| General information | | DisProt: | DP00332 | | Name: | Bone sialoprotein 2 | | Synonym(s): | SIAL_HUMAN
Bone sialoprotein II
BSP II
Cell-binding sialoprotein
Integrin-binding sialoprotein
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P21815 | | UniGene: | Hs.518726 | | SwissProt: | SIAL_HUMAN | | TrEMBL: | | | NCBI (GI): | 251757441 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 317 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MKTALILLSI LGMACAFSMK NLHRRVKIED SEENGVFKYR PRYYLYKHAY FYPHLKRFPV - 60
QGSSDSSEEN GDDSSEEEEE EEETSNEGEN NEESNEDEDS EAENTTLSAT TLGYGEDATP - 120
GTGYTGLAAI QLPKKAGDIT NKATKEKESD EEEEEEEEGN ENEESEAEVD ENEQGINGTS - 180
TNSTEAENGN GSSGVDNGEE GEEESVTGAN AEGTTETGGQ GKGTSKTTTS PNGGFEPTTP - 240
PQVYRTTSPP FGKTTTVEYE GEYEYTGAND YDNGYEIYES ENGEPRGDNY RAYEDEYSYF - 300
KGQGYDGYDG QNYYHHQ
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| Functional narrative |
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.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered - Extended | | Name: | | | Location: | 1 - 317 | | Length: | 317 | | Region sequence: |
MKTALILLSILGMACAFSMKNLHRRVKIEDSEENGVFKYRPRYYLYKHAYFYPHLKRFPV
QGSSDSSEENGDDSSEEEEEEEETSNEGENNEESNEDEDSEAENTTLSATTLGYGEDATP
GTGYTGLAAIQLPKKAGDITNKATKEKESDEEEEEEEEGNENEESEAEVDENEQGINGTS
TNSTEAENGNGSSGVDNGEEGEEESVTGANAEGTTETGGQGKGTSKTTTSPNGGFEPTTP
PQVYRTTSPPFGKTTTVEYEGEYEYTGANDYDNGYEIYESENGEPRGDNYRAYEDEYSYF
KGQGYDGYDGQNYYHHQ | | Modification type: | | | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (303 K; )
| References:
- Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS. "Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin." Biochem Biophys Res Commun. 2001; 280(2): 460-5. PubMed: 11162539
| Comments:
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| Comments |
The paper referenced has a proline in position 88 but UniProt has a glycine.
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| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
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