P10451 (OSTP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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

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 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 Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	biomineral 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 inflammatory response Inferred from electronic annotation. Source: Compara negative regulation of collateral sprouting of intact axon in response to injury Inferred from electronic annotation. Source: Compara neutrophil chemotaxis Inferred from electronic annotation. Source: Compara osteoblast differentiation Inferred from electronic annotation. Source: Compara positive regulation of bone resorption Inferred from electronic annotation. Source: Compara positive regulation of cell-substrate adhesion Inferred from electronic annotation. Source: Compara response to steroid hormone stimulus Inferred from electronic annotation. Source: Compara response to vitamin D Inferred from direct assay PubMed 16720713. Source: BHF-UCL
Cellular_component	apical part of cell Inferred from electronic annotation. Source: Compara cell projection Inferred from electronic annotation. Source: Compara extracellular space Inferred from direct assay PubMed 15516325. Source: BHF-UCL membrane-bounded vesicle Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	extracellular matrix binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Potential

Chain

17 – 314

298

Osteopontin

PRO_0000020321

Regions

Motif

159 – 161

3

Cell attachment site

Amino acid modifications

Modified residue

24

1

Phosphoserine Ref.17

Modified residue

26

1

Phosphoserine Ref.17

Modified residue

27

1

Phosphoserine Ref.17

Modified residue

62

1

Phosphoserine Ref.17

Modified residue

63

1

Phosphoserine Ref.17

Modified residue

66

1

Phosphothreonine Ref.17

Modified residue

76

1

Phosphoserine Ref.17

Modified residue

78

1

Phosphoserine By similarity

Modified residue

81

1

Phosphoserine Ref.17 Ref.18

Modified residue

99

1

Phosphoserine Ref.17

Modified residue

102

1

Phosphoserine Ref.17

Modified residue

105

1

Phosphoserine Ref.17

Modified residue

108

1

Phosphoserine Ref.17

Modified residue

117

1

Phosphoserine Ref.17

Modified residue

120

1

Phosphoserine Ref.17

Modified residue

123

1

Phosphoserine Ref.17

Modified residue

126

1

Phosphoserine Ref.17

Modified residue

129

1

Phosphoserine Ref.17

Modified residue

185

1

Phosphothreonine Ref.17

Modified residue

191

1

Phosphoserine Ref.17

Modified residue

195

1

Phosphoserine Ref.17

Modified residue

215

1

Phosphoserine Ref.17

Modified residue

219

1

Phosphoserine Ref.17 Ref.20

Modified residue

224

1

Phosphoserine Ref.17 Ref.20

Modified residue

228

1

Phosphoserine Ref.17

Modified residue

234

1

Phosphoserine Ref.17 Ref.20

Modified residue

239

1

Phosphoserine By similarity

Modified residue

254

1

Phosphoserine Ref.17 Ref.20

Modified residue

263

1

Phosphoserine Ref.17

Modified residue

267

1

Phosphoserine Ref.17

Modified residue

270

1

Phosphoserine By similarity

Modified residue

275

1

Phosphoserine Ref.17

Modified residue

280

1

Phosphoserine Ref.17

Modified residue

303

1

Phosphoserine Ref.17

Modified residue

308

1

Phosphoserine Ref.17

Modified residue

310

1

Phosphoserine Ref.17

Glycosylation

79

1

N-linked (GlcNAc...) Ref.17

Glycosylation

106

1

N-linked (GlcNAc...) Ref.17

Glycosylation

134

1

O-linked (GalNAc...) Ref.17

Glycosylation

138

1

O-linked (GalNAc...) Ref.17

Glycosylation

143

1

O-linked (GalNAc...) Ref.17

Glycosylation

147

1

O-linked (GalNAc...) Ref.17

Glycosylation

152

1

O-linked (GalNAc...) Ref.17

Natural variations

Alternative sequence

31 – 57

27

Missing in isoform C.

VSP_003777

Alternative sequence

58 – 71

14

Missing in isoform B.

VSP_003778

Alternative sequence

59 – 72

14

Missing in isoform 5.

VSP_043695

Alternative sequence

95 – 116

22

Missing in isoform D.

VSP_011639

Natural variant

224

1

S → N.
Corresponds to variant rs7435825 [ dbSNP | Ensembl ].

VAR_050432

Natural variant

301

1

R → H.
Corresponds to variant rs4660 [ dbSNP | Ensembl ].

VAR_014717

Experimental info

Sequence conflict

188

1

D → H in BAA05949. Ref.6

Sequence conflict

188

1

D → H in BAA05950. Ref.6

Sequence conflict

188

1

D → H in BAA05951. Ref.6

Sequence conflict

237

1

T → A in BAA05949. Ref.6

Sequence conflict

237

1

T → A in BAA05950. Ref.6

Sequence conflict

237

1

T → A in BAA05951. Ref.6

Sequence conflict

275 – 278

4

SHEF → GNSL Ref.2

Secondary structure

1

.

.

.

314

Helix Strand Turn

Details...

Beta strand

44 – 47

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (OPN-a) (OP1B) [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 4996429EC4752B86	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
	Isoform B (OPN-b) (OP1A) [UniParc]. Checksum: E844D1466BD20E64	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
	Isoform C (OPN-c) [UniParc]. Checksum: AF604D4E223BA02F	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
	Isoform D [UniParc]. Checksum: E93E418982C3AD60	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
	Isoform 5 [UniParc]. Checksum: B844D7EBDD096CBF	FASTA	300	33,843
	10 20 30 40 50 60 MRIAVICFCL LGITCAIPVK QADSGSSEEK QLYNKYPDAV ATWLNPDPSQ KQNLLAPQTL 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

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] [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. , 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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

Osteopontin entry

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.

IPI

IPI00021000.
IPI00218874.
IPI00218875.
IPI00306339.
IPI00385896.

PIR

S09575. S50028.

RefSeq

NP_000573.1. NM_000582.2.
NP_001035147.1. NM_001040058.1.
NP_001035149.1. NM_001040060.1.
NP_001238758.1. NM_001251829.1.
NP_001238759.1. NM_001251830.1.

UniGene

Hs.313.

3D structure databases

PDBe
RCSB PDB
PDBj

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.

ProteinModelPortal

P10451.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-49933N.

IntAct

P10451. 8 interactions.

MINT

MINT-1380527.

STRING

9606.ENSP00000378517.

PTM databases

GlycoSuiteDB

P10451.

PhosphoSite

P10451.

Polymorphism databases

DMDM

129260.

Proteomic databases

PaxDb

P10451.

PRIDE

P10451.

Protocols and materials databases

DNASU

6696.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000237623; ENSP00000237623; ENSG00000118785.
ENST00000360804; ENSP00000354042; ENSG00000118785.
ENST00000395080; ENSP00000378517; ENSG00000118785.

GeneID

6696.

KEGG

hsa:6696.

UCSC

uc003hra.3. human.

Organism-specific databases

CTD

6696.

GeneCards

GC04P088896.

H-InvDB

HIX0004361.

HGNC

HGNC:11255. SPP1.

HPA

CAB002212.
HPA027541.

MIM

166490. gene.

neXtProt

NX_P10451.

PharmGKB

PA36085.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG73598.

HOGENOM

HOG000059656.

HOVERGEN

HBG001731.

InParanoid

P10451.

KO

K06250.

OMA

KQNLLAP.

PhylomeDB

P10451.

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_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P10451.

Bgee

P10451.

CleanEx

HS_SPP1.

Genevestigator

P10451.

GermOnline

ENSG00000118785. Homo sapiens.

Family and domain databases

InterPro

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

PANTHER

PTHR10607. PTHR10607. 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

ChEMBL

CHEMBL1741309.

ChiTaRS

SPP1. human.

EvolutionaryTrace

P10451.

GenomeRNAi

6696.

NextBio

26103.

PMAP-CutDB

P10451.

SOURCE

Search...

Entry information

Entry name

OSTP_HUMAN

Accession

Primary (citable) accession number: P10451
Secondary accession number(s): B2RDA1 , 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:	May 1, 2013
This is version 154 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.