RGS5_HUMAN - dbPTM
RGS5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGS5_HUMAN
UniProt AC O15539
Protein Name Regulator of G-protein signaling 5
Gene Name RGS5
Organism Homo sapiens (Human).
Sequence Length 181
Subcellular Localization Isoform 1: Cytoplasm . Membrane .
Isoform 2: Cytoplasm .
Protein Description Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha (By similarity)..
Protein Sequence MCKGLAALPHSCLERAKEIKIKLGILLQKPDSVGDLVIPYNEKPEKPAKTQKTSLDEALQWRDSLDKLLQNNYGLASFKSFLKSEFSEENLEFWIACEDYKKIKSPAKMAEKAKQIYEEFIQTEAPKEVNIDHFTKDITMKNLVEPSLSSFDMAQKRIHALMEKDSLPRFVRSEFYQELIK
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
11PhosphorylationGLAALPHSCLERAKE
HHHCCCHHHHHHHHH
20.6128464451
22UbiquitinationRAKEIKIKLGILLQK
HHHHHCHHHEEEECC
35.34-
29UbiquitinationKLGILLQKPDSVGDL
HHEEEECCCCCCCCE
51.25-
40PhosphorylationVGDLVIPYNEKPEKP
CCCEEECCCCCCCCC
25.4818083107
43UbiquitinationLVIPYNEKPEKPAKT
EEECCCCCCCCCCCC
55.64-
46UbiquitinationPYNEKPEKPAKTQKT
CCCCCCCCCCCCCCC
59.82-
52UbiquitinationEKPAKTQKTSLDEAL
CCCCCCCCCCHHHHH
45.36-
64PhosphorylationEALQWRDSLDKLLQN
HHHHHHHHHHHHHHC
29.8727535140
67UbiquitinationQWRDSLDKLLQNNYG
HHHHHHHHHHHCCCC
57.29-
73PhosphorylationDKLLQNNYGLASFKS
HHHHHCCCCHHHHHH
22.5225884760
77PhosphorylationQNNYGLASFKSFLKS
HCCCCHHHHHHHHHH
37.9524719451
79UbiquitinationNYGLASFKSFLKSEF
CCCHHHHHHHHHHCC
37.49-
80PhosphorylationYGLASFKSFLKSEFS
CCHHHHHHHHHHCCC
33.5324719451
84PhosphorylationSFKSFLKSEFSEENL
HHHHHHHHCCCHHHH
46.1217540411
114UbiquitinationAKMAEKAKQIYEEFI
HHHHHHHHHHHHHHH
48.58-
117PhosphorylationAEKAKQIYEEFIQTE
HHHHHHHHHHHHHCC
13.6025884760
127UbiquitinationFIQTEAPKEVNIDHF
HHHCCCCCCCCCCCC
79.80-
136UbiquitinationVNIDHFTKDITMKNL
CCCCCCCCCCCHHHC
46.30-
141UbiquitinationFTKDITMKNLVEPSL
CCCCCCHHHCCCCCC
38.18-
156UbiquitinationSSFDMAQKRIHALME
CHHHHHHHHHHHHHH
43.72-
164UbiquitinationRIHALMEKDSLPRFV
HHHHHHHHCCCCHHH
38.36-
166PhosphorylationHALMEKDSLPRFVRS
HHHHHHCCCCHHHHH
51.8717540411

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
84SPhosphorylationKinasePRKCAP05696
GPS
166SPhosphorylationKinasePRKCAP05696
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGS5_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 RGS5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GNAI3_HUMANGNAI3physical
9079700
GNAI2_HUMANGNAI2physical
9079700
GNAO_HUMANGNAO1physical
9079700
GNAI1_HUMANGNAI1physical
11253162
GNAI2_HUMANGNAI2physical
11253162
GNAI3_HUMANGNAI3physical
11253162
GNAO_HUMANGNAO1physical
11253162
GNAQ_HUMANGNAQphysical
11253162
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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RGS5_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP