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Q02809

- PLOD1_HUMAN

UniProt

Q02809 - PLOD1_HUMAN

Protein

Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1

Gene

PLOD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (25 Oct 2005)
      Previous versions | rss
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    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

    Iron.
    Ascorbate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi656 – 6561Iron
    Metal bindingi658 – 6581Iron
    Metal bindingi708 – 7081Iron
    Active sitei718 – 7181Sequence 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: UniProtKB-EC
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein modification process Source: UniProtKB
    2. epidermis development Source: UniProtKB
    3. extracellular matrix organization Source: Reactome
    4. hydroxylysine biosynthetic process Source: UniProtKB
    5. oxidation-reduction process Source: UniProtKB
    6. response to hypoxia Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Ligandi

    Iron, Metal-binding, Vitamin C

    Enzyme and pathway databases

    ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 (EC:1.14.11.4)
    Alternative name(s):
    Lysyl hydroxylase 1
    Short name:
    LH1
    Gene namesi
    Name:PLOD1
    Synonyms:LLH, PLOD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9081. PLOD1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. rough endoplasmic reticulum membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Ehlers-Danlos syndrome 6 (EDS6) [MIM:225400]: A connective tissue disorder characterized by generalized joint hypermobility, hyperextensible skin, atrophic cutaneous scars due to tissue fragility, progressive kyphoscoliosis already present at birth, ocular manifestations, arterial rupture, easy bruising, severe neonatal muscle hypotonia and delayed motor development.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti367 – 3715Missing in EDS6. 1 Publication
    VAR_009269
    Natural varianti446 – 4461W → G in EDS6. 1 Publication
    VAR_023466
    Natural varianti532 – 5321Missing in EDS6. 1 Publication
    VAR_006354
    Natural varianti612 – 6121W → C in EDS6. 1 Publication
    VAR_006355
    Natural varianti667 – 6671A → T in EDS6. 1 Publication
    Corresponds to variant rs199730384 [ dbSNP | Ensembl ].
    VAR_023467
    Natural varianti678 – 6781G → R in EDS6. 1 Publication
    VAR_006356
    Natural varianti706 – 7061H → R in EDS6. 1 Publication
    VAR_023468

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi369 – 3691C → A: Loss of activity. 2 Publications

    Keywords - Diseasei

    Disease mutation, Ehlers-Danlos syndrome

    Organism-specific databases

    MIMi225400. phenotype.
    Orphaneti1900. Ehlers-Danlos syndrome, kyphoscoliotic type.
    PharmGKBiPA33411.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Chaini19 – 727709Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1PRO_0000024678Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi197 – 1971N-linked (GlcNAc...)Curated
    Glycosylationi538 – 5381N-linked (GlcNAc...)Curated
    Glycosylationi686 – 6861N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ02809.
    PaxDbiQ02809.
    PeptideAtlasiQ02809.
    PRIDEiQ02809.

    PTM databases

    PhosphoSiteiQ02809.

    Expressioni

    Gene expression databases

    ArrayExpressiQ02809.
    BgeeiQ02809.
    CleanExiHS_PLOD1.
    GenevestigatoriQ02809.

    Organism-specific databases

    HPAiHPA049137.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi111366. 31 interactions.
    IntActiQ02809. 14 interactions.
    MINTiMINT-1134973.
    STRINGi9606.ENSP00000196061.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02809.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini636 – 72792Fe2OG dioxygenasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG311199.
    HOGENOMiHOG000231099.
    HOVERGENiHBG053618.
    InParanoidiQ02809.
    KOiK00473.
    OrthoDBiEOG79PJNP.
    PhylomeDBiQ02809.
    TreeFamiTF313826.

    Family and domain databases

    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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q02809-1) [UniParc]FASTAAdd to Basket

    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

    MRPLLLLALL GWLLLAEAKG DAKPEDNLLV LTVATKETEG FRRFKRSAQF    50
    FNYKIQALGL GEDWNVEKGT SAGGGQKVRL LKKALEKHAD KEDLVILFAD 100
    SYDVLFASGP RELLKKFRQA RSQVVFSAEE LIYPDRRLET KYPVVSDGKR 150
    FLGSGGFIGY APNLSKLVAE WEGQDSDSDQ LFYTKIFLDP EKREQINITL 200
    DHRCRIFQNL DGALDEVVLK FEMGHVRARN LAYDTLPVLI HGNGPTKLQL 250
    NYLGNYIPRF WTFETGCTVC DEGLRSLKGI GDEALPTVLV GVFIEQPTPF 300
    VSLFFQRLLR LHYPQKHMRL FIHNHEQHHK AQVEEFLAQH GSEYQSVKLV 350
    GPEVRMANAD ARNMGADLCR QDRSCTYYFS VDADVALTEP NSLRLLIQQN 400
    KNVIAPLMTR HGRLWSNFWG ALSADGYYAR SEDYVDIVQG RRVGVWNVPY 450
    ISNIYLIKGS ALRGELQSSD LFHHSKLDPD MAFCANIRQQ DVFMFLTNRH 500
    TLGHLLSLDS YRTTHLHNDL WEVFSNPEDW KEKYIHQNYT KALAGKLVET 550
    PCPDVYWFPI FTEVACDELV EEMEHFGQWS LGNNKDNRIQ GGYENVPTID 600
    IHMNQIGFER EWHKFLLEYI APMTEKLYPG YYTRAQFDLA FVVRYKPDEQ 650
    PSLMPHHDAS TFTINIALNR VGVDYEGGGC RFLRYNCSIR APRKGWTLMH 700
    PGRLTHYHEG LPTTRGTRYI AVSFVDP 727
    Length:727
    Mass (Da):83,550
    Last modified:October 25, 2005 - v2
    Checksum:i6C3E0C11B15D598C
    GO
    Isoform 2 (identifier: Q02809-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         25-25: E → EAPCCQEGLRAGGSGSLHLGRDFTVLAGARGSPSPSVSSIPRFWIPGS

    Note: No experimental confirmation available.

    Show »
    Length:774
    Mass (Da):88,273
    Checksum:i27DBE64A45B2A163
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671E → D.
    Corresponds to variant rs7551068 [ dbSNP | Ensembl ].
    VAR_032754
    Natural varianti84 – 841A → T.
    Corresponds to variant rs34878020 [ dbSNP | Ensembl ].
    VAR_032755
    Natural varianti99 – 991A → T.2 Publications
    Corresponds to variant rs7551175 [ dbSNP | Ensembl ].
    VAR_014220
    Natural varianti120 – 1201A → S.1 Publication
    Corresponds to variant rs2273285 [ dbSNP | Ensembl ].
    VAR_032756
    Natural varianti123 – 1231Q → H in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035479
    Natural varianti367 – 3715Missing in EDS6. 1 Publication
    VAR_009269
    Natural varianti446 – 4461W → G in EDS6. 1 Publication
    VAR_023466
    Natural varianti532 – 5321Missing in EDS6. 1 Publication
    VAR_006354
    Natural varianti612 – 6121W → C in EDS6. 1 Publication
    VAR_006355
    Natural varianti667 – 6671A → T in EDS6. 1 Publication
    Corresponds to variant rs199730384 [ dbSNP | Ensembl ].
    VAR_023467
    Natural varianti678 – 6781G → R in EDS6. 1 Publication
    VAR_006356
    Natural varianti706 – 7061H → R in EDS6. 1 Publication
    VAR_023468

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei25 – 251E → EAPCCQEGLRAGGSGSLHLG RDFTVLAGARGSPSPSVSSI PRFWIPGS in isoform 2. 1 PublicationVSP_056300

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06419 mRNA. Translation: AAA60116.1.
    AF490527
    , AF490514, AF490515, AF490516, AF490517, AF490518, AF490519, AF490520, AF490521, AF490522, AF490523, AF490524, AF490525, AF490526 Genomic DNA. Translation: AAM12752.1.
    AK299150 mRNA. Translation: BAG61199.1.
    AK316285 mRNA. Translation: BAH14656.1.
    AL096840 Genomic DNA. Translation: CAC19722.1.
    BC016657 mRNA. Translation: AAH16657.1.
    CCDSiCCDS142.1.
    PIRiA38206.
    RefSeqiNP_000293.2. NM_000302.3.
    UniGeneiHs.75093.

    Genome annotation databases

    EnsembliENST00000196061; ENSP00000196061; ENSG00000083444.
    ENST00000376369; ENSP00000365548; ENSG00000083444.
    GeneIDi5351.
    KEGGihsa:5351.
    UCSCiuc001atm.3. human.

    Polymorphism databases

    DMDMi78099790.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06419 mRNA. Translation: AAA60116.1 .
    AF490527
    , AF490514 , AF490515 , AF490516 , AF490517 , AF490518 , AF490519 , AF490520 , AF490521 , AF490522 , AF490523 , AF490524 , AF490525 , AF490526 Genomic DNA. Translation: AAM12752.1 .
    AK299150 mRNA. Translation: BAG61199.1 .
    AK316285 mRNA. Translation: BAH14656.1 .
    AL096840 Genomic DNA. Translation: CAC19722.1 .
    BC016657 mRNA. Translation: AAH16657.1 .
    CCDSi CCDS142.1.
    PIRi A38206.
    RefSeqi NP_000293.2. NM_000302.3.
    UniGenei Hs.75093.

    3D structure databases

    ProteinModelPortali Q02809.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111366. 31 interactions.
    IntActi Q02809. 14 interactions.
    MINTi MINT-1134973.
    STRINGi 9606.ENSP00000196061.

    Chemistry

    DrugBanki DB00350. Minoxidil.
    DB00139. Succinic acid.
    DB00126. Vitamin C.

    PTM databases

    PhosphoSitei Q02809.

    Polymorphism databases

    DMDMi 78099790.

    Proteomic databases

    MaxQBi Q02809.
    PaxDbi Q02809.
    PeptideAtlasi Q02809.
    PRIDEi Q02809.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000196061 ; ENSP00000196061 ; ENSG00000083444 .
    ENST00000376369 ; ENSP00000365548 ; ENSG00000083444 .
    GeneIDi 5351.
    KEGGi hsa:5351.
    UCSCi uc001atm.3. human.

    Organism-specific databases

    CTDi 5351.
    GeneCardsi GC01P011994.
    GeneReviewsi PLOD1.
    HGNCi HGNC:9081. PLOD1.
    HPAi HPA049137.
    MIMi 153454. gene.
    225400. phenotype.
    neXtProti NX_Q02809.
    Orphaneti 1900. Ehlers-Danlos syndrome, kyphoscoliotic type.
    PharmGKBi PA33411.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG311199.
    HOGENOMi HOG000231099.
    HOVERGENi HBG053618.
    InParanoidi Q02809.
    KOi K00473.
    OrthoDBi EOG79PJNP.
    PhylomeDBi Q02809.
    TreeFami TF313826.

    Enzyme and pathway databases

    Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.

    Miscellaneous databases

    ChiTaRSi PLOD1. human.
    GenomeRNAii 5351.
    NextBioi 20742.
    PROi Q02809.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02809.
    Bgeei Q02809.
    CleanExi HS_PLOD1.
    Genevestigatori Q02809.

    Family and domain databases

    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

    1. "Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3-p36.2."
      Hautala T., Byers M.G., Eddy R.L., Shows T.B., Kivirikko K.I., Myllylae R.
      Genomics 13:62-69(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 19-28 AND 332-34, VARIANT THR-99.
      Tissue: Placenta.
    2. "Structure and expression of the human lysyl hydroxylase gene (PLOD): introns 9 and 16 contain Alu sequences at the sites of recombination in Ehlers-Danlos syndrome type VI patients."
      Heikkinen J., Hautala T., Kivirikko K.I., Myllylae R.
      Genomics 24:464-471(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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 2).
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(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] (ISOFORM 1), VARIANTS THR-99 AND SER-120.
      Tissue: Skin.
    6. "Site-directed mutagenesis of human lysyl hydroxylase expressed in insect cells. Identification of histidine residues and an aspartic acid residue critical for catalytic activity."
      Pirskanen A., Kaimio A.M., Myllylae R., Kivirikko K.I.
      J. Biol. Chem. 271:9398-9402(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "A patient with Ehlers-Danlos syndrome type VI is a compound heterozygote for mutations in the lysyl hydroxylase gene."
      Ha V.T., Marshall M.K., Elsas L.J., Pinnell S.R., Yeowell H.N.
      J. Clin. Invest. 93:1716-1721(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDS6 GLU-532 DEL AND ARG-678.
    9. "Ehlers-Danlos syndrome type VI: lysyl hydroxylase deficiency due to a novel point mutation (W612C)."
      Brinckmann J., Acil Y., Feshchenko S., Katzer E., Brenner R., Kulozik A., Kugler S.
      Arch. Dermatol. Res. 290:181-186(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS6 CYS-612.
    10. "Deletion of cysteine 369 in lysyl hydroxylase 1 eliminates enzyme activity and causes Ehlers-Danlos syndrome type VI."
      Yeowell H.N., Allen J.D., Walker L.C., Overstreet M.A., Murad S., Thai S.F.
      Matrix Biol. 19:37-46(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS6 367-ASP--GLN-371 DEL, MUTAGENESIS OF CYS-369.
    11. "Nevo syndrome is allelic to the kyphoscoliotic type of the Ehlers-Danlos syndrome (EDS VIA)."
      Giunta C., Randolph A., Al-Gazali L.I., Brunner H.G., Kraenzlin M.E., Steinmann B.
      Am. J. Med. Genet. A 133:158-164(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN EDS6.
    12. "A novel mutation in the lysyl hydroxylase 1 gene causes decreased lysyl hydroxylase activity in an Ehlers-Danlos VIA patient."
      Walker L.C., Overstreet M.A., Siddiqui A., De Paepe A., Ceylaner G., Malfait F., Symoens S., Atsawasuwan P., Yamauchi M., Ceylaner S., Bank R.A., Yeowell H.N.
      J. Invest. Dermatol. 124:914-918(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS6 GLY-446.
    13. "Mutation analysis of the PLOD1 gene: an efficient multistep approach to the molecular diagnosis of the kyphoscoliotic type of Ehlers-Danlos syndrome (EDS VIA)."
      Giunta C., Randolph A., Steinmann B.
      Mol. Genet. Metab. 86:269-276(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDS6 THR-667 AND ARG-706.
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-123.

    Entry informationi

    Entry nameiPLOD1_HUMAN
    AccessioniPrimary (citable) accession number: Q02809
    Secondary accession number(s): B4DR87, Q96AV9, Q9H132
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: October 25, 2005
    Last modified: October 1, 2014
    This is version 169 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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