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Database: UniProt
Entry: P97492
LinkDB: P97492
Original site: P97492 
ID   RGS14_MOUSE             Reviewed;         547 AA.
AC   P97492; Q8K2R4; Q9DCD1;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   01-OCT-2014, entry version 124.
DE   RecName: Full=Regulator of G-protein signaling 14;
DE            Short=RGS14;
DE   AltName: Full=RAP1/RAP2-interacting protein;
DE            Short=RPIP1;
GN   Name=Rgs14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RA   Janoueix-Lerosey I., Tavitian A., de Gunzburg J.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-547.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   FUNCTION, INTERACTION WITH GNAO1, RABGEF1 AND RAP2A, SUBCELLULAR
RP   LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=10926822; DOI=10.1042/0264-6021:3500019;
RA   Traver S., Bidot C., Spassky N., Baltauss T., De Tand M.F.,
RA   Thomas J.L., Zalc B., Janoueix-Lerosey I., Gunzburg J.D.;
RT   "RGS14 is a novel Rap effector that preferentially regulates the
RT   GTPase activity of galphao.";
RL   Biochem. J. 350:19-29(2000).
RN   [6]
RP   FUNCTION, INTERACTION WITH GNAI1; GNAI2; RABGEF1 AND RAP2A, AND
RP   MUTAGENESIS OF 92-GLU-ASN-93; ARG-336 AND ARG-519.
RX   PubMed=15112653; DOI=10.1042/BJ20031889;
RA   Traver S., Splingard A., Gaudriault G., De Gunzburg J.;
RT   "The RGS (regulator of G-protein signalling) and GoLoco domains of
RT   RGS14 co-operate to regulate Gi-mediated signalling.";
RL   Biochem. J. 379:627-632(2004).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15525537; DOI=10.1016/j.devcel.2004.10.004;
RA   Martin-McCaffrey L., Willard F.S., Oliveira-dos-Santos A.J.,
RA   Natale D.R., Snow B.E., Kimple R.J., Pajak A., Watson A.J.,
RA   Dagnino L., Penninger J.M., Siderovski D.P., D'Souza S.J.;
RT   "RGS14 is a mitotic spindle protein essential from the first division
RT   of the mammalian zygote.";
RL   Dev. Cell 7:763-769(2004).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15917656;
RA   Martin-McCaffrey L., Willard F.S., Pajak A., Dagnino L.,
RA   Siderovski D.P., D'Souza S.J.;
RT   "RGS14 is a microtubule-associated protein.";
RL   Cell Cycle 4:953-960(2005).
RN   [9]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF 92-GLU-ASN-93; SER-261;
RP   ARG-336; HIS-409; THR-497; 506-LEU-LEU-507 AND GLN-518.
RX   PubMed=15520006; DOI=10.1074/jbc.M413554200;
RA   Cho H., Kim D.U., Kehrl J.H.;
RT   "RGS14 is a centrosomal and nuclear cytoplasmic shuttling protein that
RT   traffics to promyelocytic leukemia nuclear bodies following heat
RT   shock.";
RL   J. Biol. Chem. 280:805-814(2005).
RN   [10]
RP   FUNCTION, AND MUTAGENESIS OF ARG-336 AND HIS-409.
RX   PubMed=16246175; DOI=10.1042/BJ20051086;
RA   Mittal V., Linder M.E.;
RT   "Biochemical characterization of RGS14: RGS14 activity towards G-
RT   protein alpha subunits is independent of its binding to Rap2A.";
RL   Biochem. J. 394:309-315(2006).
RN   [11]
RP   INTERACTION WITH GNAI1, AND MUTAGENESIS OF 92-GLU-ASN-93 AND GLN-518.
RX   PubMed=17635935; DOI=10.1083/jcb.200604114;
RA   Cho H., Kehrl J.H.;
RT   "Localization of Gi alpha proteins in the centrosomes and at the
RT   midbody: implication for their role in cell division.";
RL   J. Cell Biol. 178:245-255(2007).
RN   [12]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=20837545; DOI=10.1073/pnas.1005362107;
RA   Lee S.E., Simons S.B., Heldt S.A., Zhao M., Schroeder J.P.,
RA   Vellano C.P., Cowan D.P., Ramineni S., Yates C.K., Feng Y., Smith Y.,
RA   Sweatt J.D., Weinshenker D., Ressler K.J., Dudek S.M., Hepler J.R.;
RT   "RGS14 is a natural suppressor of both synaptic plasticity in CA2
RT   neurons and hippocampal-based learning and memory.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:16994-16998(2010).
RN   [13]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=21158412; DOI=10.1021/bi101910n;
RA   Vellano C.P., Shu F.J., Ramineni S., Yates C.K., Tall G.G.,
RA   Hepler J.R.;
RT   "Activation of the regulator of G protein signaling 14-Galphai1-GDP
RT   signaling complex is regulated by resistance to inhibitors of
RT   cholinesterase-8A.";
RL   Biochemistry 50:752-762(2011).
RN   [14]
RP   STRUCTURE BY NMR OF 366-456.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the RAS-binding domain of mouse RGS14.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Acts as a regulator of G protein signaling (RGS).
CC       Modulates G protein alpha subunits nucleotide exchange and
CC       hydrolysis activities by functioning either as a GTPase-activating
CC       protein (GAP), thereby driving G protein alpha subunits into their
CC       inactive GDP-bound form, or as a GDP-dissociation inhibitor (GDI).
CC       Confers GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but
CC       not G(o) alpha subunit GNAO1 and G(i) alpha subunit GNAI2. Confers
CC       GAP activity on G(o) alpha subunit GNAI0 and G(i) alpha subunits
CC       GNAI2 and GNAI3. May act as a scaffold integrating G protein and
CC       Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived
CC       growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a
CC       process depending on its interaction with HRAS and that is
CC       reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator
CC       of microtubule polymerisation and spindle organization through a
CC       G(i)-alpha-dependent mechanism. Plays a role in cell division;
CC       required for completion of the first mitotic division of the
CC       embryo. Involved in visual memory processing capacity; when
CC       overexpressed in the V2 secondary visual cortex area. Involved in
CC       hippocampal-based learning and memory; acts as a suppressor of
CC       synaptic plasticity in CA2 neurons. Required for the nerve growth
CC       factor (NGF)-mediated neurite outgrowth. Involved in stress
CC       resistance. {ECO:0000269|PubMed:10926822,
CC       ECO:0000269|PubMed:15112653, ECO:0000269|PubMed:15525537,
CC       ECO:0000269|PubMed:15917656, ECO:0000269|PubMed:16246175,
CC       ECO:0000269|PubMed:20837545}.
CC   -!- SUBUNIT: Found in a complex with at least BRAF, HRAS, MAP2K1,
CC       MAPK3 and RGS14. Interacts with RIC8A (via C-terminus). Interacts
CC       (via RBD 1 domain) with HRAS (active GTP-bound form
CC       preferentially). Interacts (via RBD domains) with BRAF (via N-
CC       terminus); the interaction mediates the formation of a ternary
CC       complex with RAF1. Interacts (via RBD domains) with RAF1 (via N-
CC       terminus); the interaction mediates the formation of a ternary
CC       complex with BRAF. Interacts with KRAS (active GTP-bound form
CC       preferentially), MRAS (active GTP-bound form preferentially), NRAS
CC       (active GTP-bound form preferentially) and RRAS (active GTP-bound
CC       form preferentially). Interacts with GNAI1 (via active GTP- or
CC       inactive GDP-bound forms); the interaction prevents association of
CC       RGS14 with centrosomes or nuclear localization. Interacts with
CC       GNAI2. Interacts with GNAI3 (via active GTP- or inactive GDP-bound
CC       forms); the interaction prevents association of RGS14 with
CC       centrosomes or nuclear localization. Associates with microtubules
CC       (By similarity). Interacts with GNAO1 and GNAI2. Interacts (via
CC       RGS and GoLoco domains) GNAI1; the interaction occurs in the
CC       centrosomes. Interacts with RABGEF1; the interactions is GTP-
CC       dependent. Interacts with RAP2A; the interactions is GTP-dependent
CC       and does not alter its function on G(i) alpha subunits either as
CC       GAP or as GDI. {ECO:0000250, ECO:0000269|PubMed:10926822,
CC       ECO:0000269|PubMed:15112653, ECO:0000269|PubMed:17635935}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Cytoplasm.
CC       Membrane. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton,
CC       spindle. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center,
CC       centrosome. Cell projection, dendrite. Cell projection, dendritic
CC       spine. Cell junction, synapse, postsynaptic cell membrane,
CC       postsynaptic density. Note=Localizes with spindle poles during
CC       metaphase. Shuttles between the nucleus and cytoplasm in a CRM1-
CC       dependent manner. Recruited from the cytosol to the plasma
CC       membrane by the inactive GDP-bound forms of G(i) alpha subunits
CC       GNAI1 and GNAI3. Recruited from the cytosol to membranes by the
CC       active GTP-bound form of HRAS. Colocalizes with G(i) alpha subunit
CC       GNAI1 and RIC8A at the plasma membrane. Colocalizes with BRAF and
CC       RAF1 in both the cytoplasm and membranes (By similarity).
CC       Associates with the perinuclear sheaths of microtubules (MTs)
CC       surrounding the pronuclei, prior to segregating to the anastral
CC       mitotic apparatus and subsequently the barrel- shaped cytoplasmic
CC       bridge between the nascent nuclei of the emerging 2-cell embryo.
CC       Localizes to a perinuclear compartment near the microtubule-
CC       organizing center (MTOC). Expressed in the nucleus during
CC       interphase and segregates to the centrosomes and astral MTs during
CC       mitosis. Shuttles between the nucleus and cytoplasm in a CRM1-
CC       dependent manner. Relocalizes to the nucleus in PML nuclear bodies
CC       in respons to heat stress. Colocalizes with RIC8A in CA2
CC       hippocampal neurons. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in pyramidal neurons of the CA1, CA2
CC       and fasciola cinerea (FC) subregions of the hippocampus and in the
CC       olfactory cortex (at protein level). Expressed in brain, spleen,
CC       heart, liver, lung, kidney, skin and thymus (at protein level).
CC       Expressed in granular layer of the cerebellum, forbrain, striatum,
CC       layer V of the cortex, olfactory cortex, tubercules, subthalamic
CC       and hippocampus, particularly in the CA2 region, to a lesser
CC       extent in the CA1 region and the external layer of the dentate
CC       gyrus. Expressed in neurons. {ECO:0000269|PubMed:10926822,
CC       ECO:0000269|PubMed:15525537, ECO:0000269|PubMed:20837545,
CC       ECO:0000269|PubMed:21158412}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in germinal vesicle oocytes, not in
CC       metaphase II oocytes. Expressed in embryo from 8.5 through 16.5
CC       dpc (at protein level). Expressed in the zygote through to the
CC       blastocyst stage. Expressed in area lateral to the rhombencephalic
CC       floor plate at 12 dpc. Expressed in the anterior region of the
CC       brain, including the telencephalic olfactive nuclei and the
CC       hippocampus anlage at 17 dpc. {ECO:0000269|PubMed:10926822,
CC       ECO:0000269|PubMed:15525537}.
CC   -!- DOMAIN: The RGS domain is necessary for GTPase-activating protein
CC       (GAP) activity for G subunits and localization to the nucleus and
CC       centrosomes. {ECO:0000250}.
CC   -!- DOMAIN: The GoLoco domain is necessary for GDP-dissociation
CC       inhibitor (GDI) activity, translocation out of the nucleus and
CC       interaction with G(i) alpha subunits GNAI1, GNAI2 and GNAI3.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The RBD domains are necessary for localization to the
CC       nucleus and centrosomes. {ECO:0000250}.
CC   -!- PTM: Phosphorylated by PKC. Phosphorylation is increased in
CC       presence of forskolin and may enhance the GDI activity on G(i)
CC       alpha subunit GNAI1 (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice show an
CC       enhancement of postsynaptic long-term potentiation (LTP) responses
CC       in the CA2 neurons of the hippocampus that is correlated with an
CC       increase of spatial learning and object recognition memory (OMR).
CC       {ECO:0000269|PubMed:15525537, ECO:0000269|PubMed:20837545}.
CC   -!- SIMILARITY: Contains 1 GoLoco domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00097}.
CC   -!- SIMILARITY: Contains 2 RBD (Ras-binding) domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00262}.
CC   -!- SIMILARITY: Contains 1 RGS domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00171}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=A balanced mind - Issue
CC       132 of October 2011;
CC       URL="http://web.expasy.org/spotlight/back_issues/132";
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DR   EMBL; U85055; AAB41893.1; -; mRNA.
DR   EMBL; CT009762; CAX16109.1; -; Genomic_DNA.
DR   EMBL; BC030321; AAH30321.1; -; mRNA.
DR   EMBL; AK002891; BAB22436.1; -; mRNA.
DR   CCDS; CCDS36674.1; -.
DR   RefSeq; NP_058038.2; NM_016758.3.
DR   UniGene; Mm.1426; -.
DR   PDB; 1WFY; NMR; -; A=366-456.
DR   PDBsum; 1WFY; -.
DR   ProteinModelPortal; P97492; -.
DR   SMR; P97492; 56-189, 365-459, 499-534.
DR   BioGrid; 206175; 1.
DR   IntAct; P97492; 2.
DR   MINT; MINT-4132298; -.
DR   STRING; 10090.ENSMUSP00000068731; -.
DR   PhosphoSite; P97492; -.
DR   MaxQB; P97492; -.
DR   PaxDb; P97492; -.
DR   PRIDE; P97492; -.
DR   Ensembl; ENSMUST00000063771; ENSMUSP00000068731; ENSMUSG00000052087.
DR   GeneID; 51791; -.
DR   KEGG; mmu:51791; -.
DR   UCSC; uc007qqq.2; mouse.
DR   CTD; 10636; -.
DR   MGI; MGI:1859709; Rgs14.
DR   eggNOG; NOG253607; -.
DR   GeneTree; ENSGT00700000104412; -.
DR   HOGENOM; HOG000049111; -.
DR   HOVERGEN; HBG061568; -.
DR   InParanoid; Q8K2R4; -.
DR   KO; K17706; -.
DR   OMA; PPRTQDK; -.
DR   OrthoDB; EOG7XDBF0; -.
DR   TreeFam; TF328814; -.
DR   EvolutionaryTrace; P97492; -.
DR   NextBio; 308020; -.
DR   PRO; PR:P97492; -.
DR   ArrayExpress; P97492; -.
DR   Bgee; P97492; -.
DR   CleanEx; MM_RGS14; -.
DR   Genevestigator; P97492; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR   GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR   GO; GO:0005092; F:GDP-dissociation inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0032794; F:GTPase activating protein binding; IPI:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0030159; F:receptor signaling complex scaffold activity; ISS:UniProtKB.
DR   GO; GO:0005057; F:receptor signaling protein activity; IDA:UniProtKB.
DR   GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR   GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR   GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:GOC.
DR   GO; GO:0007612; P:learning; IMP:UniProtKB.
DR   GO; GO:0007616; P:long-term memory; IMP:UniProtKB.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IDA:UniProtKB.
DR   GO; GO:0007067; P:mitotic nuclear division; IMP:MGI.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:UniProtKB.
DR   GO; GO:0031914; P:negative regulation of synaptic plasticity; IMP:UniProtKB.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; IDA:UniProtKB.
DR   GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IDA:GOC.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
DR   GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; IDA:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR   GO; GO:0038032; P:termination of G-protein coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0008542; P:visual learning; ISS:UniProtKB.
DR   GO; GO:0010070; P:zygote asymmetric cell division; IMP:UniProtKB.
DR   Gene3D; 1.10.196.10; -; 1.
DR   InterPro; IPR003109; GoLoco_motif.
DR   InterPro; IPR003116; Raf-like_ras-bd.
DR   InterPro; IPR024066; Regulat_G_prot_signal_dom1.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   InterPro; IPR000342; RGS_dom.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   Pfam; PF02188; GoLoco; 1.
DR   Pfam; PF02196; RBD; 2.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00390; GoLoco; 1.
DR   SMART; SM00455; RBD; 2.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; SSF48097; 1.
DR   SUPFAM; SSF54236; SSF54236; 2.
DR   PROSITE; PS50877; GOLOCO; 1.
DR   PROSITE; PS50898; RBD; 2.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cell junction; Cell membrane;
KW   Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Developmental protein; GTPase activation; Membrane; Microtubule;
KW   Nucleus; Phosphoprotein; Postsynaptic cell membrane;
KW   Reference proteome; Repeat; Signal transduction inhibitor; Synapse.
FT   CHAIN         1    547       Regulator of G-protein signaling 14.
FT                                /FTId=PRO_0000204218.
FT   DOMAIN       67    184       RGS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00171}.
FT   DOMAIN      303    374       RBD 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00262}.
FT   DOMAIN      376    446       RBD 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00262}.
FT   DOMAIN      500    522       GoLoco. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00097}.
FT   REGION      300    427       Necessary for interaction with RABGEF1.
FT   MOD_RES      20     20       Phosphoserine. {ECO:0000250}.
FT   MOD_RES      42     42       Phosphoserine. {ECO:0000250}.
FT   MOD_RES      45     45       Phosphoserine. {ECO:0000250}.
FT   MUTAGEN      92     93       EN->AA: Inhibits GAP activity. Does not
FT                                inhibit interaction with GNAI1 in the
FT                                centrosomes. Reduces the down-regulation
FT                                of G(i)-dependent signaling. Does not
FT                                affect subcellular location and does not
FT                                promote gene transcription activation.
FT                                Inhibits strongly the down-regulation of
FT                                G(i)-dependent signaling; when associated
FT                                with F-519. Inhibits the interaction with
FT                                GNAI1 in the centrosomes; when associated
FT                                with A-518.
FT   MUTAGEN     261    261       S->A: Does not affect subcellular
FT                                location; when associated with A-497.
FT                                {ECO:0000269|PubMed:15520006}.
FT   MUTAGEN     336    336       R->L: Reduces interaction with RABGEF1
FT                                and RAP2A. Strongly reduces interaction
FT                                with RAP2A; when associated with L-409.
FT                                {ECO:0000269|PubMed:15112653,
FT                                ECO:0000269|PubMed:15520006,
FT                                ECO:0000269|PubMed:16246175}.
FT   MUTAGEN     409    409       H->L: Does not reduce interaction with
FT                                RAP2A. Strongly reduces interaction with
FT                                RAP2A; when associated with L-336.
FT                                {ECO:0000269|PubMed:15520006,
FT                                ECO:0000269|PubMed:16246175}.
FT   MUTAGEN     497    497       T->A: Does not affect subcellular
FT                                location; when associated with A-261.
FT                                {ECO:0000269|PubMed:15520006}.
FT   MUTAGEN     506    507       LL->AA: Strongly expressed in the
FT                                nucleus, mainly associated with PML
FT                                nuclear bodies but not with centrosomes.
FT                                Promotes gene transcription activation.
FT   MUTAGEN     518    518       Q->A: Inhibits GDI activity. Does not
FT                                inhibit interaction with GNAI1 in the
FT                                centrosomes, does not affect subcellular
FT                                location and does not promote gene
FT                                transcription activation. Inhibits
FT                                interaction with GNAI1 in the
FT                                centrosomes; when associated with A-92-
FT                                93-A. {ECO:0000269|PubMed:15520006,
FT                                ECO:0000269|PubMed:17635935}.
FT   MUTAGEN     519    519       R->F: Reduces interaction with GNAI1 and
FT                                GNAI2. Inhibits strongly the down-
FT                                regulation of G(i)-dependent signaling;
FT                                when associated with A-92-93-A.
FT                                {ECO:0000269|PubMed:15112653}.
FT   CONFLICT    209    209       Missing (in Ref. 4; BAB22436).
FT                                {ECO:0000305}.
FT   CONFLICT    431    431       N -> T (in Ref. 1; AAB41893).
FT                                {ECO:0000305}.
FT   STRAND      375    392
FT   STRAND      394    397
FT   TURN        398    402
FT   HELIX       403    406
FT   TURN        407    410
FT   TURN        413    415
FT   HELIX       433    435
FT   STRAND      436    439
FT   STRAND      441    443
FT   STRAND      451    454
SQ   SEQUENCE   547 AA;  59847 MW;  51BDE89E58F1E2C3 CRC64;
     MPGKPKHLGV PNGRMVLAVS DGELTSTAGS QAQGEGRGSS LSIHSLPSGP SSPFSTEEQP
     VASWAQSFER LLQDPRGLAY FTEFLKKEFS AENVTFWKAC ERFQQIPASD TKQLAQEAHN
     IYHEFLSSQA LSPVNIDRQA WLSEEVLAQP RPDMFRAQQL QIFNLMKFDS YARFVKSPLY
     QECLLAEAEG RPLREPGSSH LGSPDTARKK PKLKPGKSLP LGVEELGQLP LAEGPCGRPL
     RKSFRREMTG GAMNSALRRE SQGSLNSSAS LDLGFLAFVS SKSESHRKSL GSGESESESR
     PGKYCCVYLP DGTASLALAR PGLTIRDMLA GICEKRGLSL PDIKVYLVGN EQKALVLDQD
     CTVLADQEVR LENRITFQLE LVGLERVVRI SAKPTKRLQE ALQPILAKHG LSLDQVVLHR
     PGEKQPMDLE NPVSSVASQT LVLDTPPDAK MSEARSISPC RSQGCLPRTQ TKDSHLPPSS
     SSLLVEDASS STGNRQTCDI EGLVELLNRV QSSGAHDQRG LLRKEDLVLP EFLQLPSQRP
     GSREAPP
//
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