[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
DOI=10.1074/jbc.272.11.6831; PubMed=9054364 [NCBI, ExPASy, EBI, Israel, Japan]
Valtavaara M.,
Papponen H.,
Pirttila A.M.,
Hiltunen K.,
Helander H.,
Myllylae R.;
"Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle.";
J. Biol. Chem. 272:6831-6834(1997).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
TISSUE=Skin fibroblast;
DOI=10.1016/S0945-053X(99)00013-X; PubMed=10372558 [NCBI, ExPASy, EBI, Israel, Japan]
Yeowell H.N.,
Walker L.C.;
"Tissue specificity of a new splice form of the human lysyl hydroxylase 2 gene.";
Matrix Biol. 18:179-187(1999).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[4]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320 AND TYR-323, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P.,
Lewandrowski U.,
Wiesner J.,
Wortelkamp S.,
Moebius J.,
Schuetz C.,
Walter U.,
Gambaryan S.,
Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
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[5]
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VARIANTS BRKS2 VAL-601 AND ILE-608.
DOI=10.1074/jbc.M307380200; PubMed=12881513 [NCBI, ExPASy, EBI, Israel, Japan]
van der Slot A.J.,
Zuurmond A.-M.,
Bardoel A.F.J.,
Wijmenga C.,
Pruijs H.E.H.,
Sillence D.O.,
Brinckmann J.,
Abraham D.J.,
Black C.M.,
Verzijl N.,
DeGroot J.,
Hanemaaijer R.,
TeKoppele J.M.,
Huizinga T.W.J.,
Bank R.A.;
"Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis.";
J. Biol. Chem. 278:40967-40972(2003).
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[6]
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VARIANT BRKS2 HIS-598.
DOI=10.1002/ajmg.a.30231; PubMed=15523624 [NCBI, ExPASy, EBI, Israel, Japan]
Ha-Vinh R.,
Alanay Y.,
Bank R.A.,
Campos-Xavier A.B.,
Zankl A.,
Superti-Furga A.,
Bonafe L.;
"Phenotypic and molecular characterization of Bruck syndrome (osteogenesis imperfecta with contractures of the large joints) caused by a recessive mutation in PLOD2.";
Am. J. Med. Genet. A 131:115-120(2004).
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- FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
- CATALYTIC ACTIVITY: Procollagen L-lysine + 2-oxoglutarate + O2 = procollagen 5-hydroxy-L-lysine + succinate + CO2.
- COFACTOR: Iron (By similarity).
- COFACTOR: Ascorbate (By similarity).
- SUBUNIT: Homodimer (By similarity).
- INTERACTION:
Q9Y230:RUVBL2; NbExp=1; IntAct=EBI-1047459, EBI-352939;
- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side.
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
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| Name | 2 |
| Synonyms | A |
| Isoform ID | O00469-2 |
| Features which should be applied to build the isoform sequence: VSP_013467. |
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- TISSUE SPECIFICITY: Highly expressed in pancreas and muscle. Isoform 1 and isoform 2 are expressed in the majority of the examined cell types. Isoform 2 is specifically expressed in skin, lung, dura and aorta.
- DISEASE: Defects in PLOD2 are the cause of Bruck syndrome 2 (BRKS2) [MIM:609220]. Bruck syndrome [MIM:259450], also known as osteogenesis imperfecta with congenital joint contractures, is an autosomal recessive disease characterized by generalized osteopenia, joint contractures at birth, fragile bones and short stature. It can be distinguished from osteogenesis imperfecta by the absence of hearing loss and dentinogenesis imperfecta, and by the presence of clubfoot and congenital joint limitations. The molecular defect is an aberrant cross-linking of bone collagen, due to underhydroxylation of lysine residues within the telopeptides of type I collagen, whereas the lysine residues in the triple helix are normal.
- SIMILARITY: Contains 1 PKHD (prolyl/lysyl hydroxylase) domain.
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