue: 4
Pages: 898-905
•
•
•
•
•
Protein
P17427
Organism: Mus musculus/domesticus
Length: 938  
Fragment?: false
•
•
•
•
•
Protein
P17426
Organism: Mus musculus/domesticus
Length: 977  
Fragment?: false
•
•
•
•
•
Protein
O35643
Organism: Mus musculus/domesticus
Length: 943  
Fragment?: false
•
•
•
•
•
Protein
Q9DBG3
Organism: Mus musculus/domesticus
Length: 937  
Fragment?: false
•
•
•
•
•
Protein
Q3TVN4
Organism: Mus musculus/domesticus
Length: 943  
Fragment?: false
•
•
•
•
•
Protein
Q8CC13
Organism: Mus musculus/domesticus
Length: 953  
Fragment?: false
•
•
•
•
•
Protein
Q69ZW4
Organism: Mus musculus/domesticus
Length: 967  
Fragment?: true
•
•
•
•
•
Protein
H3BKM0
Organism: Mus musculus/domesticus
Length: 913  
Fragment?: false
•
•
•
•
•
Protein
Q5SVG5
Organism: Mus musculus/domesticus
Length: 916  
Fragment?: false
•
•
•
•
•
Protein
Q6NXY3
Organism: Mus musculus/domesticus
Length: 542  
Fragment?: true
•
•
•
•
•
Protein
Q6PEE6
Organism: Mus musculus/domesticus
Length: 938  
Fragment?: false
•
•
•
•
•
Protein
Q5SWR1
Organism: Mus musculus/domesticus
Length: 951  
Fragment?: false
•
•
•
•
•
Protein
H3BIY9
Organism: Mus musculus/domesticus
Length: 942  
Fragment?: false
•
•
•
•
•
Protein
Q3U7X9
Organism: Mus musculus/domesticus
Length: 938  
Fragment?: false
•
•
•
•
•
Protein
Q5SVG4
Organism: Mus musculus/domesticus
Length: 923  
Fragment?: false
•
•
•
•
•
Protein
Q3U1K9
Organism: Mus musculus/domesticus
Length: 943  
Fragment?: false
•
•
•
•
•
Publication
12858162 | -
First Author: Miller GJ
Year: 2003
Journal: Nat Struct Biol
Title: Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3.
Volume: 10
Issue: 8
Pages: 599-606
•
•
•
•
•
Publication
11598180 | -
First Author: Boehm M
Year: 2001
Journal: Mol Biol Cell
Title: Adaptins: the final recount.
Volume: 12
Issue: 10
Pages: 2907-20
•
•
•
•
•
Publication
17449236 | -
First Author: Voglmaier SM
Year: 2007
Journal: Curr Opin Neurobiol
Title: Do different endocytic pathways make different synaptic vesicles?
Volume: 17
Issue: 3
Pages: 374-80
•
•
•
•
•
Publication
15261670 | -
First Author: McMahon HT
Year: 2004
Journal: Curr Opin Cell Biol
Title: COP and clathrin-coated vesicle budding: different pathways, common approaches.
Volume: 16
Issue: 4
Pages: 379-91
•
•
•
•
•




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