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Q99983

- OMD_HUMAN

UniProt

Q99983 - OMD_HUMAN

Protein

Osteomodulin

Gene

OMD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    May be implicated in biomineralization processes. Has a function in binding of osteoblasts via the alpha(V)beta(3)-integrin By similarity.By similarity

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cell adhesion Source: UniProtKB-KW
    3. glycosaminoglycan metabolic process Source: Reactome
    4. keratan sulfate biosynthetic process Source: Reactome
    5. keratan sulfate catabolic process Source: Reactome
    6. keratan sulfate metabolic process Source: Reactome
    7. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_121120. Keratan sulfate biosynthesis.
    REACT_121313. Keratan sulfate degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Osteomodulin
    Alternative name(s):
    Keratan sulfate proteoglycan osteomodulin
    Short name:
    KSPG osteomodulin
    Osteoadherin
    Short name:
    OSAD
    Gene namesi
    Name:OMD
    Synonyms:SLRR2C
    ORF Names:UNQ190/PRO216
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:8134. OMD.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. Golgi lumen Source: Reactome
    3. lysosomal lumen Source: Reactome
    4. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31921.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 421401OsteomodulinPRO_0000032754Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei22 – 221Sulfotyrosine1 Publication
    Modified residuei25 – 251Sulfotyrosine1 Publication
    Modified residuei31 – 311Sulfotyrosine1 Publication
    Modified residuei39 – 391Sulfotyrosine1 Publication
    Modified residuei51 – 511Sulfotyrosine1 Publication
    Modified residuei58 – 581Sulfotyrosine1 Publication
    Modified residuei77 – 771Sulfotyrosine1 Publication
    Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi321 ↔ 353By similarity
    Modified residuei416 – 4161Sulfotyrosine1 Publication
    Modified residuei417 – 4171Sulfotyrosine1 Publication

    Post-translational modificationi

    Binds keratan sulfate chains.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Proteoglycan, Sulfation

    Proteomic databases

    PaxDbiQ99983.
    PRIDEiQ99983.

    Expressioni

    Tissue specificityi

    Bone specific.

    Gene expression databases

    BgeeiQ99983.
    CleanExiHS_OMD.
    GenevestigatoriQ99983.

    Interactioni

    Subunit structurei

    Binds the alpha(V)beta(3)-integrin.By similarity

    Protein-protein interaction databases

    STRINGi9606.ENSP00000364700.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99983.
    SMRiQ99983. Positions 63-366.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 9139LRRNTAdd
    BLAST
    Repeati92 – 11322LRR 1Add
    BLAST
    Repeati116 – 12914LRR 2Add
    BLAST
    Repeati142 – 16423LRR 3Add
    BLAST
    Repeati165 – 18420LRR 4Add
    BLAST
    Repeati187 – 21024LRR 5Add
    BLAST
    Repeati213 – 23321LRR 6Add
    BLAST
    Repeati234 – 25522LRR 7Add
    BLAST
    Repeati258 – 28023LRR 8Add
    BLAST
    Repeati281 – 29414LRR 9Add
    BLAST
    Repeati301 – 32121LRR 10Add
    BLAST
    Repeati331 – 35323LRR 11Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi62 – 7817Cys-richAdd
    BLAST
    Compositional biasi385 – 40925Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Contains 11 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRNT domain.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4886.
    HOGENOMiHOG000234447.
    HOVERGENiHBG108061.
    InParanoidiQ99983.
    KOiK08124.
    OMAiFYIPRNL.
    OrthoDBiEOG741Z2B.
    PhylomeDBiQ99983.
    TreeFamiTF334562.

    Family and domain databases

    InterProiIPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view]
    PfamiPF13855. LRR_8. 2 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 8 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q99983-1 [UniParc]FASTAAdd to Basket

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    MGFLSPIYVI FFFFGVKVHC QYETYQWDED YDQEPDDDYQ TGFPFRQNVD    50
    YGVPFHQYTL GCVSECFCPT NFPSSMYCDN RKLKTIPNIP MHIQQLYLQF 100
    NEIEAVTANS FINATHLKEI NLSHNKIKSQ KIDYGVFAKL PNLLQLHLEH 150
    NNLEEFPFPL PKSLERLLLG YNEISKLQTN AMDGLVNLTM LDLCYNYLHD 200
    SLLKDKIFAK MEKLMQLNLC SNRLESMPPG LPSSLMYLSL ENNSISSIPE 250
    KYFDKLPKLH TLRMSHNKLQ DIPYNIFNLP NIVELSVGHN KLKQAFYIPR 300
    NLEHLYLQNN EIEKMNLTVM CPSIDPLHYH HLTYIRVDQN KLKEPISSYI 350
    FFCFPHIHTI YYGEQRSTNG QTIQLKTQVF RRFPDDDDES EDHDDPDNAH 400
    ESPEQEGAEG HFDLHYYENQ E 421
    Length:421
    Mass (Da):49,492
    Last modified:May 1, 1997 - v1
    Checksum:iCED47B2BC33BB872
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti200 – 2001D → G.
    Corresponds to variant rs34069871 [ dbSNP | Ensembl ].
    VAR_052014
    Natural varianti212 – 2121E → G.
    Corresponds to variant rs34413259 [ dbSNP | Ensembl ].
    VAR_052015
    Natural varianti221 – 2211S → N.
    Corresponds to variant rs34860658 [ dbSNP | Ensembl ].
    VAR_052016
    Natural varianti282 – 2821I → T.
    Corresponds to variant rs35779901 [ dbSNP | Ensembl ].
    VAR_052017
    Natural varianti353 – 3531C → W.
    Corresponds to variant rs34059114 [ dbSNP | Ensembl ].
    VAR_052018

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000114 mRNA. Translation: BAA19055.1.
    AB009589 Genomic DNA. Translation: BAA23982.1.
    AY358872 mRNA. Translation: AAQ89231.1.
    AL137848 Genomic DNA. Translation: CAI16696.1.
    CH471089 Genomic DNA. Translation: EAW62821.1.
    BC046356 mRNA. Translation: AAH46356.1.
    CCDSiCCDS6696.1.
    RefSeqiNP_005005.1. NM_005014.2.
    UniGeneiHs.94070.

    Genome annotation databases

    EnsembliENST00000375550; ENSP00000364700; ENSG00000127083.
    GeneIDi4958.
    KEGGihsa:4958.
    UCSCiuc004asd.4. human.

    Polymorphism databases

    DMDMi20138850.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000114 mRNA. Translation: BAA19055.1 .
    AB009589 Genomic DNA. Translation: BAA23982.1 .
    AY358872 mRNA. Translation: AAQ89231.1 .
    AL137848 Genomic DNA. Translation: CAI16696.1 .
    CH471089 Genomic DNA. Translation: EAW62821.1 .
    BC046356 mRNA. Translation: AAH46356.1 .
    CCDSi CCDS6696.1.
    RefSeqi NP_005005.1. NM_005014.2.
    UniGenei Hs.94070.

    3D structure databases

    ProteinModelPortali Q99983.
    SMRi Q99983. Positions 63-366.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000364700.

    Polymorphism databases

    DMDMi 20138850.

    Proteomic databases

    PaxDbi Q99983.
    PRIDEi Q99983.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375550 ; ENSP00000364700 ; ENSG00000127083 .
    GeneIDi 4958.
    KEGGi hsa:4958.
    UCSCi uc004asd.4. human.

    Organism-specific databases

    CTDi 4958.
    GeneCardsi GC09M095176.
    HGNCi HGNC:8134. OMD.
    neXtProti NX_Q99983.
    PharmGKBi PA31921.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000234447.
    HOVERGENi HBG108061.
    InParanoidi Q99983.
    KOi K08124.
    OMAi FYIPRNL.
    OrthoDBi EOG741Z2B.
    PhylomeDBi Q99983.
    TreeFami TF334562.

    Enzyme and pathway databases

    Reactomei REACT_121120. Keratan sulfate biosynthesis.
    REACT_121313. Keratan sulfate degradation.

    Miscellaneous databases

    GeneWikii OMD_(gene).
    GenomeRNAii 4958.
    NextBioi 19096.
    PROi Q99983.

    Gene expression databases

    Bgeei Q99983.
    CleanExi HS_OMD.
    Genevestigatori Q99983.

    Family and domain databases

    InterProi IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view ]
    Pfami PF13855. LRR_8. 2 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view ]
    SMARTi SM00369. LRR_TYP. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 8 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The cloning of a cDNA for novel genes expressed in human osteoblast."
      Ohno I., Hashimoto J., Takaoka K., Ochi T., Okubo K., Matsubara K.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Osteoblast.
    2. "Human osteomodulin gene: intron-exon junctions and chromosomal localization."
      Ohno I., Matsubara K., Okubo K.
      Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Brain.
    7. "Identification of tyrosine sulfation in extracellular leucine-rich repeat proteins using mass spectrometry."
      Onnerfjord P., Heathfield T.F., Heinegaard D.
      J. Biol. Chem. 279:26-33(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SULFATION AT TYR-22; TYR-25; TYR-31; TYR-39; TYR-51; TYR-58; TYR-77; TYR-416 AND TYR-417, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiOMD_HUMAN
    AccessioniPrimary (citable) accession number: Q99983
    Secondary accession number(s): Q5TBF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 11, 2002
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 128 of the entry and version 1 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 9
      Human chromosome 9: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3