|  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 125 out of 125 for Mon2

<< First    < Previous  |  Next >    Last >>
0.019s
Type Details Score
Protein Domain
Type: Domain
Description: This is theN-terminal domain of Mon2- and BIG1-like proteins, the dimerisation and cyclophilin-binding domain (DCB) [, ]. The N terminus of Mon2 (Ysl2) binds to Arf-Like small GTPase Arl1, and shows homology to brefeldin A-inhibited guanine-exchange factor (BIG) domains []. Mon2 and BIG1-like proteins play an important role in membrane traffic and Golgi homeostasis [, , ]. This domain is sufficient for targeting BIG1 to the Golgi.
Protein
Organism: Mus musculus/domesticus
Length: 436  
Fragment?: false
Publication
First Author: Gillingham AK
Year: 2006
Journal: J Biol Chem
Title: Mon2, a relative of large Arf exchange factors, recruits Dop1 to the Golgi apparatus.
Volume: 281
Issue: 4
Pages: 2273-80
Protein
Organism: Mus musculus/domesticus
Length: 551  
Fragment?: true
Publication
First Author: Lowery J
Year: 2013
Journal: J Biol Chem
Title: The Sec7 guanine nucleotide exchange factor GBF1 regulates membrane recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to the trans-Golgi network (TGN).
Volume: 288
Issue: 16
Pages: 11532-45
Protein Domain
Type: Domain
Description: This entry represent the HUS regulatory domain found towards the N terminus in guanine nucleotide exchange factors involved Golgi transport, such as budding yeast protein Sec7, protein Mon2 and BIG1-like proteins [, ].Sec7 and its homologues are guanine nucleotide exchange factors (GEFs) involved in the secretory pathway []. The full-length Sec7 functions proximally in the secretory pathway as a protein binding scaffold for the coat protein complexes COPII-COPI []. The COPII-COPI-protein switch is necessary for maturation of the vesicular-tubular cluster, VTC, intermediate compartments for Golgi compartment biogenesis. This N-terminal domain however does not appear to be binding either of the COP or the ARF [].Mon2 is distantly related to the Arf1 guanine nucleotide exchange factors (GEFs), such as Sec7. However, it lacks the Sec7 domain that catalyses nucleotide exchange on Arf1. Instead, Mon2 acts as a scaffold to recruit the Golgi-localised pool of Dop1 [].
Publication
First Author: Deitz SB
Year: 2000
Journal: Traffic
Title: Sec7p directs the transitions required for yeast Golgi biogenesis.
Volume: 1
Issue: 2
Pages: 172-83
Publication
First Author: Galindo A
Year: 2016
Journal: Cell Rep
Title: Structural Insights into Arl1-Mediated Targeting of the Arf-GEF BIG1 to the trans-Golgi.
Volume: 16
Issue: 3
Pages: 839-50
Protein Domain
Type: Domain
Description: This entry represents a HDS (homology downstream of Sec7) domain found towards the C-terminal of guanine nucleotide exchange factors involved Golgi transport, such as budding yeast protein Sec7, protein Mon2 and BIG1-like proteins [, ]. Sec7 is involved in the secretory pathway as a protein binding scaffold for the COPII-COPI protein switch for maturation of the VTC intermediate compartments for Golgi compartment biogenesis []. Sec7 has four conserved HDS1-4 domains which act to integrate the signals from several small GTPases, including Arf1 itself, to switch Sec7 from a strongly autoinhibited to a strongly auto activated form [].
Publication
First Author: Achstetter T
Year: 1988
Journal: J Biol Chem
Title: SEC7 encodes an unusual, high molecular weight protein required for membrane traffic from the yeast Golgi apparatus.
Volume: 263
Issue: 24
Pages: 11711-7
Publication    
First Author: Richardson BC
Year: 2016
Journal: Elife
Title: The Sec7 N-terminal regulatory domains facilitate membrane-proximal activation of the Arf1 GTPase.
Volume: 5
Protein
Organism: Mus musculus/domesticus
Length: 2170  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1709  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 747  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1846  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1792  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 817  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1054  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 794  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1803  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1861  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1050  
Fragment?: true
Publication
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
Publication
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
Publication
First Author: Church DM
Year: 2009
Journal: PLoS Biol
Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume: 7
Issue: 5
Pages: e1000112