Summary: GLUT4 regulating protein TUG
This is the Wikipedia entry entitled "TUG-UBL1 protein domain". More...
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TUG-UBL1 protein domain Edit Wikipedia article
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solution structure and backbone dynamics of an n-terminal ubiquitin-like domain in the glut4-tethering protein, tug
In molecular biology, TUG-UBL1 refers to a protein that regulates a glucose transporter called GLUT4. TUG-UBL1 is an acronym for Tether containing UBX domain for GLUT4-Ubiquitin Like 1, this is encoded for by the gene, ASPSCR1.
When insulin is secreted, glucose uptake of cells increase, since insulin stimulates GLUT4 to move from the intracellular surface to the outer surface. In a similar fashion, TUG retains GLUT4 within unstimulated celled, but when insulin is secreted it causes GLUT4 to dissociate and so GLUT4 moves to the cell surface. TUG binds directly and specifically to a large intracellular loop in GLUT4. It acts as a tethering protein, which along with other proteins, retain GLUT4 within cells in the absence of insulin. Additionally, when the protein TUG becomes disrupted it appears to accelerate the degradation of GLUT4 in lysosomes. However, the functional role of the TUG–UBL1 domain remains to be elucidated.
N-terminal ubiquitin-like domain (TUG–UBL1) has a tertiary structure of TUG–UBL1, which consists of a beta-grasp or ubiquitin-like topology for this domain. This comprises a five-stranded beta-sheet, a single major alpha-helix (residues 32–42), and two short helices.
TUG releases the GLUT4 containing vesicles (GSVs) in response to insulin stimulation which allows it to move to the plasma membrane. TUG has an N-terminal ubiquitin-like protein domain (UBL1) which in similar proteins appears to participate in protein-protein interactions. The region does have an area of negative electrostatic potential and increased backbone motility which leads to suggestions of a potential protein-protein interaction site.
- Yu C, Cresswell J, Löffler MG, Bogan JS (2007). "The glucose transporter 4-regulating protein TUG is essential for highly insulin-responsive glucose uptake in 3T3-L1 adipocytes.". J Biol Chem 282 (10): 7710–22. doi:10.1074/jbc.M610824200. PMC 2243252. PMID 17202135.
- Tettamanzi MC, Yu C, Bogan JS, Hodsdon ME (2006). "Solution structure and backbone dynamics of an N-terminal ubiquitin-like domain in the GLUT4-regulating protein, TUG.". Protein Sci 15 (3): 498–508. doi:10.1110/ps.051901806. PMC 2249771. PMID 16501224.
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GLUT4 regulating protein TUG Provide feedback
TUG is a GLUT4 regulating protein and functions to retain membrane vesicles containing GLUT4 intracellularly. TUG releases the GLUT4 containing vesicles to the cellular exocytic machinery in response to insulin stimulation which allows translocation to the plasma membrane . TUG has an N-terminal ubiquitin-like domain (UBL1) which in similar proteins appears to participate in protein-protein interactions . The region does have a area of negative electrostatic potential and increased backbone motility which leads to suggestions of a potential protein-protein interaction site .
Tettamanzi MC, Yu C, Bogan JS, Hodsdon ME; , Protein Sci. 2006;15:498-508.: Solution structure and backbone dynamics of an N-terminal ubiquitin-like domain in the GLUT4-regulating protein, TUG. PUBMED:16501224 EPMC:16501224
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR021569
TUG is a GLUT4 regulating protein and functions to retain membrane vesicles containing GLUT4 intracellularly. TUG releases the GLUT4 containing vesicles to the cellular exocytic machinery in response to insulin stimulation which allows translocation to the plasma membrane [PUBMED:16501224]. TUG has an N-terminal ubiquitin-like domain (UBL1) which in similar proteins appears to participate in protein-protein interactions [PUBMED:16501224]. The region does have a area of negative electrostatic potential and increased backbone motility which leads to suggestions of a potential protein-protein interaction site [PUBMED:16501224].
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This family includes proteins that share the ubiquitin fold. It currently unites four SCOP superfamilies.
The clan contains the following 41 members:APG12 Atg8 Blt1 Caps_synth_GfcC CIDE-N Cobl DUF1315 DUF2407 DUF4430 DWNN FERM_N Lambda_tail_I Multi_ubiq NQRA_SLBB PB1 PI3K_rbd Plug Prok_Ub RA Rad60-SLD Rad60-SLD_2 Ras_bdg_2 RBD SLBB Telomere_Sde2 TGS ThiS ThiS-like TmoB TUG-UBL1 Ub-Mut7C Ub-RnfH ubiquitin Ubiquitin_2 Ubiquitin_3 UBX Ufm1 UN_NPL4 Urm1 YchF-GTPase_C YukD
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Curation and family details
|Number in seed:||28|
|Number in full:||216|
|Average length of the domain:||62.90 aa|
|Average identity of full alignment:||38 %|
|Average coverage of the sequence by the domain:||12.64 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||3|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the TUG-UBL1 domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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