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Osteopontin (Bone sialoprotein 1) (Nephropontin) (Secreted phosphoprotein 1) (SPP-1) (Urinary stone protein) (Uropontin)

 OSTP_HUMAN              Reviewed;         314 AA.
P10451; B2RDA1; Q15681; Q15682; Q15683; Q4W597; Q567T5; Q8NBK2;
Q96IZ1;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
23-MAY-2018, entry version 202.
RecName: Full=Osteopontin;
AltName: Full=Bone sialoprotein 1;
AltName: Full=Nephropontin;
AltName: Full=Secreted phosphoprotein 1;
Short=SPP-1;
AltName: Full=Urinary stone protein;
AltName: Full=Uropontin;
Flags: Precursor;
Name=SPP1; Synonyms=BNSP, OPN; ORFNames=PSEC0156;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=2726470; DOI=10.1093/nar/17.8.3306;
Kiefer M.C., Bauer D.M., Barr P.J.;
"The cDNA and derived amino acid sequence for human osteopontin.";
Nucleic Acids Res. 17:3306-3306(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
PubMed=1974876; DOI=10.1016/0888-7543(90)90191-V;
Young M.F., Kerr J.M., Termine J.D., Wewer U.M., Wang M.G.,
McBride O.W., Fisher L.W.;
"cDNA cloning, mRNA distribution and heterogeneity, chromosomal
location, and RFLP analysis of human osteopontin (OPN).";
Genomics 7:491-502(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=1729712; DOI=10.1073/pnas.89.1.426;
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.;
"Inhibition of calcium oxalate crystal growth in vitro by uropontin:
another member of the aspartic acid-rich protein superfamily.";
Proc. Natl. Acad. Sci. U.S.A. 89:426-430(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
PubMed=7665163; DOI=10.1006/geno.1995.1018;
Crosby A.H., Edwards S.J., Murray J.C., Dixon M.J.;
"Genomic organization of the human osteopontin gene: exclusion of the
locus from a causative role in the pathogenesis of dentinogenesis
imperfecta type II.";
Genomics 27:155-160(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
TISSUE=Liver;
PubMed=7945249; DOI=10.1042/bj3030255;
Hijiya N., Setoguchi M., Matsuura K., Higuchi Y., Akizuki S.,
Yamamoto S.;
"Cloning and characterization of the human osteopontin gene and its
promoter.";
Biochem. J. 303:255-262(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
PubMed=7837791;
Saitoh Y., Kuratsu J., Takeshima H., Yamamoto S., Ushio Y.;
"Expression of osteopontin in human glioma. Its correlation with the
malignancy.";
Lab. Invest. 72:55-63(1995).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Brain;
Yu W., Sarginson J., Gibbs R.A.;
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
Sivakumar S., Niranjali Devaraj S.;
"Osteopontin splice variants in Indian breast cancer patients as
biomarker.";
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; C AND 5).
TISSUE=Kidney, and Subthalamic nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
TISSUE=Placenta;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
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.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Yu Z., Zheng Z., Tang T., Fu Y.;
"A computer system platform used to predict novel genes.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; B AND C).
TISSUE=Brain, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 67-278.
TISSUE=Kidney;
PubMed=1575754; DOI=10.1016/0006-291X(92)90669-C;
Kohri K., Suzuki Y., Yoshida K., Yamamoto K., Amasaki N., Yamate T.,
Umekawa T., Iguchi M., Sinohara H., Kurita T.;
"Molecular cloning and sequencing of cDNA encoding urinary stone
protein, which is identical to osteopontin.";
Biochem. Biophys. Res. Commun. 184:859-864(1992).
[16]
PROTEIN SEQUENCE OF 17-23 AND 169-182.
TISSUE=Milk;
PubMed=2736258; DOI=10.1016/0167-4838(89)90092-7;
Senger D.R., Perruzzi C.A., Papadopoulos A., Tenen D.G.;
"Purification of a human milk protein closely similar to tumor-
secreted phosphoproteins and osteopontin.";
Biochim. Biophys. Acta 996:43-48(1989).
[17]
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, AND GLYCOSYLATION AT
ASN-79; ASN-106; THR-134; THR-138; THR-143; THR-147 AND THR-152.
TISSUE=Milk;
PubMed=15869464; DOI=10.1042/BJ20050341;
Christensen B., Nielsen M.S., Haselmann K.F., Petersen T.E.,
Sorensen E.S.;
"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.";
Biochem. J. 390:285-292(2005).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pituitary;
PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-224; SER-234
AND SER-254, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
PHOSPHORYLATION BY FAM20C.
PubMed=22582013; DOI=10.1126/science.1217817;
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.;
"Secreted kinase phosphorylates extracellular proteins that regulate
biomineralization.";
Science 336:1150-1153(2012).
[21]
GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23234360; DOI=10.1021/pr300963h;
Halim A., Ruetschi U., Larson G., Nilsson J.;
"LC-MS/MS characterization of O-glycosylation sites and glycan
structures of human cerebrospinal fluid glycoproteins.";
J. Proteome Res. 12:573-584(2013).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
PHOSPHORYLATION AT SER-26; SER-27; SER-62; SER-63; THR-190; SER-191;
SER-195; SER-215; SER-219; SER-224; TYR-225; SER-228; SER-234;
THR-237; SER-239; SER-243; SER-254; SER-258; SER-263; SER-267;
SER-270; SER-275; SER-280; SER-291; SER-303; SER-308; SER-310 AND
SER-311.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
-!- FUNCTION: Binds tightly to hydroxyapatite. Appears to form an
integral part of the mineralized matrix. Probably important to
cell-matrix interaction.
-!- FUNCTION: 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. {ECO:0000250}.
-!- SUBUNIT: Ligand for integrin alpha-V/beta-3.
-!- INTERACTION:
P16070:CD44; NbExp=4; IntAct=EBI-723648, EBI-490245;
Q8IXL6:FAM20C; NbExp=3; IntAct=EBI-723648, EBI-7147442;
P50222:MEOX2; NbExp=3; IntAct=EBI-723648, EBI-748397;
O43765:SGTA; NbExp=8; IntAct=EBI-723648, EBI-347996;
Q96EQ0:SGTB; NbExp=4; IntAct=EBI-723648, EBI-744081;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=A; Synonyms=OPN-a, OP1B;
IsoId=P10451-1; Sequence=Displayed;
Name=B; Synonyms=OPN-b, OP1A;
IsoId=P10451-2; Sequence=VSP_003778;
Name=C; Synonyms=OPN-c;
IsoId=P10451-3; Sequence=VSP_003777;
Name=D;
IsoId=P10451-4; Sequence=VSP_011639;
Name=5;
IsoId=P10451-5; Sequence=VSP_043695;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Bone. Found in plasma.
-!- PTM: Extensively phosphorylated by FAM20C in the extracellular
medium at multiple sites within the S-x-E/pS motif.
{ECO:0000269|PubMed:15869464, ECO:0000269|PubMed:22582013,
ECO:0000269|PubMed:26091039}.
-!- PTM: N- and O-glycosylated. Isoform 5 is GalNAc O-glycosylated at
Thr-59 or Ser-62. {ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:23234360}.
-!- SIMILARITY: Belongs to the osteopontin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SPP1ID42379ch4q22.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Osteopontin entry;
URL="https://en.wikipedia.org/wiki/Osteopontin";
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EMBL; X13694; CAA31984.1; -; mRNA.
EMBL; J04765; AAA59974.1; -; mRNA.
EMBL; M83248; AAA17675.1; -; mRNA.
EMBL; U20758; AAA86886.1; -; Genomic_DNA.
EMBL; D14813; BAA03554.1; -; Genomic_DNA.
EMBL; D28759; BAA05949.1; -; mRNA.
EMBL; D28760; BAA05950.1; -; mRNA.
EMBL; D28761; BAA05951.1; -; mRNA.
EMBL; AF052124; AAC28619.1; -; mRNA.
EMBL; AK290104; BAF82793.1; -; mRNA.
EMBL; JF412667; AEA49031.1; -; mRNA.
EMBL; AK075463; BAC11635.1; -; mRNA.
EMBL; AK290090; BAF82779.1; -; mRNA.
EMBL; AK296035; BAG58801.1; -; mRNA.
EMBL; AK315461; BAG37848.1; -; mRNA.
EMBL; DQ839491; ABI63352.1; -; mRNA.
EMBL; DQ846871; ABI63358.1; -; mRNA.
EMBL; AC131944; AAY41035.1; -; Genomic_DNA.
EMBL; CH471057; EAX06004.1; -; Genomic_DNA.
EMBL; CH471057; EAX06005.1; -; Genomic_DNA.
EMBL; CH471057; EAX06006.1; -; Genomic_DNA.
EMBL; BC007016; AAH07016.1; -; mRNA.
EMBL; BC017387; AAH17387.1; -; mRNA.
EMBL; BC022844; AAH22844.1; -; mRNA.
EMBL; BC093033; AAH93033.1; -; mRNA.
CCDS; CCDS34027.1; -. [P10451-3]
CCDS; CCDS3626.1; -. [P10451-5]
CCDS; CCDS43250.1; -. [P10451-1]
PIR; S50028; S09575.
RefSeq; NP_000573.1; NM_000582.2. [P10451-5]
RefSeq; NP_001035147.1; NM_001040058.1. [P10451-1]
RefSeq; NP_001035149.1; NM_001040060.1. [P10451-3]
RefSeq; NP_001238758.1; NM_001251829.1.
RefSeq; NP_001238759.1; NM_001251830.1.
UniGene; Hs.313; -.
PDB; 3CXD; X-ray; 2.80 A; P=40-51.
PDB; 3DSF; X-ray; 2.80 A; P=40-51.
PDBsum; 3CXD; -.
PDBsum; 3DSF; -.
DisProt; DP00214; -.
BioGrid; 112574; 81.
CORUM; P10451; -.
DIP; DIP-49933N; -.
ELM; P10451; -.
IntAct; P10451; 16.
STRING; 9606.ENSP00000378517; -.
ChEMBL; CHEMBL1741309; -.
GlyConnect; 474; -.
iPTMnet; P10451; -.
PhosphoSitePlus; P10451; -.
UniCarbKB; P10451; -.
BioMuta; SPP1; -.
DMDM; 129260; -.
PaxDb; P10451; -.
PeptideAtlas; P10451; -.
PRIDE; P10451; -.
DNASU; 6696; -.
Ensembl; ENST00000237623; ENSP00000237623; ENSG00000118785. [P10451-5]
Ensembl; ENST00000360804; ENSP00000354042; ENSG00000118785. [P10451-3]
Ensembl; ENST00000395080; ENSP00000378517; ENSG00000118785. [P10451-1]
Ensembl; ENST00000614857; ENSP00000477824; ENSG00000118785. [P10451-4]
GeneID; 6696; -.
KEGG; hsa:6696; -.
UCSC; uc003hra.4; human. [P10451-1]
CTD; 6696; -.
DisGeNET; 6696; -.
EuPathDB; HostDB:ENSG00000118785.13; -.
GeneCards; SPP1; -.
H-InvDB; HIX0004361; -.
HGNC; HGNC:11255; SPP1.
HPA; CAB002212; -.
HPA; HPA027540; -.
HPA; HPA027541; -.
MalaCards; SPP1; -.
MIM; 166490; gene.
neXtProt; NX_P10451; -.
OpenTargets; ENSG00000118785; -.
Orphanet; 93552; Pediatric systemic lupus erythematosus.
Orphanet; 536; Systemic lupus erythematosus.
PharmGKB; PA36085; -.
eggNOG; ENOG410IVP1; Eukaryota.
eggNOG; ENOG41116B5; LUCA.
GeneTree; ENSGT00390000002509; -.
HOGENOM; HOG000059656; -.
HOVERGEN; HBG001731; -.
InParanoid; P10451; -.
KO; K06250; -.
OMA; VICFCLL; -.
OrthoDB; EOG091G0KVC; -.
PhylomeDB; P10451; -.
TreeFam; TF350201; -.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-186797; Signaling by PDGF.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8949275; RUNX3 Regulates Immune Response and Cell Migration.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; P10451; -.
ChiTaRS; SPP1; human.
EvolutionaryTrace; P10451; -.
GeneWiki; Osteopontin; -.
GenomeRNAi; 6696; -.
PMAP-CutDB; P10451; -.
PRO; PR:P10451; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000118785; -.
CleanEx; HS_SPP1; -.
ExpressionAtlas; P10451; baseline and differential.
Genevisible; P10451; HS.
GO; GO:0042995; C:cell projection; IEA:Ensembl.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
GO; GO:0006710; P:androgen catabolic process; IDA:CAFA.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0071394; P:cellular response to testosterone stimulus; IDA:CAFA.
GO; GO:0046697; P:decidualization; TAS:BHF-UCL.
GO; GO:0007566; P:embryo implantation; TAS:BHF-UCL.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0048685; P:negative regulation of collateral sprouting of intact axon in response to injury; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IBA:GO_Central.
GO; GO:0045780; P:positive regulation of bone resorption; IBA:GO_Central.
GO; GO:2000866; P:positive regulation of estradiol secretion; IDA:CAFA.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CAFA.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
GO; GO:0033280; P:response to vitamin D; IDA:BHF-UCL.
InterPro; IPR002038; Osteopontin.
InterPro; IPR019841; Osteopontin_CS.
PANTHER; PTHR10607; PTHR10607; 1.
Pfam; PF00865; Osteopontin; 1.
PRINTS; PR00216; OSTEOPONTIN.
SMART; SM00017; OSTEO; 1.
PROSITE; PS00884; OSTEOPONTIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Biomineralization; Cell adhesion;
Complete proteome; Cytokine; Direct protein sequencing; Glycoprotein;
Phosphoprotein; Polymorphism; Reference proteome; Secreted;
Sialic acid; Signal.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 314 Osteopontin.
/FTId=PRO_0000020321.
MOTIF 159 161 Cell attachment site.
MOD_RES 24 24 Phosphoserine.
{ECO:0000269|PubMed:15869464}.
MOD_RES 26 26 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 27 27 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 62 62 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 63 63 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 66 66 Phosphothreonine.
{ECO:0000269|PubMed:15869464}.
MOD_RES 76 76 Phosphoserine.
{ECO:0000269|PubMed:15869464}.
MOD_RES 78 78 Phosphoserine.
{ECO:0000250|UniProtKB:P31096}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000244|PubMed:16807684,
ECO:0000269|PubMed:15869464}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000269|PubMed:15869464}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000269|PubMed:15869464}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000269|PubMed:15869464}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000269|PubMed:15869464}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000269|PubMed:15869464}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000269|PubMed:15869464}.
MOD_RES 123 123 Phosphoserine.
{ECO:0000269|PubMed:15869464}.
MOD_RES 126 126 Phosphoserine.
{ECO:0000269|PubMed:15869464}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000269|PubMed:15869464}.
MOD_RES 185 185 Phosphothreonine.
{ECO:0000269|PubMed:15869464}.
MOD_RES 190 190 Phosphothreonine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 191 191 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 195 195 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 215 215 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 219 219 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 224 224 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 225 225 Phosphotyrosine.
{ECO:0000269|PubMed:26091039}.
MOD_RES 228 228 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 234 234 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 237 237 Phosphothreonine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 239 239 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 243 243 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 254 254 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 258 258 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 263 263 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 267 267 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 270 270 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 275 275 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 280 280 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 291 291 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 303 303 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 308 308 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 310 310 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:15869464,
ECO:0000269|PubMed:26091039}.
MOD_RES 311 311 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15869464}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15869464}.
CARBOHYD 134 134 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:15869464}.
CARBOHYD 138 138 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:15869464}.
CARBOHYD 143 143 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:15869464}.
CARBOHYD 147 147 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:15869464}.
CARBOHYD 152 152 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:15869464}.
VAR_SEQ 31 57 Missing (in isoform C).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7837791,
ECO:0000303|Ref.8}.
/FTId=VSP_003777.
VAR_SEQ 58 71 Missing (in isoform B).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1974876,
ECO:0000303|PubMed:7837791,
ECO:0000303|Ref.7}.
/FTId=VSP_003778.
VAR_SEQ 59 72 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043695.
VAR_SEQ 95 116 Missing (in isoform D).
{ECO:0000303|PubMed:16303743}.
/FTId=VSP_011639.
VARIANT 224 224 S -> N (in dbSNP:rs7435825).
/FTId=VAR_050432.
VARIANT 301 301 R -> H (in dbSNP:rs4660).
/FTId=VAR_014717.
CONFLICT 188 188 D -> H (in Ref. 6; BAA05949/BAA05950/
BAA05951). {ECO:0000305}.
CONFLICT 237 237 T -> A (in Ref. 6; BAA05949/BAA05950/
BAA05951). {ECO:0000305}.
CONFLICT 275 278 SHEF -> GNSL (in Ref. 2). {ECO:0000305}.
STRAND 44 47 {ECO:0000244|PDB:3CXD}.
SEQUENCE 314 AA; 35423 MW; 4996429EC4752B86 CRC64;
MRIAVICFCL LGITCAIPVK QADSGSSEEK QLYNKYPDAV ATWLNPDPSQ KQNLLAPQNA
VSSEETNDFK QETLPSKSNE SHDHMDDMDD EDDDDHVDSQ DSIDSNDSDD VDDTDDSHQS
DESHHSDESD ELVTDFPTDL PATEVFTPVV PTVDTYDGRG DSVVYGLRSK SKKFRRPDIQ
YPDATDEDIT SHMESEELNG AYKAIPVAQD LNAPSDWDSR GKDSYETSQL DDQSAETHSH
KQSRLYKRKA NDESNEHSDV IDSQELSKVS REFHSHEFHS HEDMLVVDPK SKEEDKHLKF
RISHELDSAS SEVN


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