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Q99P68

- SOST_MOUSE

UniProt

Q99P68 - SOST_MOUSE

Protein

Sclerostin

Gene

Sost

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation.By similarity

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB-KW
    2. protein binding Source: MGI

    GO - Biological processi

    1. negative regulation of BMP signaling pathway Source: MGI
    2. negative regulation of canonical Wnt signaling pathway Source: MGI
    3. negative regulation of ossification Source: MGI
    4. negative regulation of Wnt signaling pathway Source: MGI
    5. ossification Source: MGI
    6. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Biological processi

    Wnt signaling pathway

    Keywords - Ligandi

    Heparin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sclerostin
    Gene namesi
    Name:Sost
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1921749. Sost.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: InterPro
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Mice were resistant to mechanical unloading-induced bone loss.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 211188SclerostinPRO_0000033178Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi51 – 511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi78 ↔ 1321 Publication
    Disulfide bondi92 ↔ 1461 Publication
    Disulfide bondi103 ↔ 1631 Publication
    Disulfide bondi107 ↔ 1651 Publication
    Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ99P68.

    Expressioni

    Gene expression databases

    CleanExiMM_SOST.
    GenevestigatoriQ99P68.

    Interactioni

    Subunit structurei

    Interacts with LRP4 (via the extracellular domain); the interaction facilitates the inhibition of Wnt signaling. Interacts with LRP5 (via the first two YWTD-EGF repeat domains); the interaction inhibits Wnt-mediated signaling. Interacts with LRP6.By similarity

    Protein-protein interaction databases

    BioGridi216800. 2 interactions.

    Structurei

    Secondary structure

    1
    211
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni72 – 765
    Beta strandi121 – 1233
    Beta strandi133 – 14513
    Beta strandi149 – 1513
    Beta strandi153 – 16412

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KD3NMR-A60-167[»]
    ProteinModelPortaliQ99P68.
    SMRiQ99P68. Positions 71-167.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99P68.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 17091CTCKAdd
    BLAST

    Sequence similaritiesi

    Belongs to the sclerostin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG40285.
    HOGENOMiHOG000252934.
    HOVERGENiHBG003729.
    InParanoidiQ99P68.
    KOiK16834.
    PhylomeDBiQ99P68.

    Family and domain databases

    InterProiIPR008835. Sclerostin/SOSTDC1.
    IPR015665. SOST.
    [Graphical view]
    PANTHERiPTHR14903. PTHR14903. 1 hit.
    PTHR14903:SF4. PTHR14903:SF4. 1 hit.
    PfamiPF05463. Sclerostin. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q99P68-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQPSLAPCLI CLLVHAAFCA VEGQGWQAFR NDATEVIPGL GEYPEPPPEN    50
    NQTMNRAENG GRPPHHPYDA KGVSEYSCRE LHYTRFLTDG PCRSAKPVTE 100
    LVCSGQCGPA RLLPNAIGRV KWWRPNGPDF RCIPDRYRAQ RVQLLCPGGA 150
    APRSRKVRLV ASCKCKRLTR FHNQSELKDF GPETARPQKG RKPRPGARGA 200
    KANQAELENA Y 211
    Length:211
    Mass (Da):23,443
    Last modified:June 1, 2001 - v1
    Checksum:iAEB094E358E34961
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti72 – 721G → D in BAB30678. (PubMed:16141072)Curated
    Sequence conflicti72 – 721G → D in AAK13452. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF326740 mRNA. Translation: AAK13455.1.
    AK017295 mRNA. Translation: BAB30678.1.
    AF326737 Genomic DNA. Translation: AAK13452.1.
    CCDSiCCDS25481.1.
    RefSeqiNP_077769.4. NM_024449.6.
    UniGeneiMm.265602.

    Genome annotation databases

    GeneIDi74499.
    KEGGimmu:74499.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF326740 mRNA. Translation: AAK13455.1 .
    AK017295 mRNA. Translation: BAB30678.1 .
    AF326737 Genomic DNA. Translation: AAK13452.1 .
    CCDSi CCDS25481.1.
    RefSeqi NP_077769.4. NM_024449.6.
    UniGenei Mm.265602.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KD3 NMR - A 60-167 [» ]
    ProteinModelPortali Q99P68.
    SMRi Q99P68. Positions 71-167.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 216800. 2 interactions.

    Proteomic databases

    PRIDEi Q99P68.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 74499.
    KEGGi mmu:74499.

    Organism-specific databases

    CTDi 50964.
    MGIi MGI:1921749. Sost.

    Phylogenomic databases

    eggNOGi NOG40285.
    HOGENOMi HOG000252934.
    HOVERGENi HBG003729.
    InParanoidi Q99P68.
    KOi K16834.
    PhylomeDBi Q99P68.

    Miscellaneous databases

    EvolutionaryTracei Q99P68.
    NextBioi 340962.
    PROi Q99P68.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_SOST.
    Genevestigatori Q99P68.

    Family and domain databases

    InterProi IPR008835. Sclerostin/SOSTDC1.
    IPR015665. SOST.
    [Graphical view ]
    PANTHERi PTHR14903. PTHR14903. 1 hit.
    PTHR14903:SF4. PTHR14903:SF4. 1 hit.
    Pfami PF05463. Sclerostin. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: 129/SvJ.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Head.
    3. "Sclerostin binds to LRP5/6 and antagonizes canonical Wnt signaling."
      Li X., Zhang Y., Kang H., Liu W., Liu P., Zhang J., Harris S.E., Wu D.
      J. Biol. Chem. 280:19883-19887(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRP5 AND LRP6.
    4. "Sclerostin mediates bone response to mechanical unloading through antagonizing Wnt/beta-catenin signaling."
      Lin C., Jiang X., Dai Z., Guo X., Weng T., Wang J., Li Y., Feng G., Gao X., He L.
      J. Bone Miner. Res. 24:1651-1661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    5. Cited for: STRUCTURE BY NMR OF 59-167, DISULFIDE BONDS.

    Entry informationi

    Entry nameiSOST_MOUSE
    AccessioniPrimary (citable) accession number: Q99P68
    Secondary accession number(s): Q9D3L7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3