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P10451

- OSTP_HUMAN

UniProt

P10451 - OSTP_HUMAN

Protein

Osteopontin

Gene

SPP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 168 (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.By similarity

    GO - Molecular functioni

    1. extracellular matrix binding Source: Ensembl
    2. protein binding Source: IntAct

    GO - Biological processi

    1. biomineral tissue development Source: UniProtKB-KW
    2. cell adhesion Source: UniProtKB-KW
    3. decidualization Source: BHF-UCL
    4. embryo implantation Source: BHF-UCL
    5. extracellular matrix disassembly Source: Reactome
    6. extracellular matrix organization Source: Reactome
    7. inflammatory response Source: Ensembl
    8. negative regulation of collateral sprouting of intact axon in response to injury Source: Ensembl
    9. neutrophil chemotaxis Source: Ensembl
    10. osteoblast differentiation Source: Ensembl
    11. positive regulation of bone resorption Source: Ensembl
    12. positive regulation of cell-substrate adhesion Source: Ensembl
    13. response to steroid hormone Source: Ensembl
    14. response to vitamin D Source: BHF-UCL

    Keywords - Molecular functioni

    Cytokine

    Keywords - Biological processi

    Biomineralization, Cell adhesion

    Keywords - Ligandi

    Sialic acid

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_13552. Integrin cell surface interactions.
    REACT_16888. Signaling by PDGF.
    REACT_216309. Integrin cell surface interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Osteopontin
    Alternative name(s):
    Bone sialoprotein 1
    Nephropontin
    Secreted phosphoprotein 1
    Short name:
    SPP-1
    Urinary stone protein
    Uropontin
    Gene namesi
    Name:SPP1
    Synonyms:BNSP, OPN
    ORF Names:PSEC0156
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:11255. SPP1.

    Subcellular locationi

    GO - Cellular componenti

    1. apical part of cell Source: Ensembl
    2. cell projection Source: Ensembl
    3. extracellular region Source: Reactome
    4. extracellular space Source: BHF-UCL
    5. extracellular vesicular exosome Source: UniProt
    6. perinuclear region of cytoplasm Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti93552. Pediatric systemic lupus erythematosus.
    536. Systemic lupus erythematosus.
    PharmGKBiPA36085.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 314298OsteopontinPRO_0000020321Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241Phosphoserine2 Publications
    Modified residuei26 – 261Phosphoserine2 Publications
    Modified residuei27 – 271Phosphoserine2 Publications
    Modified residuei62 – 621Phosphoserine2 Publications
    Modified residuei63 – 631Phosphoserine2 Publications
    Modified residuei66 – 661Phosphothreonine2 Publications
    Modified residuei76 – 761Phosphoserine2 Publications
    Modified residuei78 – 781PhosphoserineBy similarity
    Glycosylationi79 – 791N-linked (GlcNAc...)2 Publications
    Modified residuei81 – 811Phosphoserine3 Publications
    Modified residuei99 – 991Phosphoserine2 Publications
    Modified residuei102 – 1021Phosphoserine2 Publications
    Modified residuei105 – 1051Phosphoserine2 Publications
    Glycosylationi106 – 1061N-linked (GlcNAc...)2 Publications
    Modified residuei108 – 1081Phosphoserine2 Publications
    Modified residuei117 – 1171Phosphoserine2 Publications
    Modified residuei120 – 1201Phosphoserine2 Publications
    Modified residuei123 – 1231Phosphoserine2 Publications
    Modified residuei126 – 1261Phosphoserine2 Publications
    Modified residuei129 – 1291Phosphoserine2 Publications
    Glycosylationi134 – 1341O-linked (GalNAc...)2 Publications
    Glycosylationi138 – 1381O-linked (GalNAc...)2 Publications
    Glycosylationi143 – 1431O-linked (GalNAc...)2 Publications
    Glycosylationi147 – 1471O-linked (GalNAc...)2 Publications
    Glycosylationi152 – 1521O-linked (GalNAc...)2 Publications
    Modified residuei185 – 1851Phosphothreonine2 Publications
    Modified residuei191 – 1911Phosphoserine2 Publications
    Modified residuei195 – 1951Phosphoserine2 Publications
    Modified residuei215 – 2151Phosphoserine2 Publications
    Modified residuei219 – 2191Phosphoserine3 Publications
    Modified residuei224 – 2241Phosphoserine3 Publications
    Modified residuei228 – 2281Phosphoserine2 Publications
    Modified residuei234 – 2341Phosphoserine3 Publications
    Modified residuei239 – 2391PhosphoserineBy similarity
    Modified residuei254 – 2541Phosphoserine3 Publications
    Modified residuei263 – 2631Phosphoserine2 Publications
    Modified residuei267 – 2671Phosphoserine2 Publications
    Modified residuei270 – 2701PhosphoserineBy similarity
    Modified residuei275 – 2751Phosphoserine2 Publications
    Modified residuei280 – 2801Phosphoserine2 Publications
    Modified residuei291 – 2911PhosphoserineBy similarity
    Modified residuei303 – 3031Phosphoserine2 Publications
    Modified residuei308 – 3081Phosphoserine2 Publications
    Modified residuei310 – 3101Phosphoserine2 Publications

    Post-translational modificationi

    Extensively phosphorylated by FAM20C in the extracellular medium at multiple sites within the S-x-E/pS motif.4 Publications
    N- and O-glycosylated. Isoform 5 is GalNAc O-glycosylated at Thr-59 or Ser-62.2 Publications

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP10451.
    PaxDbiP10451.
    PRIDEiP10451.

    PTM databases

    PhosphoSiteiP10451.
    UniCarbKBiP10451.

    Miscellaneous databases

    PMAP-CutDBP10451.

    Expressioni

    Tissue specificityi

    Bone. Found in plasma.

    Gene expression databases

    ArrayExpressiP10451.
    BgeeiP10451.
    CleanExiHS_SPP1.
    GenevestigatoriP10451.

    Organism-specific databases

    HPAiCAB002212.
    HPA027541.

    Interactioni

    Subunit structurei

    Ligand for integrin alpha-V/beta-3.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CD44P160702EBI-723648,EBI-490245

    Protein-protein interaction databases

    BioGridi112574. 75 interactions.
    DIPiDIP-49933N.
    IntActiP10451. 10 interactions.
    MINTiMINT-1380527.
    STRINGi9606.ENSP00000378517.

    Structurei

    Secondary structure

    1
    314
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 474

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CXDX-ray2.80P40-51[»]
    3DSFX-ray2.80P40-51[»]
    DisProtiDP00214.
    ProteinModelPortaliP10451.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10451.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi159 – 1613Cell attachment site

    Sequence similaritiesi

    Belongs to the osteopontin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG73598.
    HOGENOMiHOG000059656.
    HOVERGENiHBG001731.
    InParanoidiP10451.
    KOiK06250.
    OMAiVICFCLL.
    OrthoDBiEOG7R832D.
    PhylomeDBiP10451.
    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]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: P10451-1) [UniParc]FASTAAdd to Basket

    Also known as: OPN-a, OP1B

    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

    MRIAVICFCL LGITCAIPVK QADSGSSEEK QLYNKYPDAV ATWLNPDPSQ    50
    KQNLLAPQNA VSSEETNDFK QETLPSKSNE SHDHMDDMDD EDDDDHVDSQ 100
    DSIDSNDSDD VDDTDDSHQS DESHHSDESD ELVTDFPTDL PATEVFTPVV 150
    PTVDTYDGRG DSVVYGLRSK SKKFRRPDIQ YPDATDEDIT SHMESEELNG 200
    AYKAIPVAQD LNAPSDWDSR GKDSYETSQL DDQSAETHSH KQSRLYKRKA 250
    NDESNEHSDV IDSQELSKVS REFHSHEFHS HEDMLVVDPK SKEEDKHLKF 300
    RISHELDSAS SEVN 314
    Length:314
    Mass (Da):35,423
    Last modified:July 1, 1989 - v1
    Checksum:i4996429EC4752B86
    GO
    Isoform B (identifier: P10451-2) [UniParc]FASTAAdd to Basket

    Also known as: OPN-b, OP1A

    The sequence of this isoform differs from the canonical sequence as follows:
         58-71: Missing.

    Show »
    Length:300
    Mass (Da):33,844
    Checksum:iE844D1466BD20E64
    GO
    Isoform C (identifier: P10451-3) [UniParc]FASTAAdd to Basket

    Also known as: OPN-c

    The sequence of this isoform differs from the canonical sequence as follows:
         31-57: Missing.

    Show »
    Length:287
    Mass (Da):32,355
    Checksum:iAF604D4E223BA02F
    GO
    Isoform D (identifier: P10451-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         95-116: Missing.

    Show »
    Length:292
    Mass (Da):33,017
    Checksum:iE93E418982C3AD60
    GO
    Isoform 5 (identifier: P10451-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         59-72: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:300
    Mass (Da):33,843
    Checksum:iB844D7EBDD096CBF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti188 – 1881D → H in BAA05949. (PubMed:7837791)Curated
    Sequence conflicti188 – 1881D → H in BAA05950. (PubMed:7837791)Curated
    Sequence conflicti188 – 1881D → H in BAA05951. (PubMed:7837791)Curated
    Sequence conflicti237 – 2371T → A in BAA05949. (PubMed:7837791)Curated
    Sequence conflicti237 – 2371T → A in BAA05950. (PubMed:7837791)Curated
    Sequence conflicti237 – 2371T → A in BAA05951. (PubMed:7837791)Curated
    Sequence conflicti275 – 2784SHEF → GNSL(PubMed:1974876)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti224 – 2241S → N.
    Corresponds to variant rs7435825 [ dbSNP | Ensembl ].
    VAR_050432
    Natural varianti301 – 3011R → H.
    Corresponds to variant rs4660 [ dbSNP | Ensembl ].
    VAR_014717

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei31 – 5727Missing in isoform C. 4 PublicationsVSP_003777Add
    BLAST
    Alternative sequencei58 – 7114Missing in isoform B. 4 PublicationsVSP_003778Add
    BLAST
    Alternative sequencei59 – 7214Missing in isoform 5. 1 PublicationVSP_043695Add
    BLAST
    Alternative sequencei95 – 11622Missing in isoform D. 1 PublicationVSP_011639Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13694 mRNA. Translation: CAA31984.1.
    J04765 mRNA. Translation: AAA59974.1.
    M83248 mRNA. Translation: AAA17675.1.
    U20758 Genomic DNA. Translation: AAA86886.1.
    D14813 Genomic DNA. Translation: BAA03554.1.
    D28759 mRNA. Translation: BAA05949.1.
    D28760 mRNA. Translation: BAA05950.1.
    D28761 mRNA. Translation: BAA05951.1.
    AF052124 mRNA. Translation: AAC28619.1.
    AK290104 mRNA. Translation: BAF82793.1.
    JF412667 mRNA. Translation: AEA49031.1.
    AK075463 mRNA. Translation: BAC11635.1.
    AK290090 mRNA. Translation: BAF82779.1.
    AK296035 mRNA. Translation: BAG58801.1.
    AK315461 mRNA. Translation: BAG37848.1.
    DQ839491 mRNA. Translation: ABI63352.1.
    DQ846871 mRNA. Translation: ABI63358.1.
    AC131944 Genomic DNA. Translation: AAY41035.1.
    CH471057 Genomic DNA. Translation: EAX06004.1.
    CH471057 Genomic DNA. Translation: EAX06005.1.
    CH471057 Genomic DNA. Translation: EAX06006.1.
    BC007016 mRNA. Translation: AAH07016.1.
    BC017387 mRNA. Translation: AAH17387.1.
    BC022844 mRNA. Translation: AAH22844.1.
    BC093033 mRNA. Translation: AAH93033.1.
    CCDSiCCDS34027.1. [P10451-3]
    CCDS3626.1. [P10451-5]
    CCDS43250.1. [P10451-1]
    PIRiS50028. S09575.
    RefSeqiNP_000573.1. NM_000582.2. [P10451-5]
    NP_001035147.1. NM_001040058.1. [P10451-1]
    NP_001035149.1. NM_001040060.1. [P10451-3]
    NP_001238758.1. NM_001251829.1.
    NP_001238759.1. NM_001251830.1.
    UniGeneiHs.313.

    Genome annotation databases

    EnsembliENST00000237623; ENSP00000237623; ENSG00000118785. [P10451-5]
    ENST00000360804; ENSP00000354042; ENSG00000118785. [P10451-3]
    ENST00000395080; ENSP00000378517; ENSG00000118785. [P10451-1]
    GeneIDi6696.
    KEGGihsa:6696.
    UCSCiuc003hra.3. human. [P10451-1]
    uc003hrb.3. human. [P10451-3]
    uc003hrc.3. human. [P10451-5]

    Polymorphism databases

    DMDMi129260.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Wikipedia

    Osteopontin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13694 mRNA. Translation: CAA31984.1 .
    J04765 mRNA. Translation: AAA59974.1 .
    M83248 mRNA. Translation: AAA17675.1 .
    U20758 Genomic DNA. Translation: AAA86886.1 .
    D14813 Genomic DNA. Translation: BAA03554.1 .
    D28759 mRNA. Translation: BAA05949.1 .
    D28760 mRNA. Translation: BAA05950.1 .
    D28761 mRNA. Translation: BAA05951.1 .
    AF052124 mRNA. Translation: AAC28619.1 .
    AK290104 mRNA. Translation: BAF82793.1 .
    JF412667 mRNA. Translation: AEA49031.1 .
    AK075463 mRNA. Translation: BAC11635.1 .
    AK290090 mRNA. Translation: BAF82779.1 .
    AK296035 mRNA. Translation: BAG58801.1 .
    AK315461 mRNA. Translation: BAG37848.1 .
    DQ839491 mRNA. Translation: ABI63352.1 .
    DQ846871 mRNA. Translation: ABI63358.1 .
    AC131944 Genomic DNA. Translation: AAY41035.1 .
    CH471057 Genomic DNA. Translation: EAX06004.1 .
    CH471057 Genomic DNA. Translation: EAX06005.1 .
    CH471057 Genomic DNA. Translation: EAX06006.1 .
    BC007016 mRNA. Translation: AAH07016.1 .
    BC017387 mRNA. Translation: AAH17387.1 .
    BC022844 mRNA. Translation: AAH22844.1 .
    BC093033 mRNA. Translation: AAH93033.1 .
    CCDSi CCDS34027.1. [P10451-3 ]
    CCDS3626.1. [P10451-5 ]
    CCDS43250.1. [P10451-1 ]
    PIRi S50028. S09575.
    RefSeqi NP_000573.1. NM_000582.2. [P10451-5 ]
    NP_001035147.1. NM_001040058.1. [P10451-1 ]
    NP_001035149.1. NM_001040060.1. [P10451-3 ]
    NP_001238758.1. NM_001251829.1.
    NP_001238759.1. NM_001251830.1.
    UniGenei Hs.313.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CXD X-ray 2.80 P 40-51 [» ]
    3DSF X-ray 2.80 P 40-51 [» ]
    DisProti DP00214.
    ProteinModelPortali P10451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112574. 75 interactions.
    DIPi DIP-49933N.
    IntActi P10451. 10 interactions.
    MINTi MINT-1380527.
    STRINGi 9606.ENSP00000378517.

    PTM databases

    PhosphoSitei P10451.
    UniCarbKBi P10451.

    Polymorphism databases

    DMDMi 129260.

    Proteomic databases

    MaxQBi P10451.
    PaxDbi P10451.
    PRIDEi P10451.

    Protocols and materials databases

    DNASUi 6696.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000237623 ; ENSP00000237623 ; ENSG00000118785 . [P10451-5 ]
    ENST00000360804 ; ENSP00000354042 ; ENSG00000118785 . [P10451-3 ]
    ENST00000395080 ; ENSP00000378517 ; ENSG00000118785 . [P10451-1 ]
    GeneIDi 6696.
    KEGGi hsa:6696.
    UCSCi uc003hra.3. human. [P10451-1 ]
    uc003hrb.3. human. [P10451-3 ]
    uc003hrc.3. human. [P10451-5 ]

    Organism-specific databases

    CTDi 6696.
    GeneCardsi GC04P088896.
    H-InvDB HIX0004361.
    HGNCi HGNC:11255. SPP1.
    HPAi CAB002212.
    HPA027541.
    MIMi 166490. gene.
    neXtProti NX_P10451.
    Orphaneti 93552. Pediatric systemic lupus erythematosus.
    536. Systemic lupus erythematosus.
    PharmGKBi PA36085.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG73598.
    HOGENOMi HOG000059656.
    HOVERGENi HBG001731.
    InParanoidi P10451.
    KOi K06250.
    OMAi VICFCLL.
    OrthoDBi EOG7R832D.
    PhylomeDBi P10451.
    TreeFami TF350201.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_13552. Integrin cell surface interactions.
    REACT_16888. Signaling by PDGF.
    REACT_216309. Integrin cell surface interactions.

    Miscellaneous databases

    ChiTaRSi SPP1. human.
    EvolutionaryTracei P10451.
    GeneWikii Osteopontin.
    GenomeRNAii 6696.
    NextBioi 26103.
    PMAP-CutDB P10451.
    PROi P10451.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10451.
    Bgeei P10451.
    CleanExi HS_SPP1.
    Genevestigatori P10451.

    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. "The cDNA and derived amino acid sequence for human osteopontin."
      Kiefer M.C., Bauer D.M., Barr P.J.
      Nucleic Acids Res. 17:3306-3306(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    2. "cDNA cloning, mRNA distribution and heterogeneity, chromosomal location, and RFLP analysis of human osteopontin (OPN)."
      Young M.F., Kerr J.M., Termine J.D., Wewer U.M., Wang M.G., McBride O.W., Fisher L.W.
      Genomics 7:491-502(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
    3. "Inhibition of calcium oxalate crystal growth in vitro by uropontin: another member of the aspartic acid-rich protein superfamily."
      Shiraga H., Min W., VanDusen W.J., Clayman M.D., Miner D., Terrell C.H., Sherbotie J.R., Foreman J.W., Przysiecki C., Neilson E.G., Hoyer J.R.
      Proc. Natl. Acad. Sci. U.S.A. 89:426-430(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    4. "Genomic organization of the human osteopontin gene: exclusion of the locus from a causative role in the pathogenesis of dentinogenesis imperfecta type II."
      Crosby A.H., Edwards S.J., Murray J.C., Dixon M.J.
      Genomics 27:155-160(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
    5. "Cloning and characterization of the human osteopontin gene and its promoter."
      Hijiya N., Setoguchi M., Matsuura K., Higuchi Y., Akizuki S., Yamamoto S.
      Biochem. J. 303:255-262(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
      Tissue: Liver.
    6. "Expression of osteopontin in human glioma. Its correlation with the malignancy."
      Saitoh Y., Kuratsu J., Takeshima H., Yamamoto S., Ushio Y.
      Lab. Invest. 72:55-63(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
    7. Yu W., Sarginson J., Gibbs R.A.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
      Tissue: Brain.
    8. "Osteopontin splice variants in Indian breast cancer patients as biomarker."
      Sivakumar S., Niranjali Devaraj S.
      Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
    9. "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] (ISOFORMS A; C AND 5).
      Tissue: Kidney and Subthalamic nucleus.
    10. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
      Tissue: Placenta.
    11. "A computer system platform used to predict novel genes."
      Yu Z., Zheng Z., Tang T., Fu Y.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    12. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    14. "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] (ISOFORMS A; B AND C).
      Tissue: Brain and Kidney.
    15. "Molecular cloning and sequencing of cDNA encoding urinary stone protein, which is identical to osteopontin."
      Kohri K., Suzuki Y., Yoshida K., Yamamoto K., Amasaki N., Yamate T., Umekawa T., Iguchi M., Sinohara H., Kurita T.
      Biochem. Biophys. Res. Commun. 184:859-864(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 67-278.
      Tissue: Kidney.
    16. "Purification of a human milk protein closely similar to tumor-secreted phosphoproteins and osteopontin."
      Senger D.R., Perruzzi C.A., Papadopoulos A., Tenen D.G.
      Biochim. Biophys. Acta 996:43-48(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-23 AND 169-182.
      Tissue: Milk.
    17. "Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications."
      Christensen B., Nielsen M.S., Haselmann K.F., Petersen T.E., Sorensen E.S.
      Biochem. J. 390:285-292(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-24; SER-26; SER-27; SER-62; SER-63; THR-66; SER-76; SER-81; SER-99; SER-102; SER-108; SER-117; SER-120; SER-123; SER-129; THR-185; SER-191; SER-195; SER-215; SER-219; SER-224; SER-228; SER-234; SER-254; SER-263; SER-267; SER-275; SER-280; SER-303; SER-308; SER-310; SER-105 AND SER-126, GLYCOSYLATION AT ASN-79; ASN-106; THR-134; THR-138; THR-143; THR-147 AND THR-152.
      Tissue: Milk.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Pituitary.
    19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-224; SER-234 AND SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Secreted kinase phosphorylates extracellular proteins that regulate biomineralization."
      Tagliabracci V.S., Engel J.L., Wen J., Wiley S.E., Worby C.A., Kinch L.N., Xiao J., Grishin N.V., Dixon J.E.
      Science 336:1150-1153(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY FAM20C.
    22. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
      Halim A., Ruetschi U., Larson G., Nilsson J.
      J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiOSTP_HUMAN
    AccessioniPrimary (citable) accession number: P10451
    Secondary accession number(s): B2RDA1
    , Q15681, Q15682, Q15683, Q4W597, Q567T5, Q8NBK2, Q96IZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 168 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3