dbPTM

RGS10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RGS10_HUMAN
UniProt AC	O43665
Protein Name	Regulator of G-protein signaling 10
Gene Name	RGS10
Organism	Homo sapiens (Human).
Sequence Length	173
Subcellular Localization	Cytoplasm, cytosol . Nucleus . Forskolin treatment promotes phosphorylation and translocation to the nucleus. Isoform 2: Nucleus .
Protein Description	Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the muscarinic acetylcholine receptor CHRM2. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. [PubMed: 8774883]
Protein Sequence	MQSELCFADIHDSDGSSSSSHQSLKSTAKWAASLENLLEDPEGVKRFREFLKKEFSEENVLFWLACEDFKKMQDKTQMQEKAKEIYMTFLSSKASSQVNVEGQSRLNEKILEEPHPLMFQKLQDQIFNLMKYDSYSRFLKSDLFLKHKRTEEEEEDLPDAQTAAKRASRIYNT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7 (in isoform 3)	Phosphorylation	-	12.22	29485707
10 (in isoform 3)	Phosphorylation	-	3.31	27282143
12	Ubiquitination	LCFADIHDSDGSSSS EEECCCCCCCCCCCH	49.08	29967540
13	Phosphorylation	CFADIHDSDGSSSSS EECCCCCCCCCCCHH	29.70	-
16	Phosphorylation	DIHDSDGSSSSSHQS CCCCCCCCCCHHHHH	31.85	30576142
16 (in isoform 3)	Phosphorylation	-	31.85	25159151
19	Phosphorylation	DSDGSSSSSHQSLKS CCCCCCCHHHHHHHH	33.51	-
20	Phosphorylation	SDGSSSSSHQSLKST CCCCCCHHHHHHHHH	27.74	-
21 (in isoform 3)	Phosphorylation	-	24.17	29116813
23	Phosphorylation	SSSSSHQSLKSTAKW CCCHHHHHHHHHHHH	32.13	30576142
23	Ubiquitination	SSSSSHQSLKSTAKW CCCHHHHHHHHHHHH	32.13	29967540
24 (in isoform 3)	Phosphorylation	-	4.01	27251275
24	Phosphorylation	SSSSHQSLKSTAKWA CCHHHHHHHHHHHHH	4.01	24275569
25 (in isoform 3)	Phosphorylation	-	51.51	27542207
26 (in isoform 3)	Phosphorylation	-	38.60	27251275
27 (in isoform 3)	Phosphorylation	-	30.57	27251275
28 (in isoform 3)	Phosphorylation	-	16.69	27542207
33	Phosphorylation	STAKWAASLENLLED HHHHHHHHHHHHHHC	28.59	28102081
37	Ubiquitination	WAASLENLLEDPEGV HHHHHHHHHHCHHHH	3.96	29967540
39 (in isoform 2)	Ubiquitination	-	74.76	21890473
39	Ubiquitination	ASLENLLEDPEGVKR HHHHHHHHCHHHHHH	74.76	29967540
41	Phosphorylation	LENLLEDPEGVKRFR HHHHHHCHHHHHHHH	30.76	-
45	Ubiquitination	LEDPEGVKRFREFLK HHCHHHHHHHHHHHH	57.59	-
45 (in isoform 1)	Ubiquitination	-	57.59	21890473
53 (in isoform 3)	Ubiquitination	-	67.16	21890473
53	Ubiquitination	RFREFLKKEFSEENV HHHHHHHHHCCHHHH	67.16	29967540
66	S-palmitoylation	NVLFWLACEDFKKMQ HHHHHHHHHHHHHCC	4.89	10608901
70	Acetylation	WLACEDFKKMQDKTQ HHHHHHHHHCCCHHH	60.71	24467953
74	S-palmitoylation	EDFKKMQDKTQMQEK HHHHHCCCHHHHHHH	53.09	10608901
86	Phosphorylation	QEKAKEIYMTFLSSK HHHHHHHHHHHHHCC	7.38	28152594
86	Ubiquitination	QEKAKEIYMTFLSSK HHHHHHHHHHHHHCC	7.38	21890473
88	Phosphorylation	KAKEIYMTFLSSKAS HHHHHHHHHHHCCCC	12.40	28152594
91	Phosphorylation	EIYMTFLSSKASSQV HHHHHHHHCCCCCCC	26.12	28152594
92	Phosphorylation	IYMTFLSSKASSQVN HHHHHHHCCCCCCCC	34.09	28152594
100	Ubiquitination	KASSQVNVEGQSRLN CCCCCCCCCCCHHHH	10.32	21890473
111	Ubiquitination	SRLNEKILEEPHPLM HHHHHHHHHCCCCHH	10.12	24816145
125	Ubiquitination	MFQKLQDQIFNLMKY HHHHHHHHHHHHHCH	29.25	24816145
134	Ubiquitination	FNLMKYDSYSRFLKS HHHHCHHHHHHHHCC	23.17	21890473
134 (in isoform 2)	Ubiquitination	-	23.17	21890473
135	Phosphorylation	NLMKYDSYSRFLKSD HHHCHHHHHHHHCCC	10.85	-
140	Ubiquitination	DSYSRFLKSDLFLKH HHHHHHHCCCHHHHC	38.93	-
140 (in isoform 1)	Ubiquitination	-	38.93	21890473
141	Phosphorylation	SYSRFLKSDLFLKHK HHHHHHCCCHHHHCC	41.51	28509920
148 (in isoform 3)	Ubiquitination	-	60.47	21890473
148	Ubiquitination	SDLFLKHKRTEEEEE CCHHHHCCCCHHHHC	60.47	21890473
159 (in isoform 2)	Ubiquitination	-	59.62	21890473
159	Ubiquitination	EEEEDLPDAQTAAKR HHHCCCCHHHHHHHH	59.62	24816145
162 (in isoform 2)	Phosphorylation	-	30.24	-
162	Phosphorylation	EDLPDAQTAAKRASR CCCCHHHHHHHHHHH	30.24	26074081
165	Acetylation	PDAQTAAKRASRIYN CHHHHHHHHHHHHHC	46.14	25953088
165 (in isoform 1)	Ubiquitination	-	46.14	21890473
165	Ubiquitination	PDAQTAAKRASRIYN CHHHHHHHHHHHHHC	46.14	-
168	Phosphorylation	QTAAKRASRIYNT-- HHHHHHHHHHHCC--	24.20	10608901
171	Phosphorylation	AKRASRIYNT----- HHHHHHHHCC-----	16.19	26074081
173	Ubiquitination	RASRIYNT------- HHHHHHCC-------	24.02	24816145
173	Phosphorylation	RASRIYNT------- HHHHHHCC-------	24.02	26074081
173 (in isoform 3)	Ubiquitination	-	24.02	21890473
176	Phosphorylation	RIYNT---------- HHHCC----------		11443111

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
168	S	Phosphorylation	Kinase	PKACA	P17612	PSP
168	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
168	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
168	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RGS10_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 RGS10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SAP18_HUMAN	SAP18	physical	17353931
GNAI3_HUMAN	GNAI3	physical	8774883
A4_HUMAN	APP	physical	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 RGS10_HUMAN

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"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-66.	10608901 [Abstract]