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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.
13-NOV-2019, entry version 184.
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:
P08754:GNAI3; NbExp=3; IntAct=EBI-750603, EBI-357563;
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;
Note=No experimental confirmation available.;
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;
Note=No experimental confirmation available.;
-!- 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]
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; HPA046847; -.
HPA; HPA061819; -.
MIM; 602513; gene.
neXtProt; NX_O43566; -.
OpenTargets; ENSG00000169220; -.
PharmGKB; PA34366; -.
eggNOG; KOG3589; Eukaryota.
eggNOG; ENOG410YMJD; LUCA.
GeneTree; ENSGT00940000161364; -.
HOGENOM; HOG000049111; -.
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; -.
PRO; PR:O43566; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000169220; Expressed in 189 organ(s), highest expression level in caudate nucleus.
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:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
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; Complete proteome;
Cytoplasm; Cytoskeleton; GTPase activation; Membrane; Microtubule;
Nucleus; Phosphoprotein; Reference proteome; Repeat;
Signal transduction inhibitor; Synapse.
CHAIN 1 566 Regulator of G-protein signaling 14.
/FTId=PRO_0000204217.
DOMAIN 67 184 RGS. {ECO:0000255|PROSITE-
ProRule:PRU00171}.
DOMAIN 302 373 RBD 1. {ECO:0000255|PROSITE-
ProRule:PRU00262}.
DOMAIN 375 445 RBD 2. {ECO:0000255|PROSITE-
ProRule:PRU00262}.
DOMAIN 498 521 GoLoco. {ECO:0000255|PROSITE-
ProRule:PRU00097}.
REGION 299 425 Necessary for interaction with RABGEF1.
{ECO:0000250}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 42 42 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000250|UniProtKB:P97492}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000250|UniProtKB:O08773}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000250|UniProtKB:O08773}.
MOD_RES 288 288 Phosphoserine.
{ECO:0000250|UniProtKB:O08773}.
VAR_SEQ 1 153 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:16819986,
ECO:0000303|Ref.2, ECO:0000303|Ref.3}.
/FTId=VSP_027577.
VAR_SEQ 54 273 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_029426.
VAR_SEQ 351 351 Q -> QK (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:16819986,
ECO:0000303|Ref.2}.
/FTId=VSP_037959.
VAR_SEQ 352 354 ALV -> VGT (in isoform 2).
{ECO:0000303|Ref.2, ECO:0000303|Ref.3}.
/FTId=VSP_027578.
VAR_SEQ 355 566 Missing (in isoform 2).
{ECO:0000303|Ref.2, ECO:0000303|Ref.3}.
/FTId=VSP_027579.
CONFLICT 407 407 H -> R (in Ref. 4; BAC85600).
{ECO:0000305}.
CONFLICT 415 415 V -> A (in Ref. 1; AAY26402).
{ECO:0000305}.
CONFLICT 502 502 Missing (in Ref. 2; AAB92614).
{ECO:0000305}.
HELIX 61 65 {ECO:0000244|PDB:2JNU}.
HELIX 68 73 {ECO:0000244|PDB:2JNU}.
HELIX 75 84 {ECO:0000244|PDB:2JNU}.
STRAND 87 89 {ECO:0000244|PDB:2JNU}.
HELIX 92 105 {ECO:0000244|PDB:2JNU}.
HELIX 111 125 {ECO:0000244|PDB:2JNU}.
HELIX 144 148 {ECO:0000244|PDB:2JNU}.
TURN 152 155 {ECO:0000244|PDB:2JNU}.
HELIX 156 167 {ECO:0000244|PDB:2JNU}.
HELIX 170 174 {ECO:0000244|PDB:2JNU}.
HELIX 180 184 {ECO:0000244|PDB:2JNU}.
HELIX 499 509 {ECO:0000244|PDB:2OM2}.
STRAND 517 519 {ECO:0000244|PDB:2OM2}.
TURN 522 525 {ECO:0000244|PDB:2OM2}.
HELIX 529 531 {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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[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)
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[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)
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