CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023849
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lysyl oxidase homolog 2 
Protein Synonyms/Alias
 Lysyl oxidase-like protein 2; Lysyl oxidase-related protein 2; Lysyl oxidase-related protein WS9-14 
Gene Name
 LOXL2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
197AILSTYRKRTPVMEGacetylation[1]
209MEGYVEVKEGKTWKQacetylation[1]
225CDKHWTAKNSRVVCGacetylation[1]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 58 159 SRCR 1.
 DOMAIN 188 302 SRCR 2.
 DOMAIN 326 425 SRCR 3.
 DOMAIN 435 544 SRCR 4.
 REGION 548 751 Lysyl-oxidase like.
 METAL 626 626 Copper (Potential).
 METAL 628 628 Copper (Potential).
 METAL 630 630 Copper (Potential).
 MOD_RES 689 689 2',4',5'-topaquinone (By similarity).
 CARBOHYD 288 288 N-linked (GlcNAc...) (Potential).
 CARBOHYD 455 455 N-linked (GlcNAc...) (complex).
 CARBOHYD 644 644 N-linked (GlcNAc...) (complex).
 DISULFID 84 148 By similarity.
 DISULFID 97 158 By similarity.
 DISULFID 128 138 By similarity.
 DISULFID 218 291 By similarity.
 DISULFID 231 301 By similarity.
 DISULFID 265 275 By similarity.
 DISULFID 351 414 By similarity.
 DISULFID 364 424 By similarity.
 DISULFID 395 405 By similarity.
 DISULFID 464 530 By similarity.
 DISULFID 477 543 By similarity.
 DISULFID 511 521 By similarity.
 DISULFID 573 579 By similarity.
 DISULFID 625 673 By similarity.
 DISULFID 657 663 By similarity.
 DISULFID 685 695 By similarity.
 DISULFID 732 746 By similarity.
 CROSSLNK 653 689 Lysine tyrosylquinone (Lys-Tyr).  
Keyword
 Basement membrane; Chromatin regulator; Chromosome; Complete proteome; Copper; Disulfide bond; Extracellular matrix; Glycoprotein; LTQ; Metal-binding; Nucleus; Oxidoreductase; Polymorphism; Reference proteome; Repeat; Repressor; Secreted; Signal; TPQ; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 774 AA 
Protein Sequence
MERPLCSHLC SCLAMLALLS PLSLAQYDSW PHYPEYFQQP APEYHQPQAP ANVAKIQLRL 60
AGQKRKHSEG RVEVYYDGQW GTVCDDDFSI HAAHVVCREL GYVEAKSWTA SSSYGKGEGP 120
IWLDNLHCTG NEATLAACTS NGWGVTDCKH TEDVGVVCSD KRIPGFKFDN SLINQIENLN 180
IQVEDIRIRA ILSTYRKRTP VMEGYVEVKE GKTWKQICDK HWTAKNSRVV CGMFGFPGER 240
TYNTKVYKMF ASRRKQRYWP FSMDCTGTEA HISSCKLGPQ VSLDPMKNVT CENGLPAVVS 300
CVPGQVFSPD GPSRFRKAYK PEQPLVRLRG GAYIGEGRVE VLKNGEWGTV CDDKWDLVSA 360
SVVCRELGFG SAKEAVTGSR LGQGIGPIHL NEIQCTGNEK SIIDCKFNAE SQGCNHEEDA 420
GVRCNTPAMG LQKKLRLNGG RNPYEGRVEV LVERNGSLVW GMVCGQNWGI VEAMVVCRQL 480
GLGFASNAFQ ETWYWHGDVN SNKVVMSGVK CSGTELSLAH CRHDGEDVAC PQGGVQYGAG 540
VACSETAPDL VLNAEMVQQT TYLEDRPMFM LQCAMEENCL SASAAQTDPT TGYRRLLRFS 600
SQIHNNGQSD FRPKNGRHAW IWHDCHRHYH SMEVFTHYDL LNLNGTKVAE GHKASFCLED 660
TECEGDIQKN YECANFGDQG ITMGCWDMYR HDIDCQWVDI TDVPPGDYLF QVVINPNFEV 720
AESDYSNNIM KCRSRYDGHR IWMYNCHIGG SFSEETEKKF EHFSGLLNNQ LSPQ 774 
Gene Ontology
 GO:0005604; C:basement membrane; ISS:UniProtKB.
 GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
 GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO:0016020; C:membrane; IEA:InterPro.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0005507; F:copper ion binding; IEA:InterPro.
 GO:0009055; F:electron carrier activity; TAS:UniProtKB.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0070492; F:oligosaccharide binding; IDA:UniProtKB.
 GO:0004720; F:protein-lysine 6-oxidase activity; IDA:UniProtKB.
 GO:0005044; F:scavenger receptor activity; IEA:InterPro.
 GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
 GO:0007568; P:aging; TAS:ProtInc.
 GO:0007155; P:cell adhesion; TAS:ProtInc.
 GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
 GO:0043542; P:endothelial cell migration; IMP:UniProtKB.
 GO:0001935; P:endothelial cell proliferation; IMP:UniProtKB.
 GO:0001837; P:epithelial to mesenchymal transition; IDA:UniProtKB.
 GO:0016570; P:histone modification; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0032332; P:positive regulation of chondrocyte differentiation; ISS:UniProtKB.
 GO:0018277; P:protein deamination; IDA:UniProtKB.
 GO:0046688; P:response to copper ion; IDA:UniProtKB.
 GO:0001666; P:response to hypoxia; ISS:UniProtKB.
 GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001695; Lysyl_oxidase.
 IPR019828; Lysyl_oxidase_CS.
 IPR001190; Srcr_rcpt.
 IPR017448; Srcr_rcpt-rel. 
Pfam
 PF01186; Lysyl_oxidase
 PF00530; SRCR 
SMART
 SM00202; SR 
PROSITE
 PS00926; LYSYL_OXIDASE
 PS00420; SRCR_1
 PS50287; SRCR_2 
PRINTS
 PR00074; LYSYLOXIDASE.
 PR00258; SPERACTRCPTR.