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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.

Miscellaneous

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

GO - Molecular functioni

  • integrin binding Source: CAFA

GO - Biological processi

  • bone mineralization Source: Ensembl
  • cell adhesion Source: UniProtKB
  • cellular response to growth factor stimulus Source: UniProtKB
  • extracellular matrix organization Source: UniProtKB
  • osteoblast differentiation Source: UniProtKB
  • positive regulation of cell adhesion Source: CAFA

Keywordsi

Biological processBiomineralization, Cell adhesion
LigandSialic acid

Enzyme and pathway databases

ReactomeiR-HSA-216083. Integrin cell surface interactions.
R-HSA-3000178. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:5341. IBSP.

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: GO_Central
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • membrane Source: UniProtKB
  • vesicle Source: UniProtKB

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi3381.
OpenTargetsiENSG00000029559.
PharmGKBiPA29590.

Polymorphism and mutation databases

BioMutaiIBSP.
DMDMi317373545.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 16Add BLAST16
ChainiPRO_000002033017 – 317Bone sialoprotein 2Add BLAST301

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31Phosphoserine1 Publication1
Modified residuei67PhosphoserineBy similarity1
Modified residuei74PhosphoserineBy similarity1
Modified residuei75PhosphoserineBy similarity1
Modified residuei94PhosphoserineBy similarity1
Modified residuei100PhosphoserineBy similarity1
Glycosylationi104N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi119O-linked (GalNAc...) threonine1 Publication1
Glycosylationi122O-linked (GalNAc...) threonine1 Publication1
Modified residuei149PhosphoserineBy similarity1
Glycosylationi177N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi182N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi190N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi227O-linked (GalNAc...) threonine1 Publication1
Glycosylationi228O-linked (GalNAc...) threonine1 Publication1
Glycosylationi229O-linked (GalNAc...) threonine1 Publication1
Glycosylationi238O-linked (GalNAc...) threonine1 Publication1
Glycosylationi239O-linked (GalNAc...) threonine1 Publication1
Modified residuei280PhosphoserineBy similarity1
Modified residuei313Sulfotyrosine1 Publication1
Modified residuei314Sulfotyrosine1 Publication1

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.
PeptideAtlasiP21815.
PRIDEiP21815.

PTM databases

iPTMnetiP21815.
PhosphoSitePlusiP21815.

Expressioni

Gene expression databases

BgeeiENSG00000029559.
CleanExiHS_IBSP.
GenevisibleiP21815. HS.

Interactioni

GO - Molecular functioni

  • integrin binding Source: CAFA

Protein-protein interaction databases

STRINGi9606.ENSP00000226284.

Structurei

3D structure databases

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

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi286 – 288Cell attachment site3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi65 – 173Asp/Glu-rich (acidic)Add BLAST109
Compositional biasi76 – 83Poly-Glu8
Compositional biasi151 – 158Poly-Glu8

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1181. Eukaryota.
ENOG4111M3T. LUCA.
GeneTreeiENSGT00390000002485.
HOGENOMiHOG000234824.
HOVERGENiHBG007981.
InParanoidiP21815.
KOiK06253.
OMAiLYKHAYF.
OrthoDBiEOG091G0UXJ.
PhylomeDBiP21815.
TreeFamiTF338678.

Family and domain databases

InterProiView protein in InterPro
IPR008412. BSP_II.
PANTHERiPTHR10345. PTHR10345. 1 hit.
PfamiView protein in Pfam
PF05432. BSP_II. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti94S → L in AAC37560 (PubMed:8061918).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_058014195G → E2 PublicationsCorresponds to variant dbSNP:rs1054627Ensembl.1
Natural variantiVAR_058015213D → G4 PublicationsCorresponds to variant dbSNP:rs13144371Ensembl.1
Natural variantiVAR_058016219R → G2 PublicationsCorresponds to variant dbSNP:rs17013181Ensembl.1
Natural variantiVAR_056579256T → A. Corresponds to variant dbSNP:rs17013182Ensembl.1
Natural variantiVAR_056580268A → V1 PublicationCorresponds to variant dbSNP:rs1054628Ensembl.1
Natural variantiVAR_058017270E → D2 PublicationsCorresponds to variant dbSNP:rs1054629Ensembl.1

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.5. human.

Keywords - Coding sequence diversityi

Polymorphism

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 one 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.

Entry informationi

Entry nameiSIAL_HUMAN
AccessioniPrimary (citable) accession number: P21815
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 11, 2011
Last modified: May 10, 2017
This is version 140 of the entry and version 4 of the sequence. See 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

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