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P28300

- LYOX_HUMAN

UniProt

P28300 - LYOX_HUMAN

Protein

Protein-lysine 6-oxidase

Gene

LOX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (01 Oct 1993)
      Previous versions | rss
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    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 – 2921CopperSequence Analysis
    Metal bindingi294 – 2941CopperSequence Analysis
    Metal bindingi296 – 2961CopperSequence Analysis

    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

    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

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30427.

    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

    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.
    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 146 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