RGS20_HUMAN - dbPTM
RGS20_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGS20_HUMAN
UniProt AC O76081
Protein Name Regulator of G-protein signaling 20
Gene Name RGS20
Organism Homo sapiens (Human).
Sequence Length 388
Subcellular Localization Membrane
Lipid-anchor. Nucleus. Cytoplasm. Shuttles between the cytoplasm/cell membrane and the nucleus. Anchored to the membrane through palmitoylation..
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 selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is inhibited by the phosphorylation and palmitoylation of the G-protein. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins (By similarity)..
Protein Sequence MPQLSQDNQECLQKHFSRPSIWTQFLPLFRAQRYNTDIHQITENEGDLRAVPDIKSFPPAQLPDSPAAPKLFGLLSSPLSSLARFFSHLLRRPPPEAPRRRLDFSPLLPALPAARLSRGHEELPGRLSLLLGAALALPGRPSGGRPLRPPHPVAKPREEDATAGQSSPMPQMGSERMEMRKRQMPAAQDTPGAAPGQPGAGSRGSNACCFCWCCCCSCSCLTVRNQEDQRPTIASHELRADLPTWEESPAPTLEEVNAWAQSFDKLMVTPAGRNAFREFLRTEFSEENMLFWMACEELKKEANKNIIEEKARIIYEDYISILSPKEVSLDSRVREVINRNMVEPSQHIFDDAQLQIYTLMHRDSYPRFMNSAVYKDLLQSLSEKSIEA
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
3 (in isoform 6)Phosphorylation-53.0722199227
13 (in isoform 6)Phosphorylation-49.1621815630
14 (in isoform 6)Phosphorylation-33.4021815630
77PhosphorylationKLFGLLSSPLSSLAR
HHHHHHCCHHHHHHH
29.81-
162PhosphorylationKPREEDATAGQSSPM
CCCHHCCCCCCCCCC
43.58-
166PhosphorylationEDATAGQSSPMPQMG
HCCCCCCCCCCCCCC
35.18-
174PhosphorylationSPMPQMGSERMEMRK
CCCCCCCHHHHHHHH
19.38-
190PhosphorylationQMPAAQDTPGAAPGQ
HCCCHHCCCCCCCCC
16.1328555341
235PhosphorylationDQRPTIASHELRADL
CCCCCEECCHHHCCC
17.4024961811
269PhosphorylationSFDKLMVTPAGRNAF
HHHHHEECHHHHHHH
8.0829523821
315PhosphorylationEEKARIIYEDYISIL
HHHHHHHHHHHHHHH
10.6122817900
318PhosphorylationARIIYEDYISILSPK
HHHHHHHHHHHHCHH
5.6627642862
323PhosphorylationEDYISILSPKEVSLD
HHHHHHHCHHHCCCC
32.0524719451
328PhosphorylationILSPKEVSLDSRVRE
HHCHHHCCCCHHHHH
27.7927470641
358PhosphorylationDAQLQIYTLMHRDSY
HHHHHHHHHHHHCCC
21.16-
384UbiquitinationLLQSLSEKSIEA---
HHHHHHHHHHCC---
54.05-

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

Oops, there are no upstream regulatory protein records of RGS20_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGS20_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 RGS20_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NSF_HUMANNSFphysical
17353931
GLRX3_HUMANGLRX3physical
17353931
PMVK_HUMANPMVKphysical
17353931
SPTC1_HUMANSPTLC1physical
17353931
BOLA1_HUMANBOLA1physical
17353931
S39A7_HUMANSLC39A7physical
17353931
TXLNA_HUMANTXLNAphysical
17353931
RUVB2_HUMANRUVBL2physical
17353931
TR112_HUMANTRMT112physical
17353931
FAF2_HUMANFAF2physical
17353931
SET_HUMANSETphysical
17353931
GNAZ_HUMANGNAZphysical
9748279
GNAO_HUMANGNAO1physical
18407463
CREB5_HUMANCREB5physical
25416956
GLRX3_HUMANGLRX3physical
25416956
MABP1_HUMANMAPKBP1physical
25416956
NECT3_HUMANPVRL3physical
25416956
CRCT1_HUMANCRCT1physical
25416956
KRA42_HUMANKRTAP4-2physical
25416956
PTPM1_HUMANPTPMT1physical
25416956
CTSR1_HUMANCATSPER1physical
25416956
TBC16_HUMANTBC1D16physical
25416956
LCE4A_HUMANLCE4Aphysical
25416956
KLH38_HUMANKLHL38physical
25416956
LCE1B_HUMANLCE1Bphysical
25416956
LCE2A_HUMANLCE2Aphysical
25416956
LCE2D_HUMANLCE2Dphysical
25416956
LCE3E_HUMANLCE3Ephysical
25416956
KRA56_HUMANKRTAP5-6physical
25416956
AASD1_HUMANAARSD1physical
28514442
TTC7B_HUMANTTC7Bphysical
28514442
NARF_HUMANNARFphysical
28514442
CRY1_HUMANCRY1physical
28514442
SELO_HUMANSELOphysical
28514442
GLRX3_HUMANGLRX3physical
28514442
EFR3B_HUMANEFR3Bphysical
28514442
HYCCI_HUMANFAM126Aphysical
28514442
NBN_HUMANNBNphysical
28514442
RAD50_HUMANRAD50physical
28514442
ZN664_HUMANZNF664physical
28514442
RGS19_HUMANRGS19physical
28514442
NARFL_HUMANNARFLphysical
28514442
DPH2_HUMANDPH2physical
28514442
TXLNG_HUMANTXLNGphysical
28514442
EFR3A_HUMANEFR3Aphysical
28514442
MOCOS_HUMANMOCOSphysical
28514442
MIO_HUMANMIOSphysical
28514442
BOLA1_HUMANBOLA1physical
28514442
ZY11B_HUMANZYG11Bphysical
28514442
MRE11_HUMANMRE11Aphysical
28514442
KIF3B_HUMANKIF3Bphysical
28514442
TXLNA_HUMANTXLNAphysical
28514442
TYW1_HUMANTYW1physical
28514442
ZN696_HUMANZNF696physical
28514442
TRM1L_HUMANTRMT1Lphysical
28514442
ZN444_HUMANZNF444physical
28514442
ALR_HUMANGFERphysical
28514442
PLK1_HUMANPLK1physical
28514442
KIF3A_HUMANKIF3Aphysical
28514442
DPH1_HUMANDPH1physical
28514442
NEUL_HUMANNLNphysical
28514442
PRI2_HUMANPRIM2physical
28514442
VPP1_HUMANATP6V0A1physical
28514442
CTU2_HUMANCTU2physical
28514442
TARB1_HUMANTARBP1physical
28514442
CPIN1_HUMANCIAPIN1physical
28514442
DCA10_HUMANDCAF10physical
28514442
CUL2_HUMANCUL2physical
28514442
PGP_HUMANPGPphysical
28514442

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 RGS20_HUMAN

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Related Literatures of Post-Translational Modification

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