RGS_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RGS_DROME
• UniProt AC: Q9VCX1
• Protein Name: Regulator of G-protein signaling loco
• Gene Name: loco
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1541
• Subcellular Localization: Cytoplasm. Cell membrane. Apical cell membrane. Recruited from the cytosol to the plasma membrane by the G(i) alpha subunit. Colocalizes with moody at the plasma membrane. Localizes as a crescent to the apical cortex in interphase and forms an apical
• Protein Description: Acts as a regulator of G protein signaling (RGS). Modulates G protein alpha subunits nucleotide exchange and hydrolysis activities by functioning either as a GTPase-activating protein (GAP), thereby driving G protein alpha subunits into their inactive GDP-bound form, or as a GDP-dissociation inhibitor (GDI). Confers GDI and GAP activities on G(i) alpha subunit Galphai. Confers GAP activity on G(o) alpha subunit Galphao and G(i) alpha subunit Galphai. Involved in the dorsal-ventral axis formation of the egg. Acts as a G-protein signaling for glial cell differentiation during embryogenesis; Galphai, Galphao and the G-protein coupled receptor, moody, are required in the surface glia to achieve effective insulation of the nerve cord. May be essential for nurse cell dumping during oogenesis. Required in neuroblast asymmetrical cell division. Plays a role in stress resistance and life span control..
• Protein Sequence: MHHHHPPLPITGASGSTAVGTGAAAAEDASPAANSGPAPISTSTTPSGSNSQQHQRRRKKRANYNYNGIRTVEVRRGYNGFGFTISGQQPCRLSCIISSSPAEQAGLRSGDFLISVNGLNVSKLPHETVVQLIGNSFGSIRMQIAENYYSDSSDEENAHATLRGQLLAASLRHKPRFLHHKAKLHRLRNSPQKKLNPPEAVEPHKSKSSPDHPTLKPVLEDPPLTANLSKAADVANVSAMVRAVGSAALECRVIVGYLGTIEMPKQISHSSKLQTVRSCIRKLRQEKRQPTIVLMCITPDSLSLQSSSGGVLATYSSARLNFVSSSSESENRFFGLVTSAVHNTQIEEEYEPSAGSAAAAGHISISHSCHVFVIDTKLIEHAQHLQRAHEFRLQCTRDPISNLCLEFPNNSEYVVNLVRSMYTMRILPPASRSHQADYEAGAGAAAAGGAVAAAHSPQPSNHSEISTTTSNSDSGIGFNNDCTNISDRILVVDFLAAGAGAAAAAHAGPPTYPAPARPLGIVGIPDNRLTVRAMPDHSALLRSPPASSSLRRPNLLASFNLIQSPATNLTSTRSCDDVLNLFVDDSPRTLAAVASMDDISLHSAAPSLDEGHTFAHPACVPRKMRRSLALETPTTPHKLSAQVFGQPGSRHSLGFEAIDSVQSSVSGACMDQTMDTWASLQNLHKSHKDRTSMSASSSSHCLLEATNSEPDLGNRALPANASPFRRAWGQSSFRTPRSDKVAKEQQQLGQSSPVRRTASMNASDNDMYIKTLMLDSDLKSSRSQHQLSLLQVPKVLTTPAPPSAITASVAAEGAAQDHGCPSSWAGSFERMLQDAAGMQTFSEFLKKEFSAENIYFWTACERYRLLESEADRVAQAREIFAKHLANNSSDPVNVDSQARSLTEEKLADAAPDIFAPAQKQIFSLMKFDSYQRFIRSDLYKSCVEAEQKNQPLPYSGLDLDELLKTNFHLGAFSKLKKSASNAEDRRRKSLLPWHRKTRSKSRDRTEIMADMQHALMPAPPVPQNAPLTSASLKLVCGQNSLSDLHSSRSSLSSFDAGTATGGQGASTESVYSLCRVILTDGATTIVQTRPGETVGELVERLLEKRNLVYPYYDIVFQGSTKSIDVQQPSQILAGKEVVIERRVAFKLDLPDPKVISVKSKPKKQLHEVIRPILSKYNYKMEQVQVIMRDTQVPIDLNQPVTMADGQRLRIVMVNSDFQVGGGSSMPPKQSKPMKPLPQGHLDELTNKVFNELLASKADAAASEKSRPVDLCSMKSNEAPSETSSLFERMRRQQRDGGNIPASKLPKLKKKSTSSSQQSEEAATTQAVADPKKPIIAKLKAGVKLQVTERVAEHQDELLEGLKRAQLARLEDQRGTEINFDLPDFLKNKENLSAAVSKLRKVRASLSPVSKVPATPTEIPQPAPRLSITRSQQPVSPMKVDQEPETDLPAATQDQTEFAKAPPPLPPKPKVLPIKPSNWGVAQPTGNYCNKYSPSKQVPTSPKEASKPGTFASKIPLDLGRKSLEEAGSRCAYLDEPSSSFV

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
150	Phosphorylation	QIAENYYSDSSDEEN HHHHHHCCCCCCCHH	22.21	22817900
170	Phosphorylation	RGQLLAASLRHKPRF HHHHHHHHHHCCCCH	21.96	21082442
209	Phosphorylation	EPHKSKSSPDHPTLK CCCCCCCCCCCCCCH	37.78	22817900
574	Phosphorylation	TNLTSTRSCDDVLNL CCCCCCCCHHHHHHH	23.22	22817900
595	Phosphorylation	RTLAAVASMDDISLH HHHHHHHCCCCCEEC	19.02	22817900
600	Phosphorylation	VASMDDISLHSAAPS HHCCCCCEECCCCCC	27.33	22817900
649	Phosphorylation	QVFGQPGSRHSLGFE EHHCCCCCCCCCCHH	33.24	22817900
722	Phosphorylation	RALPANASPFRRAWG CCCCCCCCCHHHHHC	25.12	22817900
731	Phosphorylation	FRRAWGQSSFRTPRS HHHHHCCCCCCCCCH	27.75	22817900
732	Phosphorylation	RRAWGQSSFRTPRSD HHHHCCCCCCCCCHH	15.74	27626673
751	Phosphorylation	EQQQLGQSSPVRRTA HHHHHCCCCCCHHHH	34.51	29892262
752	Phosphorylation	QQQLGQSSPVRRTAS HHHHCCCCCCHHHHC	21.37	25749252
763	Phosphorylation	RTASMNASDNDMYIK HHHCCCCCCCCEEEE	31.76	25749252
783	Phosphorylation	SDLKSSRSQHQLSLL CCCCCCCCHHHHHHH	33.68	22817900
788	Phosphorylation	SRSQHQLSLLQVPKV CCCHHHHHHHCCCCE	22.06	21082442
989	Phosphorylation	AEDRRRKSLLPWHRK HHHHHHHHHCHHHHH	33.07	22817900
1272	Phosphorylation	SRPVDLCSMKSNEAP CCCCCHHCCCCCCCC	36.22	25749252
1275	Phosphorylation	VDLCSMKSNEAPSET CCHHCCCCCCCCHHH	31.12	19429919
1280	Phosphorylation	MKSNEAPSETSSLFE CCCCCCCHHHHHHHH	61.63	19429919
1282	Phosphorylation	SNEAPSETSSLFERM CCCCCHHHHHHHHHH	28.14	19429919
1283	Phosphorylation	NEAPSETSSLFERMR CCCCHHHHHHHHHHH	22.46	19429919
1284	Phosphorylation	EAPSETSSLFERMRR CCCHHHHHHHHHHHH	44.49	19429919
1404	Phosphorylation	KLRKVRASLSPVSKV HHHHHHHHCCCCCCC	20.86	19429919
1406	Phosphorylation	RKVRASLSPVSKVPA HHHHHHCCCCCCCCC	22.29	19429919
1414	Phosphorylation	PVSKVPATPTEIPQP CCCCCCCCCCCCCCC	25.36	21082442
1492	Phosphorylation	GNYCNKYSPSKQVPT CCCCCCCCCCCCCCC	25.06	21082442
1494	Phosphorylation	YCNKYSPSKQVPTSP CCCCCCCCCCCCCCC	29.76	21082442
1500	Phosphorylation	PSKQVPTSPKEASKP CCCCCCCCCCCCCCC	28.09	22817900
1522	Phosphorylation	PLDLGRKSLEEAGSR CCCCCCHHHHHHHHC	39.39	19429919

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RGS_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RGS_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RGS_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HMX_DROME	Hmx	physical	14605208
UBE2S_DROME	CG8188	physical	18430931
GNAI_DROME	Galphai	physical	15937221

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.