RGS14_HUMAN
ID RGS14_HUMAN Reviewed; 566 AA.
AC O43566; O43565; Q506M1; Q6ZWA4; Q8TD62;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 4.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Regulator of G-protein signaling 14;
DE Short=RGS14;
GN Name=RGS14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=16819986; DOI=10.1111/j.1460-9568.2006.04838.x;
RA Lopez-Aranda M.F., Acevedo M.J., Carballo F.J., Gutierrez A., Khan Z.U.;
RT "Localization of the GoLoco motif carrier regulator of G-protein signalling
RT 12 and 14 proteins in monkey and rat brain.";
RL Eur. J. Neurosci. 23:2971-2982(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RA Chatterjee T.K., Fisher R.A.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [7]
RP FUNCTION, ASSOCIATION WITH MICROTUBULES, 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 [8]
RP FUNCTION.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-42 AND SER-45, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 497-532.
RX PubMed=17603074; DOI=10.1016/j.jmb.2007.05.096;
RA Sammond D.W., Eletr Z.M., Purbeck C., Kimple R.J., Siderovski D.P.,
RA Kuhlman B.;
RT "Structure-based protocol for identifying mutations that enhance protein-
RT protein binding affinities.";
RL J. Mol. Biol. 371:1392-1404(2007).
RN [11]
RP STRUCTURE BY NMR OF 56-207, AND INTERACTION WITH GNAI1.
RX PubMed=18434541; DOI=10.1073/pnas.0801508105;
RA Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J.,
RA Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A.,
RA Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P.;
RT "Structural diversity in the RGS domain and its interaction with
RT heterotrimeric G protein alpha-subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 497-532 IN COMPLEX WITH GNAI1 AND
RP GDP.
RX PubMed=21115486; DOI=10.1074/jbc.m110.190496;
RA Bosch D.E., Kimple A.J., Sammond D.W., Muller R.E., Miley M.J., Machius M.,
RA Kuhlman B., Willard F.S., Siderovski D.P.;
RT "Structural determinants of affinity enhancement between GoLoco motifs and
RT G-protein alpha subunit mutants.";
RL J. Biol. Chem. 286:3351-3358(2011).
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 the nerve growth factor (NGF)-mediated
CC neurite outgrowth. Involved in stress resistance. May be involved in
CC visual memory processing capacity and hippocampal-based learning and
CC memory. {ECO:0000269|PubMed:15917656, ECO:0000269|PubMed:17635935}.
CC -!- SUBUNIT: Interacts with GNAO1, GNAI2 and GNAI3 (By similarity).
CC Interacts with GNAI1 (PubMed:18434541, PubMed:21115486). Interacts (via
CC RGS and GoLoco domains) with GNAI1; the interaction occurs in the
CC centrosomes. Interaction with GNAI1 or GNAI3 (via active GTP- or
CC inactive GDP-bound forms) prevents association of RGS14 with
CC centrosomes or nuclear localization (By similarity). Interacts with
CC RABGEF1; the interactions is GTP-dependent. 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 (By similarity). Associates with
CC microtubules (PubMed:15917656). Found in a complex with at least BRAF,
CC HRAS, MAP2K1, MAPK3 and RGS14. Interacts with RIC8A (via C-terminus).
CC Interacts (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 complex
CC with RAF1. Interacts (via RBD domains) with RAF1 (via N-terminus); the
CC interaction mediates the formation of a ternary complex with BRAF.
CC Interacts with KRAS (active GTP-bound form preferentially), MRAS
CC (active GTP-bound form preferentially), NRAS (active GTP-bound form
CC preferentially) and RRAS (active GTP-bound form preferentially).
CC {ECO:0000250|UniProtKB:O08773, ECO:0000250|UniProtKB:P97492,
CC ECO:0000269|PubMed:15917656, ECO:0000269|PubMed:18434541,
CC ECO:0000269|PubMed:21115486}.
CC -!- INTERACTION:
CC O43566; P08754: GNAI3; NbExp=4; IntAct=EBI-750603, EBI-357563;
CC O43566; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-750603, EBI-717399;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, PML body
CC {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:15917656}. Membrane
CC {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:15917656}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}.
CC Postsynaptic density {ECO:0000250}. Note=Associates with the
CC perinuclear sheaths of microtubules (MTs) surrounding the pronuclei,
CC prior to segregating to the anastral mitotic apparatus and subsequently
CC the barrel-shaped cytoplasmic bridge between the nascent nuclei of the
CC emerging 2-cell embryo. Localizes to a perinuclear compartment near the
CC microtubule-organizing center (MTOC). Expressed in the nucleus during
CC interphase and segregates to the centrosomes and astral MTs during
CC mitosis. Relocalizes to the nucleus in PML nuclear bodies in response
CC to heat stress. Colocalizes with RIC8A in CA2 hippocampal neurons.
CC Localizes to spindle poles during metaphase. Shuttles between the
CC nucleus and cytoplasm in a CRM1-dependent manner. Recruited from the
CC cytosol to the plasma membrane by the inactive GDP-bound forms of G(i)
CC alpha subunits GNAI1 and GNAI3. Recruited from the cytosol to membranes
CC by the active GTP-bound form of HRAS. Colocalizes with G(i) alpha
CC subunit GNAI1 and RIC8A at the plasma membrane. Colocalizes with BRAF
CC and RAF1 in both the cytoplasm and membranes (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O43566-7; Sequence=Displayed;
CC Name=2;
CC IsoId=O43566-4; Sequence=VSP_027577, VSP_027578, VSP_027579;
CC Name=3;
CC IsoId=O43566-5; Sequence=VSP_027577, VSP_037959;
CC Name=4;
CC IsoId=O43566-6; Sequence=VSP_029426, VSP_037959;
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 -!- SEQUENCE CAUTION:
CC Sequence=AAB92614.1; Type=Frameshift; Evidence={ECO:0000305};
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; AY987041; AAY26402.1; -; mRNA.
DR EMBL; AF037194; AAB92613.1; -; mRNA.
DR EMBL; AF037195; AAB92614.1; ALT_FRAME; mRNA.
DR EMBL; AF493936; AAM12650.1; -; mRNA.
DR EMBL; AK123382; BAC85600.1; -; mRNA.
DR EMBL; AC146507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014094; AAH14094.1; -; mRNA.
DR CCDS; CCDS43405.1; -. [O43566-7]
DR RefSeq; NP_006471.2; NM_006480.4. [O43566-7]
DR PDB; 2JNU; NMR; -; A=56-207.
DR PDB; 2OM2; X-ray; 2.20 A; B/D=497-532.
DR PDB; 2XNS; X-ray; 3.41 A; C/D=497-517.
DR PDB; 3ONW; X-ray; 2.38 A; C/D=497-532.
DR PDB; 3QI2; X-ray; 2.80 A; C/D=497-532.
DR PDBsum; 2JNU; -.
DR PDBsum; 2OM2; -.
DR PDBsum; 2XNS; -.
DR PDBsum; 3ONW; -.
DR PDBsum; 3QI2; -.
DR AlphaFoldDB; O43566; -.
DR BMRB; O43566; -.
DR SMR; O43566; -.
DR BioGRID; 115880; 20.
DR DIP; DIP-41167N; -.
DR IntAct; O43566; 11.
DR MINT; O43566; -.
DR STRING; 9606.ENSP00000386229; -.
DR iPTMnet; O43566; -.
DR PhosphoSitePlus; O43566; -.
DR BioMuta; RGS14; -.
DR EPD; O43566; -.
DR jPOST; O43566; -.
DR MassIVE; O43566; -.
DR MaxQB; O43566; -.
DR PaxDb; O43566; -.
DR PeptideAtlas; O43566; -.
DR PRIDE; O43566; -.
DR ProteomicsDB; 49054; -. [O43566-7]
DR ProteomicsDB; 49055; -. [O43566-4]
DR ProteomicsDB; 49056; -. [O43566-5]
DR ProteomicsDB; 49057; -. [O43566-6]
DR ABCD; O43566; 1 sequenced antibody.
DR Antibodypedia; 29266; 340 antibodies from 40 providers.
DR DNASU; 10636; -.
DR Ensembl; ENST00000408923.8; ENSP00000386229.3; ENSG00000169220.18. [O43566-7]
DR GeneID; 10636; -.
DR KEGG; hsa:10636; -.
DR MANE-Select; ENST00000408923.8; ENSP00000386229.3; NM_006480.5; NP_006471.2.
DR UCSC; uc003mgf.4; human. [O43566-7]
DR CTD; 10636; -.
DR DisGeNET; 10636; -.
DR GeneCards; RGS14; -.
DR HGNC; HGNC:9996; RGS14.
DR HPA; ENSG00000169220; Tissue enhanced (brain).
DR MIM; 602513; gene.
DR neXtProt; NX_O43566; -.
DR OpenTargets; ENSG00000169220; -.
DR PharmGKB; PA34366; -.
DR VEuPathDB; HostDB:ENSG00000169220; -.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000161364; -.
DR HOGENOM; CLU_024780_1_1_1; -.
DR InParanoid; O43566; -.
DR OMA; SQGCLPR; -.
DR OrthoDB; 275783at2759; -.
DR PhylomeDB; O43566; -.
DR TreeFam; TF328814; -.
DR PathwayCommons; O43566; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; O43566; -.
DR SIGNOR; O43566; -.
DR BioGRID-ORCS; 10636; 9 hits in 1086 CRISPR screens.
DR ChiTaRS; RGS14; human.
DR EvolutionaryTrace; O43566; -.
DR GeneWiki; RGS14; -.
DR GenomeRNAi; 10636; -.
DR Pharos; O43566; Tbio.
DR PRO; PR:O43566; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O43566; protein.
DR Bgee; ENSG00000169220; Expressed in granulocyte and 156 other tissues.
DR ExpressionAtlas; O43566; baseline and differential.
DR Genevisible; O43566; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISS: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; IEA:Ensembl.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IDA:UniProtKB.
DR GO; GO:0032794; F:GTPase activating protein binding; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; TAS:Reactome.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0031914; P:negative regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0006913; P:nucleocytoplasmic transport; ISS: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; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central.
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; ISS: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; Alternative splicing; Cell cycle; Cell division;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; GTPase activation;
KW Membrane; Microtubule; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Signal transduction inhibitor; Synapse.
FT CHAIN 1..566
FT /note="Regulator of G-protein signaling 14"
FT /id="PRO_0000204217"
FT DOMAIN 67..184
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 302..373
FT /note="RBD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 375..445
FT /note="RBD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 498..521
FT /note="GoLoco"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT REGION 19..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..425
FT /note="Necessary for interaction with RABGEF1"
FT /evidence="ECO:0000250"
FT REGION 451..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97492"
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 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08773"
FT VAR_SEQ 1..153
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16819986, ECO:0000303|Ref.2,
FT ECO:0000303|Ref.3"
FT /id="VSP_027577"
FT VAR_SEQ 54..273
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029426"
FT VAR_SEQ 351
FT /note="Q -> QK (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16819986, ECO:0000303|Ref.2"
FT /id="VSP_037959"
FT VAR_SEQ 352..354
FT /note="ALV -> VGT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3"
FT /id="VSP_027578"
FT VAR_SEQ 355..566
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2, ECO:0000303|Ref.3"
FT /id="VSP_027579"
FT CONFLICT 407
FT /note="H -> R (in Ref. 4; BAC85600)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="V -> A (in Ref. 1; AAY26402)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="Missing (in Ref. 2; AAB92614)"
FT /evidence="ECO:0000305"
FT HELIX 61..65
FT /evidence="ECO:0007829|PDB:2JNU"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:2JNU"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:2JNU"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2JNU"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:2JNU"
FT HELIX 111..125
FT /evidence="ECO:0007829|PDB:2JNU"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:2JNU"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:2JNU"
FT HELIX 156..167
FT /evidence="ECO:0007829|PDB:2JNU"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:2JNU"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:2JNU"
FT HELIX 499..509
FT /evidence="ECO:0007829|PDB:2OM2"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:2OM2"
FT TURN 522..525
FT /evidence="ECO:0007829|PDB:2OM2"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:2OM2"
SQ 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
