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 27-MAR-2024, entry version 206. 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"; 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 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; 12. 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; 9606-ENSP00000386229; -. DR PeptideAtlas; 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; 376 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 AGR; HGNC:9996; -. DR CTD; 10636; -. DR DisGeNET; 10636; -. DR GeneCards; RGS14; -. DR HGNC; HGNC:9996; RGS14. DR HPA; ENSG00000169220; Tissue enriched (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; 22856at2759; -. 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; 12 hits in 1164 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 158 other cell types or tissues. DR ExpressionAtlas; O43566; baseline and differential. 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: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:0050769; P:positive regulation of neurogenesis; 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; cd17137; RBD1_RGS14; 1. DR CDD; cd17139; RBD2_RGS14; 1. DR CDD; cd08743; RGS_RGS14; 1. DR Gene3D; 1.10.196.10; -; 1. DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1. DR IDEAL; IID00692; -. DR InterPro; IPR003109; GoLoco_motif. DR InterPro; IPR046992; RBD1_RGS14. DR InterPro; IPR046993; RBD2_RGS14. DR InterPro; IPR003116; RBD_dom. DR InterPro; IPR016137; RGS. DR InterPro; IPR046995; RGS10/12/14-like. 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; REGULATOR OF G-PROTEIN SIGNALING 14; 1. DR PANTHER; PTHR45945; REGULATOR OF G-PROTEIN SIGNALING LOCO; 1. DR Pfam; PF02188; GoLoco; 1. DR Pfam; PF02196; RBD; 1. 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; Regulator of G-protein signaling, RGS; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 2. DR PROSITE; PS50877; GOLOCO; 1. DR PROSITE; PS50898; RBD; 2. DR PROSITE; PS50132; RGS; 1. DR Genevisible; O43566; HS. 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 //