UniProt ID | SSR2_HUMAN | |
---|---|---|
UniProt AC | P30874 | |
Protein Name | Somatostatin receptor type 2 | |
Gene Name | SSTR2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 369 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein. Cytoplasm. Located mainly at the cell surface under basal conditions. Agonist stimulation results in internalization to the cytoplasm. |
|
Protein Description | Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and PLC via pertussis toxin insensitive as well as sensitive G proteins. Inhibits calcium entry by suppressing voltage-dependent calcium channels. Acts as the functionally dominant somatostatin receptor in pancreatic alpha- and beta-cells where it mediates the inhibitory effect of somatostatin-14 on hormone secretion. Inhibits cell growth through enhancement of MAPK1 and MAPK2 phosphorylation and subsequent up-regulation of CDKN1B. Stimulates neuronal migration and axon outgrowth and may participate in neuron development and maturation during brain development. Mediates negative regulation of insulin receptor signaling through PTPN6. Inactivates SSTR3 receptor function following heterodimerization.. | |
Protein Sequence | MDMADEPLNGSHTWLSIPFDLNGSVVSTNTSNQTEPYYDLTSNAVLTFIYFVVCIIGLCGNTLVIYVILRYAKMKTITNIYILNLAIADELFMLGLPFLAMQVALVHWPFGKAICRVVMTVDGINQFTSIFCLTVMSIDRYLAVVHPIKSAKWRRPRTAKMITMAVWGVSLLVILPIMIYAGLRSNQWGRSSCTINWPGESGAWYTGFIIYTFILGFLVPLTIICLCYLFIIIKVKSSGIRVGSSKRKKSEKKVTRMVSIVVAVFIFCWLPFYIFNVSSVSMAISPTPALKGMFDFVVVLTYANSCANPILYAFLSDNFKKSFQNVLCLVKVSGTDDGERSDSKQDKSRLNETTETQRTLLNGDLQTSI | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
9 | N-linked_Glycosylation | DMADEPLNGSHTWLS CCCCCCCCCCCEEEE | 61.71 | UniProtKB CARBOHYD | |
22 | N-linked_Glycosylation | LSIPFDLNGSVVSTN EECEEECCCCEEECC | 42.40 | UniProtKB CARBOHYD | |
29 | N-linked_Glycosylation | NGSVVSTNTSNQTEP CCCEEECCCCCCCCC | 33.72 | UniProtKB CARBOHYD | |
32 | N-linked_Glycosylation | VVSTNTSNQTEPYYD EEECCCCCCCCCCCC | 51.24 | UniProtKB CARBOHYD | |
66 | Phosphorylation | CGNTLVIYVILRYAK HCCHHHHHHHHHHHC | 3.64 | 25884760 | |
71 | Phosphorylation | VIYVILRYAKMKTIT HHHHHHHHHCCCCCC | 13.71 | 16917505 | |
137 | Phosphorylation | IFCLTVMSIDRYLAV HHHHHHHCCCHHHHH | 19.59 | - | |
248 | Acetylation | RVGSSKRKKSEKKVT CCCCCCCCCCHHHHH | 65.47 | 30592679 | |
322 | Phosphorylation | LSDNFKKSFQNVLCL HCHHHHHHHCCEEEE | 32.43 | 29116813 | |
328 | S-palmitoylation | KSFQNVLCLVKVSGT HHHCCEEEEEEECCC | 3.41 | - | |
341 | Phosphorylation | GTDDGERSDSKQDKS CCCCCCCCCCHHHHH | 41.77 | 21330405 | |
343 | Phosphorylation | DDGERSDSKQDKSRL CCCCCCCCHHHHHHH | 33.20 | 21330405 | |
344 | Ubiquitination | DGERSDSKQDKSRLN CCCCCCCHHHHHHHC | 68.46 | 32142685 | |
348 | Phosphorylation | SDSKQDKSRLNETTE CCCHHHHHHHCCCHH | 50.74 | - | |
353 | Phosphorylation | DKSRLNETTETQRTL HHHHHCCCHHHHHHH | 28.94 | 21343287 | |
354 | Phosphorylation | KSRLNETTETQRTLL HHHHCCCHHHHHHHH | 30.75 | 21343287 | |
356 | Phosphorylation | RLNETTETQRTLLNG HHCCCHHHHHHHHCC | 22.66 | - | |
359 | Phosphorylation | ETTETQRTLLNGDLQ CCHHHHHHHHCCCCC | 26.27 | - | |
367 | Phosphorylation | LLNGDLQTSI----- HHCCCCCCCC----- | 35.37 | 26471730 | |
368 | Phosphorylation | LNGDLQTSI------ HCCCCCCCC------ | 17.22 | 26471730 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SSR2_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 SSR2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SHAN1_HUMAN | SHANK1 | physical | 10551867 | |
A4_HUMAN | APP | physical | 21832049 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
D00442 | Octreotide (USAN/INN) | |||||
D02108 | Indium In 111 pentetreotide (USP); OctreoScan (TN) | |||||
D02250 | Octreotide acetate (JAN); Octreotide diacetate; Sandostatin (TN) | |||||
D04666 | Lanreotide acetate (JAN/USAN); Somatuline (TN) | |||||
D05230 | Octreotide pamoate (USAN) | |||||
D06281 | Vapreotide (USAN/INN) | |||||
D06495 | Octreotide acetate (USAN); Sandostatin (TN) | |||||
D07431 | Somatostatin (INN) | |||||
D09988 | Vapreotide acetate (USAN) | |||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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