dbPTM

RGS19_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RGS19_HUMAN
UniProt AC	P49795
Protein Name	Regulator of G-protein signaling 19
Gene Name	RGS19
Organism	Homo sapiens (Human).
Sequence Length	217
Subcellular Localization	Membrane Lipid-anchor.
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-alpha subfamily 1 members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein..
Protein Sequence	MPTPHEAEKQITGPEEADRPPSMSSHDTASPAAPSRNPCCLCWCCCCSCSWNQERRRAWQASRESKLQPLPSCEVCATPSPEEVQSWAQSFDKLMHSPAGRSVFRAFLRTEYSEENMLFWLACEELKAEANQHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINKKMQEPSAHTFDDAQLQIYTLMHRDSYPRFLSSPTYRALLLQGPSQSSSEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	HEAEKQITGPEEADR HHHHHHCCCCHHCCC	44.16	23312004
22	Phosphorylation	EEADRPPSMSSHDTA HHCCCCCCCCCCCCC	33.70	26657352
24	Phosphorylation	ADRPPSMSSHDTASP CCCCCCCCCCCCCCC	28.94	26657352
25	Phosphorylation	DRPPSMSSHDTASPA CCCCCCCCCCCCCCC	19.42	26657352
28	Phosphorylation	PSMSSHDTASPAAPS CCCCCCCCCCCCCCC	24.50	26434552
30	Phosphorylation	MSSHDTASPAAPSRN CCCCCCCCCCCCCCC	19.71	23312004
35	Phosphorylation	TASPAAPSRNPCCLC CCCCCCCCCCCEEEH	39.71	23312004
62	Phosphorylation	RRRAWQASRESKLQP HHHHHHHHHHHHCCC	22.83	28450419
65	Phosphorylation	AWQASRESKLQPLPS HHHHHHHHHCCCCCC	37.24	28450419
72	Phosphorylation	SKLQPLPSCEVCATP HHCCCCCCCCCCCCC	30.50	26657352
78	Phosphorylation	PSCEVCATPSPEEVQ CCCCCCCCCCHHHHH	21.12	28450419
80	Phosphorylation	CEVCATPSPEEVQSW CCCCCCCCHHHHHHH	40.36	28450419
86	Phosphorylation	PSPEEVQSWAQSFDK CCHHHHHHHHHHHHH	29.56	28450419
97	Phosphorylation	SFDKLMHSPAGRSVF HHHHHHCCHHHHHHH	11.50	28348404
102	Phosphorylation	MHSPAGRSVFRAFLR HCCHHHHHHHHHHHH	25.37	28555341
138	Ubiquitination	NQHVVDEKARLIYED HHHCCCHHHHHHHHH	34.05	2190698
143	Phosphorylation	DEKARLIYEDYVSIL CHHHHHHHHHHHHHC	13.82	21945579
146	Phosphorylation	ARLIYEDYVSILSPK HHHHHHHHHHHCCCC	5.55	21945579
148	Phosphorylation	LIYEDYVSILSPKEV HHHHHHHHHCCCCCC	16.16	21945579
151	Phosphorylation	EDYVSILSPKEVSLD HHHHHHCCCCCCCHH	32.05	21945579
153	Ubiquitination	YVSILSPKEVSLDSR HHHHCCCCCCCHHHH	68.33	-
156	Phosphorylation	ILSPKEVSLDSRVRE HCCCCCCCHHHHHHH	27.79	27470641
185	Phosphorylation	DDAQLQIYTLMHRDS CHHHHHHHHHHHCCC	4.85	27642862
186	Phosphorylation	DAQLQIYTLMHRDSY HHHHHHHHHHHCCCC	21.16	27642862
192	Phosphorylation	YTLMHRDSYPRFLSS HHHHHCCCCCHHHCC	36.67	27642862
193	Phosphorylation	TLMHRDSYPRFLSSP HHHHCCCCCHHHCCH	11.61	27642862
198	Phosphorylation	DSYPRFLSSPTYRAL CCCCHHHCCHHHHHH	31.40	28796482
199	Phosphorylation	SYPRFLSSPTYRALL CCCHHHCCHHHHHHH	24.33	28796482
201	Phosphorylation	PRFLSSPTYRALLLQ CHHHCCHHHHHHHHC	27.82	20166139
202	Phosphorylation	RFLSSPTYRALLLQG HHHCCHHHHHHHHCC	9.40	25884760
211	Phosphorylation	ALLLQGPSQSSSEA- HHHHCCCCCCCCCC-	49.90	23911959
213	Phosphorylation	LLQGPSQSSSEA--- HHCCCCCCCCCC---	39.92	23911959
214	Phosphorylation	LQGPSQSSSEA---- HCCCCCCCCCC----	25.26	22617229
215	Phosphorylation	QGPSQSSSEA----- CCCCCCCCCC-----	42.67	22617229

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
24	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
24	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
24	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
151	S	Phosphorylation	Kinase	MK01	P28482	PhosphoELM
151	S	Phosphorylation	Kinase	MAPK3	P27361	Uniprot
151	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
151	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
201	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
201	T	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RGS19_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 RGS19_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GNAZ_HUMAN	GNAZ	physical	8986788
GNAO_HUMAN	GNAO1	physical	8986788
GNAI2_HUMAN	GNAI2	physical	8986788
GNAI3_HUMAN	GNAI3	physical	8986788
GNAI1_HUMAN	GNAI1	physical	10364213
GNAO_HUMAN	GNAO1	physical	10364213
GNAI3_HUMAN	GNAI3	physical	10364213
GNAI1_HUMAN	GNAI1	physical	8986788
GNAI3_HUMAN	GNAI3	physical	8524874
GNAI3_HUMAN	GNAI3	physical	16293724

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 RGS19_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Erk1/2-dependent phosphorylation of Galpha-interacting proteinstimulates its GTPase accelerating activity and autophagy in humancolon cancer cells."; Ogier-Denis E., Pattingre S., El Benna J., Codogno P.; J. Biol. Chem. 275:39090-39095(2000). Cited for: PHOSPHORYLATION AT SER-151, AND MUTAGENESIS OF SER-151.	10993892 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASSSPECTROMETRY.	18691976 [Abstract]