Search results for YLR157W-E

Showing 30 results out of 159

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Results (30 results from a total of 159)

e-

Identifier: R-ALL-879326
Compartment: cytosol
Primary external reference: ChEBI: electron: 10545

e-

Identifier: R-ALL-917828
Compartment: extracellular region
Primary external reference: ChEBI: electron: 10545

e-

Identifier: R-ALL-76342
Compartment: endoplasmic reticulum lumen
Primary external reference: ChEBI: electron: 10545
Identifier: R-ALL-4419987
Compartment: cytosol
Primary external reference: ChEBI: 2-trans,6-trans-farnesyl diphosphate(3-): 175763
Identifier: R-HSA-2326867
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-198912
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-198192
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-NUL-2534247
Species: Canis familiaris, Homo sapiens
Compartment: plasma membrane, cytosol
Caspase-3 (Steinhusen et al. 2001) and calpain-1 (Rios-Doria et al. 2003) cleave E-cadherin in its cytoplasmic part releasing an intracellular 37 kDa C-terminal fragment termed CTF3.
Identifier: R-NUL-2534209
Species: Mus musculus, Homo sapiens
Compartment: plasma membrane
E-cadherin is cleaved close to the transmembrane region by presenilin-1 (Marambaud et al. 2002), the catalytic subunit of gamma-secretase (Herreman et al. 2003, Li et al. 2003), producing a soluble fragment termed CTF2.
Identifier: R-HSA-199062
Species: Homo sapiens
Compartment: plasma membrane
After interaction with its ligand HLA-E, which is expressed on normal cells, the C-type lectin inhibitory receptor CD94/NKG2A suppresses activation signaling processes. CD94/NKG2A receptors continuously recycle from the cell surface through endosomal compartments and back again in a process that requires energy and the cytoskeleton. This steady state process appears to be largely unaffected by exposure to ligand.
Identifier: R-HSA-2534305
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-2534301
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-3827963
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-3828004
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-3828003
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-2870221
Species: Homo sapiens
Compartment: plasma membrane
E-selectin is an adhesion molecule on the cell surface of endothelial cells. It participates in the binding of leukocytes to activated blood vascular endothelium during inflammation or metastasis (Haraldsen G et al. 1996). Leucocytes express E-selectin ligand 1 (ESL-1) and P-selectin glycoprotein ligand-1 (PCGL-1) which were identified as the ligands for E-selectin (Graves BJ et al 1994; Asa D et al 1995). E-selectin has been also implicated in mediating tissue-specific homing primitive hematopoietic progenitor cells (HPCs) into bone marrow (BM). PCGL-1, CD43, CD44 were shown to function as E-selectin ligands on human BM cells (Dimitroff CJ et al. 2001; Katayama Y et al. 2003; Merzaban JS et al. 2011).
Identifier: R-HSA-2162192
Species: Homo sapiens
Compartment: mitochondrial inner membrane, mitochondrial matrix
4-Hydroxybenzoate polyprenyltransferase (COQ2) catalyses the combination of 4-hydroxybenzoic acid, aka para-hydroxybenzoic acid (PHB), with the polyisoprenoid tail all-trans-decaprenyl diphosphate (all-E-10PrP2) to form 3-decaprenyl-4-hydroxybenzoate (DHB) (Forsgren et al., 2004; Lopez-Martin ef al., 2007; Tekle et al., 2008).
Identifier: R-HSA-4755545
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane, cytosol
The ER membrane-associated enzyme dehydrodolichyl diphosphate synthase (DHDDS) (Endo et al. 2003) normally mediates the sequential head-to-tail cis addition of multiple isopentyl pyrophosphate (IPP) molecules to farnesyl pyrophosphate (E,E-FPP) to produce polyprenol pyrophosphate (pPPP) (Shridas et al. 2003). Dolichol in humans contain homologues ranging from 17-23 isoprene units, the most common homologues contain 19 or 20 isoprene units (Freeman et al. 1980). Dolichol is an important substrate in the N-glycosylation of proteins, including rhodopsin.

Defects in DHDDS cause retinitis pigmentosa 59 (RP59; MIM:613861), a pigment retinopathy, characterised by retinal pigment deposits (visible on fundus examination) and primary loss of rod photoreceptors followed by secondary loss of cone photoreceptors. Sufferers typically have night vision blindness and loss of mid to peripheral vision. As the condition progresses, they lose far peripheral vision and eventually central vision (Zuchner et al. 2011). The founder missense mutation K42E in Ashkenazi Jewish ethnicity can cause RP59. The Lys42 residue is highly conserved across different species and is positioned close to the catalytic centre of DHDDS and to its substrate binding site for E,E-FPP (Zuchner et al. 2011, Zelinger et al. 2011).
Identifier: R-HSA-3827958
Species: Homo sapiens
Compartment: plasma membrane
E-cadherin (CDH1) localizes to the lateral membrane of differentiated epithelia, providing the structural foundation for adherens junctions, multiprotein complexes that link cell-cell contacts to the actin cytoskeleton and various signaling molecules (Perez-Moreno et al. 2003, Baum & Georgiou 2011). The extracellular domain has five cadherin-type repeat ectodomain (EC) modules; the most membrane-distal EC mediates binding with CDH1 on adjacent cells (Boggon et al. 2002). Calcium ions bind between the EC domains of two CDH1 peptides to form a dimer with a rod-like conformation (Boggon et al. 2002) which is required for cell-cell interaction (Gumbiner 1996, Patel et al. 2006). The cytoplasmic tail of E-cadherin binds to the armadillo repeat protein beta-catenin, a target of the Wnt signaling pathway and a cofactor for TCF/LEF-mediated transcription (Gavard & Mège 2005). Beta-catenin in turn binds alpha-catenin, which interacts with the actin microfilament network, actin and the actin-binding proteins vinculin, formins, alpha-actinin, zonula occludin protein, and afadin (Bershadsky 2004). Cell–cell adhesions also contain desmosomes, which link cell contacts to intermediate filaments, and nectin-based, calcium-independent adhesions, which are linked to actin (Takai & Nakanishi 2003, Yin and Green 2004). The critical importance of E-cadherin to normal development and tissue function is demonstrated by embryonic lethal E-cadherin gene mouse knockouts (Larue et al. 1994). Loss of cadherin-based cell-cell adhesion is a hallmark of carcinogenesis, correlating with tumour progression, allowing cells to escape normal growth control signals, resulting in loss of differentiation and increased cell proliferation associated with invasive behaviour (Frixen et al. 1991, Capaldo & Macara 2007). Full-length 120-kDa CDH1 protein is cleaved in the ectodomain close to the plasma membrane by a number of metalloproteases, generating an extracellular 38-kDa C-terminal fragment (CTF) termed CTF1 which can be further processed by a gamma-secretase-like activity to a soluble 33-kDa CTF2 (Marambaud et al. 2002, Roy & Berx 2008). MMP3, MMP7 (Noë et al. 2001, canine MMPs), MMP9 (Symowicz et al. 2007), plasmin (Ryniers et al. 2002, canine plasmin), Kallikrien 7 (Johnson et al. 2007), ADAM10 (Maretzky et al. 2005) and ADAM15 (Najy et al. 2008) all cleave CDH1 extracellularly, close to the transmembrane region. Presenilin-1 (Marambaud et al. 2002), the catalytic subunit of gamma-secretase (Herreman et al. 2003, Li et al. 2003), cleaves CDH1 producing a soluble 33-kDa fragment termed CTF2. Other enzymes like caspase-3 (Steinhusen et al. 2001) and calpain-1 (Rios-Doria et al. 2003) cleave E-cadherin in its cytoplasmic part releasing an intracellular 37 kDa c-terminal fragment.
Identifier: R-HSA-4224014
Species: Homo sapiens
Compartment: plasma membrane
E-cadherin (CDH1) localizes to the lateral membrane of differentiated epithelia, providing the structural foundation for adherens junctions, multiprotein complexes that link cell-cell contacts to the actin cytoskeleton and various signaling molecules (Perez-Moreno et al. 2003, Baum & Georgiou 2011). The extracellular domain has five cadherin-type repeat ectodomain (EC) modules; the most membrane-distal EC mediates binding with CDH1 on adjacent cells (Boggon et al. 2002). Calcium ions cross-link the EC domains of two CDH1 peptides to form a dimer with a rod-like conformation (Boggon et al. 2002) which is required for cell-cell interaction (Gumbiner 1996, Patel et al. 2006). The cytoplasmic tail of E-cadherin binds to the armadillo repeat protein beta-catenin, a target of the Wnt signaling pathway and a cofactor for TCF/LEF-mediated transcription (Gavard & Mège 2005). Beta-catenin in turn binds alpha-catenin, which interacts with the actin microfilament network, actin and the actin-binding proteins vinculin, formins, alpha-actinin, zonula occludin protein, and afadin (Bershadsky 2004). Cell–cell adhesions also contain desmosomes, which link cell contacts to intermediate filaments, and nectin-based, calcium-independent adhesions, which are linked to actin (Takai & Nakanishi 2003, Yin and Green 2004). The critical importance of E-cadherin to normal development and tissue function is demonstrated by embryonic lethal E-cadherin gene mouse knockouts (Larue et al. 1994). Loss of cadherin-based cell-cell adhesion is a hallmark of carcinogenesis, correlating with tumour progression, allowing cells to escape normal growth control signals, resulting in loss of differentiation and increased cell proliferation associated with invasive behaviour (Frixen et al. 1991, Capaldo & Macara 2007).

Full-length 120-kDa CDH1 protein is cleaved in the ectodomain close to the plasma membrane by a number of metalloproteases, generating an extracellular 38-kDa C-terminal fragment (CTF) termed CTF1 which can be further processed by a gamma-secretase-like activity to a soluble 33-kDa CTF2 (Marambaud et al. 2002, Roy & Berx 2008). MMP3, MMP7 (Noë et al. 2001, canine MMPs), MMP9 (Symowicz et al. 2007), plasmin (Ryniers et al. 2002, canine plasmin), Kallikrien 7 (Johnson et al. 2007), ADAM10 (Maretzky et al. 2005) and ADAM15 (Najy et al. 2008) all cleave CDH1 extracellularly, close to the transmembrane region.

Presenilin-1 (Marambaud et al. 2002), the catalytic subunit of gamma-secretase (Herreman et al. 2003, Li et al. 2003), cleaves CDH1 producing a soluble 33-kDa fragment termed CTF2. Other enzymes like caspase-3 (Steinhusen et al. 2001) and calpain-1 (Rios-Doria et al. 2003) cleave E-cadherin in its cytoplasmic part releasing an intracellular 37 kDa c-terminal fragment.
Identifier: R-HSA-1454843
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
E-cadherin (CDH1) localizes to the lateral membrane of differentiated epithelia, providing the structural foundation for adherens junctions, multiprotein complexes that link cell-cell contacts to the actin cytoskeleton and various signaling molecules (Perez-Moreno et al. 2003, Baum & Georgiou 2011). The extracellular domain has five cadherin-type repeat ectodomain (EC) modules; the most membrane-distal EC mediates binding with CDH1 on adjacent cells (Boggon et al. 2002). Calcium ions bind between the EC domains of two CDH1 peptides to form a dimer with a rod-like conformation (Boggon et al. 2002) which is required for cell-cell interaction (Gumbiner 1996, Patel et al. 2006). The cytoplasmic tail of E-cadherin binds to the armadillo repeat protein beta-catenin, a target of the Wnt signaling pathway and a cofactor for TCF/LEF-mediated transcription (Gavard & Mège 2005). Beta-catenin in turn binds alpha-catenin, which interacts with the actin microfilament network, actin and the actin-binding proteins vinculin, formins, alpha-actinin, zonula occludin protein, and afadin (Bershadsky 2004). Cell–cell adhesions also contain desmosomes, which link cell contacts to intermediate filaments, and nectin-based, calcium-independent adhesions, which are linked to actin (Takai & Nakanishi 2003, Yin and Green 2004). The critical importance of E-cadherin to normal development and tissue function is demonstrated by embryonic lethal E-cadherin gene mouse knockouts (Larue et al. 1994). Loss of cadherin-based cell-cell adhesion is a hallmark of carcinogenesis, correlating with tumour progression, allowing cells to escape normal growth control signals, resulting in loss of differentiation and increased cell proliferation associated with invasive behaviour (Frixen et al. 1991, Capaldo & Macara 2007). Full-length 120-kDa CDH1 protein is cleaved in the ectodomain close to the plasma membrane by a number of metalloproteases, generating an extracellular 38-kDa C-terminal fragment (CTF) termed CTF1 which can be further processed by a gamma-secretase-like activity to a soluble 33-kDa CTF2 (Marambaud et al. 2002, Roy & Berx 2008). MMP3, MMP7 (Noë et al. 2001, canine MMPs), MMP9 (Symowicz et al. 2007), plasmin (Ryniers et al. 2002, canine plasmin), Kallikrien 7 (Johnson et al. 2007), ADAM10 (Maretzky et al. 2005) and ADAM15 (Najy et al. 2008) all cleave CDH1 extracellularly, close to the transmembrane region. Presenilin-1 (Marambaud et al. 2002), the catalytic subunit of gamma-secretase (Herreman et al. 2003, Li et al. 2003), cleaves CDH1 producing a soluble 33-kDa fragment termed CTF2. Other enzymes like caspase-3 (Steinhusen et al. 2001) and calpain-1 (Rios-Doria et al. 2003) cleave E-cadherin in its cytoplasmic part releasing an intracellular 37 kDa C-terminal fragment.
Identifier: R-NUL-2534162
Species: Canis familiaris, Homo sapiens
Compartment: plasma membrane, extracellular region
Full-length 120-kDa CDH1 protein is cleaved in the ectodomain close to the plasma membrane by a number of metalloproteases, generating an extracellular 38-kDa C-terminal fragment (CTF) termed CTF1 which can be further processed by a gamma-secretase-like activity to a soluble 33-kDa CTF2 (Marambaud et al. 2002, Roy & Berx 2008). MMP3, MMP7 (Noë et al. 2001) and plasmin (Ryniers et al. 2002), all cleave dog CDH1 extracellularly, close to the transmembrane region.
Identifier: R-MMU-573311
Species: Mus musculus
Compartment: nucleoplasm
Primary external reference: UniProt: H2bc21: Q64524
Identifier: R-DME-212298
Species: Drosophila melanogaster
Compartment: nucleoplasm
Primary external reference: UniProt: P42124
Identifier: R-BTA-198912
Species: Bos taurus
Compartment: plasma membrane
This complex/polymer has been computationally inferred (based on PANTHER) from a complex/polymer involved in an event that has been demonstrated in another species.
Identifier: R-RNO-198912
Species: Rattus norvegicus
Compartment: plasma membrane
This complex/polymer has been computationally inferred (based on PANTHER) from a complex/polymer involved in an event that has been demonstrated in another species.
Identifier: R-CFA-198912
Species: Canis familiaris
Compartment: plasma membrane
This complex/polymer has been computationally inferred (based on PANTHER) from a complex/polymer involved in an event that has been demonstrated in another species.
Identifier: R-DRE-198912
Species: Danio rerio
Compartment: plasma membrane
This complex/polymer has been computationally inferred (based on PANTHER) from a complex/polymer involved in an event that has been demonstrated in another species.
Identifier: R-SSC-198912
Species: Sus scrofa
Compartment: plasma membrane
This complex/polymer has been computationally inferred (based on PANTHER) from a complex/polymer involved in an event that has been demonstrated in another species.
Identifier: R-GGA-198912
Species: Gallus gallus
Compartment: plasma membrane
This complex/polymer has been computationally inferred (based on PANTHER) from a complex/polymer involved in an event that has been demonstrated in another species.
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