P97492 (RGS14_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Regulator of G-protein signaling 14
Short name=RGS14

Alternative name(s):
RAP1/RAP2-interacting protein
Short name=RPIP1

Gene names

Name:

Rgs14

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	547 AA.
Sequence status	Complete.
Protein existence	Evidence 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 HRAS1 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.13
Subunit structure	Found in a complex with at least BRAF, HRAS1, MAP2K1, MAPK3 and RGS14. Interacts with RIC8A (via C-terminus). Interacts (via RBD 1 domain) with HRAS1 (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. Nucleus › PML body. Cytoplasm. Membrane. Cell membrane By similarity. Cytoplasm › cytoskeleton › spindle. Cytoplasm › cytoskeleton › spindle pole By similarity. Cytoplasm › cytoskeleton › centrosome. Cell projection › dendrite. Cell projection › dendritic spine. Cell junction › synapse › postsynaptic cell membrane › postsynaptic 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 HRAS1. 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.13 Ref.14
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.13 Ref.14
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.13
Sequence similarities	Contains 1 GoLoco domain. Contains 2 RBD (Ras-binding) domains. Contains 1 RGS domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Microtubule Nucleus Postsynaptic cell membrane Synapse
Domain	Repeat
Molecular function	Developmental protein GTPase activation Signal transduction inhibitor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor signaling pathway Traceable author statement PubMed 11342430. Source: MGI chromosome segregation Inferred from mutant phenotype Ref.7. Source: UniProtKB long-term memory Inferred from mutant phenotype Ref.13. Source: UniProtKB long-term synaptic potentiation Inferred from direct assay Ref.13. Source: UniProtKB mitosis 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.13. Source: UniProtKB negative regulation of synaptic plasticity Inferred from mutant phenotype Ref.13. 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 neurogenesis Inferred from sequence or structural similarity. Source: UniProtKB regulation of DNA-dependent 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_component	PML 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 intermediate filament cytoskeleton Inferred from electronic annotation. Source: Compara microtubule Inferred from electronic annotation. Source: UniProtKB-KW nuclear body Inferred from direct assay Ref.9. Source: UniProtKB plasma membrane Inferred from direct assay Ref.5. Source: UniProtKB postsynaptic density Inferred from direct assay Ref.13. Source: UniProtKB postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW spindle pole Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	GDP-dissociation inhibitor activity Inferred from sequence or structural similarity. Source: UniProtKB GTPase activator activity Inferred from direct assay Ref.5. Source: UniProtKB microtubule binding Inferred from sequence or structural similarity. 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 547

547

Regulator of G-protein signaling 14

PRO_0000204218

Regions

Domain

67 – 184

118

RGS

Domain

303 – 374

72

RBD 1

Domain

376 – 446

71

RBD 2

Domain

500 – 522

23

GoLoco

Region

300 – 427

128

Necessary for interaction with RABGEF1

Amino acid modifications

Modified residue

20

1

Phosphoserine By similarity

Modified residue

42

1

Phosphoserine By similarity

Modified residue

45

1

Phosphoserine By similarity

Modified residue

289

1

Phosphoserine Ref.12

Experimental info

Mutagenesis

92 – 93

2

EN → 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.

Mutagenesis

261

1

S → A: Does not affect subcellular location; when associated with A-497. Ref.9

Mutagenesis

336

1

R → L: Reduces interaction with RABGEF1 and RAP2A. Strongly reduces interaction with RAP2A; when associated with L-409. Ref.6 Ref.9 Ref.10

Mutagenesis

409

1

H → L: Does not reduce interaction with RAP2A. Strongly reduces interaction with RAP2A; when associated with L-336. Ref.9 Ref.10

Mutagenesis

497

1

T → A: Does not affect subcellular location; when associated with A-261. Ref.9

Mutagenesis

506 – 507

2

LL → AA: Strongly expressed in the nucleus, mainly associated with PML nuclear bodies but not with centrosomes. Promotes gene transcription activation.

Mutagenesis

518

1

Q → 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

Mutagenesis

519

1

R → 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 conflict

209

1

Missing in BAB22436. Ref.4

Sequence conflict

431

1

N → T in AAB41893. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

547

Helix Strand Turn

Details...

Beta strand

375 – 392

18

Beta strand

394 – 397

4

Turn

398 – 402

5

Helix

403 – 406

4

Turn

407 – 410

4

Turn

413 – 415

3

Helix

433 – 435

3

Beta strand

436 – 439

4

Beta strand

441 – 443

3

Beta strand

451 – 454

4

Sequences

	Sequence		Length	Mass (Da)
	P97492 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 51BDE89E58F1E2C3	FASTA	547	59,847
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, MASS SPECTROMETRY. Tissue: Melanoma.
[13]	"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.
[14]	"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.
[15]	"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.

IPI

IPI00125649.

RefSeq

NP_058038.2. NM_016758.3.

UniGene

Mm.1426.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WFY	NMR	-	A	366-456	[»]

ProteinModelPortal

P97492.

SMR

P97492. Positions 56-189, 303-459, 499-534.

ModBase

Search...

Protein-protein interaction databases

IntAct

P97492. 1 interaction.

MINT

MINT-4132298.

STRING

10090.ENSMUSP00000068731.

PTM databases

PhosphoSite

P97492.

Proteomic databases

PaxDb

P97492.

PRIDE

P97492.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000063771; ENSMUSP00000068731; ENSMUSG00000052087.

GeneID

51791.

KEGG

mmu:51791.

UCSC

uc007qqq.2. mouse.

Organism-specific databases

CTD

10636.

MGI

MGI:1859709. Rgs14.

Phylogenomic databases

eggNOG

NOG253607.

GeneTree

ENSGT00700000104412.

HOGENOM

HOG000049111.

HOVERGEN

HBG061568.

InParanoid

Q8K2R4.

KO

K16449.

OMA

CPPRTQD.

OrthoDB

EOG4RR6HP.

Gene expression databases

ArrayExpress

P97492.

Bgee

P97492.

CleanEx

MM_RGS14.

Genevestigator

P97492.

GermOnline

ENSMUSG00000052087. Mus musculus.

Family and domain databases

Gene3D

1.10.196.10. 1 hit.

InterPro

IPR003109. GoLoco_motif.
IPR003116. Raf-like_ras-bd.
IPR000342. Regulat_G_prot_signal.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
[Graphical view]

Pfam

PF02188. GoLoco. 1 hit.
PF02196. RBD. 2 hits.
PF00615. RGS. 1 hit.
[Graphical view]

PRINTS

PR01301. RGSPROTEIN.

SMART

SM00390. GoLoco. 1 hit.
SM00455. RBD. 2 hits.
SM00315. RGS. 1 hit.
[Graphical view]

SUPFAM

SSF48097. Regulat_G_prot_signal_superfam. 1 hit.

PROSITE

PS50877. GOLOCO. 1 hit.
PS50898. RBD. 2 hits.
PS50132. RGS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P97492.

NextBio

308020.

SOURCE

Search...

Entry information

Entry name

RGS14_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program