GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Regulator of G-protein signaling 16 (RGS16) (A28-RGS14P) (Retinal-specific RGS) (RGS-r) (hRGS-r) (Retinally abundant regulator of G-protein signaling)

 RGS16_HUMAN             Reviewed;         202 AA.
O15492; B2R4M4; Q5VYN9; Q99701;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
16-OCT-2019, entry version 160.
RecName: Full=Regulator of G-protein signaling 16;
Short=RGS16;
AltName: Full=A28-RGS14P;
AltName: Full=Retinal-specific RGS;
Short=RGS-r;
Short=hRGS-r;
AltName: Full=Retinally abundant regulator of G-protein signaling;
Name=RGS16; Synonyms=RGSR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-137.
TISSUE=Brain;
PubMed=9223279; DOI=10.1073/pnas.94.15.7868;
Buckbinder L., Velasco-Miguel S., Chen Y., Xu N., Talbott R.,
Gelbert L., Gao J., Seizinger B.R., Gutkind J.S., Kley N.;
"The p53 tumor suppressor targets a novel regulator of G protein
signaling.";
Proc. Natl. Acad. Sci. U.S.A. 94:7868-7872(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT ARG-137.
TISSUE=Retina;
PubMed=9469939; DOI=10.1016/s0378-1119(97)00593-3;
Snow B.E., Antonio L., Suggs S., Siderovski D.P.;
"Cloning of a retinally abundant regulator of G-protein signaling
(RGS-r/RGS16): genomic structure and chromosomal localization of the
human gene.";
Gene 206:247-253(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-137.
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-137.
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-137.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-137.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-137.
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PHOSPHORYLATION AT TYR-168 BY EGFR, FUNCTION, PHOSPHORYLATION AT
TYR-177, AND MUTAGENESIS OF TYR-168 AND TYR-177.
PubMed=11602604; DOI=10.1074/jbc.m108862200;
Derrien A., Druey K.M.;
"RGS16 function is regulated by epidermal growth factor receptor-
mediated tyrosine phosphorylation.";
J. Biol. Chem. 276:48532-48538(2001).
[10]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-190 IN COMPLEX WITH GNAI1,
FUNCTION, AND INTERACTION WITH GNAI1 AND GNAQ.
PubMed=18434541; DOI=10.1073/pnas.0801508105;
Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J.,
Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A.,
Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P.;
"Structural diversity in the RGS domain and its interaction with
heterotrimeric G protein alpha-subunits.";
Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008).
-!- FUNCTION: Regulates G protein-coupled receptor signaling cascades.
Inhibits signal transduction by increasing the GTPase activity of
G protein alpha subunits, thereby driving them into their inactive
GDP-bound form (PubMed:11602604, PubMed:18434541). Plays an
important role in the phototransduction cascade by regulating the
lifetime and effective concentration of activated transducin
alpha. May regulate extra and intracellular mitogenic signals (By
similarity). {ECO:0000250|UniProtKB:P97428,
ECO:0000269|PubMed:11602604, ECO:0000269|PubMed:18434541}.
-!- SUBUNIT: Interacts with GNAI1 and GNAQ (PubMed:18434541).
Interacts with GNAI2, GNAI3 and GNAO1 (By similarity).
{ECO:0000250|UniProtKB:P97428, ECO:0000269|PubMed:18434541}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P97428};
Lipid-anchor {ECO:0000250|UniProtKB:P97428}.
-!- TISSUE SPECIFICITY: Abundantly expressed in retina with lower
levels of expression in most other tissues.
-!- PTM: Palmitoylated on Cys-2 and/or Cys-12.
{ECO:0000250|UniProtKB:P97428}.
-!- PTM: Phosphorylated. Phosphorylation at Tyr-168 by EGFR enhances
GTPase accelerating (GAP) activity toward GNAI1.
{ECO:0000269|PubMed:11602604}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U70426; AAC16912.1; -; mRNA.
EMBL; U94829; AAC52040.1; -; mRNA.
EMBL; AF009356; AAC39642.1; -; Genomic_DNA.
EMBL; AF493937; AAM12651.1; -; mRNA.
EMBL; BT006638; AAP35284.1; -; mRNA.
EMBL; AK311880; BAG34821.1; -; mRNA.
EMBL; AL353778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91129.1; -; Genomic_DNA.
EMBL; BC006243; AAH06243.1; -; mRNA.
CCDS; CCDS1348.1; -.
RefSeq; NP_002919.3; NM_002928.3.
PDB; 2BT2; X-ray; 1.90 A; A/B/C/D/E=53-190.
PDB; 2IK8; X-ray; 2.71 A; B/D=53-190.
PDBsum; 2BT2; -.
PDBsum; 2IK8; -.
SMR; O15492; -.
BioGrid; 111936; 14.
DIP; DIP-59094N; -.
IntAct; O15492; 3.
STRING; 9606.ENSP00000356529; -.
BindingDB; O15492; -.
ChEMBL; CHEMBL3707469; -.
iPTMnet; O15492; -.
PhosphoSitePlus; O15492; -.
SwissPalm; O15492; -.
BioMuta; RGS16; -.
MassIVE; O15492; -.
PaxDb; O15492; -.
PeptideAtlas; O15492; -.
PRIDE; O15492; -.
ProteomicsDB; 48695; -.
DNASU; 6004; -.
Ensembl; ENST00000367558; ENSP00000356529; ENSG00000143333.
GeneID; 6004; -.
KEGG; hsa:6004; -.
UCSC; uc001gpl.5; human.
CTD; 6004; -.
DisGeNET; 6004; -.
GeneCards; RGS16; -.
HGNC; HGNC:9997; RGS16.
HPA; HPA053250; -.
HPA; HPA055824; -.
MIM; 602514; gene.
neXtProt; NX_O15492; -.
OpenTargets; ENSG00000143333; -.
PharmGKB; PA34367; -.
eggNOG; KOG3589; Eukaryota.
eggNOG; ENOG410YMJD; LUCA.
GeneTree; ENSGT00940000154304; -.
HOGENOM; HOG000233512; -.
InParanoid; O15492; -.
KO; K16449; -.
OMA; VNLDHET; -.
OrthoDB; 1296189at2759; -.
PhylomeDB; O15492; -.
TreeFam; TF315837; -.
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-418597; G alpha (z) signalling events.
SIGNOR; O15492; -.
EvolutionaryTrace; O15492; -.
GeneWiki; RGS16; -.
GenomeRNAi; 6004; -.
Pharos; O15492; -.
PRO; PR:O15492; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143333; Expressed in 178 organ(s), highest expression level in lateral nuclear group of thalamus.
Genevisible; O15492; HS.
GO; GO:0005737; C:cytoplasm; IDA:CACAO.
GO; GO:0031224; C:intrinsic component of membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005516; F:calmodulin binding; TAS:ProtInc.
GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; TAS:Reactome.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0007601; P:visual perception; TAS:ProtInc.
Gene3D; 1.10.196.10; -; 2.
InterPro; IPR016137; RGS.
InterPro; IPR036305; RGS_sf.
InterPro; IPR024066; RGS_subdom1/3.
Pfam; PF00615; RGS; 1.
PRINTS; PR01301; RGSPROTEIN.
SMART; SM00315; RGS; 1.
SUPFAM; SSF48097; SSF48097; 1.
PROSITE; PS50132; RGS; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; GTPase activation; Lipoprotein;
Membrane; Palmitate; Phosphoprotein; Polymorphism; Reference proteome;
Signal transduction inhibitor.
CHAIN 1 202 Regulator of G-protein signaling 16.
/FTId=PRO_0000204221.
DOMAIN 65 181 RGS. {ECO:0000255|PROSITE-
ProRule:PRU00171}.
MOD_RES 168 168 Phosphotyrosine; by EGFR.
{ECO:0000269|PubMed:11602604}.
MOD_RES 177 177 Phosphotyrosine.
{ECO:0000269|PubMed:11602604}.
LIPID 2 2 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P97428}.
LIPID 12 12 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P97428}.
VARIANT 137 137 H -> R (in dbSNP:rs1144566).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9223279,
ECO:0000269|PubMed:9469939,
ECO:0000269|Ref.3, ECO:0000269|Ref.4,
ECO:0000269|Ref.7}.
/FTId=VAR_046528.
MUTAGEN 168 168 Y->F: 30% decrease in GAP activity.
{ECO:0000269|PubMed:11602604}.
MUTAGEN 177 177 Y->F: No effect on GAP activity.
{ECO:0000269|PubMed:11602604}.
CONFLICT 42 42 F -> S (in Ref. 1; AAC16912).
{ECO:0000305}.
HELIX 53 62 {ECO:0000244|PDB:2BT2}.
HELIX 66 70 {ECO:0000244|PDB:2BT2}.
HELIX 73 85 {ECO:0000244|PDB:2BT2}.
HELIX 89 101 {ECO:0000244|PDB:2BT2}.
HELIX 107 121 {ECO:0000244|PDB:2BT2}.
HELIX 134 143 {ECO:0000244|PDB:2BT2}.
HELIX 144 146 {ECO:0000244|PDB:2BT2}.
TURN 149 152 {ECO:0000244|PDB:2BT2}.
HELIX 153 165 {ECO:0000244|PDB:2BT2}.
HELIX 167 173 {ECO:0000244|PDB:2BT2}.
HELIX 175 186 {ECO:0000244|PDB:2BT2}.
SEQUENCE 202 AA; 22749 MW; 19B384E935F3E5D1 CRC64;
MCRTLAAFPT TCLERAKEFK TRLGIFLHKS ELGCDTGSTG KFEWGSKHSK ENRNFSEDVL
GWRESFDLLL SSKNGVAAFH AFLKTEFSEE NLEFWLACEE FKKIRSATKL ASRAHQIFEE
FICSEAPKEV NIDHETHELT RMNLQTATAT CFDAAQGKTR TLMEKDSYPR FLKSPAYRDL
AAQASAASAT LSSCSLDEPS HT


Related products :

Catalog number Product name Quantity
EIAAB34546 A28-RGS14P,Homo sapiens,hRGS-r,Human,Regulator of G-protein signaling 16,Retinally abundant regulator of G-protein signaling,Retinal-specific RGS,RGS16,RGS16,RGSR,RGS-r
EIAAB34545 A28-RGS14P,Mouse,Mus musculus,Regulator of G-protein signaling 16,Retinally abundant regulator of G-protein signaling,Retinal-specific RGS,RGS16,Rgs16,Rgsr,RGS-r
EIAAB34543 Rat,Rattus norvegicus,Regulator of G-protein signaling 16,Retinally abundant regulator of G-protein signaling,Retinal-specific RGS,RGS16,Rgs16,Rgsr,RGS-r
EIAAB34544 Bos taurus,Bovine,Regulator of G-protein signaling 16,Retinally abundant regulator of G-protein signaling,Retinal-specific RGS,RGS16,RGS16,RGS-r
15-288-21321 Regulator of G-protein signaling 16 - RGS16; Retinally abundant regulator of G-protein signaling; RGS-R; A28-RGS14P Polyclonal 0.05 mg
18-003-42464 Regulator of G-protein signaling 16 - RGS16; Retinally abundant regulator of G-protein signaling; RGS-R; A28-RGS14P Polyclonal 0.1 mg Protein A
15-288-21321 Regulator of G-protein signaling 16 - RGS16; Retinally abundant regulator of G-protein signaling; RGS-R; A28-RGS14P Polyclonal 0.1 mg
EIAAB34563 G(z)GAP,Gz-GAP,Gz-selective GTPase-activating protein,Homo sapiens,Human,Regulator of G-protein signaling 20,Regulator of G-protein signaling Z1,Regulator of Gz-selective protein signaling 1,RGS20,RGS
EIAAB34564 Bos taurus,Bovine,Regulator of G-protein signaling 20,Retina-specific regulator of G-protein signaling 1,Ret-RGS1,RGS20,RGS20
29-804 RGS8 is a member of the regulator of G protein signaling (RGS) family and is a protein with a single RGS domain. Regulator of G protein signaling (RGS) proteins are regulatory and structural component 0.1 mg
RGS16 RGS16 Gene regulator of G-protein signaling 16
pro-798 Recombinant Human Regulator of G-Protein Signaling 16 RGS16 10
pro-798 Recombinant Human Regulator of G-Protein Signaling 16 RGS16 1mg
CSB-EL019647RA Rat Regulator of G-protein signaling 16(RGS16) ELISA kit 96T
201-20-4869 RGS16{regulator of G-protein signaling 16}rabbit.pAb 0.2ml
pro-798 Recombinant Human Regulator of G-Protein Signaling 16 RGS16 2
G7072 Regulator of G-protein signaling 16 (RGS16), Rat, ELISA Kit 96T
G7069 Regulator of G-protein signaling 16 (RGS16), Bovine, ELISA Kit 96T
G7071 Regulator of G-protein signaling 16 (RGS16), Mouse, ELISA Kit 96T
CSB-EL019647HU Human Regulator of G-protein signaling 16(RGS16) ELISA kit 96T
CSB-EL019647MO Mouse Regulator of G-protein signaling 16(RGS16) ELISA kit 96T
CSB-EL019647BO Bovine Regulator of G-protein signaling 16(RGS16) ELISA kit 96T
G7070 Regulator of G-protein signaling 16 (RGS16), Human, ELISA Kit 96T
CSB-EL019647RA Rat Regulator of G-protein signaling 16(RGS16) ELISA kit SpeciesRat 96T
CSB-EL019647BO Bovine Regulator of G-protein signaling 16(RGS16) ELISA kit SpeciesBovine 96T
Pathways :
WP2032: TSH signaling pathway
WP1049: G Protein Signaling Pathways
WP2292: Chemokine signaling pathway
WP73: G Protein Signaling Pathways
WP35: G Protein Signaling Pathways
WP931: G Protein Signaling Pathways
WP2272: Pathogenic Escherichia coli infection
WP232: G Protein Signaling Pathways
WP813: G Protein Signaling Pathways
WP2203: TSLP Signaling Pathway
WP211: BMP signaling pathway
WP1165: G Protein Signaling Pathways
WP1689: Porphyrin and chlorophyll metabolism
WP1371: G Protein Signaling Pathways
WP860: EGFR1 Signaling Pathway
WP752: EGFR1 Signaling Pathway
WP978: EGFR1 Signaling Pathway
WP572: EGFR1 Signaling Pathway
WP5: EGFR1 Signaling Pathway
WP1154: p38 MAPK Signaling Pathway
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1309: Toll-like receptor signaling pathway
WP450: IL-2 Signaling Pathway
WP138: Androgen receptor signaling pathway
WP65: Insulin Signaling

Related Genes :
[RGS16 RGSR] Regulator of G-protein signaling 16 (RGS16) (A28-RGS14P) (Retinal-specific RGS) (RGS-r) (hRGS-r) (Retinally abundant regulator of G-protein signaling)
[Rgs16 Rgsr] Regulator of G-protein signaling 16 (RGS16) (A28-RGS14P) (Retinal-specific RGS) (RGS-r) (Retinally abundant regulator of G-protein signaling)
[Rgs16 Rgsr] Regulator of G-protein signaling 16 (RGS16) (Retinal-specific RGS) (RGS-r) (Retinally abundant regulator of G-protein signaling)
[GDE1 MIR16] Glycerophosphodiester phosphodiesterase 1 (EC 3.1.4.-) (EC 3.1.4.44) (Membrane-interacting protein of RGS16) (RGS16-interacting membrane protein)
[Gde1 Mir16] Glycerophosphodiester phosphodiesterase 1 (EC 3.1.4.-) (EC 3.1.4.44) (Membrane-interacting protein of RGS16)
[Gde1 Mir16] Glycerophosphodiester phosphodiesterase 1 (EC 3.1.4.-) (EC 3.1.4.44) (Membrane-interacting protein of RGS16)
[RGS9] Regulator of G-protein signaling 9 (RGS9)
[Rgs14] Regulator of G-protein signaling 14 (RGS14) (RAP1/RAP2-interacting protein) (RPIP1)
[RGS16] Regulator of G-protein signaling 16 (RGS16) (Retinal-specific RGS) (RGS-r) (Retinally abundant regulator of G-protein signaling)
[Rgs14] Regulator of G-protein signaling 14 (RGS14)
[Rgs7bp D13Bwg1146e R7bp] Regulator of G-protein signaling 7-binding protein (R7 family-binding protein)
[Rgs4] Regulator of G-protein signaling 4 (RGP4) (RGS4)
[RGS1 At3g26090 MPE11.27 MPE11.28] Regulator of G-protein signaling 1 (AtRGS1)
[loco CG5248] Regulator of G-protein signaling loco (RGS) (Locomotion defects protein) (Loco)
[RGS4] Regulator of G-protein signaling 4 (RGP4) (RGS4)
[RGS14] Regulator of G-protein signaling 14 (RGS14)
[RGS16] Regulator of G-protein signaling 16 (poRGS16)
[GDE1 MIR16] Glycerophosphodiester phosphodiesterase 1 (EC 3.1.4.-) (EC 3.1.4.44) (Membrane-interacting protein of RGS16)
[Rgs4] Regulator of G-protein signaling 4 (RGS4)
[GNAI3] Guanine nucleotide-binding protein G(i) subunit alpha (G(i) alpha-3)
[rgs-7 F56B6.2] Regulator of G-protein signaling rgs-7 (Protein C2-RGS) (Regulator of G-protein signaling c2)
[Gnai1 Gnai-1] Guanine nucleotide-binding protein G(i) subunit alpha-1 (Adenylate cyclase-inhibiting G alpha protein)
[Rgs7bp R7bp] Regulator of G-protein signaling 7-binding protein (R7 family-binding protein)
[GPSM2 LGN] G-protein-signaling modulator 2 (Mosaic protein LGN)
[GNAI1] Guanine nucleotide-binding protein G(i) subunit alpha-1 (Adenylate cyclase-inhibiting G alpha protein)
[tat] Protein Tat (Transactivating regulatory protein)
[GPA1 At2g26300 T1D16.6] Guanine nucleotide-binding protein alpha-1 subunit (GP-alpha-1)
[tat] Protein Tat (Transactivating regulatory protein)
[RGS9BP R9AP] Regulator of G-protein signaling 9-binding protein (RGS9-anchoring protein)
[Gnai3] Guanine nucleotide-binding protein G(i) subunit alpha (G(i) alpha-3)

Bibliography :