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P97492

- RGS14_MOUSE

UniProt

P97492 - RGS14_MOUSE

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Protein

Regulator of G-protein signaling 14

Gene
Rgs14
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.6 Publications

GO - Molecular functioni

  1. GDP-dissociation inhibitor activity Source: UniProtKB
  2. GTPase activating protein binding Source: UniProtKB
  3. GTPase activator activity Source: UniProtKB
  4. microtubule binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. receptor signaling complex scaffold activity Source: UniProtKB
  7. receptor signaling protein activity Source: UniProtKB

GO - Biological processi

  1. cell division Source: UniProtKB
  2. chromosome segregation Source: UniProtKB
  3. G-protein coupled receptor signaling pathway Source: MGI
  4. intracellular signal transduction Source: GOC
  5. learning Source: UniProtKB
  6. long-term memory Source: UniProtKB
  7. long-term synaptic potentiation Source: UniProtKB
  8. mitotic nuclear division Source: MGI
  9. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
  10. negative regulation of MAP kinase activity Source: UniProtKB
  11. negative regulation of synaptic plasticity Source: UniProtKB
  12. nucleocytoplasmic transport Source: UniProtKB
  13. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  14. positive regulation of GTPase activity Source: GOC
  15. positive regulation of neurogenesis Source: UniProtKB
  16. regulation of DNA-templated transcription in response to stress Source: UniProtKB
  17. response to oxidative stress Source: UniProtKB
  18. spindle organization Source: UniProtKB
  19. termination of G-protein coupled receptor signaling pathway Source: InterPro
  20. visual learning Source: UniProtKB
  21. zygote asymmetric cell division Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, GTPase activation, Signal transduction inhibitor

Keywords - Biological processi

Cell cycle, Cell division

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 14
Short name:
RGS14
Alternative name(s):
RAP1/RAP2-interacting protein
Short name:
RPIP1
Gene namesi
Name:Rgs14
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1859709. Rgs14.

Subcellular locationi

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.5 Publications

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. centrosome Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. dendrite Source: UniProtKB
  5. dendritic spine Source: UniProtKB
  6. intermediate filament cytoskeleton Source: Ensembl
  7. microtubule Source: UniProtKB-KW
  8. nuclear body Source: UniProtKB
  9. nucleus Source: UniProtKB
  10. plasma membrane Source: UniProtKB
  11. PML body Source: UniProtKB-SubCell
  12. postsynaptic density Source: UniProtKB
  13. postsynaptic membrane Source: UniProtKB-KW
  14. spindle Source: UniProtKB
  15. spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule, Nucleus, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

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).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi92 – 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.
Mutagenesisi261 – 2611S → A: Does not affect subcellular location; when associated with A-497. 1 Publication
Mutagenesisi336 – 3361R → L: Reduces interaction with RABGEF1 and RAP2A. Strongly reduces interaction with RAP2A; when associated with L-409. 3 Publications
Mutagenesisi409 – 4091H → L: Does not reduce interaction with RAP2A. Strongly reduces interaction with RAP2A; when associated with L-336. 2 Publications
Mutagenesisi497 – 4971T → A: Does not affect subcellular location; when associated with A-261. 1 Publication
Mutagenesisi506 – 5072LL → AA: Strongly expressed in the nucleus, mainly associated with PML nuclear bodies but not with centrosomes. Promotes gene transcription activation.
Mutagenesisi518 – 5181Q → 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. 2 Publications
Mutagenesisi519 – 5191R → F: Reduces interaction with GNAI1 and GNAI2. Inhibits strongly the down-regulation of G(i)-dependent signaling; when associated with A-92-93-A. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Regulator of G-protein signaling 14PRO_0000204218Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphoserine By similarity
Modified residuei42 – 421Phosphoserine By similarity
Modified residuei45 – 451Phosphoserine By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP97492.
PaxDbiP97492.
PRIDEiP97492.

PTM databases

PhosphoSiteiP97492.

Expressioni

Tissue specificityi

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.4 Publications

Developmental stagei

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.2 Publications

Gene expression databases

ArrayExpressiP97492.
BgeeiP97492.
CleanExiMM_RGS14.
GenevestigatoriP97492.

Interactioni

Subunit structurei

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.3 Publications

Protein-protein interaction databases

BioGridi206175. 1 interaction.
IntActiP97492. 2 interactions.
MINTiMINT-4132298.
STRINGi10090.ENSMUSP00000068731.

Structurei

Secondary structure

1
547
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi375 – 39218
Beta strandi394 – 3974
Turni398 – 4025
Helixi403 – 4064
Turni407 – 4104
Turni413 – 4153
Helixi433 – 4353
Beta strandi436 – 4394
Beta strandi441 – 4433
Beta strandi451 – 4544

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WFYNMR-A366-456[»]
ProteinModelPortaliP97492.
SMRiP97492. Positions 56-189, 365-459, 499-534.

Miscellaneous databases

EvolutionaryTraceiP97492.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 184118RGSAdd
BLAST
Domaini303 – 37472RBD 1Add
BLAST
Domaini376 – 44671RBD 2Add
BLAST
Domaini500 – 52223GoLocoAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni300 – 427128Necessary for interaction with RABGEF1Add
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 GoLoco domain.
Contains 1 RGS domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG253607.
GeneTreeiENSGT00700000104412.
HOGENOMiHOG000049111.
HOVERGENiHBG061568.
InParanoidiQ8K2R4.
KOiK17706.
OMAiPPRTQDK.
OrthoDBiEOG7XDBF0.
TreeFamiTF328814.

Family and domain databases

Gene3Di1.10.196.10. 1 hit.
InterProiIPR003109. 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]
PfamiPF02188. GoLoco. 1 hit.
PF02196. RBD. 2 hits.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00390. GoLoco. 1 hit.
SM00455. RBD. 2 hits.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF54236. SSF54236. 2 hits.
PROSITEiPS50877. GOLOCO. 1 hit.
PS50898. RBD. 2 hits.
PS50132. RGS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97492-1 [UniParc]FASTAAdd to Basket

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MPGKPKHLGV PNGRMVLAVS DGELTSTAGS QAQGEGRGSS LSIHSLPSGP    50
SSPFSTEEQP VASWAQSFER LLQDPRGLAY FTEFLKKEFS AENVTFWKAC 100
ERFQQIPASD TKQLAQEAHN IYHEFLSSQA LSPVNIDRQA WLSEEVLAQP 150
RPDMFRAQQL QIFNLMKFDS YARFVKSPLY QECLLAEAEG RPLREPGSSH 200
LGSPDTARKK PKLKPGKSLP LGVEELGQLP LAEGPCGRPL RKSFRREMTG 250
GAMNSALRRE SQGSLNSSAS LDLGFLAFVS SKSESHRKSL GSGESESESR 300
PGKYCCVYLP DGTASLALAR PGLTIRDMLA GICEKRGLSL PDIKVYLVGN 350
EQKALVLDQD CTVLADQEVR LENRITFQLE LVGLERVVRI SAKPTKRLQE 400
ALQPILAKHG LSLDQVVLHR PGEKQPMDLE NPVSSVASQT LVLDTPPDAK 450
MSEARSISPC RSQGCLPRTQ TKDSHLPPSS SSLLVEDASS STGNRQTCDI 500
EGLVELLNRV QSSGAHDQRG LLRKEDLVLP EFLQLPSQRP GSREAPP 547
Length:547
Mass (Da):59,847
Last modified:July 27, 2011 - v2
Checksum:i51BDE89E58F1E2C3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091Missing in BAB22436. 1 Publication
Sequence conflicti431 – 4311N → T in AAB41893. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U85055 mRNA. Translation: AAB41893.1.
CT009762 Genomic DNA. Translation: CAX16109.1.
BC030321 mRNA. Translation: AAH30321.1.
AK002891 mRNA. Translation: BAB22436.1.
CCDSiCCDS36674.1.
RefSeqiNP_058038.2. NM_016758.3.
UniGeneiMm.1426.

Genome annotation databases

EnsembliENSMUST00000063771; ENSMUSP00000068731; ENSMUSG00000052087.
GeneIDi51791.
KEGGimmu:51791.
UCSCiuc007qqq.2. mouse.

Cross-referencesi

Web resourcesi

Protein Spotlight

A balanced mind - Issue 132 of October 2011

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U85055 mRNA. Translation: AAB41893.1 .
CT009762 Genomic DNA. Translation: CAX16109.1 .
BC030321 mRNA. Translation: AAH30321.1 .
AK002891 mRNA. Translation: BAB22436.1 .
CCDSi CCDS36674.1.
RefSeqi NP_058038.2. NM_016758.3.
UniGenei Mm.1426.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WFY NMR - A 366-456 [» ]
ProteinModelPortali P97492.
SMRi P97492. Positions 56-189, 365-459, 499-534.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 206175. 1 interaction.
IntActi P97492. 2 interactions.
MINTi MINT-4132298.
STRINGi 10090.ENSMUSP00000068731.

PTM databases

PhosphoSitei P97492.

Proteomic databases

MaxQBi P97492.
PaxDbi P97492.
PRIDEi P97492.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000063771 ; ENSMUSP00000068731 ; ENSMUSG00000052087 .
GeneIDi 51791.
KEGGi mmu:51791.
UCSCi uc007qqq.2. mouse.

Organism-specific databases

CTDi 10636.
MGIi MGI:1859709. Rgs14.

Phylogenomic databases

eggNOGi NOG253607.
GeneTreei ENSGT00700000104412.
HOGENOMi HOG000049111.
HOVERGENi HBG061568.
InParanoidi Q8K2R4.
KOi K17706.
OMAi PPRTQDK.
OrthoDBi EOG7XDBF0.
TreeFami TF328814.

Miscellaneous databases

EvolutionaryTracei P97492.
NextBioi 308020.
PROi P97492.
SOURCEi Search...

Gene expression databases

ArrayExpressi P97492.
Bgeei P97492.
CleanExi MM_RGS14.
Genevestigatori P97492.

Family and domain databases

Gene3Di 1.10.196.10. 1 hit.
InterProi IPR003109. 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 ]
Pfami PF02188. GoLoco. 1 hit.
PF02196. RBD. 2 hits.
PF00615. RGS. 1 hit.
[Graphical view ]
PRINTSi PR01301. RGSPROTEIN.
SMARTi SM00390. GoLoco. 1 hit.
SM00455. RBD. 2 hits.
SM00315. RGS. 1 hit.
[Graphical view ]
SUPFAMi SSF48097. SSF48097. 1 hit.
SSF54236. SSF54236. 2 hits.
PROSITEi PS50877. GOLOCO. 1 hit.
PS50898. RBD. 2 hits.
PS50132. RGS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. 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.

Entry informationi

Entry nameiRGS14_MOUSE
AccessioniPrimary (citable) accession number: P97492
Secondary accession number(s): Q8K2R4, Q9DCD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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