Lysyl oxidase

LOX
Identifiers
Aliases	LOX, entrez:4015
External IDs	OMIM: 153455 MGI: 96817 HomoloGene: 1741 GeneCards: LOX
Gene ontology Molecular function • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor • metal ion binding • protein binding • oxidoreductase activity • copper ion binding • protein-lysine 6-oxidase activity Cellular component • collagen trimer • proteinaceous extracellular matrix • nucleus • extracellular region • extracellular space Biological process • collagen fibril organization • lung development • response to steroid hormone • extracellular matrix organization • wound healing • aorta development • heart development • cellular protein modification process • blood vessel development • response to hormone • elastic fiber assembly • oxidation-reduction process • response to drug • blood vessel morphogenesis Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4015	16948
Ensembl	ENSG00000113083	ENSMUSG00000024529
UniProt	P28300	P28301
RefSeq (mRNA)	NM_002317 NM_001178102 NM_001317073	NM_010728 NM_001286181 NM_001286182
RefSeq (protein)	NP_001171573 NP_001304002 NP_002308	NP_001273110.1 NP_001273111.1 NP_034858.2 NP_001273110 NP_001273111 NP_034858
Location (UCSC)	Chr 5: 122.06 – 122.08 Mb	Chr 18: 52.52 – 52.53 Mb
PubMed search

protein-lysine 6-oxidase
Lox mechanism
Identifiers
EC number	1.4.3.13
CAS number	99676-44-5
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

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PMC	articles
PubMed	articles
NCBI	proteins

4015

16948

ENSG00000113083

ENSMUSG00000024529

P28300

P28301

NM_002317
NM_001178102
NM_001317073

NM_010728
NM_001286181
NM_001286182

NP_001171573
NP_001304002
NP_002308

NP_034858

Lysyl oxidase (LOX), also known as protein-lysine 6-oxidase, is a protein that, in humans, is encoded by the LOX gene. Its inhibition can cause osteolathyrism, but, at the same time, its upregulation by tumor cells may promote metastasis of the existing tumor, causing it to become malignant and cancerous.

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