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Protein

Bone sialoprotein 2

Gene

IBSP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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: UniProtKB
  3. cellular response to growth factor stimulus Source: UniProtKB
  4. extracellular matrix organization Source: UniProtKB
  5. osteoblast differentiation Source: UniProtKB
Complete GO annotation...

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 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:5341. IBSP.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProtKB
  3. membrane Source: UniProtKB
  4. membrane-bounded vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29590.

Polymorphism and mutation databases

BioMutaiIBSP.
DMDMi317373545.

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.
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.
GeneTreeiENSGT00390000002485.
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

        10         20         30         40         50
MKTALILLSI LGMACAFSMK NLHRRVKIED SEENGVFKYR PRYYLYKHAY
60 70 80 90 100
FYPHLKRFPV QGSSDSSEEN GDDSSEEEEE EEETSNEGEN NEESNEDEDS
110 120 130 140 150
EAENTTLSAT TLGYGEDATP GTGYTGLAAI QLPKKAGDIT NKATKEKESD
160 170 180 190 200
EEEEEEEEGN ENEESEAEVD ENEQGINGTS TNSTEAENGN GSSGGDNGEE
210 220 230 240 250
GEEESVTGAN AEDTTETGRQ GKGTSKTTTS PNGGFEPTTP PQVYRTTSPP
260 270 280 290 300
FGKTTTVEYE GEYEYTGANE YDNGYEIYES ENGEPRGDNY RAYEDEYSYF
310
KGQGYDGYDG QNYYHHQ
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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiIBSP.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

DisProtiDP00332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000226284.

PTM databases

PhosphoSiteiP21815.

Polymorphism and mutation databases

BioMutaiIBSP.
DMDMi317373545.

Proteomic databases

PaxDbiP21815.
PRIDEiP21815.

Protocols and materials databases

DNASUi3381.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3381.
GeneCardsiGC04P088720.
H-InvDBHIX0031506.
HGNCiHGNC:5341. IBSP.
MIMi147563. gene.
neXtProtiNX_P21815.
PharmGKBiPA29590.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG238366.
GeneTreeiENSGT00390000002485.
HOGENOMiHOG000234824.
HOVERGENiHBG007981.
InParanoidiP21815.
KOiK06253.
OMAiAYEDEYS.
OrthoDBiEOG7NW6BX.
PhylomeDBiP21815.
TreeFamiTF338678.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikiiBone_sialoprotein.
GenomeRNAii3381.
NextBioi13366.
PROiP21815.
SOURCEiSearch...

Gene expression databases

BgeeiP21815.
CleanExiHS_IBSP.
GenevestigatoriP21815.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 123 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.