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P97492 (RGS14_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of G-protein signaling 14

Short name=RGS14
Alternative name(s):
RAP1/RAP2-interacting protein
Short name=RPIP1
Gene names
Name:Rgs14
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length547 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a regulator of G protein signaling (RGS). Modulates G protein alpha subunits nucleotide exchange and hydrolysis activities by functioning either as a GTPase-activating protein (GAP), thereby driving G protein alpha subunits into their inactive GDP-bound form, or as a GDP-dissociation inhibitor (GDI). Confers GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but not G(o) alpha subunit GNAO1 and G(i) alpha subunit GNAI2. Confers GAP activity on G(o) alpha subunit GNAI0 and G(i) alpha subunits GNAI2 and GNAI3. May act as a scaffold integrating G protein and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a process depending on its interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism. Plays a role in cell division; required for completion of the first mitotic division of the embryo. Involved in visual memory processing capacity; when overexpressed in the V2 secondary visual cortex area. Involved in hippocampal-based learning and memory; acts as a suppressor of synaptic plasticity in CA2 neurons. Required for the nerve growth factor (NGF)-mediated neurite outgrowth. Involved in stress resistance. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.12

Subunit structure

Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14. Interacts with RIC8A (via C-terminus). Interacts (via RBD 1 domain) with HRAS (active GTP-bound form preferentially). Interacts (via RBD domains) with BRAF (via N-terminus); the interaction mediates the formation of a ternary complex with RAF1. Interacts (via RBD domains) with RAF1 (via N-terminus); the interaction mediates the formation of a ternary complex with BRAF. Interacts with KRAS (active GTP-bound form preferentially), MRAS (active GTP-bound form preferentially), NRAS (active GTP-bound form preferentially) and RRAS (active GTP-bound form preferentially). Interacts with GNAI1 (via active GTP- or inactive GDP-bound forms); the interaction prevents association of RGS14 with centrosomes or nuclear localization. Interacts with GNAI2. Interacts with GNAI3 (via active GTP- or inactive GDP-bound forms); the interaction prevents association of RGS14 with centrosomes or nuclear localization. Associates with microtubules By similarity. Interacts with GNAO1 and GNAI2. Interacts (via RGS and GoLoco domains) GNAI1; the interaction occurs in the centrosomes. Interacts with RABGEF1; the interactions is GTP-dependent. Interacts with RAP2A; the interactions is GTP-dependent and does not alter its function on G(i) alpha subunits either as GAP or as GDI. Ref.5 Ref.6 Ref.11

Subcellular location

Nucleus. NucleusPML body. Cytoplasm. Membrane. Cell membrane By similarity. Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle pole By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cell projectiondendrite. Cell projectiondendritic spine. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Note: Localizes with spindle poles during metaphase. Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. Recruited from the cytosol to the plasma membrane by the inactive GDP-bound forms of G(i) alpha subunits GNAI1 and GNAI3. Recruited from the cytosol to membranes by the active GTP-bound form of HRAS. Colocalizes with G(i) alpha subunit GNAI1 and RIC8A at the plasma membrane. Colocalizes with BRAF and RAF1 in both the cytoplasm and membranes By similarity. Associates with the perinuclear sheaths of microtubules (MTs) surrounding the pronuclei, prior to segregating to the anastral mitotic apparatus and subsequently the barrel- shaped cytoplasmic bridge between the nascent nuclei of the emerging 2-cell embryo. Localizes to a perinuclear compartment near the microtubule-organizing center (MTOC). Expressed in the nucleus during interphase and segregates to the centrosomes and astral MTs during mitosis. Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. Relocalizes to the nucleus in PML nuclear bodies in respons to heat stress. Colocalizes with RIC8A in CA2 hippocampal neurons. Ref.5 Ref.8 Ref.9 Ref.12 Ref.13

Tissue specificity

Expressed in pyramidal neurons of the CA1, CA2 and fasciola cinerea (FC) subregions of the hippocampus and in the olfactory cortex (at protein level). Expressed in brain, spleen, heart, liver, lung, kidney, skin and thymus (at protein level). Expressed in granular layer of the cerebellum, forbrain, striatum, layer V of the cortex, olfactory cortex, tubercules, subthalamic and hippocampus, particularly in the CA2 region, to a lesser extent in the CA1 region and the external layer of the dentate gyrus. Expressed in neurons. Ref.5 Ref.7 Ref.12 Ref.13

Developmental stage

Expressed in germinal vesicle oocytes, not in metaphase II oocytes. Expressed in embryo from 8.5 through 16.5 dpc (at protein level). Expressed in the zygote through to the blastocyst stage. Expressed in area lateral to the rhombencephalic floor plate at 12 dpc. Expressed in the anterior region of the brain, including the telencephalic olfactive nuclei and the hippocampus anlage at 17 dpc. Ref.5 Ref.7

Domain

The RGS domain is necessary for GTPase-activating protein (GAP) activity for G subunits and localization to the nucleus and centrosomes By similarity.

The GoLoco domain is necessary for GDP-dissociation inhibitor (GDI) activity, translocation out of the nucleus and interaction with G(i) alpha subunits GNAI1, GNAI2 and GNAI3 By similarity.

The RBD domains are necessary for localization to the nucleus and centrosomes By similarity.

Post-translational modification

Phosphorylated by PKC. Phosphorylation is increased in presence of forskolin and may enhance the GDI activity on G(i) alpha subunit GNAI1 By similarity.

Disruption phenotype

No visible phenotype. Mice show an enhancement of postsynaptic long-term potentiation (LTP) responses in the CA2 neurons of the hippocampus that is correlated with an increase of spatial learning and object recognition memory (OMR). Ref.7 Ref.12

Sequence similarities

Contains 1 GoLoco domain.

Contains 2 RBD (Ras-binding) domains.

Contains 1 RGS domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Microtubule
Nucleus
Postsynaptic cell membrane
Synapse
   DomainRepeat
   Molecular functionDevelopmental protein
GTPase activation
Signal transduction inhibitor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 11342430. Source: MGI

cell division

Inferred from sequence or structural similarity. Source: UniProtKB

chromosome segregation

Inferred from mutant phenotype Ref.7. Source: UniProtKB

intracellular signal transduction

Inferred from direct assay Ref.5. Source: GOC

learning

Inferred from mutant phenotype Ref.12. Source: UniProtKB

long-term memory

Inferred from mutant phenotype Ref.12. Source: UniProtKB

long-term synaptic potentiation

Inferred from direct assay Ref.12. Source: UniProtKB

mitotic nuclear division

Inferred from mutant phenotype Ref.7. Source: MGI

negative regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of MAP kinase activity

Inferred from mutant phenotype Ref.12. Source: UniProtKB

negative regulation of synaptic plasticity

Inferred from mutant phenotype Ref.12. Source: UniProtKB

nucleocytoplasmic transport

Inferred from direct assay Ref.9. Source: UniProtKB

platelet-derived growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of GTPase activity

Inferred from direct assay Ref.5. Source: GOC

positive regulation of neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of DNA-templated transcription in response to stress

Inferred from direct assay Ref.9. Source: UniProtKB

response to oxidative stress

Inferred from sequence or structural similarity. Source: UniProtKB

spindle organization

Inferred from mutant phenotype Ref.7. Source: UniProtKB

termination of G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

visual learning

Inferred from sequence or structural similarity. Source: UniProtKB

zygote asymmetric cell division

Inferred from mutant phenotype Ref.7. Source: UniProtKB

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

centrosome

Inferred from direct assay Ref.9Ref.7. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.5Ref.9Ref.7. Source: UniProtKB

dendrite

Inferred from direct assay Ref.12. Source: UniProtKB

dendritic spine

Inferred from direct assay Ref.12. Source: UniProtKB

intermediate filament cytoskeleton

Inferred from electronic annotation. Source: Ensembl

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear body

Inferred from direct assay Ref.9. Source: UniProtKB

nucleus

Inferred from direct assay Ref.9Ref.7. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.5. Source: UniProtKB

postsynaptic density

Inferred from direct assay Ref.12. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-KW

spindle

Inferred from direct assay Ref.7Ref.8. Source: UniProtKB

spindle pole

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionGDP-dissociation inhibitor activity

Inferred from sequence or structural similarity. Source: UniProtKB

GTPase activating protein binding

Inferred from physical interaction Ref.5Ref.11. Source: UniProtKB

GTPase activator activity

Inferred from direct assay Ref.5. Source: UniProtKB

microtubule binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

receptor signaling complex scaffold activity

Inferred from sequence or structural similarity. Source: UniProtKB

receptor signaling protein activity

Inferred from direct assay Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 547547Regulator of G-protein signaling 14
PRO_0000204218

Regions

Domain67 – 184118RGS
Domain303 – 37472RBD 1
Domain376 – 44671RBD 2
Domain500 – 52223GoLoco
Region300 – 427128Necessary for interaction with RABGEF1

Amino acid modifications

Modified residue201Phosphoserine By similarity
Modified residue421Phosphoserine By similarity
Modified residue451Phosphoserine By similarity

Experimental info

Mutagenesis92 – 932EN → AA: Inhibits GAP activity. Does not inhibit interaction with GNAI1 in the centrosomes. Reduces the down-regulation of G(i)-dependent signaling. Does not affect subcellular location and does not promote gene transcription activation. Inhibits strongly the down-regulation of G(i)-dependent signaling; when associated with F-519. Inhibits the interaction with GNAI1 in the centrosomes; when associated with A-518.
Mutagenesis2611S → A: Does not affect subcellular location; when associated with A-497. Ref.9
Mutagenesis3361R → L: Reduces interaction with RABGEF1 and RAP2A. Strongly reduces interaction with RAP2A; when associated with L-409. Ref.6 Ref.9 Ref.10
Mutagenesis4091H → L: Does not reduce interaction with RAP2A. Strongly reduces interaction with RAP2A; when associated with L-336. Ref.9 Ref.10
Mutagenesis4971T → A: Does not affect subcellular location; when associated with A-261. Ref.9
Mutagenesis506 – 5072LL → AA: Strongly expressed in the nucleus, mainly associated with PML nuclear bodies but not with centrosomes. Promotes gene transcription activation.
Mutagenesis5181Q → A: Inhibits GDI activity. Does not inhibit interaction with GNAI1 in the centrosomes, does not affect subcellular location and does not promote gene transcription activation. Inhibits interaction with GNAI1 in the centrosomes; when associated with A-92-93-A. Ref.9 Ref.11
Mutagenesis5191R → F: Reduces interaction with GNAI1 and GNAI2. Inhibits strongly the down-regulation of G(i)-dependent signaling; when associated with A-92-93-A. Ref.6
Sequence conflict2091Missing in BAB22436. Ref.4
Sequence conflict4311N → T in AAB41893. Ref.1

Secondary structure

................. 547
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P97492 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 51BDE89E58F1E2C3

FASTA54759,847
        10         20         30         40         50         60 
MPGKPKHLGV PNGRMVLAVS DGELTSTAGS QAQGEGRGSS LSIHSLPSGP SSPFSTEEQP 

        70         80         90        100        110        120 
VASWAQSFER LLQDPRGLAY FTEFLKKEFS AENVTFWKAC ERFQQIPASD TKQLAQEAHN 

       130        140        150        160        170        180 
IYHEFLSSQA LSPVNIDRQA WLSEEVLAQP RPDMFRAQQL QIFNLMKFDS YARFVKSPLY 

       190        200        210        220        230        240 
QECLLAEAEG RPLREPGSSH LGSPDTARKK PKLKPGKSLP LGVEELGQLP LAEGPCGRPL 

       250        260        270        280        290        300 
RKSFRREMTG GAMNSALRRE SQGSLNSSAS LDLGFLAFVS SKSESHRKSL GSGESESESR 

       310        320        330        340        350        360 
PGKYCCVYLP DGTASLALAR PGLTIRDMLA GICEKRGLSL PDIKVYLVGN EQKALVLDQD 

       370        380        390        400        410        420 
CTVLADQEVR LENRITFQLE LVGLERVVRI SAKPTKRLQE ALQPILAKHG LSLDQVVLHR 

       430        440        450        460        470        480 
PGEKQPMDLE NPVSSVASQT LVLDTPPDAK MSEARSISPC RSQGCLPRTQ TKDSHLPPSS 

       490        500        510        520        530        540 
SSLLVEDASS STGNRQTCDI EGLVELLNRV QSSGAHDQRG LLRKEDLVLP EFLQLPSQRP 


GSREAPP 

« Hide

References

« Hide 'large scale' references
[1]Janoueix-Lerosey I., Tavitian A., de Gunzburg J.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N-3.
Tissue: Mammary tumor.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-547.
Strain: C57BL/6J.
Tissue: Kidney.
[5]"RGS14 is a novel Rap effector that preferentially regulates the GTPase activity of galphao."
Traver S., Bidot C., Spassky N., Baltauss T., De Tand M.F., Thomas J.L., Zalc B., Janoueix-Lerosey I., Gunzburg J.D.
Biochem. J. 350:19-29(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GNAO1, RABGEF1 AND RAP2A, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[6]"The RGS (regulator of G-protein signalling) and GoLoco domains of RGS14 co-operate to regulate Gi-mediated signalling."
Traver S., Splingard A., Gaudriault G., De Gunzburg J.
Biochem. J. 379:627-632(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GNAI1; GNAI2; RABGEF1 AND RAP2A, MUTAGENESIS OF 92-GLU-ASN-93; ARG-336 AND ARG-519.
[7]"RGS14 is a mitotic spindle protein essential from the first division of the mammalian zygote."
Martin-McCaffrey L., Willard F.S., Oliveira-dos-Santos A.J., Natale D.R., Snow B.E., Kimple R.J., Pajak A., Watson A.J., Dagnino L., Penninger J.M., Siderovski D.P., D'Souza S.J.
Dev. Cell 7:763-769(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[8]"RGS14 is a microtubule-associated protein."
Martin-McCaffrey L., Willard F.S., Pajak A., Dagnino L., Siderovski D.P., D'Souza S.J.
Cell Cycle 4:953-960(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"RGS14 is a centrosomal and nuclear cytoplasmic shuttling protein that traffics to promyelocytic leukemia nuclear bodies following heat shock."
Cho H., Kim D.U., Kehrl J.H.
J. Biol. Chem. 280:805-814(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 92-GLU-ASN-93; SER-261; ARG-336; HIS-409; THR-497; 506-LEU-LEU-507 AND GLN-518.
[10]"Biochemical characterization of RGS14: RGS14 activity towards G-protein alpha subunits is independent of its binding to Rap2A."
Mittal V., Linder M.E.
Biochem. J. 394:309-315(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-336 AND HIS-409.
[11]"Localization of Gi alpha proteins in the centrosomes and at the midbody: implication for their role in cell division."
Cho H., Kehrl J.H.
J. Cell Biol. 178:245-255(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GNAI1, MUTAGENESIS OF 92-GLU-ASN-93 AND GLN-518.
[12]"RGS14 is a natural suppressor of both synaptic plasticity in CA2 neurons and hippocampal-based learning and memory."
Lee S.E., Simons S.B., Heldt S.A., Zhao M., Schroeder J.P., Vellano C.P., Cowan D.P., Ramineni S., Yates C.K., Feng Y., Smith Y., Sweatt J.D., Weinshenker D., Ressler K.J., Dudek S.M., Hepler J.R.
Proc. Natl. Acad. Sci. U.S.A. 107:16994-16998(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[13]"Activation of the regulator of G protein signaling 14-Galphai1-GDP signaling complex is regulated by resistance to inhibitors of cholinesterase-8A."
Vellano C.P., Shu F.J., Ramineni S., Yates C.K., Tall G.G., Hepler J.R.
Biochemistry 50:752-762(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[14]"Solution structure of the RAS-binding domain of mouse RGS14."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 366-456.
+Additional computationally mapped references.

Web resources

Protein Spotlight

A balanced mind - Issue 132 of October 2011

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85055 mRNA. Translation: AAB41893.1.
CT009762 Genomic DNA. Translation: CAX16109.1.
BC030321 mRNA. Translation: AAH30321.1.
AK002891 mRNA. Translation: BAB22436.1.
CCDSCCDS36674.1.
RefSeqNP_058038.2. NM_016758.3.
UniGeneMm.1426.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WFYNMR-A366-456[»]
ProteinModelPortalP97492.
SMRP97492. Positions 56-189, 365-459, 499-534.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206175. 1 interaction.
IntActP97492. 2 interactions.
MINTMINT-4132298.
STRING10090.ENSMUSP00000068731.

PTM databases

PhosphoSiteP97492.

Proteomic databases

MaxQBP97492.
PaxDbP97492.
PRIDEP97492.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063771; ENSMUSP00000068731; ENSMUSG00000052087.
GeneID51791.
KEGGmmu:51791.
UCSCuc007qqq.2. mouse.

Organism-specific databases

CTD10636.
MGIMGI:1859709. Rgs14.

Phylogenomic databases

eggNOGNOG253607.
GeneTreeENSGT00700000104412.
HOGENOMHOG000049111.
HOVERGENHBG061568.
InParanoidQ8K2R4.
KOK17706.
OMAPPRTQDK.
OrthoDBEOG7XDBF0.
TreeFamTF328814.

Gene expression databases

ArrayExpressP97492.
BgeeP97492.
CleanExMM_RGS14.
GenevestigatorP97492.

Family and domain databases

Gene3D1.10.196.10. 1 hit.
InterProIPR003109. GoLoco_motif.
IPR003116. Raf-like_ras-bd.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF02188. GoLoco. 1 hit.
PF02196. RBD. 2 hits.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR01301. RGSPROTEIN.
SMARTSM00390. GoLoco. 1 hit.
SM00455. RBD. 2 hits.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
SSF54236. SSF54236. 2 hits.
PROSITEPS50877. GOLOCO. 1 hit.
PS50898. RBD. 2 hits.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP97492.
NextBio308020.
PROP97492.
SOURCESearch...

Entry information

Entry nameRGS14_MOUSE
AccessionPrimary (citable) accession number: P97492
Secondary accession number(s): Q8K2R4, Q9DCD1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot