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Protein

Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1

Gene

PLOD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 bindingi656 – 6561Iron
Metal bindingi658 – 6581Iron
Metal bindingi708 – 7081Iron
Active sitei718 – 7181Sequence Analysis

GO - Molecular functioni

GO - Biological processi

  • cellular protein modification process Source: UniProtKB
  • epidermis development Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • hydroxylysine biosynthetic process Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • response to hypoxia Source: UniProtKB
Complete GO annotation...

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9081. PLOD1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Ehlers-Danlos syndrome 6 (EDS6)6 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:225400
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. 1 Publication

Keywords - Diseasei

Disease mutation, Ehlers-Danlos syndrome

Organism-specific databases

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

Chemistry

DrugBankiDB00139. Succinic acid.
DB00126. Vitamin C.

Polymorphism and mutation databases

BioMutaiPLOD1.
DMDMi78099790.

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

BgeeiQ02809.
CleanExiHS_PLOD1.
ExpressionAtlasiQ02809. baseline and differential.
GenevestigatoriQ02809.

Organism-specific databases

HPAiHPA049137.
HPA055799.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi111366. 32 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.
GeneTreeiENSGT00550000074427.
HOGENOMiHOG000231099.
HOVERGENiHBG053618.
InParanoidiQ02809.
KOiK00473.
OMAiIGDEALP.
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. AlignAdd to basket

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

        10         20         30         40         50
MRPLLLLALL GWLLLAEAKG DAKPEDNLLV LTVATKETEG FRRFKRSAQF
60 70 80 90 100
FNYKIQALGL GEDWNVEKGT SAGGGQKVRL LKKALEKHAD KEDLVILFAD
110 120 130 140 150
SYDVLFASGP RELLKKFRQA RSQVVFSAEE LIYPDRRLET KYPVVSDGKR
160 170 180 190 200
FLGSGGFIGY APNLSKLVAE WEGQDSDSDQ LFYTKIFLDP EKREQINITL
210 220 230 240 250
DHRCRIFQNL DGALDEVVLK FEMGHVRARN LAYDTLPVLI HGNGPTKLQL
260 270 280 290 300
NYLGNYIPRF WTFETGCTVC DEGLRSLKGI GDEALPTVLV GVFIEQPTPF
310 320 330 340 350
VSLFFQRLLR LHYPQKHMRL FIHNHEQHHK AQVEEFLAQH GSEYQSVKLV
360 370 380 390 400
GPEVRMANAD ARNMGADLCR QDRSCTYYFS VDADVALTEP NSLRLLIQQN
410 420 430 440 450
KNVIAPLMTR HGRLWSNFWG ALSADGYYAR SEDYVDIVQG RRVGVWNVPY
460 470 480 490 500
ISNIYLIKGS ALRGELQSSD LFHHSKLDPD MAFCANIRQQ DVFMFLTNRH
510 520 530 540 550
TLGHLLSLDS YRTTHLHNDL WEVFSNPEDW KEKYIHQNYT KALAGKLVET
560 570 580 590 600
PCPDVYWFPI FTEVACDELV EEMEHFGQWS LGNNKDNRIQ GGYENVPTID
610 620 630 640 650
IHMNQIGFER EWHKFLLEYI APMTEKLYPG YYTRAQFDLA FVVRYKPDEQ
660 670 680 690 700
PSLMPHHDAS TFTINIALNR VGVDYEGGGC RFLRYNCSIR APRKGWTLMH
710 720
PGRLTHYHEG LPTTRGTRYI AVSFVDP
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:
EMBLi
GenBanki
DDBJi
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. [Q02809-1]
PIRiA38206.
RefSeqiNP_000293.2. NM_000302.3. [Q02809-1]
UniGeneiHs.75093.

Genome annotation databases

EnsembliENST00000196061; ENSP00000196061; ENSG00000083444. [Q02809-1]
GeneIDi5351.
KEGGihsa:5351.
UCSCiuc001atm.3. human. [Q02809-1]
uc010obb.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q02809-1]
PIRiA38206.
RefSeqiNP_000293.2. NM_000302.3. [Q02809-1]
UniGeneiHs.75093.

3D structure databases

ProteinModelPortaliQ02809.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111366. 32 interactions.
IntActiQ02809. 14 interactions.
MINTiMINT-1134973.
STRINGi9606.ENSP00000196061.

Chemistry

DrugBankiDB00139. Succinic acid.
DB00126. Vitamin C.

PTM databases

PhosphoSiteiQ02809.

Polymorphism and mutation databases

BioMutaiPLOD1.
DMDMi78099790.

Proteomic databases

MaxQBiQ02809.
PaxDbiQ02809.
PeptideAtlasiQ02809.
PRIDEiQ02809.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000196061; ENSP00000196061; ENSG00000083444. [Q02809-1]
GeneIDi5351.
KEGGihsa:5351.
UCSCiuc001atm.3. human. [Q02809-1]
uc010obb.2. human.

Organism-specific databases

CTDi5351.
GeneCardsiGC01P011994.
GeneReviewsiPLOD1.
HGNCiHGNC:9081. PLOD1.
HPAiHPA049137.
HPA055799.
MIMi153454. gene.
225400. phenotype.
neXtProtiNX_Q02809.
Orphaneti1900. Ehlers-Danlos syndrome, kyphoscoliotic type.
PharmGKBiPA33411.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG311199.
GeneTreeiENSGT00550000074427.
HOGENOMiHOG000231099.
HOVERGENiHBG053618.
InParanoidiQ02809.
KOiK00473.
OMAiIGDEALP.
OrthoDBiEOG79PJNP.
PhylomeDBiQ02809.
TreeFamiTF313826.

Enzyme and pathway databases

ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

ChiTaRSiPLOD1. human.
GenomeRNAii5351.
NextBioi20742.
PROiQ02809.
SOURCEiSearch...

Gene expression databases

BgeeiQ02809.
CleanExiHS_PLOD1.
ExpressionAtlasiQ02809. baseline and differential.
GenevestigatoriQ02809.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. 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: May 27, 2015
This is version 175 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.