Q9Y4K0 (LOXL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

LOXL2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	774 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular matrix › basement 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 process	Transcription Transcription regulation
Cellular component	Basement membrane Chromosome Extracellular matrix Nucleus Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Chromatin regulator Oxidoreductase Repressor
PTM	Disulfide bond Glycoprotein LTQ TPQ
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aging Traceable author statement Ref.1. Source: ProtInc cell adhesion Traceable author statement Ref.1. Source: ProtInc 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-dependent Inferred from direct assay Ref.7. 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	basement 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_function	chromatin 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 residue binding Inferred from direct assay Ref.16. Source: UniProtKB oligosaccharide binding Inferred from direct assay Ref.17. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 774	749	Lysyl oxidase homolog 2		PRO_0000018532
Regions
	Domain	58 – 159	102	SRCR 1
	Domain	188 – 302	115	SRCR 2
	Domain	326 – 425	100	SRCR 3
	Domain	435 – 544	110	SRCR 4
	Region	548 – 751	204	Lysyl-oxidase like
Sites
	Metal binding	626	1	Copper Potential
	Metal binding	628	1	Copper Potential
	Metal binding	630	1	Copper Potential
Amino acid modifications
	Modified residue	689	1	2',4',5'-topaquinone By similarity
	Glycosylation	288	1	N-linked (GlcNAc...) Potential
	Glycosylation	455	1	N-linked (GlcNAc...) (complex) Ref.17
	Glycosylation	644	1	N-linked (GlcNAc...) (complex) Ref.17
	Disulfide bond	84 ↔ 148		By similarity
	Disulfide bond	97 ↔ 158		By similarity
	Disulfide bond	128 ↔ 138		By similarity
	Disulfide bond	218 ↔ 291		By similarity
	Disulfide bond	231 ↔ 301		By similarity
	Disulfide bond	265 ↔ 275		By similarity
	Disulfide bond	351 ↔ 414		By similarity
	Disulfide bond	364 ↔ 424		By similarity
	Disulfide bond	395 ↔ 405		By similarity
	Disulfide bond	464 ↔ 530		By similarity
	Disulfide bond	477 ↔ 543		By similarity
	Disulfide bond	511 ↔ 521		By similarity
	Disulfide bond	573 ↔ 579		By similarity
	Disulfide bond	625 ↔ 673		By similarity
	Disulfide bond	657 ↔ 663		By similarity
	Disulfide bond	685 ↔ 695		By similarity
	Disulfide bond	732 ↔ 746		By similarity
	Cross-link	653 ↔ 689		Lysine tyrosylquinone (Lys-Tyr)
Natural variations
	Natural variant	308	1	S → R. Corresponds to variant rs4871866 [ dbSNP | Ensembl ].		VAR_050009
	Natural variant	359	1	S → W. Corresponds to variant rs4602894 [ dbSNP | Ensembl ].		VAR_050010
	Natural variant	570	1	M → L. Ref.3 Ref.5 Corresponds to variant rs1063582 [ dbSNP | Ensembl ].		VAR_024527
Experimental info
	Mutagenesis	455	1	N → Q: Inhibits secretion. Ref.17
	Mutagenesis	626 – 628	3	HRH → ARA: Loss of catalytic activity and abolishes ability to repress transcription. Ref.16
	Mutagenesis	644	1	N → Q: Inhibits secretion. Ref.17
	Mutagenesis	689	1	Y → F: Does not affect ability to inhibit keratinocyte differentiation. Ref.15
	Sequence conflict	184	1	E → K in BAG35197. Ref.2
	Sequence conflict	239	1	E → G in BAD96197. Ref.3
	Sequence conflict	295	1	L → Q in AAD34343. Ref.6
	Sequence conflict	536	1	Q → R in BAG35197. Ref.2
	Sequence conflict	652	1	H → Q in AAD34343. Ref.6
	Sequence conflict	746	1	C → S in AAD34343. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q9Y4K0 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 9DF5D25D4824BCCD	FASTA	774	86,725
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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. , 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.
IPI	IPI00294839.
RefSeq	NP_002309.1. NM_002318.2.
UniGene	Hs.626637.
3D structure databases
ProteinModelPortal	Q9Y4K0.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4053647.
STRING	9606.ENSP00000373783.
PTM databases
PhosphoSite	Q9Y4K0.
Polymorphism databases
DMDM	13878585.
Proteomic databases
PaxDb	Q9Y4K0.
PRIDE	Q9Y4K0.
Protocols and materials databases
DNASU	4017.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000389131; ENSP00000373783; ENSG00000134013.
GeneID	4017.
KEGG	hsa:4017.
UCSC	uc003xdh.1. human.
Organism-specific databases
CTD	4017.
GeneCards	GC08M023210.
H-InvDB	HIX0007387.
HGNC	HGNC:6666. LOXL2.
HPA	CAB025848.
MIM	606663. gene.
neXtProt	NX_Q9Y4K0.
PharmGKB	PA30429.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG40770.
HOGENOM	HOG000220841.
HOVERGEN	HBG052336.
InParanoid	Q9Y4K0.
KO	K00280.
OMA	FSMDCTG.
OrthoDB	EOG4B8JCF.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	Q9Y4K0.
Bgee	Q9Y4K0.
CleanEx	HS_LOXL2.
Genevestigator	Q9Y4K0.
GermOnline	ENSG00000134013. Homo sapiens.
Family and domain databases
InterPro	IPR001695. Lysyl_oxidase. IPR019828. Lysyl_oxidase_CS. IPR001190. Srcr_rcpt. IPR017448. Srcr_rcpt-rel. [Graphical view]
Pfam	PF01186. Lysyl_oxidase. 1 hit. PF00530. SRCR. 4 hits. [Graphical view]
PRINTS	PR00074. LYSYLOXIDASE. PR00258. SPERACTRCPTR.
SMART	SM00202. SR. 4 hits. [Graphical view]
SUPFAM	SSF56487. Srcr_receptor. 4 hits.
PROSITE	PS00926. LYSYL_OXIDASE. 1 hit. PS00420. SRCR_1. 2 hits. PS50287. SRCR_2. 4 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LOXL2. human.
GenomeRNAi	4017.
NextBio	15762.
SOURCE	Search...

Entry information

Entry name

LOXL2_HUMAN

Accession

Primary (citable) accession number: Q9Y4K0
Secondary accession number(s): B2R5Q0 , Q53HV3, Q9BW70, Q9Y5Y8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.