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Protein

Regulator of G-protein signaling 13

Gene

Rgs13

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein 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 both G(i)-alpha and G(q)-alpha.

GO - Biological processi

  • G-protein coupled receptor signaling pathway Source: MGI
  • negative regulation of G-protein coupled receptor protein signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 13
Short name:
RGS13
Gene namesi
Name:Rgs13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2180585. Rgs13.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158Regulator of G-protein signaling 13PRO_0000204216Add
BLAST

Proteomic databases

PaxDbiQ8K443.
PRIDEiQ8K443.

PTM databases

iPTMnetiQ8K443.
PhosphoSiteiQ8K443.

Expressioni

Gene expression databases

BgeeiQ8K443.
CleanExiMM_RGS13.
GenevisibleiQ8K443. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Tomm70aQ9CZW512EBI-645999,EBI-642469

Protein-protein interaction databases

BioGridi232932. 2 interactions.
IntActiQ8K443. 1 interaction.
STRINGi10090.ENSMUSP00000058813.

Structurei

3D structure databases

ProteinModelPortaliQ8K443.
SMRiQ8K443. Positions 32-146.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 150117RGSPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3589. Eukaryota.
ENOG410YMJD. LUCA.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233513.
HOVERGENiHBG013233.
InParanoidiQ8K443.
KOiK16449.
OMAiCWICKLC.
OrthoDBiEOG7VHSZ5.
PhylomeDBiQ8K443.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
InterProiIPR016137. RGS.
IPR024066. RGS_subdom1.
[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.

Q8K443-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRHICWICK LCRDESKRLP SNLTLDEVLK WAQSLESLMA TKYGPIVYTA
60 70 80 90 100
YLKLEHSDEN IKFWMACETY KKIASRRGRI SRAKKLYNIY IQPQSPREIN
110 120 130 140 150
IDSTTREAII KSIREPTQTC FEEAQKIVYM HMEMDSYPRF LKSEMYQQLL

KTVQSQSS
Length:158
Mass (Da):18,729
Last modified:October 1, 2002 - v1
Checksum:iAC5DD876F4020C1A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF498319 mRNA. Translation: AAM74139.1.
AK043268 mRNA. Translation: BAC31511.1.
BC049624 mRNA. Translation: AAH49624.1.
CCDSiCCDS15348.1.
RefSeqiNP_694811.1. NM_153171.4.
XP_006529676.1. XM_006529613.2.
UniGeneiMm.38271.

Genome annotation databases

EnsembliENSMUST00000052375; ENSMUSP00000058813; ENSMUSG00000051079.
ENSMUST00000111941; ENSMUSP00000107572; ENSMUSG00000051079.
GeneIDi246709.
KEGGimmu:246709.
UCSCiuc007cxh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF498319 mRNA. Translation: AAM74139.1.
AK043268 mRNA. Translation: BAC31511.1.
BC049624 mRNA. Translation: AAH49624.1.
CCDSiCCDS15348.1.
RefSeqiNP_694811.1. NM_153171.4.
XP_006529676.1. XM_006529613.2.
UniGeneiMm.38271.

3D structure databases

ProteinModelPortaliQ8K443.
SMRiQ8K443. Positions 32-146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi232932. 2 interactions.
IntActiQ8K443. 1 interaction.
STRINGi10090.ENSMUSP00000058813.

PTM databases

iPTMnetiQ8K443.
PhosphoSiteiQ8K443.

Proteomic databases

PaxDbiQ8K443.
PRIDEiQ8K443.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052375; ENSMUSP00000058813; ENSMUSG00000051079.
ENSMUST00000111941; ENSMUSP00000107572; ENSMUSG00000051079.
GeneIDi246709.
KEGGimmu:246709.
UCSCiuc007cxh.1. mouse.

Organism-specific databases

CTDi6003.
MGIiMGI:2180585. Rgs13.

Phylogenomic databases

eggNOGiKOG3589. Eukaryota.
ENOG410YMJD. LUCA.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233513.
HOVERGENiHBG013233.
InParanoidiQ8K443.
KOiK16449.
OMAiCWICKLC.
OrthoDBiEOG7VHSZ5.
PhylomeDBiQ8K443.
TreeFamiTF315837.

Miscellaneous databases

PROiQ8K443.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K443.
CleanExiMM_RGS13.
GenevisibleiQ8K443. MM.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
InterProiIPR016137. RGS.
IPR024066. RGS_subdom1.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RGS13 regulates germinal center B lymphocytes responsiveness to CXC chemokine ligand (CXCL)12 and CXCL13."
    Shi G.X., Harrison K., Wilson G.L., Moratz C., Kehrl J.H.
    J. Immunol. 169:2507-2515(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. "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: Cerebellum.
  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].
    Tissue: Brain.

Entry informationi

Entry nameiRGS13_MOUSE
AccessioniPrimary (citable) accession number: Q8K443
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 105 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.