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Protein Page:
Sialoprotein-2 (human)

Overview
Sialoprotein-2 Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. Promotes Arg-Gly-Asp-dependent cell attachment. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Cell adhesion; Secreted; Motility/polarity/chemotaxis
Cellular Component: extracellular space; membrane; extracellular region
Biological Process: osteoblast differentiation; extracellular matrix organization and biogenesis; biomineral formation; cell adhesion
Reference #:  P21815 (UniProtKB)
Alt. Names/Synonyms: BNSP; Bone sialoprotein 2; Bone sialoprotein II; BSP; BSP II; BSP-II; Cell-binding sialoprotein; IBSP; Integrin-binding sialoprotein; SIAL; SP-II
Gene Symbols: IBSP
Molecular weight: 35,148 Da
Basal Isoelectric point: 4.14  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Sialoprotein-2

Protein Structure Not Found.


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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

 
0 1 T3-p _____MKtALILLsI
0 1 S9-p KtALILLsILGMACA
0 1 S18-p LGMACAFsMKNLHRR
2 2 S31-p RRVKIEDsEENGVFK
0 1 Y39-p EENGVFKyRPRYYLY
0 1 G62 LKRFPVQGSSDSSEE
1 0 S64 RFPVQGSSDSSEENG
1 0 S66 PVQGSSDSSEENGDD
1 1 S67 VQGSSDSSEENGDDS
2 1 S74 SEENGDDSSEEEEEE
2 1 S75 EENGDDSSEEEEEEE
1 0 S85 EEEEEETSNEGENNE
0 1 S94 EGENNEESNEDEDSE
0 1 S100 ESNEDEDSEAENTTL
2 1 S149 KATKEKESDEEEEEE
0 1 T207-p EGEEESVtGANAEDT
0 1 S225-p GRQGKGTsKTtTSPN
0 1 T228-p GKGTsKTtTSPNGGF
0 1 T246-p TPPQVYRtTSPPFGK
0 1 S280 NGYEIYESENGEPRG
1 1 G307 FKGQGYDGYDGQNYY
  mouse

 
T3 _____MKTALILLSI
S9 KTALILLSILGMACA
S18 LGMACAFSMKNFHRR
S31 RRIKAEDSEENGVFK
Y39 EENGVFKYRPRYFLY
G62 LKRFPVQGGSDSSEE
S64 RFPVQGGSDSSEENG
S66 PVQGGSDSSEENGDG
S67 VQGGSDSSEENGDGD
S75 EENGDGDSSEEEGEE
S76 ENGDGDSSEEEGEEE
S86 EGEEEETSNEEENNE
S95 EEENNEDSEGNEDQE
A103 EGNEDQEAEAENSTL
S155 RAPKVKESDEEEEEE
T215 EAEEASVTEAGAEGT
- gap
T235 LTSVGTQTAVLLNGF
T254 PPPEAYGTTSPPIRK
N287 NEYEVYDNENGEPRG
G314 YKGHGYEGYEGQNYY
  rat

 
T3 _____MKTALILLCI
C9 KTALILLCILGMASA
S18 LGMASAFSMKNFHRR
S31-p RRIKAEDsEENGVFK
Y39 EENGVFKYRPRYFLY
G63 LKRFPVQGGSDSSEE
S65 RFPVQGGSDSSEENG
S67 PVQGGSDSSEENGDG
S68 VQGGSDSSEENGDGD
S76-p EENGDGDssEEEGEE
S77-p ENGDGDssEEEGEEE
S87 EGEEEETSNEEENNE
S96 EEENNEDSEGNEDQE
A104 EGNEDQEAEAENATL
S153-p KAPKMKEsDEEEEEE
T210 EAEEASVTEAGAEGT
- gap
T231 LTSYGTTTAVLLNGF
T250 PPPEAYGTTSPPARK
E283 TAYETYDENNGEPRG
G310 YKGHGYEGYEGQDYY
  cow

 
T3 _____MKTVLILLSI
S9 KTVLILLSILGMACA
S18 LGMACALSMKNLNRR
S31-p RRAKLEDsEENGVFK
Y39 EENGVFKYRPQYYVY
S62-p LKRFAVQsSsDssEE
S64-p RFAVQsSsDssEENG
S66-p AVQsSsDssEENGNG
S67-p VQsSsDssEENGNGD
S75-p EENGNGDssEEEEEE
S76-p ENGNGDssEEEEEEE
S86-p EEEEEETsNEEGNNG
S98-p NNGGNEDsDENEDEE
S106-p DENEDEEsEAENTTL
S154-p KATKEDEsDEEEEEE
T209 DGEEESVTEANTEGI
- gap
T223 ITVAGETTTSPNGGF
T242 PHQEVYGTTPPPFGK
S273-p NGYEIYEsENGDPRG
S300-p YKGRGYDsYDGQDYY
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