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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.
17-JUN-2020, entry version 164.
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}.
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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; -.
Antibodypedia; 34439; 330 antibodies.
DNASU; 6004; -.
Ensembl; ENST00000367558; ENSP00000356529; ENSG00000143333.
GeneID; 6004; -.
KEGG; hsa:6004; -.
UCSC; uc001gpl.5; human.
CTD; 6004; -.
DisGeNET; 6004; -.
EuPathDB; HostDB:ENSG00000143333.6; -.
GeneCards; RGS16; -.
HGNC; HGNC:9997; RGS16.
HPA; ENSG00000143333; Tissue enhanced (thyroid).
MIM; 602514; gene.
neXtProt; NX_O15492; -.
OpenTargets; ENSG00000143333; -.
PharmGKB; PA34367; -.
eggNOG; KOG3589; Eukaryota.
eggNOG; ENOG410YMJD; LUCA.
GeneTree; ENSGT00940000154304; -.
HOGENOM; CLU_059863_3_0_1; -.
InParanoid; O15492; -.
KO; K16449; -.
OMA; MCRTLAT; -.
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; -.
BioGRID-ORCS; 6004; 1 hit in 787 CRISPR screens.
EvolutionaryTrace; O15492; -.
GeneWiki; RGS16; -.
GenomeRNAi; 6004; -.
Pharos; O15492; Tbio.
PRO; PR:O15492; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; O15492; protein.
Bgee; ENSG00000143333; Expressed in lateral nuclear group of thalamus and 177 other tissues.
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.
IDEAL; IID00607; -.
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; GTPase activation; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Polymorphism; Reference proteome;
Signal transduction inhibitor.
CHAIN 1..202
/note="Regulator of G-protein signaling 16"
/id="PRO_0000204221"
DOMAIN 65..181
/note="RGS"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
MOD_RES 168
/note="Phosphotyrosine; by EGFR"
/evidence="ECO:0000269|PubMed:11602604"
MOD_RES 177
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:11602604"
LIPID 2
/note="S-palmitoyl cysteine"
/evidence="ECO:0000250|UniProtKB:P97428"
LIPID 12
/note="S-palmitoyl cysteine"
/evidence="ECO:0000250|UniProtKB:P97428"
VARIANT 137
/note="H -> R (in dbSNP:rs1144566)"
/evidence="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"
/id="VAR_046528"
MUTAGEN 168
/note="Y->F: 30% decrease in GAP activity."
/evidence="ECO:0000269|PubMed:11602604"
MUTAGEN 177
/note="Y->F: No effect on GAP activity."
/evidence="ECO:0000269|PubMed:11602604"
CONFLICT 42
/note="F -> S (in Ref. 1; AAC16912)"
/evidence="ECO:0000305"
HELIX 53..62
/evidence="ECO:0000244|PDB:2BT2"
HELIX 66..70
/evidence="ECO:0000244|PDB:2BT2"
HELIX 73..85
/evidence="ECO:0000244|PDB:2BT2"
HELIX 89..101
/evidence="ECO:0000244|PDB:2BT2"
HELIX 107..121
/evidence="ECO:0000244|PDB:2BT2"
HELIX 134..143
/evidence="ECO:0000244|PDB:2BT2"
HELIX 144..146
/evidence="ECO:0000244|PDB:2BT2"
TURN 149..152
/evidence="ECO:0000244|PDB:2BT2"
HELIX 153..165
/evidence="ECO:0000244|PDB:2BT2"
HELIX 167..173
/evidence="ECO:0000244|PDB:2BT2"
HELIX 175..186
/evidence="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


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WP2292: Chemokine signaling pathway
WP2032: TSH signaling pathway
WP1049: G Protein Signaling Pathways
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
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP1348: Androgen Receptor Signaling Pathway
WP450: IL-2 Signaling Pathway
WP152: FGF signaling pathway
WP65: Insulin Signaling
WP1772: Apoptosis Modulation and 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)
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[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)
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[Rgs14] Regulator of G-protein signaling 14 (RGS14) (RAP1/RAP2-interacting protein) (RPIP1)
[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)
[RGS4] Regulator of G-protein signaling 4 (RGP4) (RGS4)
[loco CG5248] Regulator of G-protein signaling loco (RGS) (Locomotion defects protein) (Loco)
[RGS1 At3g26090 MPE11.27 MPE11.28] Regulator of G-protein signaling 1 (AtRGS1)
[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)
[Rgs7bp R7bp] Regulator of G-protein signaling 7-binding protein (R7 family-binding protein)
[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)
[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)
[tat] Protein Tat (Transactivating regulatory protein)
[GPA1 At2g26300 T1D16.6] Guanine nucleotide-binding protein alpha-1 subunit (GP-alpha-1)
[Gnai3] Guanine nucleotide-binding protein G(i) subunit alpha (G(i) alpha-3)
[Gnai3 Gnai-3] Guanine nucleotide-binding protein G(i) subunit alpha (G(i) alpha-3)

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