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Lysyl oxidase homolog 2 (house mouse)

Protein
Encoding Gene
Dates
  • Create:
    2017-04-15
  • Modify:
    2025-01-17
Description
A lysyl oxidase homolog 2 that is encoded in the genome of mouse.
Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (By similarity). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (By similarity). Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (By similarity). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (By similarity). LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2 (PMID: 25959397). 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 (By similarity). During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription (By similarity). SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits (By similarity). Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction (By similarity). When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (By similarity). Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding (By similarity). Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (PMID: 21071451).

1 Names and Identifiers

1.1 Synonyms

  • Lysyl oxidase homolog 2
  • EC 1.4.3.13
  • Lysyl oxidase-like protein 2

1.2 Other Identifiers

1.2.1 RefSeq Accession

1.2.2 UniProt ID

1.2.3 Enzyme Commission (EC) Number

1.2.4 PRO ID

1.2.5 ChEMBL Target ID

1.2.6 NCBI Proteins

1.2.7 GlyCosmos Protein

1.2.8 STRING Protein ID

1.2.9 Wikidata

1.2.10 IntAct Protein

1.2.11 InterPro Protein

3 Chemicals and Bioactivities

3.1 Tested Compounds

4 BioAssays

5 Sequence

>sp|P58022|LOXL2_MOUSE Lysyl oxidase homolog 2 (Run BLAST)

MELHFGSCLSGCLALLVLLPSLSLAQYEGWPYQLQYPEYFQQPAPEHHQRQVPSDVVKIQVRLAGQKRKHNEGRVEVYYEGQWGTVCDDDFSIHAAHVVCRQVGYVEAKSWAASSSYGPGEGPIWLDNIYCTGKESTLASCSSNGWGVTDCKHTEDVGVVCSEKRIPGFKFDNSLINQIESLNIQVEDIRIRPILSAFRHRKPVTEGYVEVKEGKAWKQICNKHWTAKNSHVVCGMFGFPAEKTYNPKAYKTFASRRKLRYWKFSMNCTGTEAHISSCKLGPSVTRDPVKNATCENGQPAVVSCVPSQIFSPDGPSRFRKAYKPEQPLVRLRGGAQVGEGRVEVLKNGEWGTICDDKWDLVSASVVCRELGFGTAKEAITGSRLGQGIGPIHLNEVQCTGTEKSIIDCKFNTESQGCNHEEDAGVRCNIPIMGFQKKVRLNGGRNPYEGRVEVLTERNGSLVWGTVCGQNWGIVEAMVVCRQLGLGFASNAFQETWYWHGNIFANNVVMSGVKCSGTELSLAHCRHDEEVACPEGGVRFGAGVACSETAPDLVLNAEIVQQTAYLEDRPMSLLQCAMEENCLSASAVHTDPTRGHRRLLRFSSQIHNNGQSDFRPKNGRHAWIWHDCHRHYHSMEVFTYYDLLSLNGTKVAEGHKASFCLEDTECEGDIQKSYECANFGEQGITMGCWDMYRHDIDCQWIDITDVPPGDYLFQVVINPNYEVPESDFSNNIMKCRSRYDGYRIWMYNCHVGGAFSEETEQKFEHFSGLLNNQLSVQ

6 3D Structures

6.1 AlphaFold Structures

Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605

7 Domains

7.1 CDD Domains

7.2 InterPro Domains

8 Interactions and Pathways

8.1 Interactions

9 Biochemical Reactions

10 Literature

10.1 Consolidated References

11 Patents

12 Classification

12.1 ChEMBL Target Tree

12.2 Enzyme Classification

13 Information Sources

  1. NCBI Protein
    LICENSE
    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. BioGRID
    LICENSE
    The MIT License (MIT); Copyright Mike Tyers Lab
    https://wiki.thebiogrid.org/doku.php/terms_and_conditions
  4. STRING: functional protein association networks
  5. ChEMBL
    LICENSE
    Access to the web interface of ChEMBL is made under the EBI's Terms of Use (http://www.ebi.ac.uk/Information/termsofuse.html). The ChEMBL data is made available on a Creative Commons Attribution-Share Alike 3.0 Unported License (http://creativecommons.org/licenses/by-sa/3.0/).
    http://www.ebi.ac.uk/Information/termsofuse.html
  6. GlyCosmos Glycoscience Portal
    LICENSE
    All copyrightable parts of the datasets in GlyCosmos are under the Creative Commons Attribution (CC BY 4.0) License.
    https://glycosmos.org/license
  7. IntAct Molecular Interaction Database
    LICENSE
    Creative Commons Attribution 4.0 International (CC BY 4.0) License
    https://www.ebi.ac.uk/intact/about#license_privacy
  8. InterPro
    LICENSE
    All of the InterPro, Pfam, PRINTS and SFLD downloadable data provided on the InterPro website is freely available under CC0 1.0 Universal (CC0 1.0) Public Domain Dedication.
    https://www.ebi.ac.uk/interpro/about/license/
  9. NCBI Conserved Domains (CDD)
    LICENSE
    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  10. Protein Ontology
    LICENSE
    PRO is distributed under the Creative Commons CC-BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).
  11. UniProt
    LICENSE
    We have chosen to apply the Creative Commons Attribution (CC BY 4.0, http://creativecommons.org/licenses/by/4.0/) License to all copyrightable parts of our databases.
    https://www.uniprot.org/help/license
  12. Wikidata
  13. Swiss Institute of Bioinformatics ENZYME
    LICENSE
    Copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution (CC BY 4.0) License (https://creativecommons.org/licenses/by/4.0/).
    https://enzyme.expasy.org/enzyme.get
    Enzyme Classification
    https://enzyme.expasy.org/
  14. AlphaFold DB
    LICENSE
    All of the data provided is freely available for both academic and commercial use under Creative Commons Attribution 4.0 (CC-BY 4.0) licence terms.
    https://alphafold.ebi.ac.uk/faq
  15. Rhea - annotated reactions database
    LICENSE
    Rhea has chosen to apply the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/). This means that you are free to copy, distribute, display and make commercial use of the database in all legislations, provided you credit (cite) Rhea.
    https://www.rhea-db.org/help/license-disclaimer
CONTENTS