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Protein Page:
osteopontin (human)

Overview
osteopontin Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Belongs to the osteopontin family. 5 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Secreted; Secreted, signal peptide
Chromosomal Location of Human Ortholog: 4q22.1
Cellular Component: extracellular space; cell projection; perinuclear region of cytoplasm; apical part of cell; extracellular region
Molecular Function: protein binding; extracellular matrix binding; cytokine activity
Biological Process: neutrophil chemotaxis; extracellular matrix organization and biogenesis; decidualization; osteoblast differentiation; extracellular matrix disassembly; response to vitamin D; biomineral formation; response to steroid hormone stimulus; negative regulation of collateral sprouting of intact axon in response to injury; positive regulation of bone resorption; cell adhesion; inflammatory response; embryo implantation
Reference #:  P10451 (UniProtKB)
Alt. Names/Synonyms: BNSP; Bone sialoprotein 1; bone sialoprotein I; BSPI; early T-lymphocyte activation 1; ETA-1; MGC110940; Nephropontin; OPN; Osteopontin; osteopontin/immunoglobulin alpha 1 heavy chain constant region fusion protein; OSTP; Secreted phosphoprotein 1; secreted phosphoprotein 1 (osteopontin, bone sialoprotein I, early T-lymphocyte activation 1); secreted phosphoprotein-1 (osteopontin, bone sialoprotein); SPP-1; SPP1; SPP1/CALPHA1 fusion; Urinary stone protein; Uropontin
Gene Symbols: SPP1
Molecular weight: 35,423 Da
Basal Isoelectric point: 4.37  Predict pI for various phosphorylation states
Select Structure to View Below

osteopontin

Protein Structure Not Found.


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Sites Implicated In
activity, inhibited: S117‑p, S120‑p, S123‑p, S126‑p, S129‑p
molecular association, regulation: S117‑p, S120‑p, S123‑p, S126‑p, S129‑p

Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 4 S24-p IPVKQADsGssEEKQ
0 7 S26-p VKQADsGssEEKQLY
0 9 S27-p KQADsGssEEKQLYN
0 13 S62-p LAPQNAVssEEtNDF
0 13 S63-p APQNAVssEEtNDFK
0 4 T66-p NAVssEEtNDFKQET
0 1 T73 tNDFKQETLPsKsNE
0 4 S76-p FKQETLPsKsNEsHD
0 4 S78-p QETLPsKsNEsHDHM
1 5 S81-p LPsKsNEsHDHMDDM
0 3 S99-p DDDDHVDsQDsIDsN
0 3 S102-p DHVDsQDsIDsNDsD
0 3 S105-p DsQDsIDsNDsDDVD
0 3 S108-p DsIDsNDsDDVDDTD
1 3 S117-p DVDDTDDsHQsDEsH
1 3 S120-p DTDDsHQsDEsHHsD
1 4 S123-p DsHQsDEsHHsDEsD
1 4 S126-p QsDEsHHsDEsDELV
1 4 S129-p EsHHsDEsDELVtDF
0 1 T134-p DEsDELVtDFPtDLP
0 1 T138-p ELVtDFPtDLPAtEV
0 1 T143-p FPtDLPAtEVFtPVV
0 1 T147-p LPAtEVFtPVVPtVD
0 1 T152-p VFtPVVPtVDTYDGR
0 2 S162 TYDGRGDSVVyGLRS
0 1 Y165-p GRGDSVVyGLRSKSK
0 3 P177 KSKKFRRPDIQYPDA
0 5 T185-p DIQYPDAtDEDItsH
0 1 T190-p DAtDEDItsHMEsEE
0 4 S191-p AtDEDItsHMEsEEL
0 6 S195-p DItsHMEsEELNGAY
0 3 L198 sHMEsEELNGAYKAI
0 1 A201 EsEELNGAYKAIPVA
0 3 S215-p AQDLNAPsDWDsRGK
0 7 S219-p NAPsDWDsRGKDsYE
0 1 D223 DWDsRGKDsYETsQL
0 6 S224-p WDsRGKDsYETsQLD
0 2 T227 RGKDsYETsQLDDQs
0 4 S228-p GKDsYETsQLDDQsA
0 7 S234-p TsQLDDQsAETHSHK
0 1 T237 LDDQsAETHSHKQSR
0 1 S239 DQsAETHSHKQSRLY
0 5 S243 ETHSHKQSRLYKRKA
0 7 Y246 SHKQSRLYKRKANDE
0 1 N251 RLYKRKANDEsNEHs
0 1 - gap
0 13 S254-p KRKANDEsNEHsDVI
0 5 S258-p NDEsNEHsDVIDsQE
0 3 S263-p EHsDVIDsQELsKVs
0 3 S267-p VIDsQELsKVsREFH
0 7 S270-p sQELsKVsREFHsHE
0 3 S275-p KVsREFHsHEFHsHE
0 3 S280-p FHsHEFHsHEDMLVV
0 5 S291-p MLVVDPKsKEEDKHL
0 17 S303-p KHLKFRIsHELDsAs
0 14 S308-p RIsHELDsAssEVN_
0 5 A309 IsHELDsAssEVN__
0 16 S310-p sHELDsAssEVN___
0 4 S311-p HELDsAssEVN____
  osteopontin iso5  
S24 IPVKQADSGSSEEKQ
S26 VKQADSGSSEEKQLY
S27 KQADSGSSEEKQLYN
- gap
- gap
- gap
T59-p QNLLAPQtLPsKSNE
S62-p LAPQtLPsKSNESHD
S64 PQtLPsKSNESHDHM
S67 LPsKSNESHDHMDDM
S85 DDDDHVDSQDSIDSN
S88 DHVDSQDSIDSNDSD
S91 DSQDSIDSNDSDDVD
S94 DSIDSNDSDDVDDTD
S103 DVDDTDDSHQSDESH
S106 DTDDSHQSDESHHSD
S109 DSHQSDESHHSDESD
S112 QSDESHHSDESDELV
S115 ESHHSDESDELVTDF
T120 DESDELVTDFPTDLP
T124 ELVTDFPTDLPATEV
T129 FPTDLPATEVFTPVV
T133 LPATEVFTPVVPTVD
T138 VFTPVVPTVDTYDGR
S148 TYDGRGDSVVYGLRS
Y151 GRGDSVVYGLRSKSK
P163 KSKKFRRPDIQYPDA
T171 DIQYPDATDEDITSH
T176 DATDEDITSHMESEE
S177 ATDEDITSHMESEEL
S181 DITSHMESEELNGAY
L184 SHMESEELNGAYKAI
A187 ESEELNGAYKAIPVA
S201 AQDLNAPSDWDSRGK
S205 NAPSDWDSRGKDSYE
D209 DWDSRGKDSYETSQL
S210 WDSRGKDSYETSQLD
T213 RGKDSYETSQLDDQS
S214 GKDSYETSQLDDQSA
S220 TSQLDDQSAETHSHK
T223 LDDQSAETHSHKQSR
S225 DQSAETHSHKQSRLY
S229 ETHSHKQSRLYKRKA
Y232 SHKQSRLYKRKANDE
N237 RLYKRKANDESNEHS
- gap
S240 KRKANDESNEHSDVI
S244 NDESNEHSDVIDSQE
S249 EHSDVIDSQELSKVS
S253 VIDSQELSKVSREFH
S256 SQELSKVSREFHSHE
S261 KVSREFHSHEFHSHE
S266 FHSHEFHSHEDMLVV
S277 MLVVDPKSKEEDKHL
S289 KHLKFRISHELDSAS
S294 RISHELDSASSEVN_
A295 ISHELDSASSEVN__
S296 SHELDSASSEVN___
S297 HELDSASSEVN____
  mouse

 
S24-p LPVKVTDsGssEEKL
S26-p VKVTDsGssEEKLYS
S27-p KVTDsGssEEKLYSL
S61-p LAPQNAVssEEKDDF
S62-p APQNAVssEEKDDFK
K65 NAVssEEKDDFKQET
T72 KDDFKQETLPsNsNE
S75-p FKQETLPsNsNEsHD
S77-p QETLPsNsNEsHDHM
S80-p LPsNsNEsHDHMDDD
S100-p DDGDHAEsEDsVDsD
S103-p DHAEsEDsVDsDEsD
S106-p EsEDsVDsDEsDEsH
S109-p DsVDsDEsDEsHHsD
- gap
- gap
S112-p DsDEsDEsHHsDEsD
S115-p EsDEsHHsDEsDETV
S118-p EsHHsDEsDETVTAS
T123 DEsDETVTASTQADT
- gap
A128 TVTASTQADTFTPIV
T132 STQADTFTPIVPTVD
T137 TFTPIVPTVDVPNGR
S147-p VPNGRGDsLAYGLRS
Y150 GRGDsLAYGLRSKSR
S162-p KSRSFQVsDEQYPDA
T170-p DEQYPDAtDEDLtSH
T175-p DAtDEDLtSHMKsGE
S176 AtDEDLtSHMKsGEs
S180-p DLtSHMKsGEsKEsL
S183-p SHMKsGEsKEsLDVI
S186-p KsGEsKEsLDVIPVA
S200 AQLLSMPSDQDNNGK
N204 SMPSDQDNNGKGSHE
G208 DQDNNGKGSHESSQL
S209 QDNNGKGSHESSQLD
S212 NGKGSHESSQLDEPs
S213 GKGSHESSQLDEPsL
S219-p SSQLDEPsLETHRLE
T222 LDEPsLETHRLEHsK
R224 EPsLETHRLEHsKEs
S228-p ETHRLEHsKEsQEsA
S231-p RLEHsKEsQEsADQs
- gap
- gap
S234-p HsKEsQEsADQsDVI
S238-p sQEsADQsDVIDSQA
S243 DQsDVIDSQASSKAs
S247 VIDSQASSKAsLEHQ
S250-p SQASSKAsLEHQSHK
S255 KAsLEHQSHKFHSHK
S260 HQSHKFHSHKDKLVL
S271-p KLVLDPKsKEDDRYL
S283-p RYLKFRIsHELEsss
S288-p RIsHELEssssEVN_
S289-p IsHELEssssEVN__
S290-p sHELEssssEVN___
S291-p HELEssssEVN____
  rat

 
F24 LPVKVAEFGssEEKA
S26-p VKVAEFGssEEKAHY
S27-p KVAEFGssEEKAHYS
S62-p LAPQNSVssEEtDDF
S63-p APQNSVssEEtDDFK
T66-p NSVssEEtDDFKQET
T73 tDDFKQETLPSNsNE
S76 FKQETLPSNsNEsHD
S78-p QETLPSNsNEsHDHM
S81-p LPSNsNEsHDHMDDD
S100 DDGDHAESEDSVNSD
S103 DHAESEDSVNSDESD
S106 ESEDSVNSDESDESH
S109 DSVNSDESDESHHSD
- gap
- gap
S112 NSDESDESHHSDESD
S115 ESDESHHSDESDESF
S118 ESHHSDESDESFTAS
T123 DESDESFTASTQADV
- gap
A128 SFTASTQADVLTPIA
T132 STQADVLTPIAPTVD
T137 VLTPIAPTVDVPDGR
S147 VPDGRGDSLAYGLRS
Y150 GRGDSLAYGLRSKSR
S162-p KSRSFPVsDEQYPDA
T170-p DEQYPDAtDEDLTsR
T175 DAtDEDLTsRMKsQE
S176-p AtDEDLTsRMKsQEs
S180-p DLTsRMKsQEsDEAI
S183-p sRMKsQEsDEAIKVI
A186 KsQEsDEAIKVIPVA
S200 AQRLSVPSDQDSNGK
S204 SVPSDQDSNGKtsHE
T208-p DQDSNGKtsHEssQL
S209-p QDSNGKtsHEssQLD
S212-p NGKtsHEssQLDEPs
S213-p GKtsHEssQLDEPsV
S219-p ssQLDEPsVEtHsLE
T222-p LDEPsVEtHsLEQSK
S224-p EPsVEtHsLEQSKEY
S228 EtHsLEQSKEYKQRA
Y231 sLEQSKEYKQRAsHE
S236-p KEYKQRAsHESTEQS
S248-p EQSDAIDsAEKPDAI
S257-p EKPDAIDsAERsDAI
S261-p AIDsAERsDAIDSQA
S266 ERsDAIDSQASSKAs
S270 AIDSQASSKAsLEHQ
S273-p SQASSKAsLEHQsHE
S278-p KAsLEHQsHEFHsHE
S283-p HQsHEFHsHEDKLVL
S294-p KLVLDPKsKEDDRYL
S306-p RYLKFRIsHELEsss
S311-p RIsHELEsssSEVN_
S312-p IsHELEsssSEVN__
S313-p sHELEsssSEVN___
S314 HELEsssSEVN____
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