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P21815

- SIAL_HUMAN

UniProt

P21815 - SIAL_HUMAN

Protein

Bone sialoprotein 2

Gene

IBSP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 4 (11 Jan 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.

    GO - Biological processi

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

    Keywords - Biological processi

    Biomineralization, Cell adhesion

    Keywords - Ligandi

    Sialic acid

    Enzyme and pathway databases

    ReactomeiREACT_13552. Integrin cell surface interactions.
    REACT_163906. ECM proteoglycans.

    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
    Synonyms:BNSP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:5341. IBSP.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: UniProt
    3. membrane Source: UniProt
    4. membrane-bounded vesicle Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29590.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Add
    BLAST
    Chaini17 – 317301Bone sialoprotein 2PRO_0000020330Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei31 – 311Phosphoserine1 Publication
    Modified residuei67 – 671PhosphoserineBy similarity
    Modified residuei74 – 741PhosphoserineBy similarity
    Modified residuei75 – 751PhosphoserineBy similarity
    Modified residuei94 – 941PhosphoserineBy similarity
    Modified residuei100 – 1001PhosphoserineBy similarity
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi119 – 1191O-linked (GalNAc...)1 Publication
    Glycosylationi122 – 1221O-linked (GalNAc...)1 Publication
    Modified residuei149 – 1491PhosphoserineBy similarity
    Glycosylationi177 – 1771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi227 – 2271O-linked (GalNAc...)1 Publication
    Glycosylationi228 – 2281O-linked (GalNAc...)1 Publication
    Glycosylationi229 – 2291O-linked (GalNAc...)1 Publication
    Glycosylationi238 – 2381O-linked (GalNAc...)1 Publication
    Glycosylationi239 – 2391O-linked (GalNAc...)1 Publication
    Modified residuei280 – 2801PhosphoserineBy similarity
    Modified residuei313 – 3131Sulfotyrosine1 Publication
    Modified residuei314 – 3141Sulfotyrosine1 Publication

    Post-translational modificationi

    N-glycosylated; glycans consist of sialylated and core-fucosylated bi-, tri- and tetraantennary chains.1 Publication
    O-glycosylated at eight sites; mucin-type glycans contain Gal, GlcNAc, GalNAc and terminal NeuAc.1 Publication
    Sulfated on either Tyr-313 or Tyr-314.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein, Sulfation

    Proteomic databases

    PaxDbiP21815.
    PRIDEiP21815.

    PTM databases

    PhosphoSiteiP21815.

    Expressioni

    Gene expression databases

    BgeeiP21815.
    CleanExiHS_IBSP.
    GenevestigatoriP21815.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000226284.

    Structurei

    3D structure databases

    DisProtiDP00332.
    ProteinModelPortaliP21815.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi286 – 2883Cell attachment site

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi65 – 173109Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi76 – 838Poly-Glu
    Compositional biasi151 – 1588Poly-Glu

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG238366.
    HOGENOMiHOG000234824.
    HOVERGENiHBG007981.
    InParanoidiP21815.
    KOiK06253.
    OMAiAYEDEYS.
    OrthoDBiEOG7NW6BX.
    PhylomeDBiP21815.
    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.

    P21815-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTALILLSI LGMACAFSMK NLHRRVKIED SEENGVFKYR PRYYLYKHAY    50
    FYPHLKRFPV QGSSDSSEEN GDDSSEEEEE EEETSNEGEN NEESNEDEDS 100
    EAENTTLSAT TLGYGEDATP GTGYTGLAAI QLPKKAGDIT NKATKEKESD 150
    EEEEEEEEGN ENEESEAEVD ENEQGINGTS TNSTEAENGN GSSGGDNGEE 200
    GEEESVTGAN AEDTTETGRQ GKGTSKTTTS PNGGFEPTTP PQVYRTTSPP 250
    FGKTTTVEYE GEYEYTGANE YDNGYEIYES ENGEPRGDNY RAYEDEYSYF 300
    KGQGYDGYDG QNYYHHQ 317
    Length:317
    Mass (Da):35,148
    Last modified:January 11, 2011 - v4
    Checksum:i736CB6B8C3716FE7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941S → L in AAC37560. (PubMed:8061918)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti195 – 1951G → E.2 Publications
    Corresponds to variant rs1054627 [ dbSNP | Ensembl ].
    VAR_058014
    Natural varianti213 – 2131D → G.4 Publications
    Corresponds to variant rs13144371 [ dbSNP | Ensembl ].
    VAR_058015
    Natural varianti219 – 2191R → G.2 Publications
    Corresponds to variant rs17013181 [ dbSNP | Ensembl ].
    VAR_058016
    Natural varianti256 – 2561T → A.
    Corresponds to variant rs17013182 [ dbSNP | Ensembl ].
    VAR_056579
    Natural varianti268 – 2681A → V.1 Publication
    Corresponds to variant rs1054628 [ dbSNP | Ensembl ].
    VAR_056580
    Natural varianti270 – 2701E → D.2 Publications
    Corresponds to variant rs1054629 [ dbSNP | Ensembl ].
    VAR_058017

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05213 mRNA. Translation: AAC95490.1.
    L09558
    , L09554, L09555, L09556, L09557 Genomic DNA. Translation: AAA60549.1.
    L24759, L24757 Genomic DNA. Translation: AAC37560.1.
    AC093768 Genomic DNA. No translation available.
    CCDSiCCDS3624.1.
    PIRiA35043. GEHUS.
    RefSeqiNP_004958.2. NM_004967.3.
    UniGeneiHs.518726.

    Genome annotation databases

    EnsembliENST00000226284; ENSP00000226284; ENSG00000029559.
    GeneIDi3381.
    KEGGihsa:3381.
    UCSCiuc003hqx.4. human.

    Polymorphism databases

    DMDMi317373545.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05213 mRNA. Translation: AAC95490.1 .
    L09558
    , L09554 , L09555 , L09556 , L09557 Genomic DNA. Translation: AAA60549.1 .
    L24759 , L24757 Genomic DNA. Translation: AAC37560.1 .
    AC093768 Genomic DNA. No translation available.
    CCDSi CCDS3624.1.
    PIRi A35043. GEHUS.
    RefSeqi NP_004958.2. NM_004967.3.
    UniGenei Hs.518726.

    3D structure databases

    DisProti DP00332.
    ProteinModelPortali P21815.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000226284.

    PTM databases

    PhosphoSitei P21815.

    Polymorphism databases

    DMDMi 317373545.

    Proteomic databases

    PaxDbi P21815.
    PRIDEi P21815.

    Protocols and materials databases

    DNASUi 3381.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000226284 ; ENSP00000226284 ; ENSG00000029559 .
    GeneIDi 3381.
    KEGGi hsa:3381.
    UCSCi uc003hqx.4. human.

    Organism-specific databases

    CTDi 3381.
    GeneCardsi GC04P088720.
    H-InvDB HIX0031506.
    HGNCi HGNC:5341. IBSP.
    MIMi 147563. gene.
    neXtProti NX_P21815.
    PharmGKBi PA29590.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238366.
    HOGENOMi HOG000234824.
    HOVERGENi HBG007981.
    InParanoidi P21815.
    KOi K06253.
    OMAi AYEDEYS.
    OrthoDBi EOG7NW6BX.
    PhylomeDBi P21815.
    TreeFami TF338678.

    Enzyme and pathway databases

    Reactomei REACT_13552. Integrin cell surface interactions.
    REACT_163906. ECM proteoglycans.

    Miscellaneous databases

    GeneWikii Bone_sialoprotein.
    GenomeRNAii 3381.
    NextBioi 13366.
    PROi P21815.
    SOURCEi Search...

    Gene expression databases

    Bgeei P21815.
    CleanExi HS_IBSP.
    Genevestigatori P21815.

    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. "Human bone sialoprotein. Deduced protein sequence and chromosomal localization."
      Fisher L.W., McBride O.W., Termine J.D., Young M.F.
      J. Biol. Chem. 265:2347-2351(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLY-213; GLY-219 AND VAL-268.
    2. "The human bone sialoprotein gene (IBSP): genomic localization and characterization."
      Kerr J.M., Fisher L.W., Termine J.D., Wang M.G., McBride W., Young M.F.
      Genomics 17:408-415(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-195; GLY-213; GLY-219 AND ASP-270.
    3. "Characterization of the human bone sialoprotein (BSP) gene and its promoter sequence."
      Kim R.H., Shapiro H.S., Li J.J., Wrana J.L., Sodek J.
      Matrix Biol. 14:31-40(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-195; GLY-213 AND ASP-270.
    4. "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].
    5. "Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone."
      Fisher L.W., Hawkins G.R., Tuross N., Termine J.D.
      J. Biol. Chem. 262:9702-9708(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
    6. "Structural characterization of human recombinant and bone-derived bone sialoprotein. Functional implications for cell attachment and hydroxyapatite binding."
      Wuttke M., Muller S., Nitsche D.P., Paulsson M., Hanisch F.G., Maurer P.
      J. Biol. Chem. 276:36839-36848(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT THR-119; THR-122; THR-227; THR-228; THR-229; THR-238 AND THR-239, STRUCTURE OF CARBOHYDRATE, VARIANT GLY-213, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Posttranslational modifications to human bone sialoprotein determined by mass spectrometry."
      Zaia J., Boynton R., Heinegard D., Barry F.
      Biochemistry 40:12983-12991(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-31, SULFATION AT TYR-313 AND TYR-314, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiSIAL_HUMAN
    AccessioniPrimary (citable) accession number: P21815
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 118 of the entry and version 4 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

    Miscellaneous

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

    Keywords - Technical termi

    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

    External Data

    Dasty 3