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LOXL2

lysyl oxidase-like 2

Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). When secreted in extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. When nuclear, acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin, probably by mediating deamination of histone H3. Also involved in E-cadherin repression following hypoxia, a hallmark of epithelial to mesenchymal transition believed to amplify tumor aggressiveness, suggesting that it may play a role in tumor progression. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation.

Gene Name: lysyl oxidase-like 2
Synonyms: LOXL2, Lysyl oxidase-like protein 2, Lysyl oxidase related 2, Lysyl oxidase-like 2, WS9-14, LOR2, Lysyl oxidase homolog 2
Target Sequences: NM_002318 NP_002309.1 Q9Y4K0

Publications (1)

1
B lymphocytes directly contribute to tissue fibrosis in patients with IgG4-related disease. Emanuel Della-Torre, Elena Rigamonti, Cory Perugino, Simona Baghai-Sain, Na Sun, Naoki Kaneko, Takashi Maehara, Lucrezia Rovati, Maurilio Ponzoni, Raffaella Milani, Marco Lanzillotta, Vinay Mahajan, Hamid Mattoo, Ivan Molineris, Vikram Deshpande, John H Stone, Massimo Falconi, Angelo A Manfredi, Shiv Pillai. The Journal of allergy and clinical immunology. 2019 Mar;145:968-981e14. [Full Text Article] [PubMed:31319101] [PMC:PMC6960365] Related Antibodies: LS-A9350.

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The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).