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P10451

- OSTP_HUMAN

UniProt

P10451 - OSTP_HUMAN

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Protein
Osteopontin
Gene
SPP1, BNSP, OPN, PSEC0156
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. extracellular matrix binding Source: Ensembl
  2. protein binding Source: IntAct

GO - Biological processi

  1. biomineral tissue development Source: UniProtKB-KW
  2. cell adhesion Source: UniProtKB-KW
  3. decidualization Source: BHF-UCL
  4. embryo implantation Source: BHF-UCL
  5. extracellular matrix disassembly Source: Reactome
  6. extracellular matrix organization Source: Reactome
  7. inflammatory response Source: Ensembl
  8. negative regulation of collateral sprouting of intact axon in response to injury Source: Ensembl
  9. neutrophil chemotaxis Source: Ensembl
  10. osteoblast differentiation Source: Ensembl
  11. positive regulation of bone resorption Source: Ensembl
  12. positive regulation of cell-substrate adhesion Source: Ensembl
  13. response to steroid hormone Source: Ensembl
  14. response to vitamin D Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Biomineralization, Cell adhesion

Keywords - Ligandi

Sialic acid

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_13552. Integrin cell surface interactions.
REACT_16888. Signaling by PDGF.
REACT_216309. Integrin cell surface interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Osteopontin
Alternative name(s):
Bone sialoprotein 1
Nephropontin
Secreted phosphoprotein 1
Short name:
SPP-1
Urinary stone protein
Uropontin
Gene namesi
Name:SPP1
Synonyms:BNSP, OPN
ORF Names:PSEC0156
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:11255. SPP1.

Subcellular locationi

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. cell projection Source: Ensembl
  3. extracellular region Source: Reactome
  4. extracellular space Source: BHF-UCL
  5. extracellular vesicular exosome Source: UniProt
  6. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

Orphaneti93552. Pediatric systemic lupus erythematosus.
536. Systemic lupus erythematosus.
PharmGKBiPA36085.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616 Reviewed prediction
Add
BLAST
Chaini17 – 314298Osteopontin
PRO_0000020321Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Phosphoserine1 Publication
Modified residuei26 – 261Phosphoserine1 Publication
Modified residuei27 – 271Phosphoserine1 Publication
Modified residuei62 – 621Phosphoserine1 Publication
Modified residuei63 – 631Phosphoserine1 Publication
Modified residuei66 – 661Phosphothreonine1 Publication
Modified residuei76 – 761Phosphoserine1 Publication
Modified residuei78 – 781Phosphoserine By similarity
Glycosylationi79 – 791N-linked (GlcNAc...)1 Publication
Modified residuei81 – 811Phosphoserine2 Publications
Modified residuei99 – 991Phosphoserine1 Publication
Modified residuei102 – 1021Phosphoserine1 Publication
Modified residuei105 – 1051Phosphoserine1 Publication
Glycosylationi106 – 1061N-linked (GlcNAc...)1 Publication
Modified residuei108 – 1081Phosphoserine1 Publication
Modified residuei117 – 1171Phosphoserine1 Publication
Modified residuei120 – 1201Phosphoserine1 Publication
Modified residuei123 – 1231Phosphoserine1 Publication
Modified residuei126 – 1261Phosphoserine1 Publication
Modified residuei129 – 1291Phosphoserine1 Publication
Glycosylationi134 – 1341O-linked (GalNAc...)1 Publication
Glycosylationi138 – 1381O-linked (GalNAc...)1 Publication
Glycosylationi143 – 1431O-linked (GalNAc...)1 Publication
Glycosylationi147 – 1471O-linked (GalNAc...)1 Publication
Glycosylationi152 – 1521O-linked (GalNAc...)1 Publication
Modified residuei185 – 1851Phosphothreonine1 Publication
Modified residuei191 – 1911Phosphoserine1 Publication
Modified residuei195 – 1951Phosphoserine1 Publication
Modified residuei215 – 2151Phosphoserine1 Publication
Modified residuei219 – 2191Phosphoserine2 Publications
Modified residuei224 – 2241Phosphoserine2 Publications
Modified residuei228 – 2281Phosphoserine1 Publication
Modified residuei234 – 2341Phosphoserine2 Publications
Modified residuei239 – 2391Phosphoserine By similarity
Modified residuei254 – 2541Phosphoserine2 Publications
Modified residuei263 – 2631Phosphoserine1 Publication
Modified residuei267 – 2671Phosphoserine1 Publication
Modified residuei270 – 2701Phosphoserine By similarity
Modified residuei275 – 2751Phosphoserine1 Publication
Modified residuei280 – 2801Phosphoserine1 Publication
Modified residuei291 – 2911Phosphoserine By similarity
Modified residuei303 – 3031Phosphoserine1 Publication
Modified residuei308 – 3081Phosphoserine1 Publication
Modified residuei310 – 3101Phosphoserine1 Publication

Post-translational modificationi

Extensively phosphorylated by FAM20C in the extracellular medium at multiple sites within the S-x-E/pS motif.2 Publications
N- and O-glycosylated. Isoform 5 is GalNAc O-glycosylated at Thr-59 or Ser-62.2 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP10451.
PaxDbiP10451.
PRIDEiP10451.

PTM databases

PhosphoSiteiP10451.
UniCarbKBiP10451.

Miscellaneous databases

PMAP-CutDBP10451.

Expressioni

Tissue specificityi

Bone. Found in plasma.

Gene expression databases

ArrayExpressiP10451.
BgeeiP10451.
CleanExiHS_SPP1.
GenevestigatoriP10451.

Organism-specific databases

HPAiCAB002212.
HPA027541.

Interactioni

Subunit structurei

Ligand for integrin alpha-V/beta-3.

Binary interactionsi

WithEntry#Exp.IntActNotes
CD44P160702EBI-723648,EBI-490245

Protein-protein interaction databases

BioGridi112574. 75 interactions.
DIPiDIP-49933N.
IntActiP10451. 9 interactions.
MINTiMINT-1380527.
STRINGi9606.ENSP00000378517.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 474

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CXDX-ray2.80P40-51[»]
3DSFX-ray2.80P40-51[»]
DisProtiDP00214.
ProteinModelPortaliP10451.

Miscellaneous databases

EvolutionaryTraceiP10451.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi159 – 1613Cell attachment site

Sequence similaritiesi

Belongs to the osteopontin family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG73598.
HOGENOMiHOG000059656.
HOVERGENiHBG001731.
InParanoidiP10451.
KOiK06250.
OMAiVICFCLL.
OrthoDBiEOG7R832D.
PhylomeDBiP10451.
TreeFamiTF350201.

Family and domain databases

InterProiIPR002038. Osteopontin.
IPR019841. Osteopontin_CS.
[Graphical view]
PANTHERiPTHR10607. PTHR10607. 1 hit.
PfamiPF00865. Osteopontin. 1 hit.
[Graphical view]
PRINTSiPR00216. OSTEOPONTIN.
SMARTiSM00017. OSTEO. 1 hit.
[Graphical view]
PROSITEiPS00884. OSTEOPONTIN. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform A (identifier: P10451-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MRIAVICFCL LGITCAIPVK QADSGSSEEK QLYNKYPDAV ATWLNPDPSQ    50
KQNLLAPQNA VSSEETNDFK QETLPSKSNE SHDHMDDMDD EDDDDHVDSQ 100
DSIDSNDSDD VDDTDDSHQS DESHHSDESD ELVTDFPTDL PATEVFTPVV 150
PTVDTYDGRG DSVVYGLRSK SKKFRRPDIQ YPDATDEDIT SHMESEELNG 200
AYKAIPVAQD LNAPSDWDSR GKDSYETSQL DDQSAETHSH KQSRLYKRKA 250
NDESNEHSDV IDSQELSKVS REFHSHEFHS HEDMLVVDPK SKEEDKHLKF 300
RISHELDSAS SEVN 314
Length:314
Mass (Da):35,423
Last modified:July 1, 1989 - v1
Checksum:i4996429EC4752B86
GO
Isoform B (identifier: P10451-2) [UniParc]FASTAAdd to Basket

Also known as: OPN-b, OP1A

The sequence of this isoform differs from the canonical sequence as follows:
     58-71: Missing.

Show »
Length:300
Mass (Da):33,844
Checksum:iE844D1466BD20E64
GO
Isoform C (identifier: P10451-3) [UniParc]FASTAAdd to Basket

Also known as: OPN-c

The sequence of this isoform differs from the canonical sequence as follows:
     31-57: Missing.

Show »
Length:287
Mass (Da):32,355
Checksum:iAF604D4E223BA02F
GO
Isoform D (identifier: P10451-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     95-116: Missing.

Show »
Length:292
Mass (Da):33,017
Checksum:iE93E418982C3AD60
GO
Isoform 5 (identifier: P10451-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     59-72: Missing.

Note: No experimental confirmation available.

Show »
Length:300
Mass (Da):33,843
Checksum:iB844D7EBDD096CBF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241S → N.
Corresponds to variant rs7435825 [ dbSNP | Ensembl ].
VAR_050432
Natural varianti301 – 3011R → H.
Corresponds to variant rs4660 [ dbSNP | Ensembl ].
VAR_014717

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei31 – 5727Missing in isoform C.
VSP_003777Add
BLAST
Alternative sequencei58 – 7114Missing in isoform B.
VSP_003778Add
BLAST
Alternative sequencei59 – 7214Missing in isoform 5.
VSP_043695Add
BLAST
Alternative sequencei95 – 11622Missing in isoform D.
VSP_011639Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881D → H in BAA05949. 1 Publication
Sequence conflicti188 – 1881D → H in BAA05950. 1 Publication
Sequence conflicti188 – 1881D → H in BAA05951. 1 Publication
Sequence conflicti237 – 2371T → A in BAA05949. 1 Publication
Sequence conflicti237 – 2371T → A in BAA05950. 1 Publication
Sequence conflicti237 – 2371T → A in BAA05951. 1 Publication
Sequence conflicti275 – 2784SHEF → GNSL1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34027.1. [P10451-3]
CCDS3626.1. [P10451-5]
CCDS43250.1. [P10451-1]
PIRiS50028. S09575.
RefSeqiNP_000573.1. NM_000582.2. [P10451-5]
NP_001035147.1. NM_001040058.1. [P10451-1]
NP_001035149.1. NM_001040060.1. [P10451-3]
NP_001238758.1. NM_001251829.1.
NP_001238759.1. NM_001251830.1.
UniGeneiHs.313.

Genome annotation databases

EnsembliENST00000237623; ENSP00000237623; ENSG00000118785. [P10451-5]
ENST00000360804; ENSP00000354042; ENSG00000118785. [P10451-3]
ENST00000395080; ENSP00000378517; ENSG00000118785. [P10451-1]
GeneIDi6696.
KEGGihsa:6696.
UCSCiuc003hra.3. human. [P10451-1]
uc003hrb.3. human. [P10451-3]
uc003hrc.3. human. [P10451-5]

Polymorphism databases

DMDMi129260.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

Osteopontin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34027.1. [P10451-3 ]
CCDS3626.1. [P10451-5 ]
CCDS43250.1. [P10451-1 ]
PIRi S50028. S09575.
RefSeqi NP_000573.1. NM_000582.2. [P10451-5 ]
NP_001035147.1. NM_001040058.1. [P10451-1 ]
NP_001035149.1. NM_001040060.1. [P10451-3 ]
NP_001238758.1. NM_001251829.1.
NP_001238759.1. NM_001251830.1.
UniGenei Hs.313.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CXD X-ray 2.80 P 40-51 [» ]
3DSF X-ray 2.80 P 40-51 [» ]
DisProti DP00214.
ProteinModelPortali P10451.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112574. 75 interactions.
DIPi DIP-49933N.
IntActi P10451. 9 interactions.
MINTi MINT-1380527.
STRINGi 9606.ENSP00000378517.

PTM databases

PhosphoSitei P10451.
UniCarbKBi P10451.

Polymorphism databases

DMDMi 129260.

Proteomic databases

MaxQBi P10451.
PaxDbi P10451.
PRIDEi P10451.

Protocols and materials databases

DNASUi 6696.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000237623 ; ENSP00000237623 ; ENSG00000118785 . [P10451-5 ]
ENST00000360804 ; ENSP00000354042 ; ENSG00000118785 . [P10451-3 ]
ENST00000395080 ; ENSP00000378517 ; ENSG00000118785 . [P10451-1 ]
GeneIDi 6696.
KEGGi hsa:6696.
UCSCi uc003hra.3. human. [P10451-1 ]
uc003hrb.3. human. [P10451-3 ]
uc003hrc.3. human. [P10451-5 ]

Organism-specific databases

CTDi 6696.
GeneCardsi GC04P088896.
H-InvDB HIX0004361.
HGNCi HGNC:11255. SPP1.
HPAi CAB002212.
HPA027541.
MIMi 166490. gene.
neXtProti NX_P10451.
Orphaneti 93552. Pediatric systemic lupus erythematosus.
536. Systemic lupus erythematosus.
PharmGKBi PA36085.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG73598.
HOGENOMi HOG000059656.
HOVERGENi HBG001731.
InParanoidi P10451.
KOi K06250.
OMAi VICFCLL.
OrthoDBi EOG7R832D.
PhylomeDBi P10451.
TreeFami TF350201.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_13552. Integrin cell surface interactions.
REACT_16888. Signaling by PDGF.
REACT_216309. Integrin cell surface interactions.

Miscellaneous databases

ChiTaRSi SPP1. human.
EvolutionaryTracei P10451.
GeneWikii Osteopontin.
GenomeRNAii 6696.
NextBioi 26103.
PMAP-CutDB P10451.
PROi P10451.
SOURCEi Search...

Gene expression databases

ArrayExpressi P10451.
Bgeei P10451.
CleanExi HS_SPP1.
Genevestigatori P10451.

Family and domain databases

InterProi IPR002038. Osteopontin.
IPR019841. Osteopontin_CS.
[Graphical view ]
PANTHERi PTHR10607. PTHR10607. 1 hit.
Pfami PF00865. Osteopontin. 1 hit.
[Graphical view ]
PRINTSi PR00216. OSTEOPONTIN.
SMARTi SM00017. OSTEO. 1 hit.
[Graphical view ]
PROSITEi PS00884. OSTEOPONTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary.
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-224; SER-234 AND SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Secreted kinase phosphorylates extracellular proteins that regulate biomineralization."
    Tagliabracci V.S., Engel J.L., Wen J., Wiley S.E., Worby C.A., Kinch L.N., Xiao J., Grishin N.V., Dixon J.E.
    Science 336:1150-1153(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY FAM20C.
  22. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
    Halim A., Ruetschi U., Larson G., Nilsson J.
    J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiOSTP_HUMAN
AccessioniPrimary (citable) accession number: P10451
Secondary accession number(s): B2RDA1
, Q15681, Q15682, Q15683, Q4W597, Q567T5, Q8NBK2, Q96IZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 3, 2014
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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