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P10923

- OSTP_MOUSE

UniProt

P10923 - OSTP_MOUSE

Protein

Osteopontin

Gene

Spp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction.
    Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity.

    GO - Molecular functioni

    1. cytokine activity Source: UniProtKB
    2. extracellular matrix binding Source: MGI

    GO - Biological processi

    1. biomineral tissue development Source: UniProtKB-KW
    2. cell adhesion Source: UniProtKB-KW
    3. negative regulation of apoptotic process Source: UniProtKB
    4. neutrophil chemotaxis Source: MGI
    5. ossification Source: InterPro
    6. positive regulation of cell-substrate adhesion Source: MGI

    Keywords - Molecular functioni

    Cytokine

    Keywords - Biological processi

    Biomineralization, Cell adhesion

    Keywords - Ligandi

    Sialic acid

    Enzyme and pathway databases

    ReactomeiREACT_199052. Degradation of the extracellular matrix.
    REACT_216309. Integrin cell surface interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Osteopontin
    Alternative name(s):
    2AR
    Bone sialoprotein 1
    Calcium oxalate crystal growth inhibitor protein
    Early T-lymphocyte activation 1 protein
    Minopontin
    Secreted phosphoprotein 1
    Short name:
    SPP-1
    Gene namesi
    Name:Spp1
    Synonyms:Eta-1, Op, Spp-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:98389. Spp1.

    Subcellular locationi

    GO - Cellular componenti

    1. apical part of cell Source: MGI
    2. cytoplasm Source: MGI
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: UniProtKB-KW

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 294278OsteopontinPRO_0000020322Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241PhosphoserineBy similarity
    Modified residuei26 – 261PhosphoserineBy similarity
    Modified residuei27 – 271PhosphoserineBy similarity
    Modified residuei61 – 611PhosphoserineBy similarity
    Modified residuei62 – 621PhosphoserineBy similarity
    Modified residuei75 – 751PhosphoserineBy similarity
    Modified residuei77 – 771PhosphoserineBy similarity
    Glycosylationi78 – 781N-linked (GlcNAc...)Sequence Analysis
    Modified residuei80 – 801PhosphoserineBy similarity
    Modified residuei106 – 1061PhosphoserineBy similarity
    Modified residuei109 – 1091PhosphoserineBy similarity
    Modified residuei112 – 1121PhosphoserineBy similarity
    Modified residuei115 – 1151PhosphoserineBy similarity
    Modified residuei118 – 1181PhosphoserineBy similarity
    Glycosylationi123 – 1231O-linked (GalNAc...)By similarity
    Glycosylationi132 – 1321O-linked (GalNAc...)By similarity
    Glycosylationi137 – 1371O-linked (GalNAc...)By similarity
    Modified residuei170 – 1701PhosphothreonineBy similarity
    Modified residuei176 – 1761PhosphoserineBy similarity
    Modified residuei180 – 1801PhosphoserineBy similarity
    Modified residuei200 – 2001PhosphoserineBy similarity
    Modified residuei209 – 2091PhosphoserineBy similarity
    Modified residuei213 – 2131PhosphoserineBy similarity
    Modified residuei219 – 2191PhosphoserineBy similarity
    Modified residuei234 – 2341PhosphoserineBy similarity
    Modified residuei243 – 2431PhosphoserineBy similarity
    Modified residuei247 – 2471PhosphoserineBy similarity
    Modified residuei250 – 2501PhosphoserineBy similarity
    Modified residuei255 – 2551PhosphoserineBy similarity
    Modified residuei260 – 2601PhosphoserineBy similarity
    Modified residuei271 – 2711PhosphoserineBy similarity
    Modified residuei283 – 2831Phosphoserine2 Publications
    Modified residuei288 – 2881Phosphoserine1 Publication
    Modified residuei290 – 2901Phosphoserine2 Publications

    Post-translational modificationi

    Extensively phosphorylated by FAM20C in the extracellular medium at multiple sites within the S-x-E/pS motif.By similarity
    N- and O-glycosylated.

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP10923.
    PRIDEiP10923.

    PTM databases

    PhosphoSiteiP10923.

    Expressioni

    Gene expression databases

    ArrayExpressiP10923.
    BgeeiP10923.
    CleanExiMM_SPP1.
    GenevestigatoriP10923.

    Interactioni

    Subunit structurei

    Ligand for integrin alpha-V/beta-3.

    Protein-protein interaction databases

    BioGridi203467. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP10923.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi144 – 1463Cell attachment site

    Sequence similaritiesi

    Belongs to the osteopontin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG73598.
    HOGENOMiHOG000059656.
    HOVERGENiHBG001731.
    KOiK06250.
    PhylomeDBiP10923.
    TreeFamiTF350201.

    Family and domain databases

    InterProiIPR002038. Osteopontin.
    IPR019841. Osteopontin_CS.
    [Graphical view]
    PANTHERiPTHR10607. PTHR10607. 1 hit.
    PfamiPF00865. Osteopontin. 1 hit.
    [Graphical view]
    PRINTSiPR00216. OSTEOPONTIN.
    SMARTiSM00017. OSTEO. 1 hit.
    [Graphical view]
    PROSITEiPS00884. OSTEOPONTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P10923-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLAVICFCL FGIASSLPVK VTDSGSSEEK LYSLHPDPIA TWLVPDPSQK    50
    QNLLAPQNAV SSEEKDDFKQ ETLPSNSNES HDHMDDDDDD DDDDGDHAES 100
    EDSVDSDESD ESHHSDESDE TVTASTQADT FTPIVPTVDV PNGRGDSLAY 150
    GLRSKSRSFQ VSDEQYPDAT DEDLTSHMKS GESKESLDVI PVAQLLSMPS 200
    DQDNNGKGSH ESSQLDEPSL ETHRLEHSKE SQESADQSDV IDSQASSKAS 250
    LEHQSHKFHS HKDKLVLDPK SKEDDRYLKF RISHELESSS SEVN 294
    Length:294
    Mass (Da):32,459
    Last modified:July 1, 1989 - v1
    Checksum:i9D5F32D67ABC53EA
    GO

    Sequence cautioni

    The sequence AAH14284.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 431L → P in CAA34276. (PubMed:2787378)Curated
    Sequence conflicti99 – 991E → G in AAA57265. (PubMed:2722855)Curated
    Sequence conflicti100 – 1001S → N in AAH14284. (PubMed:15489334)Curated
    Sequence conflicti122 – 1221V → F in CAA32165. (PubMed:2726465)Curated
    Sequence conflicti122 – 1221V → F in AAH14284. (PubMed:15489334)Curated
    Sequence conflicti142 – 1421N → D in AAH14284. (PubMed:15489334)Curated
    Sequence conflicti171 – 1711D → Y in AAH14284. (PubMed:15489334)Curated
    Sequence conflicti188 – 1881D → N in AAH14284. (PubMed:15489334)Curated
    Sequence conflicti207 – 2071K → R in AAH14284. (PubMed:15489334)Curated
    Sequence conflicti224 – 2241R → S in AAH14284. (PubMed:15489334)Curated
    Sequence conflicti232 – 2321Q → H in AAH14284. (PubMed:15489334)Curated
    Sequence conflicti277 – 2771Y → H in AAH14284. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04806 mRNA. Translation: AAA57265.1.
    X16151 mRNA. Translation: CAA34276.1.
    X13986 mRNA. Translation: CAA32165.1.
    X51834 Genomic DNA. Translation: CAA36132.1.
    BC014284 mRNA. Translation: AAH14284.1. Different initiation.
    BC057858 mRNA. Translation: AAH57858.1.
    CCDSiCCDS19486.1.
    PIRiA37818.
    RefSeqiNP_001191162.1. NM_001204233.1.
    NP_033289.2. NM_009263.3.
    UniGeneiMm.288474.

    Genome annotation databases

    EnsembliENSMUST00000031243; ENSMUSP00000031243; ENSMUSG00000029304.
    ENSMUST00000112747; ENSMUSP00000108367; ENSMUSG00000029304.
    ENSMUST00000112748; ENSMUSP00000108368; ENSMUSG00000029304.
    GeneIDi20750.
    KEGGimmu:20750.
    UCSCiuc008yki.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04806 mRNA. Translation: AAA57265.1 .
    X16151 mRNA. Translation: CAA34276.1 .
    X13986 mRNA. Translation: CAA32165.1 .
    X51834 Genomic DNA. Translation: CAA36132.1 .
    BC014284 mRNA. Translation: AAH14284.1 . Different initiation.
    BC057858 mRNA. Translation: AAH57858.1 .
    CCDSi CCDS19486.1.
    PIRi A37818.
    RefSeqi NP_001191162.1. NM_001204233.1.
    NP_033289.2. NM_009263.3.
    UniGenei Mm.288474.

    3D structure databases

    ProteinModelPortali P10923.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203467. 1 interaction.

    PTM databases

    PhosphoSitei P10923.

    Proteomic databases

    PaxDbi P10923.
    PRIDEi P10923.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031243 ; ENSMUSP00000031243 ; ENSMUSG00000029304 .
    ENSMUST00000112747 ; ENSMUSP00000108367 ; ENSMUSG00000029304 .
    ENSMUST00000112748 ; ENSMUSP00000108368 ; ENSMUSG00000029304 .
    GeneIDi 20750.
    KEGGi mmu:20750.
    UCSCi uc008yki.2. mouse.

    Organism-specific databases

    CTDi 6696.
    MGIi MGI:98389. Spp1.

    Phylogenomic databases

    eggNOGi NOG73598.
    HOGENOMi HOG000059656.
    HOVERGENi HBG001731.
    KOi K06250.
    PhylomeDBi P10923.
    TreeFami TF350201.

    Enzyme and pathway databases

    Reactomei REACT_199052. Degradation of the extracellular matrix.
    REACT_216309. Integrin cell surface interactions.

    Miscellaneous databases

    ChiTaRSi SPP1. mouse.
    NextBioi 299411.
    PROi P10923.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10923.
    Bgeei P10923.
    CleanExi MM_SPP1.
    Genevestigatori P10923.

    Family and domain databases

    InterProi IPR002038. Osteopontin.
    IPR019841. Osteopontin_CS.
    [Graphical view ]
    PANTHERi PTHR10607. PTHR10607. 1 hit.
    Pfami PF00865. Osteopontin. 1 hit.
    [Graphical view ]
    PRINTSi PR00216. OSTEOPONTIN.
    SMARTi SM00017. OSTEO. 1 hit.
    [Graphical view ]
    PROSITEi PS00884. OSTEOPONTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Osteopontin, a transformation-associated cell adhesion phosphoprotein, is induced by 12-O-tetradecanoylphorbol 13-acetate in mouse epidermis."
      Craig A.M., Smith J.H., Denhardt D.T.
      J. Biol. Chem. 264:9682-9689(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structural and functional studies of the early T lymphocyte activation 1 (Eta-1) gene. Definition of a novel T cell-dependent response associated with genetic resistance to bacterial infection."
      Patarca R., Freeman G.J., Singh R.P., Wei F.-Y., Durfee T., Blattner F., Regnier D.C., Kozak C.A., Mock B.A., Morse H.C. III, Jerrells T.R., Cantor H.
      J. Exp. Med. 170:145-161(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Nucleotide sequence of cDNA for mouse osteopontin-like protein."
      Miyazaki Y., Setoguchi M., Yoshida S., Higuchi Y., Akizuki S., Yamamoto S.
      Nucleic Acids Res. 17:3298-3298(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Macrophage.
    4. "The mouse osteopontin gene. Expression in monocytic lineages and complete nucleotide sequence."
      Miyazaki Y., Setoguchi M., Yoshida S.Y., Akizuki S., Yamamoto S.
      J. Biol. Chem. 265:14432-14438(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BALB/c.
      Tissue: Liver.
    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].
      Strain: NMRI.
      Tissue: Mammary gland.
    6. "The calcium oxalate crystal growth inhibitor protein produced by mouse kidney cortical cells in culture is osteopontin."
      Worcester E.M., Blumenthal S.S., Beshensky A.M., Lewand D.L.
      J. Bone Miner. Res. 7:1029-1036(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-37.
      Tissue: Kidney.
    7. "Definition of a specific interaction between the early T lymphocyte activation 1 (Eta-1) protein and murine macrophages in vitro and its effect upon macrophages in vivo."
      Singh R.P., Patarca R., Schwartz J., Singh P., Cantor H.
      J. Exp. Med. 171:1931-1942(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 158-176, FUNCTION.
    8. Cited for: FUNCTION.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-288 AND SER-290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiOSTP_MOUSE
    AccessioniPrimary (citable) accession number: P10923
    Secondary accession number(s): P19008, Q91VH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 141 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3