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P10451 (OSTP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Names and origin

Protein namesRecommended name:
Osteopontin
Alternative name(s):
Bone sialoprotein 1
Secreted phosphoprotein 1
Short name=SPP-1
Urinary stone protein
Nephropontin
Uropontin
Gene names
Name:SPP1
Synonyms:BNSP, OPN
ORF Names:PSEC0156
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length314 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.

Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity By similarity.

Subunit structure

Ligand for integrin alpha-V/beta-3.

Subcellular location

Secreted.

Tissue specificity

Bone. Found in plasma. Ref.14

Post-translational modification

Extensively phosphorylated on clustered serine residues. Ref.14 Ref.12 Ref.13

N- and O-glycosylated. Ref.12

Phosphorylation sites are present in the extracelllular medium.

Sequence similarities

Belongs to the osteopontin family.

Ontologies

Keywords
   Biological processBiomineralization
Cell adhesion
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   LigandSialic acid
   Molecular functionCytokine
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processbiomineral formation

Inferred from electronic annotation. Source: UniProtKB-KW

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

decidualization

Traceable author statement. Source: BHF-UCL

embryo implantation

Traceable author statement. Source: BHF-UCL

response to vitamin D

Inferred from direct assay. Source: BHF-UCL

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncytokine activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P10451-1)

Also known as: OPN-a; OP1B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: P10451-2)

Also known as: OPN-b; OP1A;

The sequence of this isoform differs from the canonical sequence as follows:
     58-71: Missing.
Isoform C (identifier: P10451-3)

Also known as: OPN-c;

The sequence of this isoform differs from the canonical sequence as follows:
     31-57: Missing.
Isoform D (identifier: P10451-4)

The sequence of this isoform differs from the canonical sequence as follows:
     95-116: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 314298Osteopontin
PRO_0000020321

Regions

Motif159 – 1613Cell attachment site

Amino acid modifications

Modified residue241Phosphoserine Ref.12
Modified residue261Phosphoserine Ref.12
Modified residue271Phosphoserine Ref.12
Modified residue621Phosphoserine Ref.12
Modified residue631Phosphoserine Ref.12
Modified residue661Phosphothreonine Ref.12
Modified residue761Phosphoserine Ref.12
Modified residue811Phosphoserine Ref.12 Ref.13
Modified residue991Phosphoserine Ref.12
Modified residue1021Phosphoserine Ref.12
Modified residue1051Phosphoserine Ref.12
Modified residue1081Phosphoserine Ref.12
Modified residue1171Phosphoserine Ref.12
Modified residue1201Phosphoserine Ref.12
Modified residue1231Phosphoserine Ref.12
Modified residue1261Phosphoserine Ref.12
Modified residue1291Phosphoserine Ref.12
Modified residue1851Phosphothreonine Ref.12
Modified residue1911Phosphoserine Ref.12
Modified residue1951Phosphoserine Ref.12
Modified residue2151Phosphoserine Ref.12
Modified residue2191Phosphoserine Ref.14 Ref.12
Modified residue2241Phosphoserine Ref.12
Modified residue2281Phosphoserine Ref.12
Modified residue2341Phosphoserine Ref.12
Modified residue2541Phosphoserine Ref.12
Modified residue2631Phosphoserine Ref.12
Modified residue2671Phosphoserine Ref.12
Modified residue2751Phosphoserine Ref.12
Modified residue2801Phosphoserine Ref.12
Modified residue3031Phosphoserine Ref.14 Ref.12
Modified residue3081Phosphoserine Ref.14 Ref.12
Modified residue3101Phosphoserine Ref.14 Ref.12
Glycosylation791N-linked (GlcNAc...) Ref.12
Glycosylation1061N-linked (GlcNAc...) Ref.12
Glycosylation1341O-linked (GalNAc...) Ref.12
Glycosylation1381O-linked (GalNAc...) Ref.12
Glycosylation1431O-linked (GalNAc...) Ref.12
Glycosylation1471O-linked (GalNAc...) Ref.12
Glycosylation1521O-linked (GalNAc...) Ref.12

Natural variations

Alternative sequence31 – 5727Missing in isoform C.
VSP_003777
Alternative sequence58 – 7114Missing in isoform B.
VSP_003778
Alternative sequence95 – 11622Missing in isoform D.
VSP_011639
Natural variant2241S → N. [dbSNP:rs7435825]
VAR_050432
Natural variant3011R → H. [dbSNP:rs4660]
VAR_014717

Experimental info

Sequence conflict1881D → H in BAA05949. Ref.6
Sequence conflict1881D → H in BAA05950. Ref.6
Sequence conflict1881D → H in BAA05951. Ref.6
Sequence conflict2371T → A in BAA05949. Ref.6
Sequence conflict2371T → A in BAA05950. Ref.6
Sequence conflict2371T → A in BAA05951. Ref.6
Sequence conflict275 – 2784SHEF → GNSL Ref.2

Secondary structure

... 314
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A (OPN-a) (OP1B) [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 4996429EC4752B86

FASTA31435,423
        10         20         30         40         50         60 
MRIAVICFCL LGITCAIPVK QADSGSSEEK QLYNKYPDAV ATWLNPDPSQ KQNLLAPQNA 

        70         80         90        100        110        120 
VSSEETNDFK QETLPSKSNE SHDHMDDMDD EDDDDHVDSQ DSIDSNDSDD VDDTDDSHQS 

       130        140        150        160        170        180 
DESHHSDESD ELVTDFPTDL PATEVFTPVV PTVDTYDGRG DSVVYGLRSK SKKFRRPDIQ 

       190        200        210        220        230        240 
YPDATDEDIT SHMESEELNG AYKAIPVAQD LNAPSDWDSR GKDSYETSQL DDQSAETHSH 

       250        260        270        280        290        300 
KQSRLYKRKA NDESNEHSDV IDSQELSKVS REFHSHEFHS HEDMLVVDPK SKEEDKHLKF 

       310 
RISHELDSAS SEVN 

« Hide

Isoform B (OPN-b) (OP1A).

Checksum: E844D1466BD20E64
Show »

FASTA30033,844
Isoform C (OPN-c).

Checksum: AF604D4E223BA02F
Show »

FASTA28732,355
Isoform D.

Checksum: E93E418982C3AD60
Show »

FASTA29233,017

References

« Hide 'large scale' references
[1]"The cDNA and derived amino acid sequence for human osteopontin."
Kiefer M.C., Bauer D.M., Barr P.J.
Nucleic Acids Res. 17:3306-3306(1989) [PubMed: 2726470] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]"cDNA cloning, mRNA distribution and heterogeneity, chromosomal location, and RFLP analysis of human osteopontin (OPN)."
Young M.F., Kerr J.M., Termine J.D., Wewer U.M., Wang M.G., McBride O.W., Fisher L.W.
Genomics 7:491-502(1990) [PubMed: 1974876] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
[3]"Inhibition of calcium oxalate crystal growth in vitro by uropontin: another member of the aspartic acid-rich protein superfamily."
Shiraga H., Min W., VanDusen W.J., Clayman M.D., Miner D., Terrell C.H., Sherbotie J.R., Foreman J.W., Przysiecki C., Neilson E.G., Hoyer J.R.
Proc. Natl. Acad. Sci. U.S.A. 89:426-430(1992) [PubMed: 1729712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[4]"Genomic organization of the human osteopontin gene: exclusion of the locus from a causative role in the pathogenesis of dentinogenesis imperfecta type II."
Crosby A.H., Edwards S.J., Murray J.C., Dixon M.J.
Genomics 27:155-160(1995) [PubMed: 7665163] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
[5]"Cloning and characterization of the human osteopontin gene and its promoter."
Hijiya N., Setoguchi M., Matsuura K., Higuchi Y., Akizuki S., Yamamoto S.
Biochem. J. 303:255-262(1994) [PubMed: 7945249] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
Tissue: Liver.
[6]"Expression of osteopontin in human glioma. Its correlation with the malignancy."
Saitoh Y., Kuratsu J., Takeshima H., Yamamoto S., Ushio Y.
Lab. Invest. 72:55-63(1995) [PubMed: 7837791] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
[7]Yu W., Sarginson J., Gibbs R.A.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Tissue: Brain.
[8]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed: 16303743] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
Tissue: Placenta.
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
Tissue: Brain and Kidney.
[10]"Molecular cloning and sequencing of cDNA encoding urinary stone protein, which is identical to osteopontin."
Kohri K., Suzuki Y., Yoshida K., Yamamoto K., Amasaki N., Yamate T., Umekawa T., Iguchi M., Sinohara H., Kurita T.
Biochem. Biophys. Res. Commun. 184:859-864(1992) [PubMed: 1575754] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 67-278.
Tissue: Kidney.
[11]"Purification of a human milk protein closely similar to tumor-secreted phosphoproteins and osteopontin."
Senger D.R., Perruzzi C.A., Papadopoulos A., Tenen D.G.
Biochim. Biophys. Acta 996:43-48(1989) [PubMed: 2736258] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-23 AND 169-182.
Tissue: Milk.
[12]"Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications."
Christensen B., Nielsen M.S., Haselmann K.F., Petersen T.E., Sorensen E.S.
Biochem. J. 390:285-292(2005) [PubMed: 15869464] [Abstract]
Cited for: PHOSPHORYLATION AT SER-24; SER-26; SER-27; SER-62; SER-63; THR-66; SER-76; SER-81; SER-99; SER-102; SER-108; SER-117; SER-120; SER-123; SER-129; THR-185; SER-191; SER-195; SER-215; SER-219; SER-224; SER-228; SER-234; SER-254; SER-263; SER-267; SER-275; SER-280; SER-303; SER-308; SER-310; SER-105 AND SER-126, GLYCOSYLATION AT ASN-79; ASN-106; THR-134; THR-138; THR-143; THR-147 AND THR-152.
Tissue: Milk.
[13]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, MASS SPECTROMETRY.
Tissue: Pituitary.
[14]"An initial characterization of the serum phosphoproteome."
Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A., Liotta L.A., Petricoin E.F. III
J. Proteome Res. 8:5523-5531(2009) [PubMed: 19824718] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-303; SER-308 AND SER-310, TISSUE SPECIFICITY, MASS SPECTROMETRY.
Tissue: Serum.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X13694 mRNA. Translation: CAA31984.1.
J04765 mRNA. Translation: AAA59974.1.
M83248 mRNA. Translation: AAA17675.1.
U20758 Genomic DNA. Translation: AAA86886.1.
D14813 Genomic DNA. Translation: BAA03554.1.
D28759 mRNA. Translation: BAA05949.1.
D28760 mRNA. Translation: BAA05950.1.
D28761 mRNA. Translation: BAA05951.1.
AF052124 mRNA. Translation: AAC28619.1.
AK075463 mRNA. Translation: BAC11635.1.
BC007016 mRNA. Translation: AAH07016.1.
BC017387 mRNA. Translation: AAH17387.1.
BC022844 mRNA. Translation: AAH22844.1.
IPIIPI00021000.
IPI00218874.
IPI00218875.
IPI00385896.
PIRS09575. S50028.
RefSeqNP_000573.1.
NP_001035147.1.
UniGeneHs.313.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CXDX-ray2.80P40-51[»]
3DSFX-ray2.80P40-51[»]
ProteinModelPortalP10451.
DisProtDP00214.
ModBaseSearch...

Protein-protein interaction databases

IntActP10451. 6 interactions.
MINTMINT-1380527.
STRINGP10451.

PTM databases

GlycoSuiteDBP10451.
PhosphoSiteP10451.

Proteomic databases

PRIDEP10451.

Genome annotation databases

EnsemblENST00000395080; ENSP00000378517; ENSG00000118785; Homo sapiens. [Genome view]
GeneID6696.
KEGGhsa:6696.
UCSCuc003hra.1. human.

Organism-specific databases

CTD6696.
GeneCardsGC04P088896.
H-InvDBHIX0004361.
HGNCHGNC:11255. SPP1.
HPACAB002212.
HPA027540.
HPA027541.
MIM166490. gene.
PharmGKBPA142672066.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG19072.
HOVERGENHBG001731.
InParanoidP10451.
OMAKQNLLAP.
OrthoDBEOG9M3CW7.
PhylomeDBP10451.

Enzyme and pathway databases

Pathway_Interaction_DBfgf_pathway. FGF signaling pathway.
avb3_integrin_pathway. Integrins in angiogenesis.
avb3_opn_pathway. Osteopontin-mediated events.
ReactomeREACT_13552. Integrin cell surface interactions.
REACT_16888. Signaling by PDGF.

Gene expression databases

ArrayExpressP10451.
BgeeP10451.
CleanExHS_SPP1.
GenevestigatorP10451.
GermOnlineENSG00000118785. Homo sapiens.

Family and domain databases

InterProIPR002038. Osteopontin.
IPR019841. Osteopontin_CS.
[Graphical view]
PANTHERPTHR10607. Osteopontin. 1 hit.
PfamPF00865. Osteopontin. 1 hit.
[Graphical view]
PRINTSPR00216. OSTEOPONTIN.
SMARTSM00017. OSTEO. 1 hit.
[Graphical view]
PROSITEPS00884. OSTEOPONTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio26103.
PMAP-CutDBP10451.
SOURCESearch...

Entry information

Entry nameOSTP_HUMAN
AccessionPrimary (citable) accession number: P10451
Secondary accession number(s): Q15681 expand/collapse secondary AC list , Q15682, Q15683, Q8NBK2, Q96IZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: August 10, 2010
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Index of human polymorphisms and disease mutations

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families