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Q9Y4K0

- LOXL2_HUMAN

UniProt

Q9Y4K0 - LOXL2_HUMAN

Protein

Lysyl oxidase homolog 2

Gene

LOXL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    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.6 Publications

    Catalytic activityi

    Peptidyl-L-lysyl-peptide + O2 + H2O = peptidyl-allysyl-peptide + NH3 + H2O2.3 Publications

    Cofactori

    Copper.By similarity
    Contains 1 lysine tyrosylquinone.By similarity

    Enzyme regulationi

    According to some reports, it is inhibited by beta-aminopropionitrile (BAPN) (PubMed:20439985 and PubMed:23319596). According to another report, it is not inhibited by beta-aminopropionitrile (BAPN) (PubMed:20306300). Specifically inhibited by a mouse monoclonal antibody AB0023, inhibition occurs in a non-competitive manner.4 Publications

    Kineticsi

    kcat is 2.04 min(-1) with tropoelastin as substrate (without the first three SRCR domains). kcat is 0.62 min(-1) with tropoelastin as substrate (without all four SRCR domains).

    1. KM=1.01 mM for 1,5-diaminopentane2 Publications
    2. KM=1.05 mM for spermine2 Publications
    3. KM=0.59 µM for tropoelastin (without the first three SRCR domains)2 Publications
    4. KM=0.62 µM for tropoelastin (without all four SRCR domains)2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi626 – 6261CopperSequence Analysis
    Metal bindingi628 – 6281CopperSequence Analysis
    Metal bindingi630 – 6301CopperSequence Analysis

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. copper ion binding Source: InterPro
    3. electron carrier activity Source: UniProtKB
    4. methylated histone binding Source: UniProtKB
    5. oligosaccharide binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein-lysine 6-oxidase activity Source: UniProtKB
    8. scavenger receptor activity Source: InterPro
    9. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. aging Source: ProtInc
    2. cell adhesion Source: ProtInc
    3. cellular protein modification process Source: UniProtKB
    4. collagen fibril organization Source: UniProtKB
    5. endothelial cell migration Source: UniProtKB
    6. endothelial cell proliferation Source: UniProtKB
    7. epithelial to mesenchymal transition Source: UniProtKB
    8. histone modification Source: UniProtKB
    9. negative regulation of transcription, DNA-templated Source: UniProtKB
    10. oxidation-reduction process Source: UniProtKB
    11. positive regulation of chondrocyte differentiation Source: UniProtKB
    12. protein deamination Source: UniProtKB
    13. response to copper ion Source: UniProtKB
    14. response to hypoxia Source: UniProtKB
    15. sprouting angiogenesis Source: UniProtKB
    16. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Oxidoreductase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    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:
    Lysyl oxidase homolog 2 (EC:1.4.3.13)
    Alternative name(s):
    Lysyl oxidase-like protein 2
    Lysyl oxidase-related protein 2
    Lysyl oxidase-related protein WS9-14
    Gene namesi
    Name:LOXL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:6666. LOXL2.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrixbasement membrane By similarity. Nucleus. Chromosome
    Note: Associated with chromatin. It is unclear how LOXL2 is nuclear: it contains a clear signal sequence and is predicted to localize in the extracellular medium. However, different reports confirmed the intracellular location and its key role in transcription regulation.

    GO - Cellular componenti

    1. basement membrane Source: UniProtKB
    2. chromosome Source: UniProtKB-SubCell
    3. extracellular space Source: UniProtKB
    4. membrane Source: InterPro
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Basement membrane, Chromosome, Extracellular matrix, Nucleus, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi455 – 4551N → Q: Inhibits secretion. 2 Publications
    Mutagenesisi626 – 6283HRH → ARA: Loss of catalytic activity and abolishes ability to repress transcription. 1 Publication
    Mutagenesisi644 – 6441N → Q: Inhibits secretion. 2 Publications
    Mutagenesisi689 – 6891Y → F: Does not affect ability to inhibit keratinocyte differentiation. 2 Publications

    Organism-specific databases

    PharmGKBiPA30429.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 774749Lysyl oxidase homolog 2PRO_0000018532Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi84 ↔ 148PROSITE-ProRule annotation
    Disulfide bondi97 ↔ 158PROSITE-ProRule annotation
    Disulfide bondi128 ↔ 138PROSITE-ProRule annotation
    Disulfide bondi218 ↔ 291PROSITE-ProRule annotation
    Disulfide bondi231 ↔ 301PROSITE-ProRule annotation
    Disulfide bondi265 ↔ 275PROSITE-ProRule annotation
    Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi351 ↔ 414PROSITE-ProRule annotation
    Disulfide bondi364 ↔ 424PROSITE-ProRule annotation
    Disulfide bondi395 ↔ 405PROSITE-ProRule annotation
    Glycosylationi455 – 4551N-linked (GlcNAc...) (complex)1 Publication
    Disulfide bondi464 ↔ 530PROSITE-ProRule annotation
    Disulfide bondi477 ↔ 543PROSITE-ProRule annotation
    Disulfide bondi511 ↔ 521PROSITE-ProRule annotation
    Disulfide bondi573 ↔ 579PROSITE-ProRule annotation
    Disulfide bondi625 ↔ 673PROSITE-ProRule annotation
    Glycosylationi644 – 6441N-linked (GlcNAc...) (complex)1 Publication
    Cross-linki653 ↔ 689Lysine tyrosylquinone (Lys-Tyr)
    Disulfide bondi657 ↔ 663PROSITE-ProRule annotation
    Disulfide bondi685 ↔ 695PROSITE-ProRule annotation
    Modified residuei689 – 68912',4',5'-topaquinoneBy similarity
    Disulfide bondi732 ↔ 746PROSITE-ProRule annotation

    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.
    N-glycosylated. N-glycosylation on Asn-455 and Asn-644 may be essential for proper folding and secretion; may be composed of a fucosylated carbohydrates attached to a trimannose N-linked glycan core.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, LTQ, TPQ

    Proteomic databases

    MaxQBiQ9Y4K0.
    PaxDbiQ9Y4K0.
    PRIDEiQ9Y4K0.

    PTM databases

    PhosphoSiteiQ9Y4K0.

    Expressioni

    Tissue specificityi

    Expressed in many tissues. Highest expression in reproductive tissues, placenta, uterus and prostate. Up-regulated in a number of cancers cells and tissues.

    Inductioni

    Strongly induced in hypoxia. Direct transcriptional target of HIF1A.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y4K0.
    BgeeiQ9Y4K0.
    CleanExiHS_LOXL2.
    GenevestigatoriQ9Y4K0.

    Organism-specific databases

    HPAiCAB025848.
    HPA036257.
    HPA056542.

    Interactioni

    Subunit structurei

    Component of some chromatin repressor complex. Interacts with SNAI1.1 Publication

    Protein-protein interaction databases

    BioGridi110201. 2 interactions.
    IntActiQ9Y4K0. 2 interactions.
    MINTiMINT-4053647.
    STRINGi9606.ENSP00000373783.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y4K0.
    SMRiQ9Y4K0. Positions 68-159, 326-424, 435-525.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 159102SRCR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini188 – 302115SRCR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini326 – 425100SRCR 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini435 – 544110SRCR 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni548 – 751204Lysyl-oxidase likeAdd
    BLAST

    Domaini

    The fourth SRCR domain plays a important role in optimizing the catalytic activity of the lysyl-oxidase like (LOX) catalytic domain.

    Sequence similaritiesi

    Belongs to the lysyl oxidase family.Curated
    Contains 4 SRCR domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG40770.
    HOGENOMiHOG000220841.
    HOVERGENiHBG052336.
    InParanoidiQ9Y4K0.
    KOiK00280.
    OMAiHFSGLIN.
    OrthoDBiEOG7SN8C6.
    PhylomeDBiQ9Y4K0.
    TreeFamiTF326061.

    Family and domain databases

    Gene3Di3.10.250.10. 4 hits.
    InterProiIPR001695. Lysyl_oxidase.
    IPR019828. Lysyl_oxidase_CS.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    [Graphical view]
    PfamiPF01186. Lysyl_oxidase. 1 hit.
    PF00530. SRCR. 4 hits.
    [Graphical view]
    PRINTSiPR00074. LYSYLOXIDASE.
    PR00258. SPERACTRCPTR.
    SMARTiSM00202. SR. 4 hits.
    [Graphical view]
    SUPFAMiSSF56487. SSF56487. 4 hits.
    PROSITEiPS00926. LYSYL_OXIDASE. 1 hit.
    PS00420. SRCR_1. 2 hits.
    PS50287. SRCR_2. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9Y4K0-1 [UniParc]FASTAAdd to Basket

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    MERPLCSHLC SCLAMLALLS PLSLAQYDSW PHYPEYFQQP APEYHQPQAP    50
    ANVAKIQLRL AGQKRKHSEG RVEVYYDGQW GTVCDDDFSI HAAHVVCREL 100
    GYVEAKSWTA SSSYGKGEGP IWLDNLHCTG NEATLAACTS NGWGVTDCKH 150
    TEDVGVVCSD KRIPGFKFDN SLINQIENLN IQVEDIRIRA ILSTYRKRTP 200
    VMEGYVEVKE GKTWKQICDK HWTAKNSRVV CGMFGFPGER TYNTKVYKMF 250
    ASRRKQRYWP FSMDCTGTEA HISSCKLGPQ VSLDPMKNVT CENGLPAVVS 300
    CVPGQVFSPD GPSRFRKAYK PEQPLVRLRG GAYIGEGRVE VLKNGEWGTV 350
    CDDKWDLVSA SVVCRELGFG SAKEAVTGSR LGQGIGPIHL NEIQCTGNEK 400
    SIIDCKFNAE SQGCNHEEDA GVRCNTPAMG LQKKLRLNGG RNPYEGRVEV 450
    LVERNGSLVW GMVCGQNWGI VEAMVVCRQL GLGFASNAFQ ETWYWHGDVN 500
    SNKVVMSGVK CSGTELSLAH CRHDGEDVAC PQGGVQYGAG VACSETAPDL 550
    VLNAEMVQQT TYLEDRPMFM LQCAMEENCL SASAAQTDPT TGYRRLLRFS 600
    SQIHNNGQSD FRPKNGRHAW IWHDCHRHYH SMEVFTHYDL LNLNGTKVAE 650
    GHKASFCLED TECEGDIQKN YECANFGDQG ITMGCWDMYR HDIDCQWVDI 700
    TDVPPGDYLF QVVINPNFEV AESDYSNNIM KCRSRYDGHR IWMYNCHIGG 750
    SFSEETEKKF EHFSGLLNNQ LSPQ 774
    Length:774
    Mass (Da):86,725
    Last modified:November 1, 1999 - v1
    Checksum:i9DF5D25D4824BCCD
    GO

    Sequence cautioni

    The sequence AAD34343.1 differs from that shown. Reason: Erroneous termination at position 775. Translated as stop.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti184 – 1841E → K in BAG35197. (PubMed:14702039)Curated
    Sequence conflicti239 – 2391E → G in BAD96197. 1 PublicationCurated
    Sequence conflicti295 – 2951L → Q in AAD34343. (PubMed:10212285)Curated
    Sequence conflicti536 – 5361Q → R in BAG35197. (PubMed:14702039)Curated
    Sequence conflicti652 – 6521H → Q in AAD34343. (PubMed:10212285)Curated
    Sequence conflicti746 – 7461C → S in AAD34343. (PubMed:10212285)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti308 – 3081S → R.
    Corresponds to variant rs4871866 [ dbSNP | Ensembl ].
    VAR_050009
    Natural varianti359 – 3591S → W.
    Corresponds to variant rs4602894 [ dbSNP | Ensembl ].
    VAR_050010
    Natural varianti570 – 5701M → L.2 Publications
    Corresponds to variant rs1063582 [ dbSNP | Ensembl ].
    VAR_024527

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U89942 mRNA. Translation: AAB49697.1.
    AK312266 mRNA. Translation: BAG35197.1.
    AK222477 mRNA. Translation: BAD96197.1.
    AC090197 Genomic DNA. No translation available.
    BC000594 mRNA. Translation: AAH00594.1.
    AF117949 mRNA. Translation: AAD34343.1. Sequence problems.
    CCDSiCCDS34864.1.
    RefSeqiNP_002309.1. NM_002318.2.
    UniGeneiHs.626637.

    Genome annotation databases

    EnsembliENST00000389131; ENSP00000373783; ENSG00000134013.
    GeneIDi4017.
    KEGGihsa:4017.
    UCSCiuc003xdh.1. human.

    Polymorphism databases

    DMDMi13878585.

    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
    U89942 mRNA. Translation: AAB49697.1 .
    AK312266 mRNA. Translation: BAG35197.1 .
    AK222477 mRNA. Translation: BAD96197.1 .
    AC090197 Genomic DNA. No translation available.
    BC000594 mRNA. Translation: AAH00594.1 .
    AF117949 mRNA. Translation: AAD34343.1 . Sequence problems.
    CCDSi CCDS34864.1.
    RefSeqi NP_002309.1. NM_002318.2.
    UniGenei Hs.626637.

    3D structure databases

    ProteinModelPortali Q9Y4K0.
    SMRi Q9Y4K0. Positions 68-159, 326-424, 435-525.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110201. 2 interactions.
    IntActi Q9Y4K0. 2 interactions.
    MINTi MINT-4053647.
    STRINGi 9606.ENSP00000373783.

    PTM databases

    PhosphoSitei Q9Y4K0.

    Polymorphism databases

    DMDMi 13878585.

    Proteomic databases

    MaxQBi Q9Y4K0.
    PaxDbi Q9Y4K0.
    PRIDEi Q9Y4K0.

    Protocols and materials databases

    DNASUi 4017.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389131 ; ENSP00000373783 ; ENSG00000134013 .
    GeneIDi 4017.
    KEGGi hsa:4017.
    UCSCi uc003xdh.1. human.

    Organism-specific databases

    CTDi 4017.
    GeneCardsi GC08M023210.
    H-InvDB HIX0007387.
    HGNCi HGNC:6666. LOXL2.
    HPAi CAB025848.
    HPA036257.
    HPA056542.
    MIMi 606663. gene.
    neXtProti NX_Q9Y4K0.
    PharmGKBi PA30429.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40770.
    HOGENOMi HOG000220841.
    HOVERGENi HBG052336.
    InParanoidi Q9Y4K0.
    KOi K00280.
    OMAi HFSGLIN.
    OrthoDBi EOG7SN8C6.
    PhylomeDBi Q9Y4K0.
    TreeFami TF326061.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi LOXL2. human.
    GeneWikii LOXL2.
    GenomeRNAii 4017.
    NextBioi 15762.
    PROi Q9Y4K0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y4K0.
    Bgeei Q9Y4K0.
    CleanExi HS_LOXL2.
    Genevestigatori Q9Y4K0.

    Family and domain databases

    Gene3Di 3.10.250.10. 4 hits.
    InterProi IPR001695. Lysyl_oxidase.
    IPR019828. Lysyl_oxidase_CS.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    [Graphical view ]
    Pfami PF01186. Lysyl_oxidase. 1 hit.
    PF00530. SRCR. 4 hits.
    [Graphical view ]
    PRINTSi PR00074. LYSYLOXIDASE.
    PR00258. SPERACTRCPTR.
    SMARTi SM00202. SR. 4 hits.
    [Graphical view ]
    SUPFAMi SSF56487. SSF56487. 4 hits.
    PROSITEi PS00926. LYSYL_OXIDASE. 1 hit.
    PS00420. SRCR_1. 2 hits.
    PS50287. SRCR_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Regulation of a novel gene encoding a lysyl oxidase-related protein in cellular adhesion and senescence."
      Saito H., Papaconstantinou J., Sato H., Goldstein S.
      J. Biol. Chem. 272:8157-8160(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
    3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-570.
      Tissue: Adipose tissue.
    4. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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], VARIANT LEU-570.
      Tissue: Kidney.
    6. "The LOXL2 gene encodes a new lysyl oxidase-like protein and is expressed at high levels in reproductive tissues."
      Jourdan-Le Saux C., Tronecker H., Bogic L., Bryant-Greenwood G.D., Boyd C.D., Csiszar K.
      J. Biol. Chem. 274:12939-12944(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 202-774.
      Tissue: Placenta and Spleen.
    7. "A molecular role for lysyl oxidase-like 2 enzyme in snail regulation and tumor progression."
      Peinado H., Del Carmen Iglesias-de la Cruz M., Olmeda D., Csiszar K., Fong K.S., Vega S., Nieto M.A., Cano A., Portillo F.
      EMBO J. 24:3446-3458(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SNAI1.
    8. "The lysyl oxidases LOX and LOXL2 are necessary and sufficient to repress E-cadherin in hypoxia: insights into cellular transformation processes mediated by HIF-1."
      Schietke R., Warnecke C., Wacker I., Schodel J., Mole D.R., Campean V., Amann K., Goppelt-Struebe M., Behrens J., Eckardt K.U., Wiesener M.S.
      J. Biol. Chem. 285:6658-6669(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    9. "Modulation of lysyl oxidase-like 2 enzymatic activity by an allosteric antibody inhibitor."
      Rodriguez H.M., Vaysberg M., Mikels A., McCauley S., Velayo A.C., Garcia C., Smith V.
      J. Biol. Chem. 285:20964-20974(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    10. Cited for: ENZYME REGULATION.
    11. "Lysyl oxidase-like protein-2 regulates sprouting angiogenesis and type IV collagen assembly in the endothelial basement membrane."
      Bignon M., Pichol-Thievend C., Hardouin J., Malbouyres M., Brechot N., Nasciutti L., Barret A., Teillon J., Guillon E., Etienne E., Caron M., Joubert-Caron R., Monnot C., Ruggiero F., Muller L., Germain S.
      Blood 118:3979-3989(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "LOXL2-mediated matrix remodeling in metastasis and mammary gland involution."
      Barker H.E., Chang J., Cox T.R., Lang G., Bird D., Nicolau M., Evans H.R., Gartland A., Erler J.T.
      Cancer Res. 71:1561-1572(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN TUMOR PROGRESSION.
    13. "Lysyl oxidase-like 2 (LOXL2), a new regulator of cell polarity required for metastatic dissemination of basal-like breast carcinomas."
      Moreno-Bueno G., Salvador F., Martin A., Floristan A., Cuevas E.P., Santos V., Montes A., Morales S., Castilla M.A., Rojo-Sebastian A., Martinez A., Hardisson D., Csiszar K., Portillo F., Peinado H., Palacios J., Cano A.
      EMBO Mol. Med. 3:528-544(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN TUMOR PROGRESSION.
    14. "The human lysyl oxidase-like 2 protein functions as an amine oxidase toward collagen and elastin."
      Kim Y.M., Kim E.C., Kim Y.
      Mol. Biol. Rep. 38:145-149(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION.
    15. "The enzymatic activity of lysyl oxidas-like-2 (LOXL2) is not required for LOXL2-induced inhibition of keratinocyte differentiation."
      Lugassy J., Zaffryar-Eilot S., Soueid S., Mordoviz A., Smith V., Kessler O., Neufeld G.
      J. Biol. Chem. 287:3541-3549(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-689.
    16. Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 626-HIS--HIS-628.
    17. "Post-translational Modifications of Recombinant Human Lysyl Oxidase-like 2 (rhLOXL2) Secreted from Drosophila S2 Cells."
      Xu L., Go E.P., Finney J., Moon H., Lantz M., Rebecchi K., Desaire H., Mure M.
      J. Biol. Chem. 288:5357-5363(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION AT ASN-455 AND ASN-644, MUTAGENESIS OF ASN-455 AND ASN-644, CROSS-LINK FORMATION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiLOXL2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4K0
    Secondary accession number(s): B2R5Q0
    , Q53HV3, Q9BW70, Q9Y5Y8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 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

    Its overexpression in a number of cancer and its ability to promote epithelial to mesenchymal transition suggest that LOXL2 might play a role in tumor progression: expression is correlated with metastasis and decreased survival in patients with aggressive breast cancer (PubMed:21732535). Allosteric inhibition by AB0023 inhibits formation of the tumor microenvironment and reduces metastatic tumor burden in xenograft models (PubMed:20818376 and PubMed:21732535). However, inhibiting the enzyme activity of LOXL2 may not be sufficient, since mutants that lack enzyme activity or inhibition of the activity by AB0023 antibody does not prevent inhibition of the differentiation of keratinocytes, thereby promoting development of squamous cell carcinomas (PubMed:22157764).2 Publications

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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

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