LOXL2
entrez
4017
canonical
uniprot
Q9Y4K0
canonical
ensembl
ENSG00000134013
resolver
ensp
ENSP00000373783
resolver
ensp
ENSP00000549631
resolver
ensp
ENSP00000549633
resolver
ensp
ENSP00000549635
resolver
ensp
ENSP00000594188
resolver
ensp
ENSP00000639439
resolver
ensp
ENSP00000639440
resolver
enst
ENST00000389131
resolver
enst
ENST00000879572
resolver
enst
ENST00000879574
resolver
enst
ENST00000879576
resolver
enst
ENST00000924129
resolver
enst
ENST00000969380
resolver
enst
ENST00000969381
resolver
genesymbol
LOXL2
resolver
hgnc
HGNC:6666
resolver
uniprot
B2R5Q0
resolver
uniprot
Q53HV3
resolver
uniprot
Q9BW70
resolver
uniprot
Q9Y5Y8
resolver
uniprot_entry
LOXL2_HUMAN
resolver
uniprot_sec
B2R5Q0
resolver
uniprot_sec
Q53HV3
resolver
uniprot_sec
Q9BW70
resolver
uniprot_sec
Q9Y5Y8
resolver
activity_regulation
ACTIVITY REGULATION: According to some reports, it is inhibited by beta-aminopropionitrile (BAPN) (PubMed:20439985, PubMed:23319596). According to another report, it is not inhibited by beta-aminopropionitrile (BAPN) (PubMed:20306300). Specifically inhibited by a mouse monoclonal antibody AB0023, inhibition occurs in a non-competitive manner. {ECO:0000269|PubMed:20306300, ECO:0000269|PubMed:20439985, ECO:0000269|PubMed:20818376, ECO:0000269|PubMed:23319596}.
uniprot
proteins
amino_acid_sequence
MERPLCSHLCSCLAMLALLSPLSLAQYDSWPHYPEYFQQPAPEYHQPQAPANVAKIQLRLAGQKRKHSEGRVEVYYDGQWGTVCDDDFSIHAAHVVCRELGYVEAKSWTASSSYGKGEGPIWLDNLHCTGNEATLAACTSNGWGVTDCKHTEDVGVVCSDKRIPGFKFDNSLINQIENLNIQVEDIRIRAILSTYRKRTPVMEGYVEVKEGKTWKQICDKHWTAKNSRVVCGMFGFPGERTYNTKVYKMFASRRKQRYWPFSMDCTGTEAHISSCKLGPQVSLDPMKNVTCENGLPAVVSCVPGQVFSPDGPSRFRKAYKPEQPLVRLRGGAYIGEGRVEVLKNGEWGTVCDDKWDLVSASVVCRELGFGSAKEAVTGSRLGQGIGPIHLNEIQCTGNEKSIIDCKFNAESQGCNHEEDAGVRCNTPAMGLQKKLRLNGGRNPYEGRVEVLVERNGSLVWGMVCGQNWGIVEAMVVCRQLGLGFASNAFQETWYWHGDVNSNKVVMSGVKCSGTELSLAHCRHDGEDVACPQGGVQYGAGVACSETAPDLVLNAEMVQQTTYLEDRPMFMLQCAMEENCLSASAAQTDPTTGYRRLLRFSSQIHNNGQSDFRPKNGRHAWIWHDCHRHYHSMEVFTHYDLLNLNGTKVAEGHKASFCLEDTECEGDIQKNYECANFGDQGITMGCWDMYRHDIDCQWVDITDVPPGDYLFQVVINPNFEVAESDYSNNIMKCRSRYDGHRIWMYNCHIGGSFSEETEKKFEHFSGLLNNQLSPQ
uniprot
proteins
ec_number
1.4.3.13
uniprot
proteins
function
FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (PubMed:27735137). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (PubMed:27735137). 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) (PubMed:27735137). 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 (PubMed:25959397). LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2 (By similarity). Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin CDH1, probably by mediating deamination of histone H3 (PubMed:16096638, PubMed:24414204, PubMed:27735137). During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription (PubMed:24239292). 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 (PubMed:24239292). 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 (PubMed:28332555). Involved in E-cadherin repression following hypoxia, a hallmark of EMT believed to amplify tumor aggressiveness, suggesting that it may play a role in tumor progression (PubMed:20026874). 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 (PubMed:20306300). Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding (PubMed:21835952). Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (By similarity). {ECO:0000250|UniProtKB:P58022, ECO:0000269|PubMed:16096638, ECO:0000269|PubMed:20026874, ECO:0000269|PubMed:20306300, ECO:0000269|PubMed:21835952, ECO:0000269|PubMed:24239292, ECO:0000269|PubMed:24414204, ECO:0000269|PubMed:25959397, ECO:0000269|PubMed:27735137}.
uniprot
proteins
mass_dalton
86725
uniprot
proteins
mutagenesis
MUTAGEN 455; /note="N->Q: Inhibits secretion."; /evidence="ECO:0000269|PubMed:23319596"; MUTAGEN 626..628; /note="HRH->ARA: Abolishes oxidase activity and oxidation of trimethylated 'Lys-4' of histone H3 but does not affect secretion, interaction with SNAI1, binding to the CDH1 promoter, repression of CDH1 transcription or ability to induce EMT."; /evidence="ECO:0000269|PubMed:24414204, ECO:0000269|PubMed:27735137"; MUTAGEN 626; /note="H->A: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:29581294"; MUTAGEN 628; /note="H->A: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:29581294"; MUTAGEN 630; /note="H->A: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:29581294"; MUTAGEN 644; /note="N->Q: Inhibits secretion."; /evidence="ECO:0000269|PubMed:23319596"; MUTAGEN 653; /note="K->A: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:29581294"; MUTAGEN 689; /note="Y->A: Loss of enzyme activity."; /evidence="ECO:0000269|PubMed:29581294"; MUTAGEN 689; /note="Y->F: Does not affect ability to inhibit keratinocyte differentiation."; /evidence="ECO:0000269|PubMed:22157764
uniprot
proteins
post_translational_modification
PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000269|PubMed:23319596, ECO:0000269|PubMed:29581294}.; PTM: N-glycosylated. N-glycosylation on Asn-455 and Asn-644 may be essential for proper folding and secretion; may be composed of a fucosylated carbohydrates attached to a trimannose N-linked glycan core. {ECO:0000269|PubMed:23319596}.
uniprot
proteins
protein_family
Lysyl oxidase family
uniprot
proteins
pubmed
10212285
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16096638
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
20026874
uniprot
proteins
pubmed
20306300
uniprot
proteins
pubmed
20439985
uniprot
proteins
pubmed
20818376
uniprot
proteins
pubmed
21233336
uniprot
proteins
pubmed
21732535
uniprot
proteins
pubmed
21835952
uniprot
proteins
pubmed
22157764
uniprot
proteins
pubmed
22204712
uniprot
proteins
pubmed
22483618
uniprot
proteins
pubmed
23319596
uniprot
proteins
pubmed
24239292
uniprot
proteins
pubmed
24414204
uniprot
proteins
pubmed
25959397
uniprot
proteins
pubmed
27339457
uniprot
proteins
pubmed
27392148
uniprot
proteins
pubmed
27735137
uniprot
proteins
pubmed
28332555
uniprot
proteins
pubmed
29581294
uniprot
proteins
pubmed
9079631
uniprot
proteins
sequence_length
774
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:23319596}. Nucleus {ECO:0000269|PubMed:22204712, ECO:0000269|PubMed:24414204}. Chromosome {ECO:0000269|PubMed:27735137}. Endoplasmic reticulum {ECO:0000269|PubMed:28332555}. Note=Associated with chromatin (PubMed:27735137). It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted (PubMed:23319596). However, a number of reports confirm its intracellular location and its key role in transcription regulation (PubMed:22204712, PubMed:22483618). {ECO:0000269|PubMed:22204712, ECO:0000269|PubMed:23319596, ECO:0000269|PubMed:24414204, ECO:0000269|PubMed:27735137}.
uniprot
proteins