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Regulator of G-protein signaling 14 (RGS14)

 RGS14_HUMAN             Reviewed;         566 AA.
O43566; O43565; Q506M1; Q6ZWA4; Q8TD62;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 4.
22-APR-2020, entry version 187.
RecName: Full=Regulator of G-protein signaling 14;
Short=RGS14;
Name=RGS14;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=16819986; DOI=10.1111/j.1460-9568.2006.04838.x;
Lopez-Aranda M.F., Acevedo M.J., Carballo F.J., Gutierrez A., Khan Z.U.;
"Localization of the GoLoco motif carrier regulator of G-protein signalling
12 and 14 proteins in monkey and rat brain.";
Eur. J. Neurosci. 23:2971-2982(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Chatterjee T.K., Fisher R.A.;
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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] (ISOFORM 4).
TISSUE=Caudate nucleus;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
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).
[7]
FUNCTION, ASSOCIATION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
PubMed=15917656; DOI=10.4161/cc.4.7.1787;
Martin-McCaffrey L., Willard F.S., Pajak A., Dagnino L., Siderovski D.P.,
D'Souza S.J.;
"RGS14 is a microtubule-associated protein.";
Cell Cycle 4:953-960(2005).
[8]
FUNCTION.
PubMed=17635935; DOI=10.1083/jcb.200604114;
Cho H., Kehrl J.H.;
"Localization of Gi alpha proteins in the centrosomes and at the midbody:
implication for their role in cell division.";
J. Cell Biol. 178:245-255(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-42 AND SER-45, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 497-532.
PubMed=17603074; DOI=10.1016/j.jmb.2007.05.096;
Sammond D.W., Eletr Z.M., Purbeck C., Kimple R.J., Siderovski D.P.,
Kuhlman B.;
"Structure-based protocol for identifying mutations that enhance protein-
protein binding affinities.";
J. Mol. Biol. 371:1392-1404(2007).
[11]
STRUCTURE BY NMR OF 56-207, AND INTERACTION WITH GNAI1.
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).
[12]
X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 497-532 IN COMPLEX WITH GNAI1 AND
GDP.
PubMed=21115486; DOI=10.1074/jbc.m110.190496;
Bosch D.E., Kimple A.J., Sammond D.W., Muller R.E., Miley M.J., Machius M.,
Kuhlman B., Willard F.S., Siderovski D.P.;
"Structural determinants of affinity enhancement between GoLoco motifs and
G-protein alpha subunit mutants.";
J. Biol. Chem. 286:3351-3358(2011).
-!- 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. Besides, modulates signal transduction via G protein alpha
subunits by functioning as a GDP-dissociation inhibitor (GDI). Has GDI
activity on G(i) alpha subunits GNAI1 and GNAI3, but not on GNAI2 and
G(o) alpha subunit GNAO1. Has GAP activity on GNAI0, GNAI2 and GNAI3.
May act as a scaffold integrating G protein and Ras/Raf MAPkinase
signaling pathways. Inhibits platelet-derived growth factor (PDGF)-
stimulated ERK1/ERK2 phosphorylation; a process depending on its
interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1.
Acts as a positive modulator of microtubule polymerisation and spindle
organization through a G(i)-alpha-dependent mechanism. Plays a role in
cell division. Required for the nerve growth factor (NGF)-mediated
neurite outgrowth. Involved in stress resistance. May be involved in
visual memory processing capacity and hippocampal-based learning and
memory. {ECO:0000269|PubMed:15917656, ECO:0000269|PubMed:17635935}.
-!- SUBUNIT: Interacts with GNAO1, GNAI2 and GNAI3 (By similarity).
Interacts with GNAI1 (PubMed:18434541, PubMed:21115486). Interacts (via
RGS and GoLoco domains) with GNAI1; the interaction occurs in the
centrosomes. Interaction with GNAI1 or GNAI3 (via active GTP- or
inactive GDP-bound forms) prevents association of RGS14 with
centrosomes or nuclear localization (By similarity). Interacts with
RABGEF1; the interactions is GTP-dependent. Interacts with RAP2A; the
interactions is GTP-dependent and does not alter its function on G(i)
alpha subunits either as GAP or as GDI (By similarity). Associates with
microtubules (PubMed:15917656). Found in a complex with at least BRAF,
HRAS, MAP2K1, MAPK3 and RGS14. Interacts with RIC8A (via C-terminus).
Interacts (via RBD 1 domain) with HRAS (active GTP-bound form
preferentially). Interacts (via RBD domains) with BRAF (via N-
terminus); the interaction mediates the formation of a ternary complex
with RAF1. Interacts (via RBD domains) with RAF1 (via N-terminus); the
interaction mediates the formation of a ternary complex with BRAF.
Interacts with KRAS (active GTP-bound form preferentially), MRAS
(active GTP-bound form preferentially), NRAS (active GTP-bound form
preferentially) and RRAS (active GTP-bound form preferentially).
{ECO:0000250|UniProtKB:O08773, ECO:0000250|UniProtKB:P97492,
ECO:0000269|PubMed:15917656, ECO:0000269|PubMed:18434541,
ECO:0000269|PubMed:21115486}.
-!- INTERACTION:
O43566; P08754: GNAI3; NbExp=4; IntAct=EBI-750603, EBI-357563;
O43566; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-750603, EBI-717399;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, PML body
{ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:15917656}. Membrane
{ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm,
cytoskeleton, spindle {ECO:0000269|PubMed:15917656}. Cytoplasm,
cytoskeleton, spindle pole {ECO:0000250}. Cell projection, dendrite
{ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell
junction, synapse, postsynaptic density {ECO:0000250}. Note=Associates
with the perinuclear sheaths of microtubules (MTs) surrounding the
pronuclei, prior to segregating to the anastral mitotic apparatus and
subsequently the barrel-shaped cytoplasmic bridge between the nascent
nuclei of the emerging 2-cell embryo. Localizes to a perinuclear
compartment near the microtubule-organizing center (MTOC). Expressed in
the nucleus during interphase and segregates to the centrosomes and
astral MTs during mitosis. Relocalizes to the nucleus in PML nuclear
bodies in response to heat stress. Colocalizes with RIC8A in CA2
hippocampal neurons. Localizes to spindle poles during metaphase.
Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner.
Recruited from the cytosol to the plasma membrane by the inactive GDP-
bound forms of G(i) alpha subunits GNAI1 and GNAI3. Recruited from the
cytosol to membranes by the active GTP-bound form of HRAS. Colocalizes
with G(i) alpha subunit GNAI1 and RIC8A at the plasma membrane.
Colocalizes with BRAF and RAF1 in both the cytoplasm and membranes (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O43566-7; Sequence=Displayed;
Name=2;
IsoId=O43566-4; Sequence=VSP_027577, VSP_027578, VSP_027579;
Name=3;
IsoId=O43566-5; Sequence=VSP_027577, VSP_037959;
Name=4;
IsoId=O43566-6; Sequence=VSP_029426, VSP_037959;
-!- DOMAIN: The RGS domain is necessary for GTPase-activating protein (GAP)
activity for G subunits and localization to the nucleus and
centrosomes. {ECO:0000250}.
-!- DOMAIN: The GoLoco domain is necessary for GDP-dissociation inhibitor
(GDI) activity, translocation out of the nucleus and interaction with
G(i) alpha subunits GNAI1, GNAI2 and GNAI3. {ECO:0000250}.
-!- DOMAIN: The RBD domains are necessary for localization to the nucleus
and centrosomes. {ECO:0000250}.
-!- PTM: Phosphorylated by PKC. Phosphorylation is increased in presence of
forskolin and may enhance the GDI activity on G(i) alpha subunit GNAI1
(By similarity). {ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=AAB92614.1; Type=Frameshift; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Protein Spotlight; Note=A balanced mind - Issue 132
of October 2011;
URL="https://web.expasy.org/spotlight/back_issues/132";
---------------------------------------------------------------------------
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EMBL; AY987041; AAY26402.1; -; mRNA.
EMBL; AF037194; AAB92613.1; -; mRNA.
EMBL; AF037195; AAB92614.1; ALT_FRAME; mRNA.
EMBL; AF493936; AAM12650.1; -; mRNA.
EMBL; AK123382; BAC85600.1; -; mRNA.
EMBL; AC146507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014094; AAH14094.1; -; mRNA.
CCDS; CCDS43405.1; -. [O43566-7]
RefSeq; NP_006471.2; NM_006480.4. [O43566-7]
PDB; 2JNU; NMR; -; A=56-207.
PDB; 2OM2; X-ray; 2.20 A; B/D=497-532.
PDB; 2XNS; X-ray; 3.41 A; C/D=497-517.
PDB; 3ONW; X-ray; 2.38 A; C/D=497-532.
PDB; 3QI2; X-ray; 2.80 A; C/D=497-532.
PDBsum; 2JNU; -.
PDBsum; 2OM2; -.
PDBsum; 2XNS; -.
PDBsum; 3ONW; -.
PDBsum; 3QI2; -.
SMR; O43566; -.
BioGrid; 115880; 17.
DIP; DIP-41167N; -.
IntAct; O43566; 11.
MINT; O43566; -.
STRING; 9606.ENSP00000386229; -.
iPTMnet; O43566; -.
PhosphoSitePlus; O43566; -.
BioMuta; RGS14; -.
EPD; O43566; -.
jPOST; O43566; -.
MassIVE; O43566; -.
MaxQB; O43566; -.
PaxDb; O43566; -.
PeptideAtlas; O43566; -.
PRIDE; O43566; -.
ProteomicsDB; 49054; -. [O43566-7]
ProteomicsDB; 49055; -. [O43566-4]
ProteomicsDB; 49056; -. [O43566-5]
ProteomicsDB; 49057; -. [O43566-6]
Antibodypedia; 29266; 307 antibodies.
DNASU; 10636; -.
Ensembl; ENST00000408923; ENSP00000386229; ENSG00000169220. [O43566-7]
GeneID; 10636; -.
KEGG; hsa:10636; -.
UCSC; uc003mgf.4; human. [O43566-7]
CTD; 10636; -.
DisGeNET; 10636; -.
GeneCards; RGS14; -.
HGNC; HGNC:9996; RGS14.
HPA; ENSG00000169220; Tissue enhanced (blood, brain).
MIM; 602513; gene.
neXtProt; NX_O43566; -.
OpenTargets; ENSG00000169220; -.
PharmGKB; PA34366; -.
eggNOG; KOG3589; Eukaryota.
eggNOG; ENOG410YMJD; LUCA.
GeneTree; ENSGT00940000161364; -.
HOGENOM; CLU_024780_1_1_1; -.
InParanoid; O43566; -.
KO; K17706; -.
OMA; RQAWIGE; -.
OrthoDB; 275783at2759; -.
PhylomeDB; O43566; -.
TreeFam; TF328814; -.
Reactome; R-HSA-418594; G alpha (i) signalling events.
SignaLink; O43566; -.
SIGNOR; O43566; -.
ChiTaRS; RGS14; human.
EvolutionaryTrace; O43566; -.
GeneWiki; RGS14; -.
GenomeRNAi; 10636; -.
Pharos; O43566; Tbio.
PRO; PR:O43566; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; O43566; protein.
Bgee; ENSG00000169220; Expressed in caudate nucleus and 188 other tissues.
ExpressionAtlas; O43566; baseline and differential.
Genevisible; O43566; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
GO; GO:0001965; F:G-protein alpha-subunit binding; IEA:Ensembl.
GO; GO:0005092; F:GDP-dissociation inhibitor activity; IDA:UniProtKB.
GO; GO:0032794; F:GTPase activating protein binding; IEA:Ensembl.
GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
GO; GO:0003924; F:GTPase activity; TAS:Reactome.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0030159; F:receptor signaling complex adaptor activity; ISS:UniProtKB.
GO; GO:0051301; P:cell division; IMP:UniProtKB.
GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0007612; P:learning; ISS:UniProtKB.
GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0031914; P:negative regulation of synaptic plasticity; ISS:UniProtKB.
GO; GO:0006913; P:nucleocytoplasmic transport; ISS:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; ISS:UniProtKB.
GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
GO; GO:0008542; P:visual learning; ISS:UniProtKB.
GO; GO:0010070; P:zygote asymmetric cell division; ISS:UniProtKB.
CDD; cd08743; RGS_RGS14; 1.
Gene3D; 1.10.196.10; -; 1.
InterPro; IPR003109; GoLoco_motif.
InterPro; IPR003116; RBD_dom.
InterPro; IPR016137; RGS.
InterPro; IPR030776; RGS14.
InterPro; IPR037881; RGS14_RGS.
InterPro; IPR036305; RGS_sf.
InterPro; IPR024066; RGS_subdom1/3.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR45945:SF2; PTHR45945:SF2; 1.
Pfam; PF02188; GoLoco; 1.
Pfam; PF02196; RBD; 2.
Pfam; PF00615; RGS; 1.
PRINTS; PR01301; RGSPROTEIN.
SMART; SM00390; GoLoco; 1.
SMART; SM00455; RBD; 2.
SMART; SM00315; RGS; 1.
SUPFAM; SSF48097; SSF48097; 1.
SUPFAM; SSF54236; SSF54236; 2.
PROSITE; PS50877; GOLOCO; 1.
PROSITE; PS50898; RBD; 2.
PROSITE; PS50132; RGS; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Cell junction; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
GTPase activation; Membrane; Microtubule; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Signal transduction inhibitor; Synapse.
CHAIN 1..566
/note="Regulator of G-protein signaling 14"
/id="PRO_0000204217"
DOMAIN 67..184
/note="RGS"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
DOMAIN 302..373
/note="RBD 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
DOMAIN 375..445
/note="RBD 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
DOMAIN 498..521
/note="GoLoco"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
REGION 299..425
/note="Necessary for interaction with RABGEF1"
/evidence="ECO:0000250"
MOD_RES 20
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332"
MOD_RES 42
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332"
MOD_RES 45
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332"
MOD_RES 199
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P97492"
MOD_RES 203
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O08773"
MOD_RES 218
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O08773"
MOD_RES 288
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:O08773"
VAR_SEQ 1..153
/note="Missing (in isoform 2 and isoform 3)"
/evidence="ECO:0000303|PubMed:16819986, ECO:0000303|Ref.2,
ECO:0000303|Ref.3"
/id="VSP_027577"
VAR_SEQ 54..273
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_029426"
VAR_SEQ 351
/note="Q -> QK (in isoform 3 and isoform 4)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:16819986, ECO:0000303|Ref.2"
/id="VSP_037959"
VAR_SEQ 352..354
/note="ALV -> VGT (in isoform 2)"
/evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3"
/id="VSP_027578"
VAR_SEQ 355..566
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3"
/id="VSP_027579"
CONFLICT 407
/note="H -> R (in Ref. 4; BAC85600)"
/evidence="ECO:0000305"
CONFLICT 415
/note="V -> A (in Ref. 1; AAY26402)"
/evidence="ECO:0000305"
CONFLICT 502
/note="Missing (in Ref. 2; AAB92614)"
/evidence="ECO:0000305"
HELIX 61..65
/evidence="ECO:0000244|PDB:2JNU"
HELIX 68..73
/evidence="ECO:0000244|PDB:2JNU"
HELIX 75..84
/evidence="ECO:0000244|PDB:2JNU"
STRAND 87..89
/evidence="ECO:0000244|PDB:2JNU"
HELIX 92..105
/evidence="ECO:0000244|PDB:2JNU"
HELIX 111..125
/evidence="ECO:0000244|PDB:2JNU"
HELIX 144..148
/evidence="ECO:0000244|PDB:2JNU"
TURN 152..155
/evidence="ECO:0000244|PDB:2JNU"
HELIX 156..167
/evidence="ECO:0000244|PDB:2JNU"
HELIX 170..174
/evidence="ECO:0000244|PDB:2JNU"
HELIX 180..184
/evidence="ECO:0000244|PDB:2JNU"
HELIX 499..509
/evidence="ECO:0000244|PDB:2OM2"
STRAND 517..519
/evidence="ECO:0000244|PDB:2OM2"
TURN 522..525
/evidence="ECO:0000244|PDB:2OM2"
HELIX 529..531
/evidence="ECO:0000244|PDB:2OM2"
SEQUENCE 566 AA; 61447 MW; 811296228B479C3D CRC64;
MPGKPKHLGV PNGRMVLAVS DGELSSTTGP QGQGEGRGSS LSIHSLPSGP SSPFPTEEQP
VASWALSFER LLQDPLGLAY FTEFLKKEFS AENVTFWKAC ERFQQIPASD TQQLAQEARN
IYQEFLSSQA LSPVNIDRQA WLGEEVLAEP RPDMFRAQQL QIFNLMKFDS YARFVKSPLY
RECLLAEAEG RPLREPGSSR LGSPDATRKK PKLKPGKSLP LGVEELGQLP PVEGPGGRPL
RKSFRRELGG TANAALRRES QGSLNSSASL DLGFLAFVSS KSESHRKSLG STEGESESRP
GKYCCVYLPD GTASLALARP GLTIRDMLAG ICEKRGLSLP DIKVYLVGNE QALVLDQDCT
VLADQEVRLE NRITFELELT ALERVVRISA KPTKRLQEAL QPILEKHGLS PLEVVLHRPG
EKQPLDLGKL VSSVAAQRLV LDTLPGVKIS KARDKSPCRS QGCPPRTQDK ATHPPPASPS
SLVKVPSSAT GKRQTCDIEG LVELLNRVQS SGAHDQRGLL RKEDLVLPEF LQLPAQGPSS
EETPPQTKSA AQPIGGSLNS TTDSAL


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Pathways :
WP1049: G Protein Signaling Pathways
WP2272: Pathogenic Escherichia coli infection
WP1165: G Protein Signaling Pathways
WP73: G Protein Signaling Pathways
WP232: G Protein Signaling Pathways
WP2203: TSLP Signaling Pathway
WP211: BMP signaling pathway
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WP1371: G Protein Signaling Pathways
WP931: G Protein Signaling Pathways
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WP2292: Chemokine signaling pathway
WP35: G Protein Signaling Pathways
WP1150: IL-3 Signaling Pathway
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WP437: EGF/EGFR Signaling Pathway
WP1370: TGF Beta Signaling Pathway
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Related Genes :
[Rgs14] Regulator of G-protein signaling 14 (RGS14)
[Rgs14] Regulator of G-protein signaling 14 (RGS14) (RAP1/RAP2-interacting protein) (RPIP1)
[RGS14] Regulator of G-protein signaling 14 (RGS14)
[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)
[Gnai1 Gnai-1] Guanine nucleotide-binding protein G(i) subunit alpha-1 (Adenylate cyclase-inhibiting G alpha protein)
[GNAI3] Guanine nucleotide-binding protein G(i) subunit alpha (G(i) alpha-3)
[Gnai2 Gnai-2] Guanine nucleotide-binding protein G(i) subunit alpha-2 (Adenylate cyclase-inhibiting G alpha protein)
[GNAI1] Guanine nucleotide-binding protein G(i) subunit alpha-1 (Adenylate cyclase-inhibiting G alpha protein)
[Gnai3 Gnai-3] Guanine nucleotide-binding protein G(i) subunit alpha (G(i) alpha-3)
[Gnai1 Gnai-1] Guanine nucleotide-binding protein G(i) subunit alpha-1 (Adenylate cyclase-inhibiting G alpha protein)
[GNAI1] Guanine nucleotide-binding protein G(i) subunit alpha-1 (Adenylate cyclase-inhibiting G alpha protein)
[Gnai3] Guanine nucleotide-binding protein G(i) subunit alpha (G(i) alpha-3)
[Mapk3 Erk1 Prkm3] Mitogen-activated protein kinase 3 (MAP kinase 3) (MAPK 3) (EC 2.7.11.24) (ERT2) (Extracellular signal-regulated kinase 1) (ERK-1) (Insulin-stimulated MAP2 kinase) (MAP kinase isoform p44) (p44-MAPK) (MNK1) (Microtubule-associated protein 2 kinase) (p44-ERK1)
[RGS1 At3g26090 MPE11.27 MPE11.28] Regulator of G-protein signaling 1 (AtRGS1)
[Map2k1 Mek1 Prkmk1] Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)
[Raf1 Raf] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
[Gnao1 Gna0 Gnao] Guanine nucleotide-binding protein G(o) subunit alpha
[RAF1 RAF] RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (cRaf) (Raf-1)
[RGS4] Regulator of G-protein signaling 4 (RGP4) (RGS4)
[GNAO1] Guanine nucleotide-binding protein G(o) subunit alpha
[Rgs7bp D13Bwg1146e R7bp] Regulator of G-protein signaling 7-binding protein (R7 family-binding protein)
[GNAI2 GNAI2B] Guanine nucleotide-binding protein G(i) subunit alpha-2 (Adenylate cyclase-inhibiting G alpha protein)
[Gnao1 Gna0 Gnao] Guanine nucleotide-binding protein G(o) subunit alpha
[Gnai2 Gnai-2] Guanine nucleotide-binding protein G(i) subunit alpha-2 (Adenylate cyclase-inhibiting G alpha protein)
[GNAI1] Guanine nucleotide-binding protein G(i) subunit alpha-1 (Adenylate cyclase-inhibiting G alpha protein)
[GNAI2] Guanine nucleotide-binding protein G(i) subunit alpha-2 (Adenylate cyclase-inhibiting G alpha protein)
[Rabgef1 Rabex5] Rab5 GDP/GTP exchange factor (Rabex-5)
[KRAS KRAS2 RASK2] GTPase KRas (K-Ras 2) (Ki-Ras) (c-K-ras) (c-Ki-ras) [Cleaved into: GTPase KRas, N-terminally processed]
[GNAI1] Guanine nucleotide-binding protein G(i) subunit alpha-1 (Adenylate cyclase-inhibiting G alpha protein)

Bibliography :
[31754202] The rs1256328 (ALPL) and rs12654812 (RGS14) Polymorphisms are Associated with Susceptibility to Calcium Nephrolithiasis in a Taiwanese population.
[31399537] Correction: 14-3-3γ binds regulator of G protein signaling 14 (RGS14) at distinct sites to inhibit the RGS14:Gα-AlF signaling complex and RGS14 nuclear localization.
[31319167] Modulation of CA2 neuronal activity increases behavioral responses to fear conditioning in female mice.
[30093406] 14-3-3γ binds regulator of G protein signaling 14 (RGS14) at distinct sites to inhibit the RGS14:Gα-AlF signaling complex and RGS14 nuclear localization.
[29911178] RGS14 Restricts Plasticity in Hippocampal CA2 by Limiting Postsynaptic Calcium Signaling.
[29654651] Enhanced longevity and metabolism by brown adipose tissue with disruption of the regulator of G protein signaling 14.
[29577426] Significant association between RGS14 rs12654812 and nephrolithiasis risk among Guangxi population in China.
[29518331] Interactome Analysis Reveals Regulator of G Protein Signaling 14 (RGS14) is a Novel Calcium/Calmodulin (Ca/CaM) and CaM Kinase II (CaMKII) Binding Partner.
[28934222] Endogenous RGS14 is a cytoplasmic-nuclear shuttling protein that localizes to juxtanuclear membranes and chromatin-rich regions of the nucleus.
[28776200] Regulator of G protein signaling 14 (RGS14) is expressed pre- and postsynaptically in neurons of hippocampus, basal ganglia, and amygdala of monkey and human brain.