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O00469

- PLOD2_HUMAN

UniProt

O00469 - PLOD2_HUMAN

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Protein

Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2

Gene

PLOD2

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

Functioni

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 activityi

L-lysine-[procollagen] + 2-oxoglutarate + O2 = (2S,5R)-5-hydroxy-L-lysine-[procollagen] + succinate + CO2.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi666 – 6661IronPROSITE-ProRule annotation
Metal bindingi668 – 6681IronPROSITE-ProRule annotation
Metal bindingi718 – 7181IronPROSITE-ProRule annotation
Active sitei728 – 7281Sequence Analysis

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. L-ascorbic acid binding Source: UniProtKB-KW
  3. procollagen-lysine 5-dioxygenase activity Source: ProtInc

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. extracellular matrix organization Source: Reactome
  3. response to hypoxia Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding, Vitamin C

Enzyme and pathway databases

BRENDAi1.14.11.4. 2681.
ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.

Names & Taxonomyi

Protein namesi
Recommended name:
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 (EC:1.14.11.4)
Alternative name(s):
Lysyl hydroxylase 2
Short name:
LH2
Gene namesi
Name:PLOD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:9082. PLOD2.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: ProtInc
  2. endoplasmic reticulum membrane Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Bruck syndrome 2 (BRKS2) [MIM:609220]: An autosomal recessive disease characterized by generalized osteopenia, congenital joint contractures, fragile bones with onset of fractures in infancy or early childhood, short stature, severe limb deformity, progressive scoliosis, and pterygia. It is distinguished from osteogenesis imperfecta by the absence of hearing loss and dentinogenesis imperfecta, and by the presence of clubfoot and congenital joint limitations.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry. The molecular defect leading to Bruck syndrome 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.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti598 – 5981R → H in BRKS2. 1 Publication
VAR_022164
Natural varianti601 – 6011G → V in BRKS2. 1 Publication
VAR_022165
Natural varianti608 – 6081T → I in BRKS2. 1 Publication
VAR_022166
PLOD2 mutations give rise to a broad variety of phenotypes with variable degrees of severity of bone fragility and joint contractures. Disease-associated mutations have been found in patients with autosomal recessive osteogenesis imperfecta (AR-OI) (PubMed:22689593).1 Publication

Keywords - Diseasei

Disease mutation, Osteogenesis imperfecta

Organism-specific databases

MIMi609220. phenotype.
Orphaneti2771. Bruck syndrome.
PharmGKBiPA33412.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 737712Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2PRO_0000024683Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)1 Publication
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
Modified residuei320 – 3201Phosphothreonine1 Publication
Modified residuei323 – 3231Phosphotyrosine1 Publication
Glycosylationi365 – 3651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi522 – 5221N-linked (GlcNAc...)1 Publication
Glycosylationi696 – 6961N-linked (GlcNAc...)Sequence Analysis
Modified residuei704 – 7041N6-succinyllysineBy similarity
Glycosylationi725 – 7251N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO00469.
PaxDbiO00469.
PRIDEiO00469.

PTM databases

PhosphoSiteiO00469.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiO00469.
CleanExiHS_PLOD2.
ExpressionAtlasiO00469. baseline and differential.
GenevestigatoriO00469.

Organism-specific databases

HPAiCAB025898.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi111367. 43 interactions.
IntActiO00469. 6 interactions.
STRINGi9606.ENSP00000282903.

Structurei

3D structure databases

ProteinModelPortaliO00469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini644 – 73794Fe2OG dioxygenasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG311199.
GeneTreeiENSGT00550000074427.
HOGENOMiHOG000231099.
HOVERGENiHBG053618.
InParanoidiO00469.
KOiK13645.
OMAiLFIHNKE.
OrthoDBiEOG79PJNP.
PhylomeDBiO00469.
TreeFamiTF313826.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR029044. Nucleotide-diphossugar_trans.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR001006. Procol_lys_dOase.
[Graphical view]
PfamiPF03171. 2OG-FeII_Oxy. 1 hit.
[Graphical view]
SMARTiSM00702. P4Hc. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS51471. FE2OG_OXY. 1 hit.
PS01325. LYS_HYDROXYLASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O00469-1) [UniParc]FASTAAdd to Basket

Also known as: A

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGGCTVKPQL LLLALVLHPW NPCLGADSEK PSSIPTDKLL VITVATKESD
60 70 80 90 100
GFHRFMQSAK YFNYTVKVLG QGEEWRGGDG INSIGGGQKV RLMKEVMEHY
110 120 130 140 150
ADQDDLVVMF TECFDVIFAG GPEEVLKKFQ KANHKVVFAA DGILWPDKRL
160 170 180 190 200
ADKYPVVHIG KRYLNSGGFI GYAPYVNRIV QQWNLQDNDD DQLFYTKVYI
210 220 230 240 250
DPLKREAINI TLDHKCKIFQ TLNGAVDEVV LKFENGKARA KNTFYETLPV
260 270 280 290 300
AINGNGPTKI LLNYFGNYVP NSWTQDNGCT LCEFDTVDLS AVDVHPNVSI
310 320 330 340 350
GVFIEQPTPF LPRFLDILLT LDYPKEALKL FIHNKEVYHE KDIKVFFDKA
360 370 380 390 400
KHEIKTIKIV GPEENLSQAE ARNMGMDFCR QDEKCDYYFS VDADVVLTNP
410 420 430 440 450
RTLKILIEQN RKIIAPLVTR HGKLWSNFWG ALSPDGYYAR SEDYVDIVQG
460 470 480 490 500
NRVGVWNVPY MANVYLIKGK TLRSEMNERN YFVRDKLDPD MALCRNAREM
510 520 530 540 550
GVFMYISNRH EFGRLLSTAN YNTSHYNNDL WQIFENPVDW KEKYINRDYS
560 570 580 590 600
KIFTENIVEQ PCPDVFWFPI FSEKACDELV EEMEHYGKWS GGKHHDSRIS
610 620 630 640 650
GGYENVPTDD IHMKQVDLEN VWLHFIREFI APVTLKVFAG YYTKGFALLN
660 670 680 690 700
FVVKYSPERQ RSLRPHHDAS TFTINIALNN VGEDFQGGGC KFLRYNCSIE
710 720 730
SPRKGWSFMH PGRLTHLHEG LPVKNGTRYI AVSFIDP
Length:737
Mass (Da):84,686
Last modified:April 26, 2005 - v2
Checksum:iC9AEA79A574D6B66
GO
Isoform 2 (identifier: O00469-2) [UniParc]FASTAAdd to Basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     500-500: M → MTLQREKDSPTPETFQMLSPPK

Show »
Length:758
Mass (Da):87,098
Checksum:iED81104976B69FC7
GO
Isoform 3 (identifier: O00469-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MGGCTVKPQLLLLALVLHPWNPCLGADSEKPSSIPT → MLENHILHKRIYILTFFSQQIFILCHAHFIFFFTVR
     37-376: Missing.
     500-500: M → MTLQREKDSPTPETFQMLSPPK

Note: No experimental confirmation available

Show »
Length:418
Mass (Da):49,142
Checksum:iA70BCF41D3E032EE
GO

Sequence cautioni

The sequence BAD93116.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti624 – 6241H → D in AAB58363. (PubMed:9054364)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti598 – 5981R → H in BRKS2. 1 Publication
VAR_022164
Natural varianti601 – 6011G → C in AR-OI; probable disease-associated mutation found in patients with osteogenesis imperfecta. 1 Publication
VAR_069531
Natural varianti601 – 6011G → V in BRKS2. 1 Publication
VAR_022165
Natural varianti608 – 6081T → I in BRKS2. 1 Publication
VAR_022166

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636MGGCT…SSIPT → MLENHILHKRIYILTFFSQQ IFILCHAHFIFFFTVR in isoform 3. 1 PublicationVSP_057221Add
BLAST
Alternative sequencei37 – 376340Missing in isoform 3. 1 PublicationVSP_057222Add
BLAST
Alternative sequencei500 – 5001M → MTLQREKDSPTPETFQMLSP PK in isoform 2 and isoform 3. 3 PublicationsVSP_013467

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84573 mRNA. Translation: AAB58363.1.
AK125700 mRNA. Translation: BAG54235.1.
AB209879 mRNA. Translation: BAD93116.1. Different initiation.
AC092982 Genomic DNA. No translation available.
AC107021 Genomic DNA. No translation available.
BC037169 mRNA. Translation: AAH37169.1.
CCDSiCCDS3131.1. [O00469-1]
CCDS3132.1. [O00469-2]
PIRiA59144.
RefSeqiNP_000926.2. NM_000935.2. [O00469-1]
NP_891988.1. NM_182943.2. [O00469-2]
UniGeneiHs.477866.

Genome annotation databases

EnsembliENST00000282903; ENSP00000282903; ENSG00000152952. [O00469-2]
ENST00000360060; ENSP00000353170; ENSG00000152952. [O00469-1]
GeneIDi5352.
KEGGihsa:5352.
UCSCiuc003evr.1. human. [O00469-2]
uc003evs.1. human. [O00469-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Osteogenesis imperfecta variant database

Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 (PLOD2)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84573 mRNA. Translation: AAB58363.1 .
AK125700 mRNA. Translation: BAG54235.1 .
AB209879 mRNA. Translation: BAD93116.1 . Different initiation.
AC092982 Genomic DNA. No translation available.
AC107021 Genomic DNA. No translation available.
BC037169 mRNA. Translation: AAH37169.1 .
CCDSi CCDS3131.1. [O00469-1 ]
CCDS3132.1. [O00469-2 ]
PIRi A59144.
RefSeqi NP_000926.2. NM_000935.2. [O00469-1 ]
NP_891988.1. NM_182943.2. [O00469-2 ]
UniGenei Hs.477866.

3D structure databases

ProteinModelPortali O00469.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111367. 43 interactions.
IntActi O00469. 6 interactions.
STRINGi 9606.ENSP00000282903.

Chemistry

DrugBanki DB00126. Vitamin C.

PTM databases

PhosphoSitei O00469.

Proteomic databases

MaxQBi O00469.
PaxDbi O00469.
PRIDEi O00469.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000282903 ; ENSP00000282903 ; ENSG00000152952 . [O00469-2 ]
ENST00000360060 ; ENSP00000353170 ; ENSG00000152952 . [O00469-1 ]
GeneIDi 5352.
KEGGi hsa:5352.
UCSCi uc003evr.1. human. [O00469-2 ]
uc003evs.1. human. [O00469-1 ]

Organism-specific databases

CTDi 5352.
GeneCardsi GC03M145787.
HGNCi HGNC:9082. PLOD2.
HPAi CAB025898.
MIMi 601865. gene.
609220. phenotype.
neXtProti NX_O00469.
Orphaneti 2771. Bruck syndrome.
PharmGKBi PA33412.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG311199.
GeneTreei ENSGT00550000074427.
HOGENOMi HOG000231099.
HOVERGENi HBG053618.
InParanoidi O00469.
KOi K13645.
OMAi LFIHNKE.
OrthoDBi EOG79PJNP.
PhylomeDBi O00469.
TreeFami TF313826.

Enzyme and pathway databases

BRENDAi 1.14.11.4. 2681.
Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

ChiTaRSi PLOD2. human.
GenomeRNAii 5352.
NextBioi 20746.
PROi O00469.
SOURCEi Search...

Gene expression databases

Bgeei O00469.
CleanExi HS_PLOD2.
ExpressionAtlasi O00469. baseline and differential.
Genevestigatori O00469.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR029044. Nucleotide-diphossugar_trans.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR006620. Pro_4_hyd_alph.
IPR001006. Procol_lys_dOase.
[Graphical view ]
Pfami PF03171. 2OG-FeII_Oxy. 1 hit.
[Graphical view ]
SMARTi SM00702. P4Hc. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
PROSITEi PS51471. FE2OG_OXY. 1 hit.
PS01325. LYS_HYDROXYLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle."
    Valtavaara M., Papponen H., Pirttila A.M., Hiltunen K., Helander H., Myllylae R.
    J. Biol. Chem. 272:6831-6834(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  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] (ISOFORM 3).
    Tissue: Esophagus.
  3. "Homo sapiens protein coding cDNA."
    Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Aortic endothelium.
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Tissue specificity of a new splice form of the human lysyl hydroxylase 2 gene."
    Yeowell H.N., Walker L.C.
    Matrix Biol. 18:179-187(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Tissue: Skin fibroblast.
  6. "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] (ISOFORM 2).
    Tissue: Placenta.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320 AND TYR-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  8. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-209 AND ASN-522.
    Tissue: Liver.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: VARIANTS BRKS2 VAL-601 AND ILE-608.
  11. "Phenotypic and molecular characterization of Bruck syndrome (osteogenesis imperfecta with contractures of the large joints) caused by a recessive mutation in PLOD2."
    Ha-Vinh R., Alanay Y., Bank R.A., Campos-Xavier A.B., Zankl A., Superti-Furga A., Bonafe L.
    Am. J. Med. Genet. A 131:115-120(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BRKS2 HIS-598.
  12. "Mutations in PLOD2 cause autosomal-recessive connective tissue disorders within the Bruck syndrome--osteogenesis imperfecta phenotypic spectrum."
    Puig-Hervas M.T., Temtamy S., Aglan M., Valencia M., Martinez-Glez V., Ballesta-Martinez M.J., Lopez-Gonzalez V., Ashour A.M., Amr K., Pulido V., Guillen-Navarro E., Lapunzina P., Caparros-Martin J.A., Ruiz-Perez V.L.
    Hum. Mutat. 33:1444-1449(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AR-OI CYS-601.

Entry informationi

Entry nameiPLOD2_HUMAN
AccessioniPrimary (citable) accession number: O00469
Secondary accession number(s): B3KWS3, Q59ED2, Q8N170
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 26, 2005
Last modified: November 26, 2014
This is version 138 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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

Dasty 3