Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P28300 (LYOX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein-lysine 6-oxidase

EC=1.4.3.13
Alternative name(s):
Lysyl oxidase
Gene names
Name:LOX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. In addition to cross-linking of extracellular matrix proteins, may have a direct role in tumor suppression.

Catalytic activity

Peptidyl-L-lysyl-peptide + O2 + H2O = peptidyl-allysyl-peptide + NH3 + H2O2.

Cofactor

Copper.

Contains 1 lysine tyrosylquinone By similarity.

Subcellular location

Secretedextracellular space.

Tissue specificity

Heart, placenta, skeletal muscle, kidney, lung and pancreas. Ref.3

Post-translational modification

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.

Proteolytically activated by BMP1 By similarity.

Miscellaneous

The propeptide plays a role in directing the deposition of this enzyme to elastic fibers, via interaction with tropoelastin By similarity.

Sequence similarities

Belongs to the lysyl oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 168147 By similarity
PRO_0000018520
Chain169 – 417249Protein-lysine 6-oxidase
PRO_0000018521

Regions

Region213 – 417205Lysyl-oxidase like

Sites

Metal binding2921Copper Potential
Metal binding2941Copper Potential
Metal binding2961Copper Potential

Amino acid modifications

Modified residue35512',4',5'-topaquinone By similarity
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation1441N-linked (GlcNAc...) Potential
Disulfide bond238 ↔ 244 By similarity
Disulfide bond291 ↔ 340 By similarity
Disulfide bond324 ↔ 330 By similarity
Disulfide bond351 ↔ 361 By similarity
Disulfide bond398 ↔ 412 By similarity
Cross-link320 ↔ 355Lysine tyrosylquinone (Lys-Tyr) By similarity

Natural variations

Natural variant1581R → Q. Ref.5 Ref.9
Corresponds to variant rs1800449 [ dbSNP | Ensembl ].
VAR_004282

Experimental info

Sequence conflict301Q → H Ref.3
Sequence conflict311P → A Ref.3
Sequence conflict951R → A Ref.3
Sequence conflict1021A → G in AAB21243. Ref.1
Sequence conflict1371A → R in AAA59525. Ref.2
Sequence conflict1371A → R in AAB23549. Ref.2
Sequence conflict1391A → P in AAB21243. Ref.1
Sequence conflict304 – 3052YD → LY in AAB21243. Ref.1
Sequence conflict3151V → W in AAB21243. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P28300 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 6412A78443E03F04

FASTA41746,944
        10         20         30         40         50         60 
MRFAWTVLLL GPLQLCALVH CAPPAAGQQQ PPREPPAAPG AWRQQIQWEN NGQVFSLLSL 

        70         80         90        100        110        120 
GSQYQPQRRR DPGAAVPGAA NASAQQPRTP ILLIRDNRTA AARTRTAGSS GVTAGRPRPT 

       130        140        150        160        170        180 
ARHWFQAGYS TSRAREAGAS RAENQTAPGE VPALSNLRPP SRVDGMVGDD PYNPYKYSDD 

       190        200        210        220        230        240 
NPYYNYYDTY ERPRPGGRYR PGYGTGYFQY GLPDLVADPY YIQASTYVQK MSMYNLRCAA 

       250        260        270        280        290        300 
EENCLASTAY RADVRDYDHR VLLRFPQRVK NQGTSDFLPS RPRYSWEWHS CHQHYHSMDE 

       310        320        330        340        350        360 
FSHYDLLDAN TQRRVAEGHK ASFCLEDTSC DYGYHRRFAC TAHTQGLSPG CYDTYGADID 

       370        380        390        400        410 
CQWIDITDVK PGNYILKVSV NPSYLVPESD YTNNVVRCDI RYTGHHAYAS GCTISPY 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of human lysyl oxidase and assignment of the gene to chromosome 5q23.3-31.2."
Haemaelaeinen E.-R., Jones T.A., Sheer D., Taskinen K., Pihlajaniemi T., Kivirikko K.I.
Genomics 11:508-516(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The complete derived amino acid sequence of human lysyl oxidase and assignment of the gene to chromosome 5 (extensive sequence homology with the murine ras recision gene)."
Mariani T.J., Trackman P.C., Kagan H.M., Eddy R.L., Shows T.B., Boyd C.D., Deak S.B.
Matrix 12:242-248(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skin.
[3]"A new gene with sequence and structural similarity to the gene encoding human lysyl oxidase."
Kim Y., Boyd C.D., Csiszar K.
J. Biol. Chem. 270:7176-7182(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[4]"Epigenetic inhibition of lysyl oxidase transcription after transformation by ras oncogene."
Contente S., Kenyon K., Sriraman P., Subramanyan S., Friedman R.M.
Mol. Cell. Biochem. 194:79-91(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-158.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[7]"Structure of the human lysyl oxidase gene."
Haemaelaeinen E.-R., Kemppainen R., Pihlajaniemi T., Kivirikko K.I.
Genomics 17:544-548(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-213.
[8]"Characterization of the human lysyl oxidase gene locus."
Svinarich D.M., Twomey T.A., Macauley S.P., Krebs C.J., Yang T.P., Krawetz S.A.
J. Biol. Chem. 267:14382-14387(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 55-216.
Tissue: Blood.
[9]"A restriction fragment length polymorphism results in a nonconservative amino acid substitution encoded within the first exon of the human lysyl oxidase gene."
Csiszar K., Mariani T.J., Gosin J.S., Deak S.B., Boyd C.D.
Genomics 16:401-406(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-158.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S78694 mRNA. Translation: AAB21243.1.
M94054 mRNA. Translation: AAA59525.1.
S45875 mRNA. Translation: AAB23549.1.
AF039291 mRNA. Translation: AAD02130.1.
AK312269 mRNA. Translation: BAG35200.1.
BC074820 mRNA. Translation: AAH74820.1.
BC074872 mRNA. Translation: AAH74872.1.
BC089436 mRNA. Translation: AAH89436.1.
L16895 Genomic DNA. Translation: AAA16870.1.
M84150 Genomic DNA. Translation: AAA59541.1.
PIROXHUL. A47529.
RefSeqNP_002308.2. NM_002317.5.
UniGeneHs.102267.

3D structure databases

ProteinModelPortalP28300.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110199. 9 interactions.
DIPDIP-49007N.
IntActP28300. 11 interactions.
STRING9606.ENSP00000231004.

Chemistry

BindingDBP28300.
ChEMBLCHEMBL2249.

PTM databases

PhosphoSiteP28300.

Proteomic databases

PaxDbP28300.
PeptideAtlasP28300.
PRIDEP28300.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000231004; ENSP00000231004; ENSG00000113083.
GeneID4015.
KEGGhsa:4015.
UCSCuc003ksu.3. human.

Organism-specific databases

CTD4015.
GeneCardsGC05M121429.
HGNCHGNC:6664. LOX.
HPAHPA053389.
MIM153455. gene.
neXtProtNX_P28300.
PharmGKBPA30427.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69196.
HOGENOMHOG000234262.
HOVERGENHBG000226.
InParanoidP28300.
KOK00277.
OMAYSDDNPY.
OrthoDBEOG7SN8C6.
PhylomeDBP28300.
TreeFamTF326061.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP28300.
BgeeP28300.
CleanExHS_LOX.
GenevestigatorP28300.

Family and domain databases

InterProIPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
[Graphical view]
PfamPF01186. Lysyl_oxidase. 1 hit.
[Graphical view]
PRINTSPR00074. LYSYLOXIDASE.
PROSITEPS00926. LYSYL_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLOX. human.
GeneWikiLysyl_oxidase.
GenomeRNAi4015.
NextBio15752.
PMAP-CutDBP28300.
PROP28300.
SOURCESearch...

Entry information

Entry nameLYOX_HUMAN
AccessionPrimary (citable) accession number: P28300
Secondary accession number(s): B2R5Q3, Q5FWF0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM