Search results for GEM

Showing 18 results out of 28

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Interactor (2 results from a total of 2)

GEM

Identifier: P55040
Species: Homo sapiens
Primary external reference: UniProt: P55040
Identifier: A6NCL1
Species: Homo sapiens
Primary external reference: UniProt: A6NCL1

Protein (5 results from a total of 12)

Identifier: R-HSA-8932878
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: GEMIN8: Q9NWZ8
Identifier: R-HSA-8932892
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: Q9NWZ8
Identifier: R-HSA-191893
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: GEMIN7: Q9H840
Identifier: R-HSA-191835
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: GEMIN2: O14893
Identifier: R-HSA-191771
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: GEMIN6: Q8WXD5

Reaction (5 results from a total of 8)

Identifier: R-HSA-68712
Species: Homo sapiens
Compartment: cytosol
At the beginning of this reaction, 1 molecule of 'ubiquitin', and 1 molecule of 'Cdt1:geminin' are present. At the end of this reaction, 1 molecule of 'geminin:ubiquitin complex', and 1 molecule of 'Cdt1' are present.

This reaction takes place in the 'cytosol'.
Identifier: R-HSA-68825
Species: Homo sapiens
Compartment: cytosol
At the beginning of this reaction, 1 molecule of 'geminin:ubiquitin complex' is present. At the end of this reaction, 1 molecule of 'ubiquitin' is present.

This reaction takes place in the 'cytosol' and is mediated by the 'endopeptidase activity' of '26S proteasome'.
Identifier: R-HSA-69299
Species: Homo sapiens
Compartment: nucleoplasm
At the beginning of this reaction, 1 molecule of 'geminin', and 1 molecule of 'CDT1' are present. At the end of this reaction, 1 molecule of 'Cdt1:geminin' is present.

This reaction takes place in the 'nucleoplasm'.
Identifier: R-HSA-9613213
Species: Homo sapiens
Compartment: nucleoplasm
NAB2 is recruited to EGR2 to the RRAD promoter through interaction with the NCD1 (NAB conserved domain 1) (Svaren et al, 1996; Svaren et al, 1998). NAB2 in turn recruits the CHD4 subunit of the NURD chromatin remodelling complex through its CID (CHD4-interacting domain) and in this manner, represses transcription from the RRAD promoter (Srinivasan et al, 2006; Mager et al, 2008). In addition to roles in cellular proliferation and cardiac function, RRAD protein is known to contribute to RHO signaling, which promotes Schwann cell migration and myelination (Zhu et al, 1999; Wang et al, 2010; Chang et al, 2007, Ward et al, 2002; Yamauchi et al, 2004; Melendez-Vasquez et al, 2004).
Identifier: R-HSA-9613219
Species: Homo sapiens
Compartment: nucleoplasm, cytosol
RRAD (Ras associated with diabetes) is a small GTP-binding member of the RAS superfaily that was originally as being overexpressed in skeletal muscle of people with type II diabetes (Reynet and Kahn, 1993; Zhu et al, 1995). RRAD has roles in cardiac regulation, and contributes to glucose metabolism and tumor metastasis through interaction with NME1 (nucleoside diphosphate kinase A) (Chang et al, 2007; Wang et al, 2010; Zhu et al, 1999; Tseng et al, 2001). In addition, RRAD contributes to Schwann cell development and myelination by modulating the RHO ROCK pathway (Ward et al, 2002; Yamauchi et al, 2004; Melendez-Vasquez et al, 2004). RRAD gene expression is positively regulated upon binding of EGR1 or EGR2 to their cognate sites in the promoter, while EGR-dependent recruitment of NAB proteins leads to EGR-mediated repression through the recruitment of chromatin remodellers and histone deacetylase complexes (Svaren et al, 2000; Mager et al, 2008). RRAD expression is repressed in Schwann cells during myelination and is upregulated in NAB knockout mice, implicating NAB proteins as negative regulators of RRAD expression (Verheijen et al, 2003; Mager et al, 2008; Desmazières et al, 2008). It is worth noting, however, that a number of genes required for Schwann cell differentiation and myelination are activated by EGR:NAB complexes at their promoters (Le et al, 2005).

Complex (3 results from a total of 3)

Identifier: R-HSA-68537
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-68585
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-156502
Species: Homo sapiens
Compartment: nucleoplasm

Set (2 results from a total of 2)

Identifier: R-HSA-419057
Species: Homo sapiens
Compartment: cytosol
ROCK I (alternatively called ROK ?) and ROCK II (also known as Rho kinase or ROK ?) were originally isolated as RhoA-GTP interacting proteins. The kinase domains of ROCK I and ROCK II are 92% identical, and so far there is no evidence that they phosphorylate different substrates. RhoA, RhoB, and RhoC associate with and activate ROCK but other GTP-binding proteins can be inhibitors, e.g. RhoE, Rad and Gem. PDK1 kinase promotes ROCK I activity not through phosphorylation but by blocking RhoE association. PLK1 can phosphorylate ROCK II and this enhances the effect of RhoA. Arachidonic acid can activate ROCK independently of Rho.
Identifier: R-HSA-4687776
Species: Homo sapiens
Compartment: cytosol
ROCK I (alternatively called ROK ?) and ROCK II (also known as Rho kinase or ROK ?) were originally isolated as RhoA-GTP interacting proteins. The kinase domains of ROCK I and ROCK II are 92% identical, and so far there is no evidence that they phosphorylate different substrates. RhoA, RhoB, and RhoC associate with and activate ROCK but other GTP-binding proteins can be inhibitors, e.g. RhoE, Rad and Gem. PDK1 kinase promotes ROCK I activity not through phosphorylation but by blocking RhoE association. PLK1 can phosphorylate ROCK II and this enhances the effect of RhoA. Arachidonic acid can activate ROCK independently of Rho.

Icon (1 results from a total of 1)

Gem

Species: Homo sapiens
Curator: Kaiqiang You
Designer: Cristoffer Sevilla
Gem icon
Nuclear bodies frequently found near or associated with Cajal bodies (also called coiled bodies or CBs). Gemini of coiled bodies, or 'gems', are similar in size and shape to CBs, and often indistinguishable under the microscope. Unlike CBs, gems do not contain small nuclear ribonucleoproteins (snRNPs); they contain a protein called survivor of motor neurons (SMN) whose function relates to snRNP biogenesis. Gems are believed to assist CBs in snRNP biogenesis, and to play a role in the etiology of spinal muscular atrophy (SMA)
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