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 18-JUL-2018, entry version 172. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Khan Z.U.; RT "Localization of the GoLoco motif carrier regulator of G-protein RT signalling 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 RT sequenced by 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., RA 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 RT project: 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., RA Siderovski D.P., 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 RT midbody: 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, RP AND 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 RT protein-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 RP GNAI1 AND 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., RA Machius M., Kuhlman B., Willard F.S., Siderovski D.P.; RT "Structural determinants of affinity enhancement between GoLoco motifs RT and 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 CC G protein alpha subunits, thereby driving them into their inactive CC GDP-bound form. Besides, modulates signal transduction via G CC protein alpha subunits by functioning as a GDP-dissociation CC inhibitor (GDI). Has GDI activity on G(i) alpha subunits GNAI1 and CC GNAI3, but not on GNAI2 and G(o) alpha subunit GNAO1. Has GAP CC activity on GNAI0, GNAI2 and GNAI3. May act as a scaffold CC integrating G protein and Ras/Raf MAPkinase signaling pathways. CC Inhibits platelet-derived growth factor (PDGF)-stimulated CC ERK1/ERK2 phosphorylation; a process depending on its interaction CC with HRAS and that is reversed by G(i) alpha subunit GNAI1. Acts CC as a positive modulator of microtubule polymerisation and spindle CC organization through a G(i)-alpha-dependent mechanism. Plays a CC role in cell division. Required for the nerve growth factor (NGF)- CC mediated neurite outgrowth. Involved in stress resistance. May be CC involved in visual memory processing capacity and hippocampal- CC based learning and memory. {ECO:0000269|PubMed:15917656, CC ECO:0000269|PubMed:17635935}. CC -!- SUBUNIT: Interacts with GNAO1, GNAI2 and GNAI3 (By similarity). CC Interacts with GNAI1 (PubMed:18434541, PubMed:21115486). Interacts CC (via RGS and GoLoco domains) with GNAI1; the interaction occurs in CC the centrosomes. Interaction with GNAI1 or GNAI3 (via active CC GTP- or inactive GDP-bound forms) prevents association of RGS14 CC with centrosomes or nuclear localization (By similarity). CC Interacts with RABGEF1; the interactions is GTP-dependent. CC Interacts with RAP2A; the interactions is GTP-dependent and does CC not alter its function on G(i) alpha subunits either as GAP or as CC GDI (By similarity). Associates with microtubules CC (PubMed:15917656). Found in a complex with at least BRAF, HRAS, CC 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 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). {ECO:0000250|UniProtKB:O08773, CC ECO:0000250|UniProtKB:P97492, ECO:0000269|PubMed:15917656, CC ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:21115486}. CC -!- INTERACTION: CC P08754:GNAI3; NbExp=3; IntAct=EBI-750603, EBI-357563; CC 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, CC cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:15917656}. Cytoplasm, cytoskeleton, spindle CC pole {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell CC projection, dendritic spine {ECO:0000250}. Cell junction, synapse, CC postsynaptic cell membrane, postsynaptic density {ECO:0000250}. CC Note=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. Relocalizes to the nucleus in PML nuclear bodies in CC response to heat stress. Colocalizes with RIC8A in CA2 hippocampal CC neurons. Localizes to spindle poles during metaphase. Shuttles CC between the nucleus and cytoplasm in a CRM1-dependent manner. CC Recruited from the cytosol to the plasma membrane by the inactive CC GDP-bound forms of G(i) alpha subunits GNAI1 and GNAI3. Recruited CC from the cytosol to membranes by the active GTP-bound form of CC HRAS. Colocalizes with G(i) alpha subunit GNAI1 and RIC8A at the CC plasma membrane. Colocalizes with BRAF and RAF1 in both the CC cytoplasm and membranes (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=O43566-7; Sequence=Displayed; CC Note=No experimental confirmation available.; 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 Note=No experimental confirmation available.; 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 -!- SEQUENCE CAUTION: CC Sequence=AAB92614.1; Type=Frameshift; Positions=337, 344, 348, 539, 544; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A balanced mind - Issue CC 132 of October 2011; CC URL="https://web.expasy.org/spotlight/back_issues/132"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Hs.9347; -. 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 ProteinModelPortal; O43566; -. DR SMR; O43566; -. DR BioGrid; 115880; 17. 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 MaxQB; O43566; -. DR PaxDb; O43566; -. DR PeptideAtlas; O43566; -. DR PRIDE; O43566; -. DR ProteomicsDB; 49054; -. DR ProteomicsDB; 49055; -. [O43566-4] DR ProteomicsDB; 49056; -. [O43566-5] DR ProteomicsDB; 49057; -. [O43566-6] DR DNASU; 10636; -. DR Ensembl; ENST00000408923; ENSP00000386229; ENSG00000169220. [O43566-7] DR GeneID; 10636; -. DR KEGG; hsa:10636; -. DR UCSC; uc003mgf.4; human. [O43566-7] DR CTD; 10636; -. DR DisGeNET; 10636; -. DR EuPathDB; HostDB:ENSG00000169220.17; -. DR GeneCards; RGS14; -. DR HGNC; HGNC:9996; RGS14. DR HPA; HPA046847; -. DR HPA; HPA061819; -. DR MIM; 602513; gene. DR neXtProt; NX_O43566; -. DR OpenTargets; ENSG00000169220; -. DR PharmGKB; PA34366; -. DR eggNOG; KOG3589; Eukaryota. DR eggNOG; ENOG410YMJD; LUCA. DR GeneTree; ENSGT00760000119142; -. DR HOGENOM; HOG000049111; -. DR HOVERGEN; HBG061568; -. DR InParanoid; O43566; -. DR KO; K17706; -. DR OMA; TGKRQTC; -. DR OrthoDB; EOG091G0BDG; -. DR PhylomeDB; O43566; -. DR TreeFam; TF328814; -. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR SignaLink; O43566; -. DR SIGNOR; O43566; -. DR ChiTaRS; RGS14; human. DR EvolutionaryTrace; O43566; -. DR GeneWiki; RGS14; -. DR GenomeRNAi; 10636; -. DR PRO; PR:O43566; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; ENSG00000169220; -. DR CleanEx; HS_RGS14; -. DR ExpressionAtlas; O43566; baseline and differential. DR Genevisible; O43566; HS. DR GO; GO:0030054; C:cell 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: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: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: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:0008017; F:microtubule binding; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0030159; F:receptor signaling complex scaffold activity; ISS:UniProtKB. DR GO; GO:0051301; P:cell division; IMP:UniProtKB. DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB. 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 protein 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: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 protein signaling pathway; TAS:ProtInc. 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; 1.10.196.10; -; 2. 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; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10845:SF179; PTHR10845:SF179; 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 junction; Cell membrane; Cell projection; Complete proteome; KW Cytoplasm; Cytoskeleton; GTPase activation; Membrane; Microtubule; KW Nucleus; Phosphoprotein; Postsynaptic cell membrane; KW Reference proteome; Repeat; Signal transduction inhibitor; Synapse. FT CHAIN 1 566 Regulator of G-protein signaling 14. FT /FTId=PRO_0000204217. FT DOMAIN 67 184 RGS. {ECO:0000255|PROSITE- FT ProRule:PRU00171}. FT DOMAIN 302 373 RBD 1. {ECO:0000255|PROSITE- FT ProRule:PRU00262}. FT DOMAIN 375 445 RBD 2. {ECO:0000255|PROSITE- FT ProRule:PRU00262}. FT DOMAIN 498 521 GoLoco. {ECO:0000255|PROSITE- FT ProRule:PRU00097}. FT REGION 299 425 Necessary for interaction with RABGEF1. FT {ECO:0000250}. FT MOD_RES 20 20 Phosphoserine. FT {ECO:0000244|PubMed:19690332}. FT MOD_RES 42 42 Phosphoserine. FT {ECO:0000244|PubMed:19690332}. FT MOD_RES 45 45 Phosphoserine. FT {ECO:0000244|PubMed:19690332}. FT MOD_RES 199 199 Phosphoserine. FT {ECO:0000250|UniProtKB:P97492}. FT MOD_RES 203 203 Phosphoserine. FT {ECO:0000250|UniProtKB:O08773}. FT MOD_RES 218 218 Phosphoserine. FT {ECO:0000250|UniProtKB:O08773}. FT MOD_RES 288 288 Phosphoserine. FT {ECO:0000250|UniProtKB:O08773}. FT VAR_SEQ 1 153 Missing (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:16819986, FT ECO:0000303|Ref.2, ECO:0000303|Ref.3}. FT /FTId=VSP_027577. FT VAR_SEQ 54 273 Missing (in isoform 4). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_029426. FT VAR_SEQ 351 351 Q -> QK (in isoform 3 and isoform 4). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:16819986, FT ECO:0000303|Ref.2}. FT /FTId=VSP_037959. FT VAR_SEQ 352 354 ALV -> VGT (in isoform 2). FT {ECO:0000303|Ref.2, ECO:0000303|Ref.3}. FT /FTId=VSP_027578. FT VAR_SEQ 355 566 Missing (in isoform 2). FT {ECO:0000303|Ref.2, ECO:0000303|Ref.3}. FT /FTId=VSP_027579. FT CONFLICT 407 407 H -> R (in Ref. 4; BAC85600). FT {ECO:0000305}. FT CONFLICT 415 415 V -> A (in Ref. 1; AAY26402). FT {ECO:0000305}. FT CONFLICT 502 502 Missing (in Ref. 2; AAB92614). FT {ECO:0000305}. FT HELIX 61 65 {ECO:0000244|PDB:2JNU}. FT HELIX 68 73 {ECO:0000244|PDB:2JNU}. FT HELIX 75 84 {ECO:0000244|PDB:2JNU}. FT STRAND 87 89 {ECO:0000244|PDB:2JNU}. FT HELIX 92 105 {ECO:0000244|PDB:2JNU}. FT HELIX 111 125 {ECO:0000244|PDB:2JNU}. FT HELIX 144 148 {ECO:0000244|PDB:2JNU}. FT TURN 152 155 {ECO:0000244|PDB:2JNU}. FT HELIX 156 167 {ECO:0000244|PDB:2JNU}. FT HELIX 170 174 {ECO:0000244|PDB:2JNU}. FT HELIX 180 184 {ECO:0000244|PDB:2JNU}. FT HELIX 499 509 {ECO:0000244|PDB:2OM2}. FT STRAND 517 519 {ECO:0000244|PDB:2OM2}. FT TURN 522 525 {ECO:0000244|PDB:2OM2}. FT HELIX 529 531 {ECO:0000244|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 //