Home

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, signal peptide; Secreted; Motility/polarity/chemotaxis Cellular Component: extracellular space; extracellular region Biological Process: extracellular matrix organization and biogenesis; ossification; 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®

Select Structure to View Below sialoprotein 2

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Modification Sites and Domains

	Modification Sites in Parent Protein, Orthologs, and Isoforms

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	2		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

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.