Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P10451 (OSTP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. Feed History...

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

Names and origin

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

Post-translational modification

Extensively phosphorylated by FAM20C in the extracellular medium at multiple sites within the S-x-E/pS motif. Ref.17 Ref.21

N- and O-glycosylated. Isoform 5 is GalNAc O-glycosylated at Thr-59 or Ser-62. Ref.17 Ref.22

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
Reference proteome
Gene Ontology (GO)
   Biological_processbiomineral tissue development

Inferred from electronic annotation. Source: UniProtKB-KW

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

decidualization

Traceable author statement PubMed 16720713. Source: BHF-UCL

embryo implantation

Traceable author statement PubMed 16720713. Source: BHF-UCL

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of collateral sprouting of intact axon in response to injury

Inferred from electronic annotation. Source: Ensembl

neutrophil chemotaxis

Inferred from electronic annotation. Source: Ensembl

osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of bone resorption

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell-substrate adhesion

Inferred from electronic annotation. Source: Ensembl

response to steroid hormone

Inferred from electronic annotation. Source: Ensembl

response to vitamin D

Inferred from direct assay PubMed 16720713. Source: BHF-UCL

   Cellular_componentapical part of cell

Inferred from electronic annotation. Source: Ensembl

cell projection

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 15516325. Source: BHF-UCL

membrane-bounded vesicle

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionextracellular matrix binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 20549562. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CD44P160702EBI-723648,EBI-490245

Alternative products

This entry describes 5 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.
Isoform 5 (identifier: P10451-5)

The sequence of this isoform differs from the canonical sequence as follows:
     59-72: Missing.
Note: No experimental confirmation available.

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.17
Modified residue261Phosphoserine Ref.17
Modified residue271Phosphoserine Ref.17
Modified residue621Phosphoserine Ref.17
Modified residue631Phosphoserine Ref.17
Modified residue661Phosphothreonine Ref.17
Modified residue761Phosphoserine Ref.17
Modified residue781Phosphoserine By similarity
Modified residue811Phosphoserine Ref.17 Ref.18
Modified residue991Phosphoserine Ref.17
Modified residue1021Phosphoserine Ref.17
Modified residue1051Phosphoserine Ref.17
Modified residue1081Phosphoserine Ref.17
Modified residue1171Phosphoserine Ref.17
Modified residue1201Phosphoserine Ref.17
Modified residue1231Phosphoserine Ref.17
Modified residue1261Phosphoserine Ref.17
Modified residue1291Phosphoserine Ref.17
Modified residue1851Phosphothreonine Ref.17
Modified residue1911Phosphoserine Ref.17
Modified residue1951Phosphoserine Ref.17
Modified residue2151Phosphoserine Ref.17
Modified residue2191Phosphoserine Ref.17 Ref.20
Modified residue2241Phosphoserine Ref.17 Ref.20
Modified residue2281Phosphoserine Ref.17
Modified residue2341Phosphoserine Ref.17 Ref.20
Modified residue2391Phosphoserine By similarity
Modified residue2541Phosphoserine Ref.17 Ref.20
Modified residue2631Phosphoserine Ref.17
Modified residue2671Phosphoserine Ref.17
Modified residue2701Phosphoserine By similarity
Modified residue2751Phosphoserine Ref.17
Modified residue2801Phosphoserine Ref.17
Modified residue2911Phosphoserine By similarity
Modified residue3031Phosphoserine Ref.17
Modified residue3081Phosphoserine Ref.17
Modified residue3101Phosphoserine Ref.17
Glycosylation791N-linked (GlcNAc...) Ref.17
Glycosylation1061N-linked (GlcNAc...) Ref.17
Glycosylation1341O-linked (GalNAc...) Ref.17
Glycosylation1381O-linked (GalNAc...) Ref.17
Glycosylation1431O-linked (GalNAc...) Ref.17
Glycosylation1471O-linked (GalNAc...) Ref.17
Glycosylation1521O-linked (GalNAc...) Ref.17

Natural variations

Alternative sequence31 – 5727Missing in isoform C.
VSP_003777
Alternative sequence58 – 7114Missing in isoform B.
VSP_003778
Alternative sequence59 – 7214Missing in isoform 5.
VSP_043695
Alternative sequence95 – 11622Missing in isoform D.
VSP_011639
Natural variant2241S → N.
Corresponds to variant rs7435825 [ dbSNP | Ensembl ].
VAR_050432
Natural variant3011R → H.
Corresponds to variant rs4660 [ dbSNP | Ensembl ].
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) [UniParc].

Checksum: E844D1466BD20E64
Show »

FASTA30033,844
Isoform C (OPN-c) [UniParc].

Checksum: AF604D4E223BA02F
Show »

FASTA28732,355
Isoform D [UniParc].

Checksum: E93E418982C3AD60
Show »

FASTA29233,017
Isoform 5 [UniParc].

Checksum: B844D7EBDD096CBF
Show »

FASTA30033,843

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]"Osteopontin splice variants in Indian breast cancer patients as biomarker."
Sivakumar S., Niranjali Devaraj S.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
[9]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; C AND 5).
Tissue: Kidney and Subthalamic nucleus.
[10]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
Tissue: Placenta.
[11]"A computer system platform used to predict novel genes."
Yu Z., Zheng Z., Tang T., Fu Y.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
[12]"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].
[13]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; B AND C).
Tissue: Brain and Kidney.
[15]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 67-278.
Tissue: Kidney.
[16]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-23 AND 169-182.
Tissue: Milk.
[17]"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] [Europe PMC] [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.
[18]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Pituitary.
[19]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-224; SER-234 AND SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Secreted kinase phosphorylates extracellular proteins that regulate biomineralization."
Tagliabracci V.S., Engel J.L., Wen J., Wiley S.E., Worby C.A., Kinch L.N., Xiao J., Grishin N.V., Dixon J.E.
Science 336:1150-1153(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY FAM20C.
[22]"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
Halim A., Ruetschi U., Larson G., Nilsson J.
J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
+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.
AK290104 mRNA. Translation: BAF82793.1.
JF412667 mRNA. Translation: AEA49031.1.
AK075463 mRNA. Translation: BAC11635.1.
AK290090 mRNA. Translation: BAF82779.1.
AK296035 mRNA. Translation: BAG58801.1.
AK315461 mRNA. Translation: BAG37848.1.
DQ839491 mRNA. Translation: ABI63352.1.
DQ846871 mRNA. Translation: ABI63358.1.
AC131944 Genomic DNA. Translation: AAY41035.1.
CH471057 Genomic DNA. Translation: EAX06004.1.
CH471057 Genomic DNA. Translation: EAX06005.1.
CH471057 Genomic DNA. Translation: EAX06006.1.
BC007016 mRNA. Translation: AAH07016.1.
BC017387 mRNA. Translation: AAH17387.1.
BC022844 mRNA. Translation: AAH22844.1.
BC093033 mRNA. Translation: AAH93033.1.
CCDSCCDS34027.1. [P10451-3]
CCDS3626.1. [P10451-5]
CCDS43250.1. [P10451-1]
PIRS09575. S50028.
RefSeqNP_000573.1. NM_000582.2. [P10451-5]
NP_001035147.1. NM_001040058.1. [P10451-1]
NP_001035149.1. NM_001040060.1. [P10451-3]
NP_001238758.1. NM_001251829.1.
NP_001238759.1. NM_001251830.1.
UniGeneHs.313.

3D structure databases

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

Protein-protein interaction databases

BioGrid112574. 75 interactions.
DIPDIP-49933N.
IntActP10451. 9 interactions.
MINTMINT-1380527.
STRING9606.ENSP00000378517.

PTM databases

PhosphoSiteP10451.
UniCarbKBP10451.

Polymorphism databases

DMDM129260.

Proteomic databases

MaxQBP10451.
PaxDbP10451.
PRIDEP10451.

Protocols and materials databases

DNASU6696.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000237623; ENSP00000237623; ENSG00000118785. [P10451-5]
ENST00000360804; ENSP00000354042; ENSG00000118785. [P10451-3]
ENST00000395080; ENSP00000378517; ENSG00000118785. [P10451-1]
GeneID6696.
KEGGhsa:6696.
UCSCuc003hra.3. human. [P10451-1]
uc003hrb.3. human. [P10451-3]
uc003hrc.3. human. [P10451-5]

Organism-specific databases

CTD6696.
GeneCardsGC04P088896.
H-InvDBHIX0004361.
HGNCHGNC:11255. SPP1.
HPACAB002212.
HPA027541.
MIM166490. gene.
neXtProtNX_P10451.
Orphanet93552. Pediatric systemic lupus erythematosus.
536. Systemic lupus erythematosus.
PharmGKBPA36085.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG73598.
HOGENOMHOG000059656.
HOVERGENHBG001731.
InParanoidP10451.
KOK06250.
OMAVICFCLL.
OrthoDBEOG7R832D.
PhylomeDBP10451.
TreeFamTF350201.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_206066. Extracellular matrix organization.

Gene expression databases

ArrayExpressP10451.
BgeeP10451.
CleanExHS_SPP1.
GenevestigatorP10451.

Family and domain databases

InterProIPR002038. Osteopontin.
IPR019841. Osteopontin_CS.
[Graphical view]
PANTHERPTHR10607. PTHR10607. 1 hit.
PfamPF00865. Osteopontin. 1 hit.
[Graphical view]
PRINTSPR00216. OSTEOPONTIN.
SMARTSM00017. OSTEO. 1 hit.
[Graphical view]
PROSITEPS00884. OSTEOPONTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSPP1. human.
EvolutionaryTraceP10451.
GeneWikiOsteopontin.
GenomeRNAi6696.
NextBio26103.
PMAP-CutDBP10451.
PROP10451.
SOURCESearch...

Entry information

Entry nameOSTP_HUMAN
AccessionPrimary (citable) accession number: P10451
Secondary accession number(s): B2RDA1 expand/collapse secondary AC list , Q15681, Q15682, Q15683, Q4W597, Q567T5, Q8NBK2, Q96IZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 166 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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