Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein-lysine 6-oxidase

Gene

LOX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi292 – 2921CopperSequence Analysis
Metal bindingi294 – 2941CopperSequence Analysis
Metal bindingi296 – 2961CopperSequence Analysis

GO - Molecular functioni

  • copper ion binding Source: ProtInc
  • protein-lysine 6-oxidase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BRENDAi1.4.3.13. 2681.
ReactomeiREACT_150206. Crosslinking of collagen fibrils.
REACT_150366. Elastic fibre formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-lysine 6-oxidase (EC:1.4.3.13)
Alternative name(s):
Lysyl oxidase
Gene namesi
Name:LOX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:6664. LOX.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30427.

Polymorphism and mutation databases

BioMutaiLOX.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 168147By similarityPRO_0000018520Add
BLAST
Chaini169 – 417249Protein-lysine 6-oxidasePRO_0000018521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi238 ↔ 244By similarity
Disulfide bondi291 ↔ 340By similarity
Cross-linki320 ↔ 355Lysine tyrosylquinone (Lys-Tyr)By similarity
Disulfide bondi324 ↔ 330By similarity
Disulfide bondi351 ↔ 361By similarity
Modified residuei355 – 35512',4',5'-topaquinoneBy similarity
Disulfide bondi398 ↔ 412By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, LTQ, TPQ

Proteomic databases

MaxQBiP28300.
PaxDbiP28300.
PeptideAtlasiP28300.
PRIDEiP28300.

PTM databases

PhosphoSiteiP28300.

Miscellaneous databases

PMAP-CutDBP28300.

Expressioni

Tissue specificityi

Heart, placenta, skeletal muscle, kidney, lung and pancreas.1 Publication

Gene expression databases

BgeeiP28300.
CleanExiHS_LOX.
ExpressionAtlasiP28300. baseline and differential.
GenevisibleiP28300. HS.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
EFEMP2O959674EBI-3893481,EBI-743414
ELNP155022EBI-3893481,EBI-1222108
FBLN5Q9UBX52EBI-3893481,EBI-947897
FBN1P355552EBI-3893481,EBI-2505934
PTPRKQ152624EBI-3893481,EBI-474052

Protein-protein interaction databases

BioGridi110199. 10 interactions.
DIPiDIP-49007N.
IntActiP28300. 18 interactions.
STRINGi9606.ENSP00000231004.

Structurei

3D structure databases

ProteinModelPortaliP28300.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni213 – 417205Lysyl-oxidase likeAdd
BLAST

Sequence similaritiesi

Belongs to the lysyl oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG69196.
GeneTreeiENSGT00760000119251.
HOGENOMiHOG000234262.
HOVERGENiHBG000226.
InParanoidiP28300.
KOiK00277.
OMAiYSDDNPY.
OrthoDBiEOG7SN8C6.
PhylomeDBiP28300.
TreeFamiTF326061.

Family and domain databases

InterProiIPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
[Graphical view]
PfamiPF01186. Lysyl_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00074. LYSYLOXIDASE.
PROSITEiPS00926. LYSYL_OXIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28300-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFAWTVLLL GPLQLCALVH CAPPAAGQQQ PPREPPAAPG AWRQQIQWEN
60 70 80 90 100
NGQVFSLLSL GSQYQPQRRR DPGAAVPGAA NASAQQPRTP ILLIRDNRTA
110 120 130 140 150
AARTRTAGSS GVTAGRPRPT ARHWFQAGYS TSRAREAGAS RAENQTAPGE
160 170 180 190 200
VPALSNLRPP SRVDGMVGDD PYNPYKYSDD NPYYNYYDTY ERPRPGGRYR
210 220 230 240 250
PGYGTGYFQY GLPDLVADPY YIQASTYVQK MSMYNLRCAA EENCLASTAY
260 270 280 290 300
RADVRDYDHR VLLRFPQRVK NQGTSDFLPS RPRYSWEWHS CHQHYHSMDE
310 320 330 340 350
FSHYDLLDAN TQRRVAEGHK ASFCLEDTSC DYGYHRRFAC TAHTQGLSPG
360 370 380 390 400
CYDTYGADID CQWIDITDVK PGNYILKVSV NPSYLVPESD YTNNVVRCDI
410
RYTGHHAYAS GCTISPY
Length:417
Mass (Da):46,944
Last modified:October 1, 1993 - v2
Checksum:i6412A78443E03F04
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301Q → H (PubMed:7706256).Curated
Sequence conflicti31 – 311P → A (PubMed:7706256).Curated
Sequence conflicti95 – 951R → A (PubMed:7706256).Curated
Sequence conflicti102 – 1021A → G in AAB21243 (PubMed:1685472).Curated
Sequence conflicti137 – 1371A → R in AAA59525 (PubMed:1357535).Curated
Sequence conflicti137 – 1371A → R in AAB23549 (PubMed:1357535).Curated
Sequence conflicti139 – 1391A → P in AAB21243 (PubMed:1685472).Curated
Sequence conflicti304 – 3052YD → LY in AAB21243 (PubMed:1685472).Curated
Sequence conflicti315 – 3151V → W in AAB21243 (PubMed:1685472).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti158 – 1581R → Q.2 Publications
Corresponds to variant rs1800449 [ dbSNP | Ensembl ].
VAR_004282

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4129.1.
PIRiA47529. OXHUL.
RefSeqiNP_002308.2. NM_002317.5.
UniGeneiHs.102267.

Genome annotation databases

EnsembliENST00000231004; ENSP00000231004; ENSG00000113083.
GeneIDi4015.
KEGGihsa:4015.
UCSCiuc003ksu.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4129.1.
PIRiA47529. OXHUL.
RefSeqiNP_002308.2. NM_002317.5.
UniGeneiHs.102267.

3D structure databases

ProteinModelPortaliP28300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110199. 10 interactions.
DIPiDIP-49007N.
IntActiP28300. 18 interactions.
STRINGi9606.ENSP00000231004.

Chemistry

BindingDBiP28300.
ChEMBLiCHEMBL2249.

PTM databases

PhosphoSiteiP28300.

Polymorphism and mutation databases

BioMutaiLOX.

Proteomic databases

MaxQBiP28300.
PaxDbiP28300.
PeptideAtlasiP28300.
PRIDEiP28300.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000231004; ENSP00000231004; ENSG00000113083.
GeneIDi4015.
KEGGihsa:4015.
UCSCiuc003ksu.3. human.

Organism-specific databases

CTDi4015.
GeneCardsiGC05M121429.
HGNCiHGNC:6664. LOX.
MIMi153455. gene.
neXtProtiNX_P28300.
PharmGKBiPA30427.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG69196.
GeneTreeiENSGT00760000119251.
HOGENOMiHOG000234262.
HOVERGENiHBG000226.
InParanoidiP28300.
KOiK00277.
OMAiYSDDNPY.
OrthoDBiEOG7SN8C6.
PhylomeDBiP28300.
TreeFamiTF326061.

Enzyme and pathway databases

BRENDAi1.4.3.13. 2681.
ReactomeiREACT_150206. Crosslinking of collagen fibrils.
REACT_150366. Elastic fibre formation.

Miscellaneous databases

ChiTaRSiLOX. human.
GeneWikiiLysyl_oxidase.
GenomeRNAii4015.
NextBioi15752.
PMAP-CutDBP28300.
PROiP28300.
SOURCEiSearch...

Gene expression databases

BgeeiP28300.
CleanExiHS_LOX.
ExpressionAtlasiP28300. baseline and differential.
GenevisibleiP28300. HS.

Family and domain databases

InterProiIPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
[Graphical view]
PfamiPF01186. Lysyl_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00074. LYSYLOXIDASE.
PROSITEiPS00926. LYSYL_OXIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiLYOX_HUMAN
AccessioniPrimary (citable) accession number: P28300
Secondary accession number(s): B2R5Q3, Q5FWF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 1, 1993
Last modified: June 24, 2015
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.