SSR2_HUMAN - dbPTM
SSR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
9N-linked_GlycosylationDMADEPLNGSHTWLS
CCCCCCCCCCCEEEE
61.71UniProtKB CARBOHYD
22N-linked_GlycosylationLSIPFDLNGSVVSTN
EECEEECCCCEEECC
42.40UniProtKB CARBOHYD
29N-linked_GlycosylationNGSVVSTNTSNQTEP
CCCEEECCCCCCCCC
33.72UniProtKB CARBOHYD
32N-linked_GlycosylationVVSTNTSNQTEPYYD
EEECCCCCCCCCCCC
51.24UniProtKB CARBOHYD
66PhosphorylationCGNTLVIYVILRYAK
HCCHHHHHHHHHHHC
3.6425884760
71PhosphorylationVIYVILRYAKMKTIT
HHHHHHHHHCCCCCC
13.7116917505
137PhosphorylationIFCLTVMSIDRYLAV
HHHHHHHCCCHHHHH
19.59-
248AcetylationRVGSSKRKKSEKKVT
CCCCCCCCCCHHHHH
65.4730592679
322PhosphorylationLSDNFKKSFQNVLCL
HCHHHHHHHCCEEEE
32.4329116813
328S-palmitoylationKSFQNVLCLVKVSGT
HHHCCEEEEEEECCC
3.41-
341PhosphorylationGTDDGERSDSKQDKS
CCCCCCCCCCHHHHH
41.7721330405
343PhosphorylationDDGERSDSKQDKSRL
CCCCCCCCHHHHHHH
33.2021330405
344UbiquitinationDGERSDSKQDKSRLN
CCCCCCCHHHHHHHC
68.4632142685
348PhosphorylationSDSKQDKSRLNETTE
CCCHHHHHHHCCCHH
50.74-
353PhosphorylationDKSRLNETTETQRTL
HHHHHCCCHHHHHHH
28.9421343287
354PhosphorylationKSRLNETTETQRTLL
HHHHCCCHHHHHHHH
30.7521343287
356PhosphorylationRLNETTETQRTLLNG
HHCCCHHHHHHHHCC
22.66-
359PhosphorylationETTETQRTLLNGDLQ
CCHHHHHHHHCCCCC
26.27-
367PhosphorylationLLNGDLQTSI-----
HHCCCCCCCC-----
35.3726471730
368PhosphorylationLNGDLQTSI------
HCCCCCCCC------
17.2226471730

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
341SPhosphorylationKinaseGRK3P35626
PSP
343SPhosphorylationKinaseGRK3P35626
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSR2_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHAN1_HUMANSHANK1physical
10551867
A4_HUMANAPPphysical
21832049

Drug and Disease Associations
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.
Regulatory Network of SSR2_HUMAN

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Related Literatures of Post-Translational Modification

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