Human Metabolome Database: Showing Protein Lysyl oxidase homolog 2 (HMDBP08250)

Identification Biological properties Gene properties Protein properties External links References XML Show 7 metabolites

Identification

HMDB Protein ID

HMDBP08250

Secondary Accession Numbers

13962

Name

Lysyl oxidase homolog 2

Synonyms

Lysyl oxidase-like protein 2
Lysyl oxidase-related protein 2
Lysyl oxidase-related protein WS9-14

Gene Name

LOXL2

Protein Type

Unknown

Biological Properties

General Function

Involved in copper ion binding

Specific Function

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.

Pathways

Not Available

Reactions

Peptidyl-L-lysyl-peptide + Oxygen + Water → peptidyl-allysyl-peptide + Ammonia + Hydrogen peroxide

details

GO Classification

Biological Process
sprouting angiogenesis
transcription, DNA-dependent
cell adhesion
aging
response to hypoxia
negative regulation of transcription, DNA-dependent
collagen fibril organization
endothelial cell migration
endothelial cell proliferation
epithelial to mesenchymal transition
histone modification
positive regulation of chondrocyte differentiation
protein deamination
Cellular Component
basement membrane
chromosome
membrane
extracellular space
nucleus
Component
cell part
membrane
Function
cation binding
ion binding
copper ion binding
oxidoreductase activity, acting on the ch-nh2 group of donors, oxygen as acceptor
oxidoreductase activity, acting on the ch-nh2 group of donors
scavenger receptor activity
transmembrane receptor activity
receptor activity
metal ion binding
binding
oxidoreductase activity
catalytic activity
signal transducer activity
transition metal ion binding
molecular transducer activity
Molecular Function
methylated histone residue binding
protein-lysine 6-oxidase activity
scavenger receptor activity
transcription corepressor activity
electron carrier activity
chromatin binding
copper ion binding
Process
metabolic process
oxidation reduction

Cellular Location

Secreted
extracellular space (Potential)

Gene Properties

Chromosome Location

Locus

8p21.3

SNPs

LOXL2

Gene Sequence

>2325 bp
ATGGAGAGGCCTCTGTGCTCCCACCTCTGCAGCTGCCTGGCTATGCTGGCCCTCCTGTCC
CCCCTGAGCCTGGCACAGTATGACAGCTGGCCCCATTACCCCGAGTACTTCCAGCAACCG
GCTCCTGAGTATCACCAGCCCCAGGCCCCCGCCAACGTGGCCAAGATTCAGCTGCGCCTG
GCTGGGCAGAAGAGGAAGCACAGCGAGGGCCGGGTGGAGGTGTACTATGATGGCCAGTGG
GGCACCGTGTGCGATGACGACTTCTCCATCCACGCTGCCCACGTCGTCTGCCGGGAGCTG
GGCTACGTGGAGGCCAAGTCCTGGACTGCCAGCTCCTCCTACGGCAAGGGAGAAGGGCCC
ATCTGGTTAGACAATCTCCACTGTACTGGCAACGAGGCGACCCTTGCAGCATGCACCTCC
AATGGCTGGGGCGTCACTGACTGCAAGCACACGGAGGATGTCGGTGTGGTGTGCAGCGAC
AAAAGGATTCCTGGGTTCAAATTTGACAATTCGTTGATCAACCAGATAGAGAACCTGAAT
ATCCAGGTGGAGGACATTCGGATTCGAGCCATCCTCTCAACCTACCGCAAGCGCACCCCA
GTGATGGAGGGCTACGTGGAGGTGAAGGAGGGCAAGACCTGGAAGCAGATCTGTGACAAG
CACTGGACGGCCAAGAATTCCCGCGTGGTCTGCGGCATGTTTGGCTTCCCTGGGGAGAGG
ACATACAATACCAAAGTGTACAAAATGTTTGCCTCACGGAGGAAGCAGCGCTACTGGCCA
TTCTCCATGGACTGCACCGGCACAGAGGCCCACATCTCCAGCTGCAAGCTGGGCCCCCAG
GTGTCACTGGACCCCATGAAGAATGTCACCTGCGAGAATGGGCTACCGGCCGTGGTGAGT
TGTGTGCCTGGGCAGGTCTTCAGCCCTGACGGACCCTCAAGATTCCGGAAAGCGTACAAG
CCAGAGCAACCCCTGGTGCGACTGAGAGGCGGTGCCTACATCGGGGAGGGCCGCGTGGAG
GTGCTCAAAAATGGAGAATGGGGGACCGTCTGCGACGACAAGTGGGACCTGGTGTCGGCC
AGTGTGGTCTGCAGAGAGCTGGGCTTTGGGAGTGCCAAAGAGGCAGTCACTGGCTCCCGA
CTGGGGCAAGGGATCGGACCCATCCACCTCAACGAGATCCAGTGCACAGGCAATGAGAAG
TCCATTATAGACTGCAAGTTCAATGCCGAGTCTCAGGGCTGCAACCACGAGGAGGATGCT
GGTGTGAGATGCAACACCCCTGCCATGGGCTTGCAGAAGAAGCTGCGCCTGAACGGCGGC
CGCAATCCCTACGAGGGCCGAGTGGAGGTGCTGGTGGAGAGAAACGGGTCCCTTGTGTGG
GGGATGGTGTGTGGCCAAAACTGGGGCATCGTGGAGGCCATGGTGGTCTGCCGCCAGCTG
GGCCTGGGATTCGCCAGCAACGCCTTCCAGGAGACCTGGTATTGGCACGGAGATGTCAAC
AGCAACAAAGTGGTCATGAGTGGAGTGAAGTGCTCGGGAACGGAGCTGTCCCTGGCGCAC
TGCCGCCACGACGGGGAGGACGTGGCCTGCCCCCAGGGCGGAGTGCAGTACGGGGCCGGA
GTTGCCTGCTCAGAAACCGCCCCTGACCTGGTCCTCAATGCGGAGATGGTGCAGCAGACC
ACCTACCTGGAGGACCGGCCCATGTTCATGCTGCAGTGTGCCATGGAGGAGAACTGCCTC
TCGGCCTCAGCCGCGCAGACCGACCCCACCACGGGCTACCGCCGGCTCCTGCGCTTCTCC
TCCCAGATCCACAACAATGGCCAGTCCGACTTCCGGCCCAAGAACGGCCGCCACGCGTGG
ATCTGGCACGACTGTCACAGGCACTACCACAGCATGGAGGTGTTCACCCACTATGACCTG
CTGAACCTCAATGGCACCAAGGTGGCAGAGGGCCACAAGGCCAGCTTCTGCTTGGAGGAC
ACAGAATGTGAAGGAGACATCCAGAAGAATTACGAGTGTGCCAACTTCGGCGATCAGGGC
ATCACCATGGGCTGCTGGGACATGTACCGCCATGACATCGACTGCCAGTGGGTTGACATC
ACTGACGTGCCCCCTGGAGACTACCTGTTCCAGGTTGTTATTAACCCCAACTTCGAGGTT
GCAGAATCCGATTACTCCAACAACATCATGAAATGCAGGAGCCGCTATGACGGCCACCGC
ATCTGGATGTACAACTGCCACATAGGTGGTTCCTTCAGCGAAGAGACGGAAAAAAAGTTT
GAGCACTTCAGCGGGCTCTTAAACAACCAGCTGTCCCCGCAGTAA

Protein Properties

Number of Residues

774

Molecular Weight

86724.305

Theoretical pI

6.38

Pfam Domain Function

Lysyl_oxidase (PF01186 )
SRCR; (PF00530 )

Signals

Not Available

Transmembrane Regions

Not Available

Protein Sequence

>Lysyl oxidase homolog 2
MERPLCSHLCSCLAMLALLSPLSLAQYDSWPHYPEYFQQPAPEYHQPQAPANVAKIQLRL
AGQKRKHSEGRVEVYYDGQWGTVCDDDFSIHAAHVVCRELGYVEAKSWTASSSYGKGEGP
IWLDNLHCTGNEATLAACTSNGWGVTDCKHTEDVGVVCSDKRIPGFKFDNSLINQIENLN
IQVEDIRIRAILSTYRKRTPVMEGYVEVKEGKTWKQICDKHWTAKNSRVVCGMFGFPGER
TYNTKVYKMFASRRKQRYWPFSMDCTGTEAHISSCKLGPQVSLDPMKNVTCENGLPAVVS
CVPGQVFSPDGPSRFRKAYKPEQPLVRLRGGAYIGEGRVEVLKNGEWGTVCDDKWDLVSA
SVVCRELGFGSAKEAVTGSRLGQGIGPIHLNEIQCTGNEKSIIDCKFNAESQGCNHEEDA
GVRCNTPAMGLQKKLRLNGGRNPYEGRVEVLVERNGSLVWGMVCGQNWGIVEAMVVCRQL
GLGFASNAFQETWYWHGDVNSNKVVMSGVKCSGTELSLAHCRHDGEDVACPQGGVQYGAG
VACSETAPDLVLNAEMVQQTTYLEDRPMFMLQCAMEENCLSASAAQTDPTTGYRRLLRFS
SQIHNNGQSDFRPKNGRHAWIWHDCHRHYHSMEVFTHYDLLNLNGTKVAEGHKASFCLED
TECEGDIQKNYECANFGDQGITMGCWDMYRHDIDCQWVDITDVPPGDYLFQVVINPNFEV
AESDYSNNIMKCRSRYDGHRIWMYNCHIGGSFSEETEKKFEHFSGLLNNQLSPQ

External Links

GenBank ID Protein

4505011

UniProtKB/Swiss-Prot ID

Q9Y4K0

UniProtKB/Swiss-Prot Entry Name

LOXL2_HUMAN

PDB IDs

Not Available

GenBank Gene ID

GeneCard ID

GenAtlas ID

HGNC ID

References

General References

Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
Saito H, Papaconstantinou J, Sato H, Goldstein S: Regulation of a novel gene encoding a lysyl oxidase-related protein in cellular adhesion and senescence. J Biol Chem. 1997 Mar 28;272(13):8157-60. [PubMed:9079631 ]
Jourdan-Le Saux C, Tronecker H, Bogic L, Bryant-Greenwood GD, Boyd CD, Csiszar K: The LOXL2 gene encodes a new lysyl oxidase-like protein and is expressed at high levels in reproductive tissues. J Biol Chem. 1999 Apr 30;274(18):12939-44. [PubMed:10212285 ]