RGS14_RAT
ID RGS14_RAT Reviewed; 544 AA.
AC O08773;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Regulator of G-protein signaling 14;
DE Short=RGS14;
GN Name=Rgs14;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9168931; DOI=10.1006/bbrc.1997.6537;
RA Snow B.E., Antonio L., Suggs S., Gutstein H.B., Siderovski D.P.;
RT "Molecular cloning and expression analysis of rat Rgs12 and Rgs14.";
RL Biochem. Biophys. Res. Commun. 233:770-777(1997).
RN [2]
RP FUNCTION, AND INTERACTION WITH GNAI1; GNAI2 AND GNAI3.
RX PubMed=11387333; DOI=10.1074/jbc.m103208200;
RA Kimple R.J., De Vries L., Tronchere H., Behe C.I., Morris R.A.,
RA Gist Farquhar M., Siderovski D.P.;
RT "RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with
RT guanine nucleotide dissociation inhibitor activity.";
RL J. Biol. Chem. 276:29275-29281(2001).
RN [3]
RP PHOSPHORYLATION, MUTAGENESIS OF SER-258 AND THR-494, AND FUNCTION.
RX PubMed=12534294; DOI=10.1021/bi026664y;
RA Hollinger S., Ramineni S., Hepler J.R.;
RT "Phosphorylation of RGS14 by protein kinase A potentiates its activity
RT toward G alpha i.";
RL Biochemistry 42:811-819(2003).
RN [4]
RP FUNCTION, AND DOMAIN.
RX PubMed=15337739; DOI=10.1074/jbc.m407409200;
RA Mittal V., Linder M.E.;
RT "The RGS14 GoLoco domain discriminates among Galphai isoforms.";
RL J. Biol. Chem. 279:46772-46778(2004).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [6]
RP INTERACTION WITH GNAI1 AND GNAI3, AND SUBCELLULAR LOCATION.
RX PubMed=16870394; DOI=10.1016/j.cellsig.2006.06.002;
RA Shu F.J., Ramineni S., Amyot W., Hepler J.R.;
RT "Selective interactions between Gi alpha1 and Gi alpha3 and the GoLoco/GPR
RT domain of RGS14 influence its dynamic subcellular localization.";
RL Cell. Signal. 19:163-176(2007).
RN [7]
RP MUTAGENESIS OF GLN-508; LEU-518; VAL-525 AND PHE-529, AND INTERACTION WITH
RP GNAI1.
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 [8]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH BRAF; HRAS; MAP2K1 AND MAPK3,
RP AND INTERACTION WITH BRAF; HRAS; KRAS; MRAS; NRAS; RAF1 AND RRAS.
RX PubMed=19319189; DOI=10.1371/journal.pone.0004884;
RA Willard F.S., Willard M.D., Kimple A.J., Soundararajan M., Oestreich E.A.,
RA Li X., Sowa N.A., Kimple R.J., Doyle D.A., Der C.J., Zylka M.J.,
RA Snider W.D., Siderovski D.P.;
RT "Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras
RT effector.";
RL PLoS ONE 4:E4884-E4884(2009).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19574389; DOI=10.1126/science.1170869;
RA Lopez-Aranda M.F., Lopez-Tellez J.F., Navarro-Lobato I., Masmudi-Martin M.,
RA Gutierrez A., Khan Z.U.;
RT "Role of layer 6 of V2 visual cortex in object-recognition memory.";
RL Science 325:87-89(2009).
RN [10]
RP FUNCTION, INTERACTION WITH BRAF; HRAS AND RAF1, MUTAGENESIS OF ARG-333 AND
RP HIS-406, AND SUBCELLULAR LOCATION.
RX PubMed=19878719; DOI=10.1016/j.cellsig.2009.10.005;
RA Shu F.J., Ramineni S., Hepler J.R.;
RT "RGS14 is a multifunctional scaffold that integrates G protein and Ras/Raf
RT MAPkinase signalling pathways.";
RL Cell. Signal. 22:366-376(2010).
RN [11]
RP FUNCTION.
RX PubMed=21255223; DOI=10.1111/j.1474-9726.2011.00678.x;
RA Lin Y.R., Kim K., Yang Y., Ivessa A., Sadoshima J., Park Y.;
RT "Regulation of longevity by regulator of G-protein signaling (RGS) protein,
RT Loco.";
RL Aging Cell 10:438-447(2011).
RN [12]
RP FUNCTION, INTERACTION WITH GNAI1 AND RIC8A, AND SUBCELLULAR LOCATION.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-143; SER-203;
RP SER-218; SER-286 AND SER-481, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [14] {ECO:0007744|PDB:1KJY}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 496-531 IN COMPLEX WITH GNAI1,
RP INTERACTION WITH GNAI1, AND FUNCTION.
RX PubMed=11976690; DOI=10.1038/416878a;
RA Kimple R.J., Kimple M.E., Betts L., Sondek J., Siderovski D.P.;
RT "Structural determinants for GoLoco-induced inhibition of nucleotide
RT release by Galpha subunits.";
RL Nature 416:878-881(2002).
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)
CC (PubMed:11976690). Has GDI activity on G(i) alpha subunits GNAI1 and
CC GNAI3, but not on GNAI2 and G(o)-alpha subunit GNAO1. Has GAP activity
CC on GNAI0, GNAI2 and GNAI3. May act as a scaffold integrating G protein
CC and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived
CC growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a process
CC depending on its interaction with HRAS and that is reversed by G(i)
CC alpha subunit GNAI1. Acts as a positive modulator of microtubule
CC polymerisation and spindle organization through a G(i)-alpha-dependent
CC mechanism. Plays a role in cell division; required for completion of
CC the first mitotic division of the embryo. Involved in visual memory
CC processing capacity; when overexpressed in the V2 secondary visual
CC cortex area. Involved in hippocampal-based learning and memory; acts as
CC a suppressor of synaptic plasticity in CA2 neurons. Required for the
CC nerve growth factor (NGF)-mediated neurite outgrowth. Involved in
CC stress resistance. {ECO:0000269|PubMed:11387333,
CC ECO:0000269|PubMed:11976690, ECO:0000269|PubMed:15337739,
CC ECO:0000269|PubMed:19319189, ECO:0000269|PubMed:19574389,
CC ECO:0000269|PubMed:19878719, ECO:0000269|PubMed:21158412,
CC ECO:0000269|PubMed:21255223}.
CC -!- SUBUNIT: Interacts with GNAI1, GNAI2 and GNAI3 (PubMed:11387333,
CC PubMed:16870394, PubMed:17603074, PubMed:21158412, PubMed:11976690).
CC Interacts with GNAO1 (By similarity). Interacts (via RGS and GoLoco
CC domains) with GNAI1; the interaction occurs in the centrosomes.
CC Interaction with GNAI1 or GNAI3 (via active GTP- or inactive GDP-bound
CC forms) prevents association of RGS14 with centrosomes or nuclear
CC localization. Interacts with RABGEF1; the interactions is GTP-
CC dependent. Interacts with RAP2A; the interactions is GTP-dependent and
CC does not alter its function on G(i) alpha subunits either as GAP or as
CC GDI. Associates with microtubules (By similarity). Found in a complex
CC with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14 (PubMed:19319189).
CC Interacts with RIC8A (via C-terminus) (PubMed:21158412). Interacts (via
CC RBD 1 domain) with HRAS (active GTP-bound form preferentially).
CC Interacts (via RBD domains) with BRAF (via N-terminus); the interaction
CC mediates the formation of a ternary complex with RAF1. Interacts (via
CC RBD domains) with RAF1 (via N-terminus); the interaction mediates the
CC formation of a ternary complex with BRAF (PubMed:19878719). Interacts
CC with KRAS (active GTP-bound form preferentially), MRAS (active GTP-
CC bound form preferentially), NRAS (active GTP-bound form preferentially)
CC and RRAS (active GTP-bound form preferentially) (PubMed:19319189).
CC {ECO:0000250|UniProtKB:O43566, ECO:0000250|UniProtKB:P97492,
CC ECO:0000269|PubMed:11387333, ECO:0000269|PubMed:11976690,
CC ECO:0000269|PubMed:16870394, ECO:0000269|PubMed:17603074,
CC ECO:0000269|PubMed:19319189, ECO:0000269|PubMed:19878719,
CC ECO:0000269|PubMed:21158412}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body {ECO:0000250}.
CC Cytoplasm. Membrane. Cell membrane. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole. Cell
CC projection, dendrite {ECO:0000250}. Cell projection, dendritic spine
CC {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Associates with
CC the perinuclear sheaths of microtubules (MTs) surrounding the
CC pronuclei, prior to segregating to the anastral mitotic apparatus and
CC subsequently the barrel-shaped cytoplasmic bridge between the nascent
CC nuclei of the emerging 2-cell embryo. Localizes to a perinuclear
CC compartment near the microtubule-organizing center (MTOC). Expressed in
CC the nucleus during interphase and segregates to the centrosomes and
CC astral MTs during mitosis. Shuttles between the nucleus and cytoplasm
CC in a CRM1-dependent manner. Relocalizes to the nucleus in PML nuclear
CC bodies in respons to heat stress. Colocalizes with RIC8A in CA2
CC hippocampal neurons (By similarity). Localizes with spindle poles
CC during metaphase. Shuttles between the nucleus and cytoplasm in a CRM1-
CC dependent manner. Recruited from the cytosol to the plasma membrane by
CC the inactive GDP-bound forms of G(i) alpha subunits GNAI1 and GNAI3.
CC Recruited 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 plasma
CC membrane. Colocalizes with BRAF and RAF1 in both the cytoplasm and
CC membranes. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons of the V2 secondary visual
CC cortex area (at protein level). Expressed at high levels in the brain
CC cortex, hippocampus, striatum, thalamus and substantia nigra, in the
CC lung, and spleen. Low expression has been found in heart, liver,
CC skeletal muscle and testis. {ECO:0000269|PubMed:16819986,
CC ECO:0000269|PubMed:19574389}.
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:0000269|PubMed:15337739}.
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.
CC {ECO:0000269|PubMed:15337739}.
CC -!- DOMAIN: The RBD domains are necessary for localization to the nucleus
CC and centrosomes. {ECO:0000269|PubMed:15337739}.
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 {ECO:0000269|PubMed:12534294}.
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DR EMBL; U92279; AAC53175.1; -; mRNA.
DR PIR; JC5503; JC5503.
DR RefSeq; NP_446216.1; NM_053764.1.
DR PDB; 1KJY; X-ray; 2.70 A; B/D=496-531.
DR PDBsum; 1KJY; -.
DR AlphaFoldDB; O08773; -.
DR BMRB; O08773; -.
DR SMR; O08773; -.
DR CORUM; O08773; -.
DR STRING; 10116.ENSRNOP00000021596; -.
DR iPTMnet; O08773; -.
DR PhosphoSitePlus; O08773; -.
DR PaxDb; O08773; -.
DR PRIDE; O08773; -.
DR ABCD; O08773; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000021596; ENSRNOP00000021596; ENSRNOG00000015616.
DR GeneID; 114705; -.
DR KEGG; rno:114705; -.
DR UCSC; RGD:620003; rat.
DR CTD; 10636; -.
DR RGD; 620003; Rgs14.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000161364; -.
DR InParanoid; O08773; -.
DR OMA; SQGCLPR; -.
DR OrthoDB; 275783at2759; -.
DR PhylomeDB; O08773; -.
DR TreeFam; TF328814; -.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR EvolutionaryTrace; O08773; -.
DR PRO; PR:O08773; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000015616; Expressed in thymus and 17 other tissues.
DR Genevisible; O08773; RN.
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:RGD.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0016604; C:nuclear body; ISS: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; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IDA:UniProtKB.
DR GO; GO:0032794; F:GTPase activating protein binding; ISO:RGD.
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; IPI:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; ISS: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; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA: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; IDA:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP: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; IDA:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0007051; P:spindle organization; ISS:UniProtKB.
DR GO; GO:0008542; P:visual learning; IMP: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 IDEAL; IID50254; -.
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; 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; 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..544
FT /note="Regulator of G-protein signaling 14"
FT /id="PRO_0000204219"
FT DOMAIN 67..184
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 300..371
FT /note="RBD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 373..443
FT /note="RBD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 497..519
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 297..424
FT /note="Necessary for interaction with RABGEF1"
FT /evidence="ECO:0000250"
FT REGION 449..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97492"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 258
FT /note="S->A: Inhibits phosphorylation; when associated with
FT A-494."
FT /evidence="ECO:0000269|PubMed:12534294"
FT MUTAGEN 333
FT /note="R->L: Abolishes the inhibition of PDGF-mediated
FT ERK1/ERK2 phosphorylation. Inhibits interaction with HRAS
FT and does not colocalize with active GTP-bound form of HRAS
FT at membranes. Does not inhibit interaction with BRAF or
FT RAF1."
FT /evidence="ECO:0000269|PubMed:19878719"
FT MUTAGEN 406
FT /note="H->A: Does not inhibit interaction and
FT colocalization with active GTP-bound form of HRAS at
FT membranes. Does not inhibit interaction with BRAF or RAF1."
FT /evidence="ECO:0000269|PubMed:19878719"
FT MUTAGEN 494
FT /note="T->A: Does not increase the GDI activity against
FT GNAI1. Does not alter GTPase activity against GNAO1 or
FT GNAI1. Inhibits phosphorylation; when associated with A-
FT 258."
FT /evidence="ECO:0000269|PubMed:12534294"
FT MUTAGEN 494
FT /note="T->D: Increases the GDI activity against GNAI1. Does
FT not alter GTPase activity against GNAO1 or GNAI1."
FT /evidence="ECO:0000269|PubMed:12534294"
FT MUTAGEN 494
FT /note="T->E: Increases the GDI activity against GNAI1. Does
FT not alter GTPase activity against GNAO1 or GNAI1."
FT /evidence="ECO:0000269|PubMed:12534294"
FT MUTAGEN 508
FT /note="Q->L: Inhibits the interaction with GNAI1."
FT /evidence="ECO:0000269|PubMed:17603074"
FT MUTAGEN 518
FT /note="L->Y: Increases the interaction with GNAI1."
FT /evidence="ECO:0000269|PubMed:17603074"
FT MUTAGEN 525
FT /note="V->W: Increases the interaction with GNAI1."
FT /evidence="ECO:0000269|PubMed:17603074"
FT MUTAGEN 529
FT /note="F->W: Increases the interaction with GNAI1."
FT /evidence="ECO:0000269|PubMed:17603074"
FT HELIX 497..505
FT /evidence="ECO:0007829|PDB:1KJY"
FT TURN 506..509
FT /evidence="ECO:0007829|PDB:1KJY"
FT HELIX 510..513
FT /evidence="ECO:0007829|PDB:1KJY"
FT HELIX 521..524
FT /evidence="ECO:0007829|PDB:1KJY"
SQ SEQUENCE 544 AA; 59492 MW; FF6B24BD2F593B4E CRC64;
MPGKPKHLGV PNGRMVLAVS DGELTSTSGS QAQGEGRGSS LSIHSLPSGP SSPFSTDEQP
VASWAQSFER LLQDPRGLAY FTEFLKKEFS AENVTFWQAC ERFQQIPASD TKQLAQEAHN
IYHEFLSSQA LSPVNIDRQA WLSEEVLAQP RPDMFRAQQL QIFNLMKFDS YARFVKSPLY
QECLLAEAEG RPLREPGSSH LGSPDTARKK PKLKPGKSLP LGVEELGQLP LAEGRPLRKS
FRREMPGGAV NSALRRESQG SLNSSASLDL GFLAFVSSKS ESHRKSLGSG EGESESRPGK
YCCVYLPDGT ASLALARPGL TIRDMLAGIC EKRGLSLPDI KVYLVGKEQK ALVLDQDCTV
LADQEVRLEN RITFQLELVG LERVVRISAK PTKRLQEALQ PILAKHGLSL DQVVLHRPGE
KQLVDLENLV SSVASQTLVL DTLPDAKTRE ASSIPPCRSQ GCLPRTQTKD SHLPPLSSSL
SVEDASGSTG KRQTCDIEGL VELLNRVQSS GAHDQRGLLR KEDLVLPEFL QLPSQRPGSQ
EAPP
