OSTP_HUMAN
ID OSTP_HUMAN Reviewed; 314 AA.
AC P10451; B2RDA1; Q15681; Q15682; Q15683; Q4W597; Q567T5; Q8NBK2; Q96IZ1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=Osteopontin {ECO:0000303|PubMed:1974876, ECO:0000303|PubMed:2726470};
DE AltName: Full=Bone sialoprotein 1;
DE AltName: Full=Nephropontin;
DE AltName: Full=Secreted phosphoprotein 1;
DE Short=SPP-1;
DE AltName: Full=Urinary stone protein {ECO:0000303|PubMed:1729712};
DE AltName: Full=Uropontin {ECO:0000303|PubMed:1729712};
DE Flags: Precursor;
GN Name=SPP1; Synonyms=BNSP, OPN; ORFNames=PSEC0156;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2726470; DOI=10.1093/nar/17.8.3306;
RA Kiefer M.C., Bauer D.M., Barr P.J.;
RT "The cDNA and derived amino acid sequence for human osteopontin.";
RL Nucleic Acids Res. 17:3306-3306(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1974876; DOI=10.1016/0888-7543(90)90191-v;
RA Young M.F., Kerr J.M., Termine J.D., Wewer U.M., Wang M.G., McBride O.W.,
RA Fisher L.W.;
RT "cDNA cloning, mRNA distribution and heterogeneity, chromosomal location,
RT and RFLP analysis of human osteopontin (OPN).";
RL Genomics 7:491-502(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1729712; DOI=10.1073/pnas.89.1.426;
RA Shiraga H., Min W., VanDusen W.J., Clayman M.D., Miner D., Terrell C.H.,
RA Sherbotie J.R., Foreman J.W., Przysiecki C., Neilson E.G., Hoyer J.R.;
RT "Inhibition of calcium oxalate crystal growth in vitro by uropontin:
RT another member of the aspartic acid-rich protein superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:426-430(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=7665163; DOI=10.1006/geno.1995.1018;
RA Crosby A.H., Edwards S.J., Murray J.C., Dixon M.J.;
RT "Genomic organization of the human osteopontin gene: exclusion of the locus
RT from a causative role in the pathogenesis of dentinogenesis imperfecta type
RT II.";
RL Genomics 27:155-160(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=7945249; DOI=10.1042/bj3030255;
RA Hijiya N., Setoguchi M., Matsuura K., Higuchi Y., Akizuki S., Yamamoto S.;
RT "Cloning and characterization of the human osteopontin gene and its
RT promoter.";
RL Biochem. J. 303:255-262(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=7837791;
RA Saitoh Y., Kuratsu J., Takeshima H., Yamamoto S., Ushio Y.;
RT "Expression of osteopontin in human glioma. Its correlation with the
RT malignancy.";
RL Lab. Invest. 72:55-63(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Sivakumar S., Niranjali Devaraj S.;
RT "Osteopontin splice variants in Indian breast cancer patients as
RT biomarker.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Kidney, and Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Yu Z., Zheng Z., Tang T., Fu Y.;
RT "A computer system platform used to predict novel genes.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 67-278.
RC TISSUE=Kidney;
RX PubMed=1575754; DOI=10.1016/0006-291x(92)90669-c;
RA Kohri K., Suzuki Y., Yoshida K., Yamamoto K., Amasaki N., Yamate T.,
RA Umekawa T., Iguchi M., Sinohara H., Kurita T.;
RT "Molecular cloning and sequencing of cDNA encoding urinary stone protein,
RT which is identical to osteopontin.";
RL Biochem. Biophys. Res. Commun. 184:859-864(1992).
RN [16]
RP PROTEIN SEQUENCE OF 17-23 AND 169-182.
RC TISSUE=Milk;
RX PubMed=2736258; DOI=10.1016/0167-4838(89)90092-7;
RA Senger D.R., Perruzzi C.A., Papadopoulos A., Tenen D.G.;
RT "Purification of a human milk protein closely similar to tumor-secreted
RT phosphoproteins and osteopontin.";
RL Biochim. Biophys. Acta 996:43-48(1989).
RN [17]
RP PHOSPHORYLATION AT SER-24; SER-26; SER-27; SER-62; SER-63; THR-66; SER-76;
RP SER-81; SER-99; SER-102; SER-108; SER-117; SER-120; SER-123; SER-129;
RP THR-185; SER-191; SER-195; SER-215; SER-219; SER-224; SER-228; SER-234;
RP SER-254; SER-263; SER-267; SER-275; SER-280; SER-303; SER-308; SER-310;
RP SER-105 AND SER-126, AND GLYCOSYLATION AT THR-134; THR-138; THR-143;
RP THR-147 AND THR-152.
RC TISSUE=Milk;
RX PubMed=15869464; DOI=10.1042/bj20050341;
RA Christensen B., Nielsen M.S., Haselmann K.F., Petersen T.E., Sorensen E.S.;
RT "Post-translationally modified residues of native human osteopontin are
RT located in clusters: identification of 36 phosphorylation and five O-
RT glycosylation sites and their biological implications.";
RL Biochem. J. 390:285-292(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-224; SER-234 AND
RP SER-254, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION BY FAM20C.
RX PubMed=22582013; DOI=10.1126/science.1217817;
RA Tagliabracci V.S., Engel J.L., Wen J., Wiley S.E., Worby C.A., Kinch L.N.,
RA Xiao J., Grishin N.V., Dixon J.E.;
RT "Secreted kinase phosphorylates extracellular proteins that regulate
RT biomineralization.";
RL Science 336:1150-1153(2012).
RN [21]
RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP PHOSPHORYLATION AT SER-26; SER-27; SER-62; SER-63; THR-190; SER-191;
RP SER-195; SER-215; SER-219; SER-224; TYR-225; SER-228; SER-234; THR-237;
RP SER-239; SER-243; SER-254; SER-258; SER-263; SER-267; SER-270; SER-275;
RP SER-280; SER-291; SER-303; SER-308; SER-310 AND SER-311.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
CC -!- FUNCTION: Major non-collagenous bone protein that binds tightly to
CC hydroxyapatite. Appears to form an integral part of the mineralized
CC matrix. Probably important to cell-matrix interaction.
CC {ECO:0000250|UniProtKB:P31096}.
CC -!- FUNCTION: Acts as a cytokine involved in enhancing production of
CC interferon-gamma and interleukin-12 and reducing production of
CC interleukin-10 and is essential in the pathway that leads to type I
CC immunity. {ECO:0000250|UniProtKB:P10923}.
CC -!- SUBUNIT: Ligand for integrin alpha-V/beta-3.
CC -!- INTERACTION:
CC P10451; P46379-2: BAG6; NbExp=3; IntAct=EBI-723648, EBI-10988864;
CC P10451; Q8IXL6: FAM20C; NbExp=3; IntAct=EBI-723648, EBI-7147442;
CC P10451; O43681: GET3; NbExp=3; IntAct=EBI-723648, EBI-2515857;
CC P10451; P50222: MEOX2; NbExp=3; IntAct=EBI-723648, EBI-748397;
CC P10451; P62166: NCS1; NbExp=3; IntAct=EBI-723648, EBI-746987;
CC P10451; O43765: SGTA; NbExp=8; IntAct=EBI-723648, EBI-347996;
CC P10451; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-723648, EBI-744081;
CC PRO_0000020321; Q8IXL6: FAM20C; NbExp=2; IntAct=EBI-11893188, EBI-7147442;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=OPN-a, OP1B;
CC IsoId=P10451-1; Sequence=Displayed;
CC Name=3; Synonyms=OPN-c;
CC IsoId=P10451-3; Sequence=VSP_003777;
CC Name=4;
CC IsoId=P10451-4; Sequence=VSP_011639;
CC Name=2; Synonyms=OPN-b, OP1A;
CC IsoId=P10451-5; Sequence=VSP_043695;
CC -!- TISSUE SPECIFICITY: Bone. Found in plasma.
CC -!- PTM: Forms covalent cross-links mediated by transglutaminase TGM2,
CC between a glutamine and the epsilon-amino group of a lysine residue,
CC forming homopolymers and heteropolymers, increasing its collagen
CC binding properties. {ECO:0000250|UniProtKB:P31096}.
CC -!- PTM: Extensively phosphorylated by FAM20C in the extracellular medium
CC at multiple sites within the S-x-E/pS motif (PubMed:15869464,
CC PubMed:22582013, PubMed:26091039). The phosphorylated form inhibits
CC hydroxyapatite crystallization. Dephosphorylation via a mechanism
CC involving ALPL/TNAP promotes hydroxyapatite crystallization (By
CC similarity). {ECO:0000250|UniProtKB:P10923,
CC ECO:0000269|PubMed:15869464, ECO:0000269|PubMed:22582013,
CC ECO:0000269|PubMed:26091039}.
CC -!- PTM: O-glycosylated. Isoform 5 is GalNAc O-glycosylated at Thr-59 or
CC Ser-62. {ECO:0000269|PubMed:15869464, ECO:0000269|PubMed:23234360}.
CC -!- SIMILARITY: Belongs to the osteopontin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SPP1ID42379ch4q22.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Osteopontin entry;
CC URL="https://en.wikipedia.org/wiki/Osteopontin";
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DR EMBL; X13694; CAA31984.1; -; mRNA.
DR EMBL; J04765; AAA59974.1; -; mRNA.
DR EMBL; M83248; AAA17675.1; -; mRNA.
DR EMBL; U20758; AAA86886.1; -; Genomic_DNA.
DR EMBL; D14813; BAA03554.1; -; Genomic_DNA.
DR EMBL; D28759; BAA05949.1; -; mRNA.
DR EMBL; D28760; BAA05950.1; -; mRNA.
DR EMBL; D28761; BAA05951.1; -; mRNA.
DR EMBL; AF052124; AAC28619.1; -; mRNA.
DR EMBL; AK290104; BAF82793.1; -; mRNA.
DR EMBL; JF412667; AEA49031.1; -; mRNA.
DR EMBL; AK075463; BAC11635.1; -; mRNA.
DR EMBL; AK290090; BAF82779.1; -; mRNA.
DR EMBL; AK296035; BAG58801.1; -; mRNA.
DR EMBL; AK315461; BAG37848.1; -; mRNA.
DR EMBL; DQ839491; ABI63352.1; -; mRNA.
DR EMBL; DQ846871; ABI63358.1; -; mRNA.
DR EMBL; AC131944; AAY41035.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX06004.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX06005.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX06006.1; -; Genomic_DNA.
DR EMBL; BC007016; AAH07016.1; -; mRNA.
DR EMBL; BC017387; AAH17387.1; -; mRNA.
DR EMBL; BC022844; AAH22844.1; -; mRNA.
DR EMBL; BC093033; AAH93033.1; -; mRNA.
DR CCDS; CCDS34027.1; -. [P10451-3]
DR CCDS; CCDS3626.1; -. [P10451-5]
DR CCDS; CCDS43250.1; -. [P10451-1]
DR PIR; S50028; S09575.
DR RefSeq; NP_000573.1; NM_000582.2. [P10451-5]
DR RefSeq; NP_001035147.1; NM_001040058.1. [P10451-1]
DR RefSeq; NP_001035149.1; NM_001040060.1. [P10451-3]
DR RefSeq; NP_001238758.1; NM_001251829.1.
DR RefSeq; NP_001238759.1; NM_001251830.1.
DR PDB; 3CXD; X-ray; 2.80 A; P=40-51.
DR PDB; 3DSF; X-ray; 2.80 A; P=40-51.
DR PDBsum; 3CXD; -.
DR PDBsum; 3DSF; -.
DR AlphaFoldDB; P10451; -.
DR PCDDB; P10451; -.
DR SMR; P10451; -.
DR BioGRID; 112574; 123.
DR CORUM; P10451; -.
DR DIP; DIP-49933N; -.
DR ELM; P10451; -.
DR IntAct; P10451; 24.
DR MINT; P10451; -.
DR STRING; 9606.ENSP00000378517; -.
DR ChEMBL; CHEMBL1741309; -.
DR GlyConnect; 474; 2 N-Linked glycans, 1 O-Linked glycan (1 site).
DR GlyGen; P10451; 8 sites, 4 N-linked glycans (1 site), 7 O-linked glycans (5 sites).
DR iPTMnet; P10451; -.
DR PhosphoSitePlus; P10451; -.
DR BioMuta; SPP1; -.
DR DMDM; 129260; -.
DR EPD; P10451; -.
DR jPOST; P10451; -.
DR MassIVE; P10451; -.
DR MaxQB; P10451; -.
DR PaxDb; P10451; -.
DR PeptideAtlas; P10451; -.
DR PRIDE; P10451; -.
DR ProteomicsDB; 52605; -. [P10451-1]
DR ProteomicsDB; 52607; -. [P10451-3]
DR ProteomicsDB; 52608; -. [P10451-4]
DR ProteomicsDB; 52609; -. [P10451-5]
DR ABCD; P10451; 14 sequenced antibodies.
DR Antibodypedia; 3695; 1494 antibodies from 49 providers.
DR CPTC; P10451; 1 antibody.
DR DNASU; 6696; -.
DR Ensembl; ENST00000237623.11; ENSP00000237623.7; ENSG00000118785.15. [P10451-5]
DR Ensembl; ENST00000360804.4; ENSP00000354042.4; ENSG00000118785.15. [P10451-3]
DR Ensembl; ENST00000395080.8; ENSP00000378517.3; ENSG00000118785.15. [P10451-1]
DR Ensembl; ENST00000614857.5; ENSP00000477824.2; ENSG00000118785.15. [P10451-1]
DR GeneID; 6696; -.
DR KEGG; hsa:6696; -.
DR MANE-Select; ENST00000395080.8; ENSP00000378517.3; NM_001040058.2; NP_001035147.1.
DR UCSC; uc003hra.4; human. [P10451-1]
DR CTD; 6696; -.
DR DisGeNET; 6696; -.
DR GeneCards; SPP1; -.
DR HGNC; HGNC:11255; SPP1.
DR HPA; ENSG00000118785; Tissue enhanced (brain, gallbladder, kidney, placenta).
DR MalaCards; SPP1; -.
DR MIM; 166490; gene.
DR neXtProt; NX_P10451; -.
DR OpenTargets; ENSG00000118785; -.
DR Orphanet; 93552; Pediatric systemic lupus erythematosus.
DR Orphanet; 536; Systemic lupus erythematosus.
DR PharmGKB; PA36085; -.
DR VEuPathDB; HostDB:ENSG00000118785; -.
DR eggNOG; ENOG502S5R4; Eukaryota.
DR GeneTree; ENSGT00390000002509; -.
DR HOGENOM; CLU_953033_0_0_1; -.
DR InParanoid; P10451; -.
DR OMA; DHSVETH; -.
DR OrthoDB; 1280650at2759; -.
DR PhylomeDB; P10451; -.
DR TreeFam; TF350201; -.
DR PathwayCommons; P10451; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-186797; Signaling by PDGF.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8949275; RUNX3 Regulates Immune Response and Cell Migration.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; P10451; -.
DR SIGNOR; P10451; -.
DR BioGRID-ORCS; 6696; 13 hits in 1072 CRISPR screens.
DR ChiTaRS; SPP1; human.
DR EvolutionaryTrace; P10451; -.
DR GeneWiki; Osteopontin; -.
DR GenomeRNAi; 6696; -.
DR Pharos; P10451; Tbio.
DR PRO; PR:P10451; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P10451; protein.
DR Bgee; ENSG00000118785; Expressed in gall bladder and 179 other tissues.
DR ExpressionAtlas; P10451; baseline and differential.
DR Genevisible; P10451; HS.
DR GO; GO:0042995; C:cell projection; IEA:Ensembl.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IPI:ARUK-UCL.
DR GO; GO:0006710; P:androgen catabolic process; IDA:CAFA.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IDA:ARUK-UCL.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IDA:CAFA.
DR GO; GO:0046697; P:decidualization; TAS:BHF-UCL.
DR GO; GO:0007566; P:embryo implantation; TAS:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0048685; P:negative regulation of collateral sprouting of intact axon in response to injury; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IBA:GO_Central.
DR GO; GO:0045780; P:positive regulation of bone resorption; IBA:GO_Central.
DR GO; GO:2000866; P:positive regulation of estradiol secretion; IDA:CAFA.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CAFA.
DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR GO; GO:0033280; P:response to vitamin D; IDA:BHF-UCL.
DR DisProt; DP00214; -.
DR IDEAL; IID00649; -.
DR InterPro; IPR002038; Osteopontin.
DR InterPro; IPR019841; Osteopontin_CS.
DR PANTHER; PTHR10607; PTHR10607; 2.
DR Pfam; PF00865; Osteopontin; 1.
DR PRINTS; PR00216; OSTEOPONTIN.
DR SMART; SM00017; OSTEO; 1.
DR PROSITE; PS00884; OSTEOPONTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Biomineralization; Cell adhesion;
KW Cytokine; Direct protein sequencing; Glycoprotein; Phosphoprotein;
KW Reference proteome; Secreted; Sialic acid; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..314
FT /note="Osteopontin"
FT /id="PRO_0000020321"
FT REGION 41..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 159..161
FT /note="Cell attachment site"
FT COMPBIAS 45..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..116
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT MOD_RES 26
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 27
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 62
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 63
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0007744|PubMed:16807684"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT MOD_RES 190
FT /note="Phosphothreonine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 191
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 195
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 215
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 219
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:21406692"
FT MOD_RES 224
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:21406692"
FT MOD_RES 225
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 228
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 234
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:21406692"
FT MOD_RES 237
FT /note="Phosphothreonine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 239
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 243
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 254
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:21406692"
FT MOD_RES 258
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 263
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 267
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 270
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 275
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 280
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 291
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 303
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 308
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 310
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:15869464,
FT ECO:0000269|PubMed:26091039"
FT MOD_RES 311
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT CARBOHYD 134
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT CARBOHYD 138
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT CARBOHYD 143
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT CARBOHYD 147
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT CARBOHYD 152
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:15869464"
FT VAR_SEQ 31..57
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7837791,
FT ECO:0000303|Ref.8"
FT /id="VSP_003777"
FT VAR_SEQ 59..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1974876,
FT ECO:0000303|PubMed:7837791, ECO:0000303|Ref.7"
FT /id="VSP_043695"
FT VAR_SEQ 95..116
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_011639"
FT VARIANT 224
FT /note="S -> N (in dbSNP:rs7435825)"
FT /id="VAR_050432"
FT VARIANT 301
FT /note="R -> H (in dbSNP:rs4660)"
FT /id="VAR_014717"
FT CONFLICT 58
FT /note="Q -> E (in Ref. 6; BAA05950)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="D -> H (in Ref. 6; BAA05949/BAA05950/BAA05951)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="T -> A (in Ref. 6; BAA05949/BAA05950/BAA05951)"
FT /evidence="ECO:0000305"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:3CXD"
SQ 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
