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Q61711

- SIAL_MOUSE

UniProt

Q61711 - SIAL_MOUSE

Protein

Bone sialoprotein 2

Gene

Ibsp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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. Promotes Arg-Gly-Asp-dependent cell attachment By similarity.By similarity

    GO - Biological processi

    1. biomineral tissue development Source: UniProtKB-KW
    2. cell adhesion Source: UniProt
    3. cellular response to growth factor stimulus Source: MGI
    4. extracellular matrix organization Source: MGI
    5. ossification Source: InterPro

    Keywords - Biological processi

    Biomineralization, Cell adhesion

    Keywords - Ligandi

    Sialic acid

    Enzyme and pathway databases

    ReactomeiREACT_196606. ECM proteoglycans.
    REACT_216309. Integrin cell surface interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bone sialoprotein 2
    Alternative name(s):
    Bone sialoprotein II
    Short name:
    BSP II
    Cell-binding sialoprotein
    Integrin-binding sialoprotein
    Gene namesi
    Name:Ibsp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:96389. Ibsp.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProt
    2. membrane-bounded vesicle Source: UniProt

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616By similarityAdd
    BLAST
    Chaini17 – 324308Bone sialoprotein 2PRO_0000020331Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei31 – 311PhosphoserineBy similarity
    Modified residuei67 – 671PhosphoserineBy similarity
    Modified residuei75 – 751PhosphoserineBy similarity
    Modified residuei76 – 761PhosphoserineBy similarity
    Modified residuei95 – 951PhosphoserineBy similarity
    Glycosylationi107 – 1071N-linked (GlcNAc...)Sequence Analysis
    Modified residuei155 – 1551PhosphoserineBy similarity
    Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence Analysis
    Modified residuei320 – 3201SulfotyrosineBy similarity
    Modified residuei321 – 3211SulfotyrosineBy similarity

    Post-translational modificationi

    N-glycosylated; glycans consist of sialylated and core-fucosylated bi-, tri- and tetraantennary chains.By similarity
    Sulfated on either Tyr-320 or Tyr-321.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein, Sulfation

    Proteomic databases

    PRIDEiQ61711.

    PTM databases

    PhosphoSiteiQ61711.

    Expressioni

    Gene expression databases

    BgeeiQ61711.
    CleanExiMM_IBSP.
    GenevestigatoriQ61711.

    Interactioni

    Protein-protein interaction databases

    IntActiQ61711. 1 interaction.
    MINTiMINT-8283231.
    STRINGi10090.ENSMUSP00000031246.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61711.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi293 – 2953Cell attachment siteSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi68 – 179112Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi77 – 848Poly-Glu
    Compositional biasi157 – 17216Poly-GluAdd
    BLAST

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG238366.
    GeneTreeiENSGT00390000002485.
    HOGENOMiHOG000234824.
    HOVERGENiHBG007981.
    InParanoidiQ80VR6.
    KOiK06253.
    OMAiAYEDEYS.
    OrthoDBiEOG7NW6BX.
    TreeFamiTF338678.

    Family and domain databases

    InterProiIPR008412. BSP_II.
    [Graphical view]
    PANTHERiPTHR10345. PTHR10345. 1 hit.
    PfamiPF05432. BSP_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q61711-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTALILLSI LGMACAFSMK NFHRRIKAED SEENGVFKYR PRYFLYKHAY    50
    FYPPLKRFPV QGGSDSSEEN GDGDSSEEEG EEEETSNEEE NNEDSEGNED 100
    QEAEAENSTL STLSGVTASY GAETTPQAQT FELAALQLPK KAGDAESRAP 150
    KVKESDEEEE EEEEEEENEN EEAEVDENEL AVNGTSTNST EVDGGNGSSG 200
    GDNGEEAEAE EASVTEAGAE GTTGGRELTS VGTQTAVLLN GFQQTTPPPE 250
    AYGTTSPPIR KSSTVEYGGE YEQTGNEYNN EYEVYDNENG EPRGDTYRAY 300
    EDEYSYYKGH GYEGYEGQNY YYHQ 324
    Length:324
    Mass (Da):35,734
    Last modified:July 27, 2011 - v2
    Checksum:iD0CD12EA82D27773
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731G → C in AAA37326. 1 PublicationCurated
    Sequence conflicti108 – 1081S → A in AAA21726. (PubMed:8180469)Curated
    Sequence conflicti108 – 1081S → A in AAA37326. 1 PublicationCurated
    Sequence conflicti259 – 2591I → V in AAA37326. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20232 mRNA. Translation: AAA21726.1.
    L23801 mRNA. Translation: AAA37326.1.
    AK132371 mRNA. Translation: BAE21132.1.
    BC045143 mRNA. Translation: AAH45143.1.
    CH466529 Genomic DNA. Translation: EDL20226.1.
    CCDSiCCDS19485.1.
    PIRiI49768.
    RefSeqiNP_032344.2. NM_008318.3.
    UniGeneiMm.4987.

    Genome annotation databases

    EnsembliENSMUST00000031246; ENSMUSP00000031246; ENSMUSG00000029306.
    GeneIDi15891.
    KEGGimmu:15891.
    UCSCiuc008ykg.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20232 mRNA. Translation: AAA21726.1 .
    L23801 mRNA. Translation: AAA37326.1 .
    AK132371 mRNA. Translation: BAE21132.1 .
    BC045143 mRNA. Translation: AAH45143.1 .
    CH466529 Genomic DNA. Translation: EDL20226.1 .
    CCDSi CCDS19485.1.
    PIRi I49768.
    RefSeqi NP_032344.2. NM_008318.3.
    UniGenei Mm.4987.

    3D structure databases

    ProteinModelPortali Q61711.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q61711. 1 interaction.
    MINTi MINT-8283231.
    STRINGi 10090.ENSMUSP00000031246.

    PTM databases

    PhosphoSitei Q61711.

    Proteomic databases

    PRIDEi Q61711.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031246 ; ENSMUSP00000031246 ; ENSMUSG00000029306 .
    GeneIDi 15891.
    KEGGi mmu:15891.
    UCSCi uc008ykg.2. mouse.

    Organism-specific databases

    CTDi 3381.
    MGIi MGI:96389. Ibsp.

    Phylogenomic databases

    eggNOGi NOG238366.
    GeneTreei ENSGT00390000002485.
    HOGENOMi HOG000234824.
    HOVERGENi HBG007981.
    InParanoidi Q80VR6.
    KOi K06253.
    OMAi AYEDEYS.
    OrthoDBi EOG7NW6BX.
    TreeFami TF338678.

    Enzyme and pathway databases

    Reactomei REACT_196606. ECM proteoglycans.
    REACT_216309. Integrin cell surface interactions.

    Miscellaneous databases

    NextBioi 288596.
    PROi Q61711.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q61711.
    CleanExi MM_IBSP.
    Genevestigatori Q61711.

    Family and domain databases

    InterProi IPR008412. BSP_II.
    [Graphical view ]
    PANTHERi PTHR10345. PTHR10345. 1 hit.
    Pfami PF05432. BSP_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Murine bone sialoprotein (BSP): cDNA cloning, mRNA expression, and genetic mapping."
      Young M.F., Ibaraki K., Kerr J.M., Lyu M.S., Kozak C.A.
      Mamm. Genome 5:108-111(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Sequence of mouse bone sialoprotein II (BSP) cDNA."
      Wuyts W., Tylzanowski P., Merregaert J.
      Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Bone.
    3. "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.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Olfactory epithelium.

    Entry informationi

    Entry nameiSIAL_MOUSE
    AccessioniPrimary (citable) accession number: Q61711
    Secondary accession number(s): Q61363, Q80VR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 98 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    It is possible that the segments of clustered carboxyl groups mediate the strong binding to hydroxyapatite.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3