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P21815 (SIAL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bone sialoprotein 2
Alternative name(s):
Bone sialoprotein II
Short name=BSP II
Cell-binding sialoprotein
Integrin-binding sialoprotein
Gene names
Name:IBSP
Synonyms:BNSP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 location

Secreted.

Post-translational modification

N-glycosylated; glycans consist of sialylated and core-fucosylated bi-, tri- and tetraantennary chains. Ref.6

O-glycosylated at eight sites; mucin-type glycans contain Gal, GlcNAc, GalNAc and terminal NeuAc. Ref.6

Sulfated on either Tyr-313 or Tyr-314.

Miscellaneous

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616
Chain17 – 317301Bone sialoprotein 2
PRO_0000020330

Regions

Motif286 – 2883Cell attachment site
Compositional bias65 – 173109Asp/Glu-rich (acidic)
Compositional bias76 – 838Poly-Glu
Compositional bias151 – 1588Poly-Glu

Amino acid modifications

Modified residue311Phosphoserine Ref.7
Modified residue671Phosphoserine By similarity
Modified residue741Phosphoserine By similarity
Modified residue751Phosphoserine By similarity
Modified residue941Phosphoserine By similarity
Modified residue1001Phosphoserine By similarity
Modified residue1491Phosphoserine By similarity
Modified residue2801Phosphoserine By similarity
Modified residue3131Sulfotyrosine Ref.7
Modified residue3141Sulfotyrosine Ref.7
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1191O-linked (GalNAc...) Probable
Glycosylation1221O-linked (GalNAc...) Probable
Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation1821N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation2271O-linked (GalNAc...) Probable
Glycosylation2281O-linked (GalNAc...) Probable
Glycosylation2291O-linked (GalNAc...) Probable
Glycosylation2381O-linked (GalNAc...) Probable
Glycosylation2391O-linked (GalNAc...) Probable

Natural variations

Natural variant1951G → E. Ref.2 Ref.3
Corresponds to variant rs1054627 [ dbSNP | Ensembl ].
VAR_058014
Natural variant2131D → G. Ref.1 Ref.2 Ref.3 Ref.6
Corresponds to variant rs13144371 [ dbSNP | Ensembl ].
VAR_058015
Natural variant2191R → G. Ref.1 Ref.2
Corresponds to variant rs17013181 [ dbSNP | Ensembl ].
VAR_058016
Natural variant2561T → A.
Corresponds to variant rs17013182 [ dbSNP | Ensembl ].
VAR_056579
Natural variant2681A → V. Ref.1
Corresponds to variant rs1054628 [ dbSNP | Ensembl ].
VAR_056580
Natural variant2701E → D. Ref.2 Ref.3
Corresponds to variant rs1054629 [ dbSNP | Ensembl ].
VAR_058017

Experimental info

Sequence conflict941S → L in AAC37560. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P21815 [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: 736CB6B8C3716FE7

FASTA31735,148
        10         20         30         40         50         60 
MKTALILLSI LGMACAFSMK NLHRRVKIED SEENGVFKYR PRYYLYKHAY FYPHLKRFPV 

        70         80         90        100        110        120 
QGSSDSSEEN GDDSSEEEEE EEETSNEGEN NEESNEDEDS EAENTTLSAT TLGYGEDATP 

       130        140        150        160        170        180 
GTGYTGLAAI QLPKKAGDIT NKATKEKESD EEEEEEEEGN ENEESEAEVD ENEQGINGTS 

       190        200        210        220        230        240 
TNSTEAENGN GSSGGDNGEE GEEESVTGAN AEDTTETGRQ GKGTSKTTTS PNGGFEPTTP 

       250        260        270        280        290        300 
PQVYRTTSPP FGKTTTVEYE GEYEYTGANE YDNGYEIYES ENGEPRGDNY RAYEDEYSYF 

       310 
KGQGYDGYDG QNYYHHQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05213 mRNA. Translation: AAC95490.1.
L09558 expand/collapse EMBL AC list , L09554, L09555, L09556, L09557 Genomic DNA. Translation: AAA60549.1.
L24759, L24757 Genomic DNA. Translation: AAC37560.1.
AC093768 Genomic DNA. No translation available.
PIRGEHUS. A35043.
RefSeqNP_004958.2. NM_004967.3.
UniGeneHs.518726.

3D structure databases

DisProtDP00332.
ProteinModelPortalP21815.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000226284.

PTM databases

PhosphoSiteP21815.

Polymorphism databases

DMDM317373545.

Proteomic databases

PaxDbP21815.
PRIDEP21815.

Protocols and materials databases

DNASU3381.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000226284; ENSP00000226284; ENSG00000029559.
GeneID3381.
KEGGhsa:3381.
UCSCuc003hqx.4. human.

Organism-specific databases

CTD3381.
GeneCardsGC04P088720.
H-InvDBHIX0031506.
HGNCHGNC:5341. IBSP.
MIM147563. gene.
neXtProtNX_P21815.
PharmGKBPA29590.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238366.
HOGENOMHOG000234824.
HOVERGENHBG007981.
InParanoidP21815.
KOK06253.
OMAAYEDEYS.
OrthoDBEOG7NW6BX.
PhylomeDBP21815.
TreeFamTF338678.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

BgeeP21815.
CleanExHS_IBSP.
GenevestigatorP21815.

Family and domain databases

InterProIPR008412. BSP_II.
[Graphical view]
PANTHERPTHR10345. PTHR10345. 1 hit.
PfamPF05432. BSP_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiBone_sialoprotein.
GenomeRNAi3381.
NextBio13366.
PROP21815.
SOURCESearch...

Entry information

Entry nameSIAL_HUMAN
AccessionPrimary (citable) accession number: P21815
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 115 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM