RGS16_HUMAN - dbPTM
RGS16_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGS16_HUMAN
UniProt AC O15492
Protein Name Regulator of G-protein signaling 16
Gene Name RGS16
Organism Homo sapiens (Human).
Sequence Length 202
Subcellular Localization Membrane
Lipid-anchor .
Protein Description Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. [PubMed: 11602604]
Protein Sequence MCRTLAAFPTTCLERAKEFKTRLGIFLHKSELGCDTGSTGKFEWGSKHSKENRNFSEDVLGWRESFDLLLSSKNGVAAFHAFLKTEFSEENLEFWLACEEFKKIRSATKLASRAHQIFEEFICSEAPKEVNIDHETHELTRMNLQTATATCFDAAQGKTRTLMEKDSYPRFLKSPAYRDLAAQASAASATLSSCSLDEPSHT
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
2S-palmitoylation------MCRTLAAFP
------CCCCCCCCC
4.5914642772
10PhosphorylationRTLAAFPTTCLERAK
CCCCCCCHHHHHHHH
24.5630631047
11PhosphorylationTLAAFPTTCLERAKE
CCCCCCHHHHHHHHH
18.4830631047
12S-palmitoylationLAAFPTTCLERAKEF
CCCCCHHHHHHHHHH
4.0114642772
41UbiquitinationCDTGSTGKFEWGSKH
CCCCCCCCCCCCCCC
39.9529967540
71PhosphorylationESFDLLLSSKNGVAA
HHHHHHHHCCCCHHH
38.96-
72PhosphorylationSFDLLLSSKNGVAAF
HHHHHHHCCCCHHHH
30.06-
73AcetylationFDLLLSSKNGVAAFH
HHHHHHCCCCHHHHH
55.1124246443
98S-palmitoylationNLEFWLACEEFKKIR
HHHHHHHHHHHHHHH
4.8912642592
167PhosphorylationRTLMEKDSYPRFLKS
CCCCCCCCCCCHHCC
48.3726074081
168PhosphorylationTLMEKDSYPRFLKSP
CCCCCCCCCCHHCCH
14.4612588871
173UbiquitinationDSYPRFLKSPAYRDL
CCCCCHHCCHHHHHH
52.2429967540
177PhosphorylationRFLKSPAYRDLAAQA
CHHCCHHHHHHHHHH
14.1912588871
190PhosphorylationQASAASATLSSCSLD
HHHHHHHHHHHCCCC
25.3626471730
192PhosphorylationSAASATLSSCSLDEP
HHHHHHHHHCCCCCC
25.5826471730
193PhosphorylationAASATLSSCSLDEPS
HHHHHHHHCCCCCCC
15.7326471730
195PhosphorylationSATLSSCSLDEPSHT
HHHHHHCCCCCCCCC
40.5826471730
200PhosphorylationSCSLDEPSHT-----
HCCCCCCCCC-----
37.4026471730
202PhosphorylationSLDEPSHT-------
CCCCCCCC-------
44.6426471730

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
168YPhosphorylationKinaseEGFRP00533
Uniprot
168YPhosphorylationKinaseLYNP07948
PSP
168YPhosphorylationKinaseSRCP12931
PSP
168YPhosphorylationKinaseSRC64-PhosphoELM
177YPhosphorylationKinaseEGFRP00533
PhosphoELM
177YPhosphorylationKinaseLYNP07948
PSP
177YPhosphorylationKinaseSRCP12931
PSP
177YPhosphorylationKinaseSRC64-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
2CPalmitoylation

-
12CPalmitoylation

-

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 RGS16_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GNAQ_HUMANGNAQphysical
14634662
GNA13_HUMANGNA13physical
14634662
GNAI3_HUMANGNAI3physical
9079700
GNAI2_HUMANGNAI2physical
9079700
GNAO_HUMANGNAO1physical
9079700
GNAI3_HUMANGNAI3physical
10072511
GNAI1_HUMANGNAI1physical
10878019
GDE1_HUMANGDE1physical
10760272
EGFR_HUMANEGFRphysical
11602604
ST14_HUMANST14physical
21988832

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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RGS16_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation.";
Derrien A., Druey K.M.;
J. Biol. Chem. 276:48532-48538(2001).
Cited for: PHOSPHORYLATION AT TYR-168 BY EGFR, PHOSPHORYLATION AT TYR-177, ANDMUTAGENESIS OF TYR-168 AND TYR-177.

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