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P28300

- LYOX_HUMAN

UniProt

P28300 - LYOX_HUMAN

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Protein
Protein-lysine 6-oxidase
Gene
LOX
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Copper.
Contains 1 lysine tyrosylquinone By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi292 – 2921Copper Reviewed prediction
Metal bindingi294 – 2941Copper Reviewed prediction
Metal bindingi296 – 2961Copper Reviewed prediction

GO - Molecular functioni

  1. copper ion binding Source: ProtInc
  2. protein binding Source: IntAct
  3. protein-lysine 6-oxidase activity Source: ProtInc

GO - Biological processi

  1. blood vessel development Source: Ensembl
  2. cellular protein modification process Source: ProtInc
  3. collagen fibril organization Source: Ensembl
  4. elastic fiber assembly Source: Ensembl
  5. extracellular matrix organization Source: Reactome
  6. lung development Source: Ensembl
  7. response to drug Source: Ensembl
  8. response to steroid hormone Source: Ensembl
  9. wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

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: Chromosome 5

Organism-specific databases

HGNCiHGNC:6664. LOX.

Subcellular locationi

GO - Cellular componenti

  1. collagen trimer Source: Ensembl
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProtKB-SubCell
  4. nucleus Source: Ensembl
  5. proteinaceous extracellular matrix Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30427.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Propeptidei22 – 168147 By similarity
PRO_0000018520Add
BLAST
Chaini169 – 417249Protein-lysine 6-oxidase
PRO_0000018521Add
BLAST

Amino acid modifications

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

ArrayExpressiP28300.
BgeeiP28300.
CleanExiHS_LOX.
GenevestigatoriP28300.

Organism-specific databases

HPAiHPA053389.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi110199. 9 interactions.
DIPiDIP-49007N.
IntActiP28300. 12 interactions.
STRINGi9606.ENSP00000231004.

Structurei

3D structure databases

ProteinModelPortaliP28300.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the lysyl oxidase family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG69196.
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

MRFAWTVLLL GPLQLCALVH CAPPAAGQQQ PPREPPAAPG AWRQQIQWEN    50
NGQVFSLLSL GSQYQPQRRR DPGAAVPGAA NASAQQPRTP ILLIRDNRTA 100
AARTRTAGSS GVTAGRPRPT ARHWFQAGYS TSRAREAGAS RAENQTAPGE 150
VPALSNLRPP SRVDGMVGDD PYNPYKYSDD NPYYNYYDTY ERPRPGGRYR 200
PGYGTGYFQY GLPDLVADPY YIQASTYVQK MSMYNLRCAA EENCLASTAY 250
RADVRDYDHR VLLRFPQRVK NQGTSDFLPS RPRYSWEWHS CHQHYHSMDE 300
FSHYDLLDAN TQRRVAEGHK ASFCLEDTSC DYGYHRRFAC TAHTQGLSPG 350
CYDTYGADID CQWIDITDVK PGNYILKVSV NPSYLVPESD YTNNVVRCDI 400
RYTGHHAYAS GCTISPY 417
Length:417
Mass (Da):46,944
Last modified:October 1, 1993 - v2
Checksum:i6412A78443E03F04
GO

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301Q → H1 Publication
Sequence conflicti31 – 311P → A1 Publication
Sequence conflicti95 – 951R → A1 Publication
Sequence conflicti102 – 1021A → G in AAB21243. 1 Publication
Sequence conflicti137 – 1371A → R in AAA59525. 1 Publication
Sequence conflicti137 – 1371A → R in AAB23549. 1 Publication
Sequence conflicti139 – 1391A → P in AAB21243. 1 Publication
Sequence conflicti304 – 3052YD → LY in AAB21243. 1 Publication
Sequence conflicti315 – 3151V → W in AAB21243. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4129.1.
PIRi A47529. OXHUL.
RefSeqi NP_002308.2. NM_002317.5.
UniGenei Hs.102267.

3D structure databases

ProteinModelPortali P28300.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110199. 9 interactions.
DIPi DIP-49007N.
IntActi P28300. 12 interactions.
STRINGi 9606.ENSP00000231004.

Chemistry

BindingDBi P28300.
ChEMBLi CHEMBL2249.

PTM databases

PhosphoSitei P28300.

Proteomic databases

MaxQBi P28300.
PaxDbi P28300.
PeptideAtlasi P28300.
PRIDEi P28300.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000231004 ; ENSP00000231004 ; ENSG00000113083 .
GeneIDi 4015.
KEGGi hsa:4015.
UCSCi uc003ksu.3. human.

Organism-specific databases

CTDi 4015.
GeneCardsi GC05M121429.
HGNCi HGNC:6664. LOX.
HPAi HPA053389.
MIMi 153455. gene.
neXtProti NX_P28300.
PharmGKBi PA30427.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG69196.
HOGENOMi HOG000234262.
HOVERGENi HBG000226.
InParanoidi P28300.
KOi K00277.
OMAi YSDDNPY.
OrthoDBi EOG7SN8C6.
PhylomeDBi P28300.
TreeFami TF326061.

Enzyme and pathway databases

Reactomei REACT_150206. Crosslinking of collagen fibrils.
REACT_150366. Elastic fibre formation.

Miscellaneous databases

ChiTaRSi LOX. human.
GeneWikii Lysyl_oxidase.
GenomeRNAii 4015.
NextBioi 15752.
PMAP-CutDB P28300.
PROi P28300.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28300.
Bgeei P28300.
CleanExi HS_LOX.
Genevestigatori P28300.

Family and domain databases

InterProi IPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
[Graphical view ]
Pfami PF01186. Lysyl_oxidase. 1 hit.
[Graphical view ]
PRINTSi PR00074. LYSYLOXIDASE.
PROSITEi PS00926. LYSYL_OXIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 145 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

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