Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Expression and purification of enzymatically active forms of the human lysyl oxidase-like protein 4.
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Recombinant human LOXL4 is an active, BAPN-inhibitable amine oxidase against the nonpeptidyl substrate benzylamine.
"The purified LOXL4 proteins showed beta-aminopropionitrile-inhibitable activity of 0.022-0.032 units/mg toward a nonpeptidyl substrate, benzylamine."
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Human LOXL4 contains four SRCR domains in addition to conserved lysyl-oxidase-family catalytic features.
"LOXL4 contains four scavenger receptor cysteine-rich domains in addition to the characteristic domains of the LOX family, including the copper-binding domain, the cytokine receptor-like domain, and the residues of the lysyl-tyrosyl quinone cofactor."
Towards a proteome-scale map of the human protein-protein interaction network.
An empirical framework for binary interactome mapping.
Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).
Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins.
A Y2H-seq approach defines the human protein methyltransferase interactome.
Elastic fibres in health and disease.
A proteome-scale map of the human interactome network.
Architecture of the human interactome defines protein communities and disease networks.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Cloning and characterization of a fifth human lysyl oxidase isoenzyme: the third member of the lysyl oxidase-related subfamily with four scavenger receptor cysteine-rich domains.
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Human LOXL4 is a 756-residue secretory protein with a 24-residue signal peptide, a conserved C-terminal lysyl oxidase domain, and four N-terminal SRCR-like domains.
"The predicted polypeptide is 756 amino acids long, including a 24-residue signal peptide. The C-terminal region contains a LO domain similar to those of LOX, LOXL, LOXL2 and LOXL3. The N-terminal region has four subregions similar to scavenger receptor cysteine-rich domains that are highly conserved with LOXL2 and LOXL3."
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Recombinant human LOXL4 was secreted without evident proteolytic processing in the tested cell system.
"Recombinant LOXL4 expressed in HT-1080 cells was secreted into the culture medium with no evident proteolytic processing."
A novel human lysyl oxidase-like gene (LOXL4) on chromosome 10q24 has an altered scavenger receptor cysteine rich domain.
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Human LOXL4 has conserved catalytic-family features and four N-terminal SRCR domains, one containing a distinctive 13-residue insertion.
"The cDNA and derived amino acid sequence of LOXL4 demonstrates a conserved C-terminal region including the characteristic copper-binding site, lysyl and tyrosyl residues and a cytokine receptor-like domain. One of the four N-terminal SRCR domains contains a 13 amino acid insertion encoded by a short exon not present within the closely homologous LOXL2 and LOXL3 genes."
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LOXL4 transcript expression was reported in multiple human tissues and cell types, with strongest tested tissue signals in pancreas and testis.
"The 3.5-kb LOXL4 mRNA is present in pancreas and testis and at lower levels in several other tissues. Fibroblasts, smooth muscle and osteosarcoma (HOS) cells express LOXL4."
Molecular cloning and biological activity of a novel lysyl oxidase-related gene expressed in cartilage.
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Mouse LOXC, the murine LOXL4 ortholog, showed BAPN-sensitive activity toward chick type I and type II collagens in conditioned medium.
"The conditioned media of COS-7 cells transfected with the full-length LOXC cDNA showed the lysyl oxidase activity in both type I and type II collagens derived from chick embryos, and these activities of LOXC were inhibited by beta-aminopropionitrile, a specific inhibitor of lysyl oxidase."
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Mouse LOXC expression increases during chondrogenic differentiation and is localized to hypertrophic and calcified growth-plate chondrocytes in vivo.
"In vivo, LOXC gene expression was localized in hypertrophic and calcified chondrocytes of growth plates in adult mice."
UniProt text export for human LOXL4 (Q96JB6)
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The reviewed Q96JB6 sequence is a 756-residue precursor with a 24-residue signal peptide and no annotated propeptide feature.
"FT SIGNAL 1..24"
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UniProt localizes LOXL4 to the secreted extracellular space, but marks that statement as inferred rather than experimentally sourced.
"CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000305}."
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UniProt attributes collagen- and elastin-directed protein-lysine oxidation to PMID:14551188, although the cached abstract reports benzylamine rather than a peptidyl substrate.
"CC -!- FUNCTION: Catalyzes the oxidative deamination of lysine and CC hydroxylysine residues in collagen and elastin, resulting in the CC formation of covalent cross-linkages, and the stabilization of collagen CC and elastin fibers. {ECO:0000269|PubMed:14551188}."
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The reviewed sequence contains a predicted copper-binding residue in its lysyl-oxidase-like catalytic region.
"FT BINDING 611 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /evidence="ECO:0000255""