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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: Cell adhesion; Secreted; Motility/polarity/chemotaxis; Secreted, signal peptide
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
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
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
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
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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