RGS4_HUMAN - dbPTM
RGS4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGS4_HUMAN
UniProt AC P49798
Protein Name Regulator of G-protein signaling 4
Gene Name RGS4
Organism Homo sapiens (Human).
Sequence Length 205
Subcellular Localization
Protein Description Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Activity on G(z)-alpha is inhibited by phosphorylation of the G-protein. Activity on G(z)-alpha and G(i)-alpha-1 is inhibited by palmitoylation of the G-protein..
Protein Sequence MCKGLAGLPASCLRSAKDMKHRLGFLLQKSDSCEHNSSHNKKDKVVICQRVSQEEVKKWAESLENLISHECGLAAFKAFLKSEYSEENIDFWISCEEYKKIKSPSKLSPKAKKIYNEFISVQATKEVNLDSCTREETSRNMLEPTITCFDEAQKKIFNLMEKDSYRRFLKSRFYLDLVNPSSCGAEKQKGAKSSADCASLVPQCA
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------MCKGLAGLP
------CCCCCCCCC
4.8721035448
11PhosphorylationGLAGLPASCLRSAKD
CCCCCCHHHHHHHHH
16.2526356563
12S-palmitoylationLAGLPASCLRSAKDM
CCCCCHHHHHHHHHH
3.8810608901
15PhosphorylationLPASCLRSAKDMKHR
CCHHHHHHHHHHHHH
27.0726356563
30PhosphorylationLGFLLQKSDSCEHNS
HHHHHHCCCCCCCCC
23.0724114839
32PhosphorylationFLLQKSDSCEHNSSH
HHHHCCCCCCCCCCC
28.6124114839
37PhosphorylationSDSCEHNSSHNKKDK
CCCCCCCCCCCCCCE
34.5824114839
38PhosphorylationDSCEHNSSHNKKDKV
CCCCCCCCCCCCCEE
36.0724114839
59 (in isoform 3)Phosphorylation-10.2729507054
78 (in isoform 3)Phosphorylation-14.46-
80 (in isoform 3)Phosphorylation-7.73-
81 (in isoform 3)Phosphorylation-34.48-
82 (in isoform 3)Phosphorylation-43.87-
92 (in isoform 3)Phosphorylation-4.28-
95S-palmitoylationNIDFWISCEEYKKIK
HCCEEEEHHHHHCCC
3.2010608901
103PhosphorylationEEYKKIKSPSKLSPK
HHHHCCCCHHHCCHH
37.5727732954
105PhosphorylationYKKIKSPSKLSPKAK
HHCCCCHHHCCHHHH
54.0127732954
108PhosphorylationIKSPSKLSPKAKKIY
CCCHHHCCHHHHHHH
28.2627732954

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
52SPhosphorylationKinasePKA-FAMILY-GPS

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

10608901
12CPalmitoylation

10608901

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 RGS4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COPB2_HUMANCOPB2physical
10982407
GNAQ_HUMANGNAQphysical
14634662
ERBB3_HUMANERBB3physical
12840049
GNAI1_HUMANGNAI1physical
9660808
GNAI2_HUMANGNAI2physical
9660808
GNAO_HUMANGNAO1physical
9660808
GNAQ_HUMANGNAQphysical
9660808
GNAI1_BOVINGNAI1physical
9405622
GNAT1_BOVINGNAT1physical
9405622
KRIT1_HUMANKRIT1physical
10747990
GABR1_HUMANGABBR1physical
17185339
GNAI1_HUMANGNAI1physical
22310500
PPCEL_HUMANPREPLphysical
28514442
GNAQ_HUMANGNAQphysical
10727532
GNAO_HUMANGNAO1physical
10727532

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
604906Schizophrenia 9 (SCZD9)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RGS4_HUMAN

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Palmitoylation of a conserved cysteine in the regulator of G proteinsignaling (RGS) domain modulates the GTPase-activating activity ofRGS4 and RGS10.";
Tu Y., Popov S., Slaughter C., Ross E.M.;
J. Biol. Chem. 274:38260-38267(1999).
Cited for: PALMITOYLATION AT CYS-2; CYS-12 AND CYS-95.

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