| UniProt ID | REG1B_HUMAN | |
|---|---|---|
| UniProt AC | P48304 | |
| Protein Name | Lithostathine-1-beta | |
| Gene Name | REG1B | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 166 | |
| Subcellular Localization | Secreted. | |
| Protein Description | Might act as an inhibitor of spontaneous calcium carbonate precipitation. May be associated with neuronal sprouting in brain, and with brain and pancreas regeneration.. | |
| Protein Sequence | MAQTNSFFMLISSLMFLSLSQGQESQTELPNPRISCPEGTNAYRSYCYYFNEDPETWVDADLYCQNMNSGNLVSVLTQAEGAFVASLIKESSTDDSNVWIGLHDPKKNRRWHWSSGSLVSYKSWDTGSPSSANAGYCASLTSCSGFKKWKDESCEKKFSFVCKFKN | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MAQTNSFFMLI ----CCCCHHHHHHH | 24.24 | 24043423 | |
| 6 | Phosphorylation | --MAQTNSFFMLISS --CCCCHHHHHHHHH | 24.21 | 24043423 | |
| 12 | Phosphorylation | NSFFMLISSLMFLSL HHHHHHHHHHHHHHH | 17.29 | 24043423 | |
| 13 | Phosphorylation | SFFMLISSLMFLSLS HHHHHHHHHHHHHHH | 19.50 | 24043423 | |
| 18 | Phosphorylation | ISSLMFLSLSQGQES HHHHHHHHHHCCCCC | 18.08 | 24043423 | |
| 20 | Phosphorylation | SLMFLSLSQGQESQT HHHHHHHHCCCCCCC | 28.96 | 24043423 | |
| 25 | Phosphorylation | SLSQGQESQTELPNP HHHCCCCCCCCCCCC | 34.22 | 24043423 | |
| 27 | O-linked_Glycosylation | SQGQESQTELPNPRI HCCCCCCCCCCCCCC | 49.09 | 7607222 | |
| 27 | Phosphorylation | SQGQESQTELPNPRI HCCCCCCCCCCCCCC | 49.09 | 24043423 | |
| 43 | Phosphorylation | CPEGTNAYRSYCYYF CCCCCCEEEEEEEEE | 11.36 | - | |
| 86 | Phosphorylation | AEGAFVASLIKESST CCCHHHHHHHHCCCC | 25.89 | 24719451 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of REG1B_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of REG1B_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of REG1B_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| BAG6_HUMAN | BAG6 | physical | 16169070 | |
| BAG6_HUMAN | BAG6 | physical | 21900206 | |
| REG1A_HUMAN | REG1A | physical | 26186194 | |
| REG1A_HUMAN | REG1A | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| O-linked Glycosylation | |
| Reference | PubMed |
| "The glycan moiety of human pancreatic lithostathine. Structurecharacterization and possible pathophysiological implications."; De Reggi M., Capon C., Gharib B., Wieruszeski J.-M., Michel R.,Fournet B.; Eur. J. Biochem. 230:503-510(1995). Cited for: GLYCOSYLATION AT THR-27. | |
