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Search results 201 to 221 out of 221 for Sec13

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Type Details Score
Protein Domain
IPR007230 | Nup98_auto-Pept-S59_dom
Type: Domain
Description: Nuclear pore complexes (NPCs) facilitate all nucleocytoplasmic transport in eukaryotic cells, playing essential roles in cellular homeostasis. The NPC is a modular structure composed of multiple copies of ~30 proteins (nucleoporins, Nups) arranged into distinct subcomplexes [, ]. A number of these peptides are synthesised as precursors and undergo self-catalyzed cleavage. The largest NPC sub-complex is the heptameric Y-shaped mammalian Nup107-Nup160 complex (called Nup84 complex in budding yeast), an essential scaffolding component of the NPC [, , ]. Nup98 and Nup96 are encoded by the same gene that produces a 190 kDa polyprotein with autoproteolytic activity which generates the N-terminal NUP98 and C-terminal NUP96 proteins, part of the Nup107-Nup160 subcomplex [, ]. The yeast homologue Nup145 undergoes the similar proteolytic event to produce Nup145N and Nup145C, which are part of the Nup84 complex. The function of the heptamer is to coat the curvature of the nuclear pore complex between the inner and outer nuclear membranes. Nup96, which is predicted to be an alpha helical solenoid, complexes with Sec13 in the middle of the heptamer. The interaction between Nup96 and Sec13 is the point of curvature in the heptameric complex [, ].The proteolytic cleavage site of yeast Nup145p has been mapped upstream of an evolutionary conserved serine residue. Then, Nup145C form the heptameric Y-complex together with six other proteins while Nup145N shuttle between the NPC and the nuclear interior. [, ].Nup98, a component of the nuclear pore that plays its primary role in the export of RNAs, is expressed in two forms, derived from alternate mRNA splicing. Both forms are processed into two peptides through autoproteolysis mediated by the C-terminal domain of hNup98. The three-dimensional structure of the C-terminal domain reveals a novel protein fold, and thus a new class of autocatalytic proteases. The structure further reveals that the suggested nucleoporin RNA binding motif is unlikely to bind to RNA [].The following nucleoporins share an ~150-residue C-terminal domain responsible for NPC targeting [, ]:Vertebrate Nup98, a component of the nuclear pore that plays its primary role in the export of RNAs.Yeast Nup100, plays an important role in several nuclear export and import pathways including poly(A)+ RNA and protein transport.Yeast Nup116, involved in mRNA export and protein transport.Yeast Nup145, involved in nuclear poly(A)+ RNA and tRNA export.The NUP C-terminal domains of Nup98 and Nup145 possess peptidase S59autoproteolytic activity. The autoproteolytic sites of Nup98 and Nup145each occur immediately C-terminal to the NUP C-terminal domain. Thus, althoughthis domain occurs in the middle of each precursor polypeptide, it winds up atthe C-terminal end of the N-terminal cleavage product. Cleavage of the peptidechains are necessary for the proper targeting to the nuclear pore [, ].The NUP C-terminal domain adopts a predominantly β-strand structure. The molecule consists of a six-stranded β-sheet sandwiched against a two-stranded β-sheet and flanked by α-helical regions. The N-terminal helical region consists of two short helices, whereas the stretch on the opposite side of molecule consists of a single, longer helix [, ].
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Protein
E9QAT4
Organism: Mus musculus/domesticus
Length: 2357  
Fragment?: false
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Protein
Q91XT4
Organism: Mus musculus/domesticus
Length: 1051  
Fragment?: false
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Protein
Q3TPG3
Organism: Mus musculus/domesticus
Length: 861  
Fragment?: false
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Protein
Q3UJE5
Organism: Mus musculus/domesticus
Length: 984  
Fragment?: false
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Protein
A0A140T8J8
Organism: Mus musculus/domesticus
Length: 1187  
Fragment?: false
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Protein
F6Q2Y9
Organism: Mus musculus/domesticus
Length: 699  
Fragment?: true
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Protein
B7ZN81
Organism: Mus musculus/domesticus
Length: 1170  
Fragment?: false
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Protein
A0A1B0GS62
Organism: Mus musculus/domesticus
Length: 230  
Fragment?: true
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Protein
A0A1B0GRA7
Organism: Mus musculus/domesticus
Length: 984  
Fragment?: false
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Protein
F7BPW6
Organism: Mus musculus/domesticus
Length: 907  
Fragment?: true
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Protein
A0A1B0GRB5
Organism: Mus musculus/domesticus
Length: 967  
Fragment?: false
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Protein
B2RQL0
Organism: Mus musculus/domesticus
Length: 1170  
Fragment?: false
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Publication
18974315 | -
First Author: Brohawn SG
Year: 2008
Journal: Science
Title: Structural evidence for common ancestry of the nuclear pore complex and vesicle coats.
Volume: 322
Issue: 5906
Pages: 1369-73
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Protein
Q8R2U0
Organism: Mus musculus/domesticus
Length: 360  
Fragment?: false
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Protein
Q3UPL0
Organism: Mus musculus/domesticus
Length: 1230  
Fragment?: false
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Protein
S4R2A9
Organism: Mus musculus/domesticus
Length: 934  
Fragment?: true
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Protein
Q9CWU9
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
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Publication
21183079 | J:292518
First Author: Huttlin EL
Year: 2010
Journal: Cell
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume: 143
Issue: 7
Pages: 1174-89
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