Osteopontin precursor - Homo sapiens (Human)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P10451 (OSTP_HUMAN)

Last modified June 16, 2009. Version 113. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

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.
Post-translational modification	Extensively phosphorylated on clustered serine residues. Ref.12 Ref.13 N- and O-glycosylated. Ref.12
Involvement in disease	This protein plays a principal role in urinary stone formation as the stone matrix.
Sequence similarities	Belongs to the osteopontin family.

Hide | Top

Ontologies

Keywords
Biological process	Biomineralization Cell adhesion
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Ligand	Sialic acid
Molecular function	Cytokine
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW decidualization Traceable author statement. Source: UniProtKB embryo implantation Traceable author statement. Source: UniProtKB ossification Inferred from electronic annotation. Source: UniProtKB-KW response to vitamin D Inferred from direct assay. Source: UniProtKB
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	cytokine activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

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.

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

Potential

Chain

17 – 314

298

Osteopontin

PRO_0000020321

Regions

Motif

159 – 161

Cell attachment site

Amino acid modifications

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphothreonine Ref.12

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphoserine Ref.12 Ref.13

Modified residue

Phosphoserine Ref.12

Modified residue

102

Phosphoserine Ref.12

Modified residue

105

Phosphoserine Ref.12

Modified residue

108

Phosphoserine Ref.12

Modified residue

117

Phosphoserine Ref.12

Modified residue

120

Phosphoserine Ref.12

Modified residue

123

Phosphoserine Ref.12

Modified residue

126

Phosphoserine Ref.12

Modified residue

129

Phosphoserine Ref.12

Modified residue

185

Phosphothreonine Ref.12

Modified residue

191

Phosphoserine Ref.12

Modified residue

195

Phosphoserine Ref.12

Modified residue

215

Phosphoserine Ref.12

Modified residue

219

Phosphoserine Ref.12

Modified residue

224

Phosphoserine Ref.12

Modified residue

228

Phosphoserine Ref.12

Modified residue

234

Phosphoserine Ref.12

Modified residue

254

Phosphoserine Ref.12

Modified residue

263

Phosphoserine Ref.12

Modified residue

267

Phosphoserine Ref.12

Modified residue

275

Phosphoserine Ref.12

Modified residue

280

Phosphoserine Ref.12

Modified residue

303

Phosphoserine Ref.12

Modified residue

308

Phosphoserine Ref.12

Modified residue

310

Phosphoserine Ref.12

Glycosylation

N-linked (GlcNAc...) Ref.12

Glycosylation

106

N-linked (GlcNAc...) Ref.12

Glycosylation

134

O-linked (GalNAc...) Ref.12

Glycosylation

138

O-linked (GalNAc...) Ref.12

Glycosylation

143

O-linked (GalNAc...) Ref.12

Glycosylation

147

O-linked (GalNAc...) Ref.12

Glycosylation

152

O-linked (GalNAc...) Ref.12

Natural variations

Alternative sequence

31 – 57

Missing in isoform C.

VSP_003777

Alternative sequence

58 – 71

Missing in isoform B.

VSP_003778

Alternative sequence

95 – 116

Missing in isoform D.

VSP_011639

Natural variant

224

S → N: dbSNP rs7435825.

VAR_050432

Natural variant

301

R → H: dbSNP rs4660.

VAR_014717

Experimental info

Sequence conflict

188

D → H in BAA05949. Ref.6

Sequence conflict

188

D → H in BAA05950. Ref.6

Sequence conflict

188

D → H in BAA05951. Ref.6

Sequence conflict

237

T → A in BAA05949. Ref.6

Sequence conflict

237

T → A in BAA05950. Ref.6

Sequence conflict

237

T → A in BAA05951. Ref.6

Sequence conflict

275 – 278

SHEF → GNSL Ref.2

Hide | Top

Sequences

Sequence		Length	Mass (Da)
Isoform A (OPN-a) (OP1B) [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 4996429EC4752B86 Show »	FASTA	314	35,423
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 »	FASTA	300	33,844
10 20 30 40 50 60 MRIAVICFCL LGITCAIPVK QADSGSSEEK QLYNKYPDAV ATWLNPDPSQ KQNLLAPETL 70 80 90 100 110 120 PSKSNESHDH MDDMDDEDDD DHVDSQDSID SNDSDDVDDT DDSHQSDESH HSDESDELVT 130 140 150 160 170 180 DFPTDLPATE VFTPVVPTVD TYDGRGDSVV YGLRSKSKKF RRPDIQYPDA TDEDITSHME 190 200 210 220 230 240 SEELNGAYKA IPVAQDLNAP SDWDSRGKDS YETSQLDDQS AETHSHKQSR LYKRKANDES 250 260 270 280 290 300 NEHSDVIDSQ ELSKVSREFH SHEFHSHEDM LVVDPKSKEE DKHLKFRISH ELDSASSEVN « Hide
Isoform C (OPN-c). Checksum: AF604D4E223BA02F Show »	FASTA	287	32,355
10 20 30 40 50 60 MRIAVICFCL LGITCAIPVK QADSGSSEEK QNAVSSEETN DFKQETLPSK SNESHDHMDD 70 80 90 100 110 120 MDDEDDDDHV DSQDSIDSND SDDVDDTDDS HQSDESHHSD ESDELVTDFP TDLPATEVFT 130 140 150 160 170 180 PVVPTVDTYD GRGDSVVYGL RSKSKKFRRP DIQYPDATDE DITSHMESEE LNGAYKAIPV 190 200 210 220 230 240 AQDLNAPSDW DSRGKDSYET SQLDDQSAET HSHKQSRLYK RKANDESNEH SDVIDSQELS 250 260 270 280 KVSREFHSHE FHSHEDMLVV DPKSKEEDKH LKFRISHELD SASSEVN « Hide
Isoform D. Checksum: E93E418982C3AD60 Show »	FASTA	292	33,017
10 20 30 40 50 60 MRIAVICFCL LGITCAIPVK QADSGSSEEK QLYNKYPDAV ATWLNPDPSQ KQNLLAPQNA 70 80 90 100 110 120 VSSEETNDFK QETLPSKSNE SHDHMDDMDD EDDDSHQSDE SHHSDESDEL VTDFPTDLPA 130 140 150 160 170 180 TEVFTPVVPT VDTYDGRGDS VVYGLRSKSK KFRRPDIQYP DATDEDITSH MESEELNGAY 190 200 210 220 230 240 KAIPVAQDLN APSDWDSRGK DSYETSQLDD QSAETHSHKQ SRLYKRKAND ESNEHSDVID 250 260 270 280 290 SQELSKVSRE FHSHEFHSHE DMLVVDPKSK EEDKHLKFRI SHELDSASSE VN « Hide

Hide | Top

References

	« Hide 'large scale' referencesShow '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]	"HRI human cDNA sequencing project." Ota T., Nishikawa T., Suzuki Y., Kawai-Hio Y., Hayashi K., Ishii S., Saito K., Yamamoto J., Wakamatsu A., Nagai T., Nakamura Y., Nagahari K., Sugano S., Isogai T. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases 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.
+	Additional computationally mapped references.

Hide | Top

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

Osteopontin entry

Hide | Top

Cross-references

Sequence databases

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.

IPI

IPI00021000.
IPI00218874.
IPI00218875.
IPI00385896.

PIR

S09575. S50028.

RefSeq

NP_000573.1.
NP_001035147.1.

UniGene

Hs.313

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CXD	X-ray	2.80	P	40-51	[»]
3DSF	X-ray	2.80	P	40-51	[»]

DisProt

DP00214.

ModBase

Search...

Protein-protein interaction databases

IntAct

P10451. 5 interactions.

PTM databases

GlycoSuiteDB

P10451.

PhosphoSite

P10451.

Proteomic databases

PRIDE

P10451.

Genome annotation databases

Ensembl

ENSG00000118785. Homo sapiens. [Contig view]

GeneID

6696.

KEGG

hsa:6696.

Organism-specific databases

GeneCards

GC04P089115.

H-InvDB

HIX0004361.

HGNC

HGNC:11255. SPP1.

HPA

CAB002212.

MIM

166490. gene.

PharmGKB

PA142672066.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P10451.

HOVERGEN

P10451.

OMA

P10451. KQNLLAP.

Enzyme and pathway databases

Pathway_Interaction_DB

fgf_pathway. FGF signaling pathway.
avb3_integrin_pathway. Integrins in angiogenesis.
avb3_opn_pathway. Osteopontin-mediated events.

Reactome

REACT_13552. Integrin cell surface interactions.

Gene expression databases

ArrayExpress

P10451.

Bgee

P10451.

CleanEx

HS_SPP1.

GermOnline

ENSG00000118785. Homo sapiens.

Family and domain databases

InterPro

IPR002038. Osteopontin.
IPR019841. Osteopontin_CS.
[Graphical view]

PANTHER

PTHR10607. Osteopontin. 1 hit.

Pfam

PF00865. Osteopontin. 1 hit.
[Graphical view]

PRINTS

PR00216. OSTEOPONTIN.

SMART

SM00017. OSTEO. 1 hit.
[Graphical view]

PROSITE

PS00884. OSTEOPONTIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

26103.

PMAP-CutDB

P10451.

SOURCE

Search...

Hide | Top

Entry information

Entry name

OSTP_HUMAN

Accession

Primary (citable) accession number: P10451
Secondary accession number(s): Q15681

Q96IZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	June 16, 2009
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top