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Q9Y4K0

- LOXL2_HUMAN

UniProt

Q9Y4K0 - LOXL2_HUMAN

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Protein

Lysyl oxidase homolog 2

Gene

LOXL2

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

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

Protein has several cofactor binding sites:

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-lysine 6-oxidase activity Source: UniProtKB
  7. scavenger receptor activity Source: InterPro
  8. 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
Complete GO annotation...

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-KW
  3. extracellular space Source: UniProtKB
  4. membrane Source: InterPro
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Chromosome, Extracellular matrix, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

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

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

BgeeiQ9Y4K0.
CleanExiHS_LOXL2.
ExpressionAtlasiQ9Y4K0. baseline and differential.
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. 10 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.
GeneTreeiENSGT00760000119251.
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

« Hide

        10         20         30         40         50
MERPLCSHLC SCLAMLALLS PLSLAQYDSW PHYPEYFQQP APEYHQPQAP
60 70 80 90 100
ANVAKIQLRL AGQKRKHSEG RVEVYYDGQW GTVCDDDFSI HAAHVVCREL
110 120 130 140 150
GYVEAKSWTA SSSYGKGEGP IWLDNLHCTG NEATLAACTS NGWGVTDCKH
160 170 180 190 200
TEDVGVVCSD KRIPGFKFDN SLINQIENLN IQVEDIRIRA ILSTYRKRTP
210 220 230 240 250
VMEGYVEVKE GKTWKQICDK HWTAKNSRVV CGMFGFPGER TYNTKVYKMF
260 270 280 290 300
ASRRKQRYWP FSMDCTGTEA HISSCKLGPQ VSLDPMKNVT CENGLPAVVS
310 320 330 340 350
CVPGQVFSPD GPSRFRKAYK PEQPLVRLRG GAYIGEGRVE VLKNGEWGTV
360 370 380 390 400
CDDKWDLVSA SVVCRELGFG SAKEAVTGSR LGQGIGPIHL NEIQCTGNEK
410 420 430 440 450
SIIDCKFNAE SQGCNHEEDA GVRCNTPAMG LQKKLRLNGG RNPYEGRVEV
460 470 480 490 500
LVERNGSLVW GMVCGQNWGI VEAMVVCRQL GLGFASNAFQ ETWYWHGDVN
510 520 530 540 550
SNKVVMSGVK CSGTELSLAH CRHDGEDVAC PQGGVQYGAG VACSETAPDL
560 570 580 590 600
VLNAEMVQQT TYLEDRPMFM LQCAMEENCL SASAAQTDPT TGYRRLLRFS
610 620 630 640 650
SQIHNNGQSD FRPKNGRHAW IWHDCHRHYH SMEVFTHYDL LNLNGTKVAE
660 670 680 690 700
GHKASFCLED TECEGDIQKN YECANFGDQG ITMGCWDMYR HDIDCQWVDI
710 720 730 740 750
TDVPPGDYLF QVVINPNFEV AESDYSNNIM KCRSRYDGHR IWMYNCHIGG
760 770
SFSEETEKKF EHFSGLLNNQ LSPQ
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 10 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 GC08M023154.
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.
GeneTreei ENSGT00760000119251.
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

Bgeei Q9Y4K0.
CleanExi HS_LOXL2.
ExpressionAtlasi Q9Y4K0. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 133 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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