RGS14_MOUSE
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 03-AUG-2022, entry version 182.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT 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 project:
RT 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 LOCATION,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=10926822; DOI=10.1042/bj3500019;
RA Traver S., Bidot C., Spassky N., Baltauss T., De Tand M.F., Thomas J.L.,
RA Zalc B., Janoueix-Lerosey I., Gunzburg J.D.;
RT "RGS14 is a novel Rap effector that preferentially regulates the GTPase
RT activity of galphao.";
RL Biochem. J. 350:19-29(2000).
RN [6]
RP FUNCTION, INTERACTION WITH GNAI1; GNAI2; RABGEF1 AND RAP2A, AND MUTAGENESIS
RP 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 RGS14
RT 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., Natale D.R.,
RA Snow B.E., Kimple R.J., Pajak A., Watson A.J., Dagnino L., Penninger J.M.,
RA Siderovski D.P., D'Souza S.J.;
RT "RGS14 is a mitotic spindle protein essential from the first division of
RT the mammalian zygote.";
RL Dev. Cell 7:763-769(2004).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15917656; DOI=10.4161/cc.4.7.1787;
RA Martin-McCaffrey L., Willard F.S., Pajak A., Dagnino L., Siderovski D.P.,
RA 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; ARG-336;
RP HIS-409; THR-497; 506-LEU-LEU-507 AND GLN-518.
RX PubMed=15520006; DOI=10.1074/jbc.m408163200;
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 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-protein
RT 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 midbody:
RT implication for their role in cell division.";
RL J. Cell Biol. 178:245-255(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND THR-249, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
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., Vellano C.P.,
RA Cowan D.P., Ramineni S., Yates C.K., Feng Y., Smith Y., Sweatt J.D.,
RA Weinshenker D., Ressler K.J., Dudek S.M., Hepler J.R.;
RT "RGS14 is a natural suppressor of both synaptic plasticity in CA2 neurons
RT and hippocampal-based learning and memory.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16994-16998(2010).
RN [14]
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., 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 [15]
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: Regulates G protein-coupled receptor signaling cascades.
CC Inhibits signal transduction by increasing the GTPase activity of G
CC protein alpha subunits, thereby driving them into their inactive GDP-
CC bound form. Besides, modulates signal transduction via G protein alpha
CC subunits by functioning as a GDP-dissociation inhibitor (GDI). Has GDI
CC activity on G(i) alpha subunits GNAI1 and GNAI3, but not on GNAI2 and
CC G(o)-alpha subunit GNAO1. Has GAP activity on GNAI0, GNAI2 and GNAI3.
CC May act as a scaffold integrating G protein and Ras/Raf MAPkinase
CC signaling pathways. Inhibits platelet-derived growth factor (PDGF)-
CC stimulated ERK1/ERK2 phosphorylation; a process depending on its
CC interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1.
CC Acts as a positive modulator of microtubule polymerisation and spindle
CC organization through a G(i)-alpha-dependent mechanism. Plays a role in
CC cell division; required for completion of the first mitotic division of
CC the 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 synaptic
CC plasticity in CA2 neurons. Required for the nerve growth factor (NGF)-
CC mediated neurite outgrowth. Involved in stress resistance.
CC {ECO:0000269|PubMed:10926822, ECO:0000269|PubMed:15112653,
CC ECO:0000269|PubMed:15525537, ECO:0000269|PubMed:15917656,
CC ECO:0000269|PubMed:16246175, ECO:0000269|PubMed:20837545}.
CC -!- SUBUNIT: Interacts with GNAI1 and GNAI2 (PubMed:15112653,
CC PubMed:17635935). Interacts with GNAI3 (By similarity). Interacts with
CC GNAO1 (PubMed:10926822). Interacts (via RGS and GoLoco domains) with
CC GNAI1; the interaction occurs in the centrosomes. Interaction with
CC GNAI1 or GNAI3 (via active GTP- or inactive GDP-bound forms) prevents
CC association of RGS14 with centrosomes or nuclear localization (By
CC similarity). Interacts with RABGEF1; the interactions is GTP-dependent
CC (PubMed:10926822, PubMed:15112653). Interacts with RAP2A; the
CC interactions is GTP-dependent and does not alter its function on G(i)
CC alpha subunits either as GAP or as GDI (PubMed:10926822,
CC PubMed:15112653). Associates with microtubules (By similarity). Found
CC in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14.
CC Interacts with RIC8A (via C-terminus). Interacts (via RBD 1 domain)
CC with HRAS (active GTP-bound form preferentially). Interacts (via RBD
CC domains) with BRAF (via N-terminus); the interaction mediates the
CC formation of a ternary complex with RAF1. Interacts (via RBD domains)
CC with RAF1 (via N-terminus); the interaction mediates the formation of a
CC ternary 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 form
CC preferentially) (By similarity). {ECO:0000250|UniProtKB:O08773,
CC ECO:0000269|PubMed:10926822, ECO:0000269|PubMed:15112653,
CC ECO:0000269|PubMed:17635935}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Cytoplasm. Membrane.
CC Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome. Cell
CC projection, dendrite. Cell projection, dendritic spine. Postsynaptic
CC density. Note=Localizes with spindle poles during metaphase. Shuttles
CC between the nucleus and cytoplasm in a CRM1-dependent manner. Recruited
CC from the cytosol to the plasma membrane by the inactive GDP-bound forms
CC of G(i) alpha subunits GNAI1 and GNAI3. Recruited from the cytosol to
CC membranes by the active GTP-bound form of HRAS. Colocalizes with G(i)
CC alpha subunit GNAI1 and RIC8A at the plasma membrane. Colocalizes with
CC BRAF and 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 mitotic
CC apparatus and subsequently the barrel- shaped cytoplasmic bridge
CC between the nascent nuclei of the emerging 2-cell embryo. Localizes to
CC a perinuclear compartment near the microtubule-organizing center
CC (MTOC). Expressed in the nucleus during interphase and segregates to
CC the centrosomes and astral MTs during mitosis. Shuttles between the
CC nucleus and cytoplasm in a CRM1-dependent manner. Relocalizes to the
CC nucleus in PML nuclear bodies in respons to heat stress. Colocalizes
CC with RIC8A in CA2 hippocampal neurons. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in pyramidal neurons of the CA1, CA2 and
CC fasciola cinerea (FC) subregions of the hippocampus and in the
CC olfactory cortex (at protein level). Expressed in brain, spleen, heart,
CC liver, lung, kidney, skin and thymus (at protein level). Expressed in
CC granular layer of the cerebellum, forbrain, striatum, layer V of the
CC cortex, olfactory cortex, tubercules, subthalamic and hippocampus,
CC particularly in the CA2 region, to a lesser extent in the CA1 region
CC and the external layer of the dentate gyrus. Expressed in neurons.
CC {ECO:0000269|PubMed:10926822, ECO:0000269|PubMed:15525537,
CC ECO:0000269|PubMed:20837545, 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 dpc (at
CC protein level). Expressed in the zygote through to the blastocyst
CC stage. Expressed in area lateral to the rhombencephalic floor plate at
CC 12 dpc. Expressed in the anterior region of the brain, including the
CC telencephalic olfactive nuclei and the hippocampus anlage at 17 dpc.
CC {ECO:0000269|PubMed:10926822, ECO:0000269|PubMed:15525537}.
CC -!- DOMAIN: The RGS domain is necessary for GTPase-activating protein (GAP)
CC activity for G subunits and localization to the nucleus and
CC centrosomes. {ECO:0000250}.
CC -!- DOMAIN: The GoLoco domain is necessary for GDP-dissociation inhibitor
CC (GDI) activity, translocation out of the nucleus and interaction with
CC G(i) alpha subunits GNAI1, GNAI2 and GNAI3. {ECO:0000250}.
CC -!- DOMAIN: The RBD domains are necessary for localization to the nucleus
CC and centrosomes. {ECO:0000250}.
CC -!- PTM: Phosphorylated by PKC. Phosphorylation is increased in presence of
CC forskolin and may enhance the GDI activity on G(i) alpha subunit GNAI1
CC (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice show an enhancement of
CC postsynaptic long-term potentiation (LTP) responses in the CA2 neurons
CC of the hippocampus that is correlated with an increase of spatial
CC learning and object recognition memory (OMR).
CC {ECO:0000269|PubMed:15525537, ECO:0000269|PubMed:20837545}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A balanced mind - Issue 132
CC of October 2011;
CC URL="https://web.expasy.org/spotlight/back_issues/132";
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DR EMBL; U85055; AAB41893.1; -; mRNA.
DR EMBL; CT009762; -; NOT_ANNOTATED_CDS; 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 PDB; 1WFY; NMR; -; A=366-456.
DR PDBsum; 1WFY; -.
DR AlphaFoldDB; P97492; -.
DR SMR; P97492; -.
DR BioGRID; 206175; 230.
DR IntAct; P97492; 2.
DR MINT; P97492; -.
DR STRING; 10090.ENSMUSP00000068731; -.
DR iPTMnet; P97492; -.
DR PhosphoSitePlus; P97492; -.
DR EPD; P97492; -.
DR jPOST; P97492; -.
DR MaxQB; P97492; -.
DR PaxDb; P97492; -.
DR PeptideAtlas; P97492; -.
DR PRIDE; P97492; -.
DR ProteomicsDB; 255192; -.
DR ABCD; P97492; 2 sequenced antibodies.
DR Antibodypedia; 29266; 340 antibodies from 40 providers.
DR DNASU; 51791; -.
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 VEuPathDB; HostDB:ENSMUSG00000052087; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000161364; -.
DR HOGENOM; CLU_024780_1_1_1; -.
DR InParanoid; P97492; -.
DR OMA; SQGCLPR; -.
DR OrthoDB; 275783at2759; -.
DR PhylomeDB; P97492; -.
DR TreeFam; TF328814; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 51791; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Rgs14; mouse.
DR EvolutionaryTrace; P97492; -.
DR PRO; PR:P97492; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P97492; protein.
DR Bgee; ENSMUSG00000052087; Expressed in granulocyte and 157 other tissues.
DR ExpressionAtlas; P97492; baseline and differential.
DR Genevisible; P97492; MM.
DR GO; GO:0070161; C:anchoring 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:0098978; C:glutamatergic synapse; IDA:SynGO.
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:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
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:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; ISS: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; IEA:InterPro.
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:0000278; P:mitotic cell cycle; IMP:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IDA: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:UniProtKB.
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:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
DR GO; GO:0008542; P:visual learning; ISS:UniProtKB.
DR GO; GO:0010070; P:zygote asymmetric cell division; IMP:UniProtKB.
DR CDD; cd08743; RGS_RGS14; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR030776; RGS14.
DR InterPro; IPR037881; RGS14_RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45945:SF2; PTHR45945:SF2; 1.
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 membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Developmental protein; GTPase activation;
KW Membrane; Microtubule; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Signal transduction inhibitor; Synapse.
FT CHAIN 1..547
FT /note="Regulator of G-protein signaling 14"
FT /id="PRO_0000204218"
FT DOMAIN 67..184
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 303..374
FT /note="RBD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 376..446
FT /note="RBD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 500..522
FT /note="GoLoco"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT REGION 19..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..427
FT /note="Necessary for interaction with RABGEF1"
FT /evidence="ECO:0000269|PubMed:15112653"
FT REGION 447..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43566"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43566"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43566"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08773"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08773"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08773"
FT MOD_RES 249
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08773"
FT MUTAGEN 92..93
FT /note="EN->AA: Inhibits GAP activity. Does not inhibit
FT interaction with GNAI1 in the centrosomes. Reduces the
FT down-regulation of G(i)-dependent signaling. Does not
FT affect subcellular location and does not promote gene
FT transcription activation. Inhibits strongly the down-
FT regulation of G(i)-dependent signaling; when associated
FT with F-519. Inhibits the interaction with GNAI1 in the
FT centrosomes; when associated with A-518."
FT /evidence="ECO:0000269|PubMed:15112653,
FT ECO:0000269|PubMed:15520006, ECO:0000269|PubMed:17635935"
FT MUTAGEN 261
FT /note="S->A: Does not affect subcellular location; when
FT associated with A-497."
FT /evidence="ECO:0000269|PubMed:15520006"
FT MUTAGEN 336
FT /note="R->L: Reduces interaction with RABGEF1 and RAP2A.
FT Strongly reduces interaction with RAP2A; when associated
FT with L-409."
FT /evidence="ECO:0000269|PubMed:15112653,
FT ECO:0000269|PubMed:15520006, ECO:0000269|PubMed:16246175"
FT MUTAGEN 409
FT /note="H->L: Does not reduce interaction with RAP2A.
FT Strongly reduces interaction with RAP2A; when associated
FT with L-336."
FT /evidence="ECO:0000269|PubMed:15520006,
FT ECO:0000269|PubMed:16246175"
FT MUTAGEN 497
FT /note="T->A: Does not affect subcellular location; when
FT associated with A-261."
FT /evidence="ECO:0000269|PubMed:15520006"
FT MUTAGEN 506..507
FT /note="LL->AA: Strongly expressed in the nucleus, mainly
FT associated with PML nuclear bodies but not with
FT centrosomes. Promotes gene transcription activation."
FT /evidence="ECO:0000269|PubMed:15520006"
FT MUTAGEN 518
FT /note="Q->A: Inhibits GDI activity. Does not inhibit
FT interaction with GNAI1 in the centrosomes, does not affect
FT subcellular location and does not promote gene
FT transcription activation. Inhibits interaction with GNAI1
FT in the centrosomes; when associated with A-92-93-A."
FT /evidence="ECO:0000269|PubMed:15520006,
FT ECO:0000269|PubMed:17635935"
FT MUTAGEN 519
FT /note="R->F: Reduces interaction with GNAI1 and GNAI2.
FT Inhibits strongly the down-regulation of G(i)-dependent
FT signaling; when associated with A-92-93-A."
FT /evidence="ECO:0000269|PubMed:15112653"
FT CONFLICT 209
FT /note="Missing (in Ref. 4; BAB22436)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="N -> T (in Ref. 1; AAB41893)"
FT /evidence="ECO:0000305"
FT STRAND 375..392
FT /evidence="ECO:0007829|PDB:1WFY"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:1WFY"
FT TURN 398..402
FT /evidence="ECO:0007829|PDB:1WFY"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:1WFY"
FT TURN 407..410
FT /evidence="ECO:0007829|PDB:1WFY"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:1WFY"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:1WFY"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:1WFY"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:1WFY"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:1WFY"
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
