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Q9CX84

- RGS19_MOUSE

UniProt

Q9CX84 - RGS19_MOUSE

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Protein

Regulator of G-protein signaling 19

Gene

Rgs19

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G-alpha subfamily 1 members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein (By similarity).By similarity

GO - Molecular functioni

  1. GTPase activator activity Source: RefGenome

GO - Biological processi

  1. positive regulation of GTPase activity Source: GOC
  2. termination of G-protein coupled receptor signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Enzyme and pathway databases

ReactomeiREACT_207651. G alpha (q) signalling events.
REACT_250376. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 19
Short name:
RGS19
Gene namesi
Name:Rgs19
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1915153. Rgs19.

Subcellular locationi

Membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

  1. brush border Source: Ensembl
  2. clathrin-coated vesicle Source: Ensembl
  3. cytoplasm Source: RefGenome
  4. plasma membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 216216Regulator of G-protein signaling 19PRO_0000204230Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei97 – 971PhosphoserineBy similarity
Modified residuei151 – 1511Phosphoserine; by MAPK1 and MAPK3By similarity

Post-translational modificationi

Fatty acylated. Heavily palmitoylated in the cysteine string motif (By similarity).By similarity
Phosphorylated, mainly on serine residues.By similarity

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ9CX84.
PaxDbiQ9CX84.
PRIDEiQ9CX84.

PTM databases

PhosphoSiteiQ9CX84.

Expressioni

Gene expression databases

BgeeiQ9CX84.
CleanExiMM_RGS19.
ExpressionAtlasiQ9CX84. baseline and differential.
GenevestigatoriQ9CX84.

Interactioni

Subunit structurei

Interacts with GIPC PDZ domain.By similarity

Protein-protein interaction databases

BioGridi208006. 1 interaction.
IntActiQ9CX84. 2 interactions.
MINTiMINT-1341963.

Structurei

3D structure databases

ProteinModelPortaliQ9CX84.
SMRiQ9CX84. Positions 24-212.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini90 – 206117RGSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni207 – 21610Interaction with GIPCBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 4911Poly-CysAdd
BLAST

Sequence similaritiesi

Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG258376.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233513.
HOVERGENiHBG013233.
InParanoidiQ9CX84.
KOiK16449.
PhylomeDBiQ9CX84.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 1 hit.
InterProiIPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
[Graphical view]
PfamiPF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
PROSITEiPS50132. RGS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CX84-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPTPHEAEKQ HTGPEEADRP PSMSSHDAAP SGPPSRNPCC LCWCCCCSCS
60 70 80 90 100
WNQERQRAWQ VSRESKLQPL PSCEVCTPPS PKEVQSWAQS FDKLMHSPTG
110 120 130 140 150
RSVFRAFLRT EYSEENMLFW LACEELKAEA NQHVVDEKAR LIYEDYVSIL
160 170 180 190 200
SPKEVSLDSR VREGINRKMQ EPSPHTFDDA QLQIYTLMHR DSYPRFLTSP
210
TYRSLLLQGA PQSSEA
Length:216
Mass (Da):24,678
Last modified:June 1, 2001 - v1
Checksum:i4F166A6607184F31
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821K → E in AAH03838. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK019401 mRNA. Translation: BAB31703.1.
BC003838 mRNA. Translation: AAH03838.1.
CCDSiCCDS17220.1.
RefSeqiNP_001278135.1. NM_001291206.1.
NP_001278136.1. NM_001291207.1.
NP_001278138.1. NM_001291209.1.
NP_001278139.1. NM_001291210.1.
NP_080722.1. NM_026446.4.
XP_006500748.1. XM_006500685.1.
UniGeneiMm.274366.

Genome annotation databases

EnsembliENSMUST00000002532; ENSMUSP00000002532; ENSMUSG00000002458.
ENSMUST00000108776; ENSMUSP00000104406; ENSMUSG00000002458.
ENSMUST00000165416; ENSMUSP00000129026; ENSMUSG00000002458.
GeneIDi56470.
KEGGimmu:56470.
UCSCiuc008onc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK019401 mRNA. Translation: BAB31703.1 .
BC003838 mRNA. Translation: AAH03838.1 .
CCDSi CCDS17220.1.
RefSeqi NP_001278135.1. NM_001291206.1.
NP_001278136.1. NM_001291207.1.
NP_001278138.1. NM_001291209.1.
NP_001278139.1. NM_001291210.1.
NP_080722.1. NM_026446.4.
XP_006500748.1. XM_006500685.1.
UniGenei Mm.274366.

3D structure databases

ProteinModelPortali Q9CX84.
SMRi Q9CX84. Positions 24-212.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208006. 1 interaction.
IntActi Q9CX84. 2 interactions.
MINTi MINT-1341963.

PTM databases

PhosphoSitei Q9CX84.

Proteomic databases

MaxQBi Q9CX84.
PaxDbi Q9CX84.
PRIDEi Q9CX84.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000002532 ; ENSMUSP00000002532 ; ENSMUSG00000002458 .
ENSMUST00000108776 ; ENSMUSP00000104406 ; ENSMUSG00000002458 .
ENSMUST00000165416 ; ENSMUSP00000129026 ; ENSMUSG00000002458 .
GeneIDi 56470.
KEGGi mmu:56470.
UCSCi uc008onc.1. mouse.

Organism-specific databases

CTDi 10287.
MGIi MGI:1915153. Rgs19.

Phylogenomic databases

eggNOGi NOG258376.
GeneTreei ENSGT00760000118903.
HOGENOMi HOG000233513.
HOVERGENi HBG013233.
InParanoidi Q9CX84.
KOi K16449.
PhylomeDBi Q9CX84.
TreeFami TF315837.

Enzyme and pathway databases

Reactomei REACT_207651. G alpha (q) signalling events.
REACT_250376. G alpha (i) signalling events.

Miscellaneous databases

NextBioi 312734.
PROi Q9CX84.
SOURCEi Search...

Gene expression databases

Bgeei Q9CX84.
CleanExi MM_RGS19.
ExpressionAtlasi Q9CX84. baseline and differential.
Genevestigatori Q9CX84.

Family and domain databases

Gene3Di 1.10.196.10. 1 hit.
InterProi IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
[Graphical view ]
Pfami PF00615. RGS. 1 hit.
[Graphical view ]
PRINTSi PR01301. RGSPROTEIN.
SMARTi SM00315. RGS. 1 hit.
[Graphical view ]
SUPFAMi SSF48097. SSF48097. 1 hit.
PROSITEi PS50132. RGS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "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].
    Strain: C57BL/6J.
    Tissue: Embryonic head.
  2. "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].
    Tissue: Mammary tumor.

Entry informationi

Entry nameiRGS19_MOUSE
AccessioniPrimary (citable) accession number: Q9CX84
Secondary accession number(s): Q99L50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3