Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Angio-associated migratory cell protein is expressed as an extracellular protein by blood-vessel-associated mesenchymal cells.
Blockade of angio-associated migratory cell protein inhibits smooth muscle cell migration and neointima formation in accelerated atherosclerosis.
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AAMP overexpression increases smooth muscle cell migration while anti-AAMP antibody and siRNA decrease it; antibody blockade also reduces neointimal SMC density and neointima formation in apoE-null mice.
"The AAMP overexpression increases, while both treatment with anti-rAAMP-ab and transfection with siRNA decreases SMC migration."
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AAMP knockdown reduces RhoA activity specifically in the membrane fraction of smooth muscle cells, linking AAMP to Rho signalling.
"Knockdown of AAMP decreases RhoA activity in the membrane fraction of SMCs."
Architecture of the human interactome defines protein communities and disease networks.
An interactome perturbation framework prioritizes damaging missense mutations for developmental disorders.
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Identification of a new immunoglobulin superfamily protein expressed in blood vessels with a heparin-binding consensus sequence.
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The AAMP-derived peptide P189 contains a heparin-binding domain with a dissociation constant of 14 pmol and mediates heparin-sensitive cell adhesion.
"The AAMP-derived peptide, P189, contains a heparin-binding domain (dissociation constant, 14 pmol) and mediates heparin-sensitive cell adhesion."
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AAMP contains immunoglobulin-like domains, the WD40 repeat motif and a heparin-binding consensus sequence, and is expressed in endothelial cells, trophoblasts and tumour cells.
"It contains immunoglobulin-like domains [one with multiple homologies to deleted in colon carcinoma (DCC) protein], the WD40 repeat motif, and a heparin-binding consensus sequence."
AAMP Regulates Endothelial Cell Migration and Angiogenesis Through RhoA/Rho Kinase Signaling.
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RhoA/Rho-kinase signalling mediates AAMP's control of endothelial cell migration and angiogenesis; AAMP knockdown reduced VEGF-induced actin stress fibres and collagen gel contraction, and knockdown or antibody blockade impaired VEGF-induced tube formation and aortic ring sprouting.
"Furthermore, we identified RhoA/Rho kinase signaling as an important factor that contributes to the action of AAMP in regulating endothelial cell migration and angiogenesis."
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VEGF upregulates AAMP expression and recruits AAMP to cell membrane protrusions.
"Moreover, VEGF recruited AAMP to the cell membrane protrusions."
AAMP promotes colorectal cancermetastasis by suppressing SMURF2-mediatedubiquitination and degradation of RhoA.
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AAMP binds RhoA and suppresses its SMURF2-mediated ubiquitination and degradation, stabilising RhoA and raising the level of active RhoA.
"AAMP stabilized RhoA by binding to it and suppressing its SMURF2-mediated ubiquitination and degradation."
Angio-associated migratory cell protein (AAMP) interacts with cell division cycle 42 (CDC42) and enhances migration and invasion in human non-small cell lung cancer cells.
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AAMP interacts with CDC42 and promotes its activation, resulting in formation of cellular protrusions and enhanced migration and invasion.
"AAMP interacted with cell division cycle 42 (CDC42) and promoted its activation, resulting in the formation of cellular protrusions."
A function for AAMP in Nod2-mediated NF-kappaB activation.
AAMP, a conserved protein with immunoglobulin and WD40 domains, regulates endothelial tube formation in vitro.
AAMP gene expression is positively regulated by VEGF
AAMP and MTSS1 Are Novel Negative Regulators of Endothelial Barrier Function Identified in a Proteomics Screen.
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siRNA depletion of AAMP significantly increases trans-endothelial electrical resistance, identifying AAMP as a negative regulator of endothelial barrier function.
"these data identify AAMP and MTSS1 as novel negative regulators of endothelial barrier function"
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AAMP controls the activity and the stability of both RhoA and RhoB - independent corroboration, in a different cell type and for a second Rho GTPase, of the SMURF2/RhoA mechanism reported in colorectal cancer cells.
"Mechanistically, AAMP controls both RhoA and RhoB activity and stability."
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In a confluent endothelial monolayer, ectopically expressed AAMP localised to nucleus and cytosol but not to the plasma membrane, a caveat on the constitutive nature of the surface pool.
"AAMP expression in the nucleus and cytosol; however, AAMP was not localized at the plasma membrane"
Affinage mechanistic annotation for AAMP (human)
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Machine-fetched Affinage record (trust gates passed) describing AAMP as a WD40- and immunoglobulin-domain protein acting as a positive regulator of Rho-family GTPases and the actin cytoskeleton, with the CDC42 activation mechanism attributed to impeding the ARHGAP1-CDC42 interaction.
"binds CDC42 to promote its activation by impeding the ARHGAP1–CDC42 interaction"