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Protein

Regulator of G-protein signaling 7-binding protein

Gene

Rgs7bp

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

Functioni

Regulator of G protein-coupled receptor (GPCR) signaling. Regulatory subunit of the R7-Gbeta5 complexes that acts by controlling the subcellular location of the R7-Gbeta5 complexes. When palmitoylated, it targets the R7-Gbeta5 complexes to the plasma membrane, leading to inhibit G protein alpha subunits. When it is unpalmitoylated, the R7-Gbeta5 complexes undergo a nuclear/cypolasmic shuttling. May also act by controlling the proteolytic stability of R7 proteins, probably by protecting them from degradation.4 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 7-binding protein
Alternative name(s):
R7 family-binding protein
Gene namesi
Name:Rgs7bp
Synonyms:D13Bwg1146e, R7bp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:106334. Rgs7bp.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi242 – 2476Missing : Abolishes nuclear localization and palmitoylation. 1 Publication
Mutagenesisi243 – 2431R → E: Abolishes nuclear localization; when associated with E-246. 1 Publication
Mutagenesisi246 – 2461R → E: Abolishes nuclear localization; when associated with E-243. 1 Publication
Mutagenesisi252 – 2532CC → AA: Abolishes palmitoylation. 1 Publication
Mutagenesisi252 – 2521C → S: Strongly reduces palmitoylation and its ability to regulate GPCR signaling. Abolishes palmitoylation ant its ability to regulate GPCR signaling; when associated with S-253. 1 Publication
Mutagenesisi253 – 2531C → S: Strongly reduces palmitoylation and its ability to regulate GPCR signaling. Abolishes palmitoylation ant its ability to regulate GPCR signaling; when associated with S-252. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257Regulator of G-protein signaling 7-binding proteinPRO_0000287596Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi252 – 2521S-palmitoyl cysteine2 Publications
Lipidationi253 – 2531S-palmitoyl cysteine2 Publications

Post-translational modificationi

Palmitoylation regulates the cell membrane and nuclear shuttling and the regulation of GPCR signaling. Upon depalmitoylation, it is targeted into the nucleus.2 Publications

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

MaxQBiQ8BQP9.
PaxDbiQ8BQP9.
PeptideAtlasiQ8BQP9.
PRIDEiQ8BQP9.

PTM databases

iPTMnetiQ8BQP9.
PhosphoSiteiQ8BQP9.
SwissPalmiQ8BQP9.

Expressioni

Tissue specificityi

Specifically expressed in the central nervous system including the retina but not in other non-neuronal tissues (at protein level).2 Publications

Gene expression databases

BgeeiQ8BQP9.
GenevisibleiQ8BQP9. MM.

Interactioni

Subunit structurei

Interacts with 'R7' family proteins RGS6, RGS7, RGS9 and RGS11. Component of some R7-Gbeta5 complex composed of some R7 protein (RGS6, RGS7, RGS9 or RGS11), Gbeta5 (GNB5) and RGS7BP.2 Publications

Protein-protein interaction databases

BioGridi206866. 5 interactions.
STRINGi10090.ENSMUSP00000066614.

Structurei

3D structure databases

ProteinModelPortaliQ8BQP9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi242 – 2476Nuclear localization signal2 Publications

Domaini

The nuclear localization signal is both required for nuclear localization and palmitoylation.1 Publication

Sequence similaritiesi

Belongs to the RGS7BP/RGS9BP family.Curated

Phylogenomic databases

eggNOGiENOG410IH1X. Eukaryota.
ENOG410YXJD. LUCA.
GeneTreeiENSGT00390000006968.
HOGENOMiHOG000154060.
HOVERGENiHBG104928.
InParanoidiQ8BQP9.
OMAiGSLQLHR.
OrthoDBiEOG741Z2Z.
PhylomeDBiQ8BQP9.
TreeFamiTF330985.

Family and domain databases

InterProiIPR026512. RGS7BP/RGS9BP.
[Graphical view]
PANTHERiPTHR21029. PTHR21029. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8BQP9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSAPNGRKK RPSRSTRSSI FQISKPPLQS GDWERRGSGS ESAHKTQRAL
60 70 80 90 100
DDCKMLVQEF NTQVALYREL VISIGDVSVS CPSLRAEMHK TRTKGCEMAR
110 120 130 140 150
QAHQKLAAIS GPEDGEIHPE ICRLYIQLQC CLEMYTTEML KSICLLGSLQ
160 170 180 190 200
FHRKGKEASG GAKNLDSKIE ENAETPALED SLSSPLESQQ QCWQVATDIE
210 220 230 240 250
NTERDMREMK NLLSKLRETM PLPLKNQDDS SLLNLTPYPM VRRRKRRFFG

LCCLVSS
Length:257
Mass (Da):29,023
Last modified:March 1, 2003 - v1
Checksum:i1825969A5E64D544
GO

Sequence cautioni

The sequence BAC29358.1 differs from that shown. Reason: Frameshift at positions 36 and 217. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151S → A in BAB32250 (PubMed:16141072).Curated
Sequence conflicti47 – 471Q → R in BAB32250 (PubMed:16141072).Curated
Sequence conflicti73 – 731S → F in BAB32250 (PubMed:16141072).Curated
Sequence conflicti138 – 1381E → Q in BAE23346 (PubMed:16141072).Curated
Sequence conflicti146 – 1461L → V in BAB32250 (PubMed:16141072).Curated
Sequence conflicti188 – 1881S → G in AAI18958 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ104214 mRNA. Translation: AAZ09201.1.
AK020910 mRNA. Translation: BAB32250.1.
AK036240 mRNA. Translation: BAC29358.1. Frameshift.
AK046733 mRNA. Translation: BAC32849.1.
AK137417 mRNA. Translation: BAE23346.1.
BC118957 mRNA. Translation: AAI18958.1.
CCDSiCCDS36774.1.
RefSeqiNP_084155.2. NM_029879.2.
UniGeneiMm.100348.

Genome annotation databases

EnsembliENSMUST00000063551; ENSMUSP00000066614; ENSMUSG00000021719.
GeneIDi52882.
KEGGimmu:52882.
UCSCiuc007rtp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ104214 mRNA. Translation: AAZ09201.1.
AK020910 mRNA. Translation: BAB32250.1.
AK036240 mRNA. Translation: BAC29358.1. Frameshift.
AK046733 mRNA. Translation: BAC32849.1.
AK137417 mRNA. Translation: BAE23346.1.
BC118957 mRNA. Translation: AAI18958.1.
CCDSiCCDS36774.1.
RefSeqiNP_084155.2. NM_029879.2.
UniGeneiMm.100348.

3D structure databases

ProteinModelPortaliQ8BQP9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206866. 5 interactions.
STRINGi10090.ENSMUSP00000066614.

PTM databases

iPTMnetiQ8BQP9.
PhosphoSiteiQ8BQP9.
SwissPalmiQ8BQP9.

Proteomic databases

MaxQBiQ8BQP9.
PaxDbiQ8BQP9.
PeptideAtlasiQ8BQP9.
PRIDEiQ8BQP9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000063551; ENSMUSP00000066614; ENSMUSG00000021719.
GeneIDi52882.
KEGGimmu:52882.
UCSCiuc007rtp.1. mouse.

Organism-specific databases

CTDi401190.
MGIiMGI:106334. Rgs7bp.

Phylogenomic databases

eggNOGiENOG410IH1X. Eukaryota.
ENOG410YXJD. LUCA.
GeneTreeiENSGT00390000006968.
HOGENOMiHOG000154060.
HOVERGENiHBG104928.
InParanoidiQ8BQP9.
OMAiGSLQLHR.
OrthoDBiEOG741Z2Z.
PhylomeDBiQ8BQP9.
TreeFamiTF330985.

Miscellaneous databases

ChiTaRSiRgs7bp. mouse.
PROiQ8BQP9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BQP9.
GenevisibleiQ8BQP9. MM.

Family and domain databases

InterProiIPR026512. RGS7BP/RGS9BP.
[Graphical view]
PANTHERiPTHR21029. PTHR21029. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family."
    Drenan R.M., Doupnik C.A., Boyle M.P., Muglia L.J., Huettner J.E., Linder M.E., Blumer K.J.
    J. Cell Biol. 169:623-633(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RGS6; RGS7; RGS9 AND RGS11, PALMITOYLATION AT CYS-252 AND CYS-253, MUTAGENESIS OF CYS-252 AND CYS-253.
    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: Brain cortex, Cerebellum and Retina.
  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].
  4. "R7BP, a novel neuronal protein interacting with RGS proteins of the R7 family."
    Martemyanov K.A., Yoo P.J., Skiba N.P., Arshavsky V.Y.
    J. Biol. Chem. 280:5133-5136(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH RGS6; RGS7; RGS9 AND RGS11.
  5. "Subcellular targeting of RGS9-2 is controlled by multiple molecular determinants on its membrane anchor, R7BP."
    Song J.H., Waataja J.J., Martemyanov K.A.
    J. Biol. Chem. 281:15361-15369(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, PALMITOYLATION AT CYS-252 AND CYS-253, MUTAGENESIS OF ARG-243; ARG-246 AND 252-CYS-CYS-253.
  6. "R7BP augments the function of RGS7*Gbeta5 complexes by a plasma membrane-targeting mechanism."
    Drenan R.M., Doupnik C.A., Jayaraman M., Buchwalter A.L., Kaltenbronn K.M., Huettner J.E., Linder M.E., Blumer K.J.
    J. Biol. Chem. 281:28222-28231(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL DOMAIN, MUTAGENESIS OF 242-ARG--ARG-247.
  7. "The membrane anchor R7BP controls the proteolytic stability of the striatal specific RGS protein, RGS9-2."
    Anderson G.R., Semenov A., Song J.H., Martemyanov K.A.
    J. Biol. Chem. 282:4772-4781(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiR7BP_MOUSE
AccessioniPrimary (citable) accession number: Q8BQP9
Secondary accession number(s): Q0VF69
, Q3UVC4, Q8CBD6, Q9CTP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 88 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.