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Q99983

- OMD_HUMAN

UniProt

Q99983 - OMD_HUMAN

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Protein

Osteomodulin

Gene

OMD

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

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
Complete GO annotation...

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. extracellular vesicular exosome Source: UniProtKB
  3. Golgi lumen Source: Reactome
  4. lysosomal lumen Source: Reactome
  5. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

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 61-364.
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.
GeneTreeiENSGT00760000118969.
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

« Hide

        10         20         30         40         50
MGFLSPIYVI FFFFGVKVHC QYETYQWDED YDQEPDDDYQ TGFPFRQNVD
60 70 80 90 100
YGVPFHQYTL GCVSECFCPT NFPSSMYCDN RKLKTIPNIP MHIQQLYLQF
110 120 130 140 150
NEIEAVTANS FINATHLKEI NLSHNKIKSQ KIDYGVFAKL PNLLQLHLEH
160 170 180 190 200
NNLEEFPFPL PKSLERLLLG YNEISKLQTN AMDGLVNLTM LDLCYNYLHD
210 220 230 240 250
SLLKDKIFAK MEKLMQLNLC SNRLESMPPG LPSSLMYLSL ENNSISSIPE
260 270 280 290 300
KYFDKLPKLH TLRMSHNKLQ DIPYNIFNLP NIVELSVGHN KLKQAFYIPR
310 320 330 340 350
NLEHLYLQNN EIEKMNLTVM CPSIDPLHYH HLTYIRVDQN KLKEPISSYI
360 370 380 390 400
FFCFPHIHTI YYGEQRSTNG QTIQLKTQVF RRFPDDDDES EDHDDPDNAH
410 420
ESPEQEGAEG HFDLHYYENQ E
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 61-364.
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.
GeneTreei ENSGT00760000118969.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 129 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