UniProt ID | NCS1_SCHPO | |
---|---|---|
UniProt AC | Q09711 | |
Protein Name | Calcium-binding protein NCS-1 | |
Gene Name | ncs1 | |
Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). | |
Sequence Length | 190 | |
Subcellular Localization |
Membrane Peripheral membrane protein . |
|
Protein Description | Negatively regulates sporulation perhaps by controlling Ca(2+)-dependent desensitization of git3.. | |
Protein Sequence | MGKSQSKLSQDQLQDLVRSTRFDKKELQQWYKGFFKDCPSGHLNKSEFQKIYKQFFPFGDPSAFAEYVFNVFDADKNGYIDFKEFICALSVTSRGELNDKLIWAFQLYDLDNNGLISYDEMLRIVDAIYKMVGSMVKLPEDEDTPEKRVNKIFNMMDKNKDGQLTLEEFCEGSKRDPTIVSALSLYDGLV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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 NCS1_SCHPO !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NCS1_SCHPO !! |
* 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 NCS1_SCHPO !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
EHS1_SCHPO | yam8 | genetic | 20018864 | |
EHS1_SCHPO | yam8 | physical | 20018864 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Myristoylation | |
Reference | PubMed |
"Fission yeast homolog of neuronal calcium sensor-1 (Ncs1p) regulatessporulation and confers calcium tolerance."; Hamasaki-Katagiri N., Molchanova T., Takeda K., Ames J.B.; J. Biol. Chem. 279:12744-12754(2004). Cited for: NUCLEOTIDE SEQUENCE [MRNA], STRUCTURE BY NMR, FUNCTION, SUBCELLULARLOCATION, MYRISTOYLATION AT GLY-2, CALCIUM-BINDING, AND MUTAGENESIS OFGLY-2; GLU-84; GLU-120 AND GLU-168. |