Version 5.4
Homo sapiens Protein: IBSP
Summary
InnateDB Protein IDBP-29242.4
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol IBSP
Protein Name integrin-binding sialoprotein
Synonyms BNSP; BSP; BSP-II; SP-II;
Species Homo sapiens
Ensembl Protein ENSP00000226284
InnateDB Gene IDBG-29240 (IBSP)
Protein Structure
UniProt Annotation
Function 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.
Subcellular Localization Secreted.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
Biological Process
GO:0001503 ossification
GO:0001649 osteoblast differentiation
GO:0007155 cell adhesion
GO:0030198 extracellular matrix organization
GO:0031214 biomineral tissue development
GO:0071363 cellular response to growth factor stimulus
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0016020 membrane
GO:0031988 membrane-bounded vesicle
Protein Structure and Domains
PDB ID
InterPro IPR008412 Bone sialoprotein II
PFAM PF05432
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P21815
PhosphoSite PhosphoSite-P21815
TrEMBL
UniProt Splice Variant
Entrez Gene 3381
UniGene Hs.518726
RefSeq NP_004958
HUGO HGNC:5341
OMIM 147563
CCDS CCDS3624
HPRD 00951
IMGT
EMBL AC093768 J05213 L09554 L09555 L09556 L09557 L09558 L24757 L24759
GenPept AAA60549 AAC37560 AAC95490

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca