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 02-OCT-2024, entry version 239. 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). RN [24] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-234 AND RP SER-308. RX PubMed=25326458; DOI=10.1074/mcp.m114.043703; RA Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L., RA Nilsson J., Larson G.; RT "Identification of chondroitin sulfate linkage region glycopeptides reveals RT prohormones as a novel class of proteoglycans."; RL Mol. Cell. Proteomics 14:41-49(2015). RN [25] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-308. RX PubMed=36213313; DOI=10.1007/s42485-022-00092-3; RA Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K., RA Pandey A.; RT "Mass spectrometric analysis of chondroitin sulfate-linked peptides."; RL J. Proteins Proteom. 13:187-203(2022). RN [26] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-234 AND RP SER-308. RX PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617; RA Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.; RT "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected RT Correlation Between Glycan Sulfation and Attachment Site Characteristics."; RL Mol. Cell. Proteomics 22:100617-100617(2023). 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: Interacts (via N-terminus) with integrin ITGA9:ITGB1. CC {ECO:0000250|UniProtKB:P10923}. 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 {ECO:0000269|PubMed:25326458, CC ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. 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: Detected in cerebrospinal fluid and urine (at CC protein level) (PubMed:25326458, PubMed:36213313, PubMed:37453717). CC Bone. Found in plasma. {ECO:0000269|PubMed:25326458, CC ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. 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 ECO:0000269|PubMed:25326458}. 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="https://atlasgeneticsoncology.org/gene/42379/SPP1"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Osteopontin entry; CC URL="https://en.wikipedia.org/wiki/Osteopontin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; P10451; 7 sites, 11 glycans. DR GlyGen; P10451; 11 sites, 4 N-linked glycans (1 site), 8 O-linked glycans (7 sites). DR iPTMnet; P10451; -. DR PhosphoSitePlus; P10451; -. DR BioMuta; SPP1; -. DR DMDM; 129260; -. DR jPOST; P10451; -. DR MassIVE; P10451; -. DR PaxDb; 9606-ENSP00000378517; -. DR PeptideAtlas; 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; 1700 antibodies from 51 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 AGR; HGNC:11255; -. 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; EWADKSH; -. DR OrthoDB; 4339959at2759; -. 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 1150 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 181 other cell types or tissues. DR ExpressionAtlas; P10451; baseline and differential. 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:0036094; F:small molecule binding; EXP:DisProt. 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: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:0045893; P:positive regulation of DNA-templated transcription; IDA:CAFA. DR GO; GO:2000866; P:positive regulation of estradiol secretion; IDA:CAFA. DR GO; GO:0036005; P:response to macrophage colony-stimulating factor; IEA:Ensembl. 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; OSTEOPONTIN; 1. DR PANTHER; PTHR10607:SF1; OSTEOPONTIN; 1. 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 Proteoglycan; Proteomics identification; Reference proteome; Secreted; KW 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 CARBOHYD 234 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:25326458, FT ECO:0000269|PubMed:37453717" FT CARBOHYD 308 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:25326458, FT ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717" 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 //