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Q9Y4K0 (LOXL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:LOXL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length774 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.16

Catalytic activity

Peptidyl-L-lysyl-peptide + O2 + H2O = peptidyl-allysyl-peptide + NH3 + H2O2. Ref.9 Ref.14 Ref.17

Cofactor

Copper By similarity.

Contains 1 lysine tyrosylquinone By similarity.

Enzyme regulation

According to some reports, it is inhibited by beta-aminopropionitrile (BAPN) (Ref.9 and Ref.17). According to another report, it is not inhibited by beta-aminopropionitrile (BAPN) (Ref.14). Specifically inhibited by a mouse monoclonal antibody AB0023, inhibition occurs in a non-competitive manner. Ref.9 Ref.10 Ref.14 Ref.17

Subunit structure

Component of some chromatin repressor complex. Interacts with SNAI1. Ref.7

Subcellular location

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. Ref.7 Ref.16 Ref.17

Tissue specificity

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

Induction

Strongly induced in hypoxia. Direct transcriptional target of HIF1A. Ref.8 Ref.9 Ref.10 Ref.14 Ref.17

Domain

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

Post-translational modification

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. Ref.17

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 (Ref.13). Allosteric inhibition by AB0023 inhibits formation of the tumor microenvironment and reduces metastatic tumor burden in xenograft models (Ref.10 and Ref.13). 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 (Ref.15).

Sequence similarities

Belongs to the lysyl oxidase family.

Contains 4 SRCR domains.

Biophysicochemical properties

Kinetic parameters:

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).

KM=1.01 mM for 1,5-diaminopentane Ref.9 Ref.17

KM=1.05 mM for spermine

KM=0.59 µM for tropoelastin (without the first three SRCR domains)

KM=0.62 µM for tropoelastin (without all four SRCR domains)

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentBasement membrane
Chromosome
Extracellular matrix
Nucleus
Secreted
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionChromatin regulator
Oxidoreductase
Repressor
   PTMDisulfide bond
Glycoprotein
LTQ
TPQ
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Traceable author statement Ref.1. Source: ProtInc

cell adhesion

Traceable author statement Ref.1. Source: ProtInc

cellular protein modification process

Inferred from direct assay Ref.17. Source: UniProtKB

collagen fibril organization

Inferred from mutant phenotype Ref.11. Source: UniProtKB

endothelial cell migration

Inferred from mutant phenotype Ref.11. Source: UniProtKB

endothelial cell proliferation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

epithelial to mesenchymal transition

Inferred from direct assay Ref.7. Source: UniProtKB

histone modification

Inferred from direct assay Ref.16. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.7. Source: UniProtKB

oxidation-reduction process

Inferred from direct assay Ref.16. Source: UniProtKB

positive regulation of chondrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

protein deamination

Inferred from direct assay Ref.16. Source: UniProtKB

response to copper ion

Inferred from direct assay Ref.17. Source: UniProtKB

response to hypoxia

Inferred from sequence or structural similarity. Source: UniProtKB

sprouting angiogenesis

Inferred from mutant phenotype Ref.11. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentbasement membrane

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from direct assay Ref.17. Source: UniProtKB

membrane

Inferred from electronic annotation. Source: InterPro

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from direct assay Ref.16. Source: UniProtKB

copper ion binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Traceable author statement Ref.1. Source: UniProtKB

methylated histone binding

Inferred from direct assay Ref.16. Source: UniProtKB

oligosaccharide binding

Inferred from direct assay Ref.17. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

protein-lysine 6-oxidase activity

Inferred from direct assay Ref.16Ref.17. Source: UniProtKB

scavenger receptor activity

Inferred from electronic annotation. Source: InterPro

transcription corepressor activity

Inferred from direct assay Ref.16. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 774749Lysyl oxidase homolog 2
PRO_0000018532

Regions

Domain58 – 159102SRCR 1
Domain188 – 302115SRCR 2
Domain326 – 425100SRCR 3
Domain435 – 544110SRCR 4
Region548 – 751204Lysyl-oxidase like

Sites

Metal binding6261Copper Potential
Metal binding6281Copper Potential
Metal binding6301Copper Potential

Amino acid modifications

Modified residue68912',4',5'-topaquinone By similarity
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation4551N-linked (GlcNAc...) (complex) Ref.17
Glycosylation6441N-linked (GlcNAc...) (complex) Ref.17
Disulfide bond84 ↔ 148 By similarity
Disulfide bond97 ↔ 158 By similarity
Disulfide bond128 ↔ 138 By similarity
Disulfide bond218 ↔ 291 By similarity
Disulfide bond231 ↔ 301 By similarity
Disulfide bond265 ↔ 275 By similarity
Disulfide bond351 ↔ 414 By similarity
Disulfide bond364 ↔ 424 By similarity
Disulfide bond395 ↔ 405 By similarity
Disulfide bond464 ↔ 530 By similarity
Disulfide bond477 ↔ 543 By similarity
Disulfide bond511 ↔ 521 By similarity
Disulfide bond573 ↔ 579 By similarity
Disulfide bond625 ↔ 673 By similarity
Disulfide bond657 ↔ 663 By similarity
Disulfide bond685 ↔ 695 By similarity
Disulfide bond732 ↔ 746 By similarity
Cross-link653 ↔ 689Lysine tyrosylquinone (Lys-Tyr)

Natural variations

Natural variant3081S → R.
Corresponds to variant rs4871866 [ dbSNP | Ensembl ].
VAR_050009
Natural variant3591S → W.
Corresponds to variant rs4602894 [ dbSNP | Ensembl ].
VAR_050010
Natural variant5701M → L. Ref.3 Ref.5
Corresponds to variant rs1063582 [ dbSNP | Ensembl ].
VAR_024527

Experimental info

Mutagenesis4551N → Q: Inhibits secretion. Ref.17
Mutagenesis626 – 6283HRH → ARA: Loss of catalytic activity and abolishes ability to repress transcription. Ref.16
Mutagenesis6441N → Q: Inhibits secretion. Ref.17
Mutagenesis6891Y → F: Does not affect ability to inhibit keratinocyte differentiation. Ref.15
Sequence conflict1841E → K in BAG35197. Ref.2
Sequence conflict2391E → G in BAD96197. Ref.3
Sequence conflict2951L → Q in AAD34343. Ref.6
Sequence conflict5361Q → R in BAG35197. Ref.2
Sequence conflict6521H → Q in AAD34343. Ref.6
Sequence conflict7461C → S in AAD34343. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9Y4K0 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 9DF5D25D4824BCCD

FASTA77486,725
        10         20         30         40         50         60 
MERPLCSHLC SCLAMLALLS PLSLAQYDSW PHYPEYFQQP APEYHQPQAP ANVAKIQLRL 

        70         80         90        100        110        120 
AGQKRKHSEG RVEVYYDGQW GTVCDDDFSI HAAHVVCREL GYVEAKSWTA SSSYGKGEGP 

       130        140        150        160        170        180 
IWLDNLHCTG NEATLAACTS NGWGVTDCKH TEDVGVVCSD KRIPGFKFDN SLINQIENLN 

       190        200        210        220        230        240 
IQVEDIRIRA ILSTYRKRTP VMEGYVEVKE GKTWKQICDK HWTAKNSRVV CGMFGFPGER 

       250        260        270        280        290        300 
TYNTKVYKMF ASRRKQRYWP FSMDCTGTEA HISSCKLGPQ VSLDPMKNVT CENGLPAVVS 

       310        320        330        340        350        360 
CVPGQVFSPD GPSRFRKAYK PEQPLVRLRG GAYIGEGRVE VLKNGEWGTV CDDKWDLVSA 

       370        380        390        400        410        420 
SVVCRELGFG SAKEAVTGSR LGQGIGPIHL NEIQCTGNEK SIIDCKFNAE SQGCNHEEDA 

       430        440        450        460        470        480 
GVRCNTPAMG LQKKLRLNGG RNPYEGRVEV LVERNGSLVW GMVCGQNWGI VEAMVVCRQL 

       490        500        510        520        530        540 
GLGFASNAFQ ETWYWHGDVN SNKVVMSGVK CSGTELSLAH CRHDGEDVAC PQGGVQYGAG 

       550        560        570        580        590        600 
VACSETAPDL VLNAEMVQQT TYLEDRPMFM LQCAMEENCL SASAAQTDPT TGYRRLLRFS 

       610        620        630        640        650        660 
SQIHNNGQSD FRPKNGRHAW IWHDCHRHYH SMEVFTHYDL LNLNGTKVAE GHKASFCLED 

       670        680        690        700        710        720 
TECEGDIQKN YECANFGDQG ITMGCWDMYR HDIDCQWVDI TDVPPGDYLF QVVINPNFEV 

       730        740        750        760        770 
AESDYSNNIM KCRSRYDGHR IWMYNCHIGG SFSEETEKKF EHFSGLLNNQ LSPQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Allosteric inhibition of lysyl oxidase-like-2 impedes the development of a pathologic microenvironment."
Barry-Hamilton V., Spangler R., Marshall D., McCauley S., Rodriguez H.M., Oyasu M., Mikels A., Vaysberg M., Ghermazien H., Wai C., Garcia C.A., Velayo A.C., Jorgensen B., Biermann D., Tsai D., Green J., Zaffryar-Eilot S., Holzer A. expand/collapse author list , Ogg S., Thai D., Neufeld G., Van Vlasselaer P., Smith V.
Nat. Med. 16:1009-1017(2010) [PubMed] [Europe PMC] [Abstract]
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]"Lysyl oxidase-like 2 deaminates lysine 4 in histone H3."
Herranz N., Dave N., Millanes-Romero A., Morey L., Diaz V.M., Lorenz-Fonfria V., Gutierrez-Gallego R., Jeronimo C., Di Croce L., Garcia de Herreros A., Peiro S.
Mol. Cell 46:369-376(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34864.1.
RefSeqNP_002309.1. NM_002318.2.
UniGeneHs.626637.

3D structure databases

ProteinModelPortalQ9Y4K0.
SMRQ9Y4K0. Positions 68-159, 326-424, 435-525.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110201. 1 interaction.
IntActQ9Y4K0. 2 interactions.
MINTMINT-4053647.
STRING9606.ENSP00000373783.

PTM databases

PhosphoSiteQ9Y4K0.

Polymorphism databases

DMDM13878585.

Proteomic databases

MaxQBQ9Y4K0.
PaxDbQ9Y4K0.
PRIDEQ9Y4K0.

Protocols and materials databases

DNASU4017.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000389131; ENSP00000373783; ENSG00000134013.
GeneID4017.
KEGGhsa:4017.
UCSCuc003xdh.1. human.

Organism-specific databases

CTD4017.
GeneCardsGC08M023210.
H-InvDBHIX0007387.
HGNCHGNC:6666. LOXL2.
HPACAB025848.
HPA036257.
HPA056542.
MIM606663. gene.
neXtProtNX_Q9Y4K0.
PharmGKBPA30429.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG40770.
HOGENOMHOG000220841.
HOVERGENHBG052336.
InParanoidQ9Y4K0.
KOK00280.
OMAHFSGLIN.
OrthoDBEOG7SN8C6.
PhylomeDBQ9Y4K0.
TreeFamTF326061.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ9Y4K0.
BgeeQ9Y4K0.
CleanExHS_LOXL2.
GenevestigatorQ9Y4K0.

Family and domain databases

Gene3D3.10.250.10. 4 hits.
InterProIPR001695. Lysyl_oxidase.
IPR019828. Lysyl_oxidase_CS.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
[Graphical view]
PfamPF01186. Lysyl_oxidase. 1 hit.
PF00530. SRCR. 4 hits.
[Graphical view]
PRINTSPR00074. LYSYLOXIDASE.
PR00258. SPERACTRCPTR.
SMARTSM00202. SR. 4 hits.
[Graphical view]
SUPFAMSSF56487. SSF56487. 4 hits.
PROSITEPS00926. LYSYL_OXIDASE. 1 hit.
PS00420. SRCR_1. 2 hits.
PS50287. SRCR_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLOXL2. human.
GeneWikiLOXL2.
GenomeRNAi4017.
NextBio15762.
PROQ9Y4K0.
SOURCESearch...

Entry information

Entry nameLOXL2_HUMAN
AccessionPrimary (citable) accession number: Q9Y4K0
Secondary accession number(s): B2R5Q0 expand/collapse secondary AC list , Q53HV3, Q9BW70, Q9Y5Y8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM