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P49802 (RGS7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of G-protein signaling 7

Short name=RGS7
Gene names
Name:RGS7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Activity on G(o)-alpha is specifically enhanced by the RGS6/GNG5 dimer. May play a role in synaptic vesicle exocytosis. May play important role in the rapid regulation of neuronal excitability and the cellular responses to short-lived stimulations By similarity.

Subunit structure

Heterodimer with GNG5. Interacts with RGS7BP, leading to regulate the subcellular location of the heterodimer formed with Gbeta5 By similarity. Interacts with 14-3-3 protein Tau and SNAPIN. Ref.7 Ref.8 Ref.9

Post-translational modification

Palmitoylated By similarity.

Phosphorylation and subsequent interaction with 14-3-3 proteins inhibits GAP activity.

Sequence similarities

Contains 1 DEP domain.

Contains 1 G protein gamma domain.

Contains 1 RGS domain.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49802-1)

Also known as: A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P49802-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     454-495: SGNSMDRRTSFEKFAQNVGRNIPIFPCHKNCTPTLRASTNLL → GKSLTSKRLTSLAQSY
Isoform 3 (identifier: P49802-3)

The sequence of this isoform differs from the canonical sequence as follows:
     454-471: Missing.
Isoform 4 (identifier: P49802-4)

The sequence of this isoform differs from the canonical sequence as follows:
     76-128: Missing.
     454-471: Missing.
Isoform 5 (identifier: P49802-5)

The sequence of this isoform differs from the canonical sequence as follows:
     473-495: RNIPIFPCHKNCTPTLRASTNLL → KSLTSKRLTSLAQSY

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495Regulator of G-protein signaling 7
PRO_0000204196

Regions

Domain37 – 11276DEP
Domain255 – 31662G protein gamma
Domain333 – 448116RGS

Amino acid modifications

Modified residue4341Phosphoserine Ref.8

Natural variations

Alternative sequence76 – 12853Missing in isoform 4.
VSP_005671
Alternative sequence454 – 49542SGNSM…STNLL → GKSLTSKRLTSLAQSY in isoform 2.
VSP_005672
Alternative sequence454 – 47118Missing in isoform 3 and isoform 4.
VSP_005673
Alternative sequence473 – 49523RNIPI…STNLL → KSLTSKRLTSLAQSY in isoform 5.
VSP_038388
Natural variant1371M → L.
Corresponds to variant rs12746550 [ dbSNP | Ensembl ].
VAR_057153
Natural variant4091Q → H. Ref.6
Corresponds to variant rs17851953 [ dbSNP | Ensembl ].
VAR_060604

Experimental info

Mutagenesis3061W → F: Diminishes interaction with Gbeta5. Ref.7
Sequence conflict261K → R in AAM12645. Ref.3
Sequence conflict2341Q → R in AAM12644. Ref.3

Secondary structure

...................... 495
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified October 18, 2001. Version 3.
Checksum: 1FCC2D60622675DE

FASTA49557,668
        10         20         30         40         50         60 
MAQGNNYGQT SNGVADESPN MLVYRKMEDV IARMQDEKNG IPIRTVKSFL SKIPSVFSGS 

        70         80         90        100        110        120 
DIVQWLIKNL TIEDPVEALH LGTLMAAHGY FFPISDHVLT LKDDGTFYRF QTPYFWPSNC 

       130        140        150        160        170        180 
WEPENTDYAV YLCKRTMQNK ARLELADYEA ESLARLQRAF ARKWEFIFMQ AEAQAKVDKK 

       190        200        210        220        230        240 
RDKIERKILD SQERAFWDVH RPVPGCVNTT EVDIKKSSRM RNPHKTRKSV YGLQNDIRSH 

       250        260        270        280        290        300 
SPTHTPTPET KPPTEDELQQ QIKYWQIQLD RHRLKMSKVA DSLLSYTEQY LEYDPFLLPP 

       310        320        330        340        350        360 
DPSNPWLSDD TTFWELEASK EPSQQRVKRW GFGMDEALKD PVGREQFLKF LESEFSSENL 

       370        380        390        400        410        420 
RFWLAVEDLK KRPIKEVPSR VQEIWQEFLA PGAPSAINLD SKSYDKTTQN VKEPGRYTFE 

       430        440        450        460        470        480 
DAQEHIYKLM KSDSYPRFIR SSAYQELLQA KKKSGNSMDR RTSFEKFAQN VGRNIPIFPC 

       490 
HKNCTPTLRA STNLL 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 993C1209EDD884EC
Show »

FASTA46954,685
Isoform 3 [UniParc].

Checksum: A7252A838E1881A9
Show »

FASTA47755,612
Isoform 4 [UniParc].

Checksum: 25A8A2F507C07E87
Show »

FASTA42449,387
Isoform 5 [UniParc].

Checksum: 50BDD0E8896444BC
Show »

FASTA48756,741

References

« Hide 'large scale' references
[1]"Interaction between RGS7 and polycystin."
Kim E., Arnould T., Sellin L., Benzing T., Comella N., Kocher O., Tsiokas L., Sukhatme V.P., Walz G.
Proc. Natl. Acad. Sci. U.S.A. 96:6371-6376(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain.
[2]"EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins."
Koelle M.R., Horvitz H.R.
Cell 84:115-125(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
Tissue: Brain.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 5), VARIANT HIS-409.
Tissue: Testis.
[7]"Fidelity of G protein beta-subunit association by the G protein gamma-subunit-like domains of RGS6, RGS7, and RGS11."
Snow B.E., Betts L., Mangion J., Sondek J., Siderovski D.P.
Proc. Natl. Acad. Sci. U.S.A. 96:6489-6494(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GBETA5, MUTAGENESIS OF TRP-306.
Tissue: Brain.
[8]"14-3-3 interacts with regulator of G protein signaling proteins and modulates their activity."
Benzing T., Yaffe M.B., Arnould T., Sellin L., Schermer B., Schilling B., Schreiber R., Kunzelmann K., Leparc G.G., Kim E., Walz G.
J. Biol. Chem. 275:28167-28172(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-434, INTERACTION WITH 14-3-3 PROTEINS.
[9]"Snapin interacts with the N-terminus of regulator of G protein signaling 7."
Hunt R.A., Edris W., Chanda P.K., Nieuwenhuijsen B., Young K.H.
Biochem. Biophys. Res. Commun. 303:594-599(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNAPIN.
[10]"Solution structure of the RGS domain of regulator of G-protein signaling 7."
RIKEN structural genomics initiative (RSGI)
Submitted (DEC-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 323-448.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF090116 mRNA. Translation: AAD34290.1.
AF090117 mRNA. Translation: AAD34291.1.
U32439 mRNA. Translation: AAC50351.1.
AF493930 mRNA. Translation: AAM12644.1.
AF493931 mRNA. Translation: AAM12645.1.
AY587875 mRNA. Translation: AAT52231.1.
AL512307 expand/collapse EMBL AC list , AL359764, AL365184, AL590682 Genomic DNA. Translation: CAH71987.1.
AL512307 expand/collapse EMBL AC list , AL359764, AL365184, AL590682 Genomic DNA. Translation: CAH71988.1.
AL512307 expand/collapse EMBL AC list , AL359764, AL365184, AL590682 Genomic DNA. Translation: CAH71989.1.
AL512307 expand/collapse EMBL AC list , AL359764, AL365184, AL590682 Genomic DNA. Translation: CAH71990.1.
AL590682 expand/collapse EMBL AC list , AL359764, AL365184, AL512307 Genomic DNA. Translation: CAH73809.1.
AL590682 expand/collapse EMBL AC list , AL359764, AL365184, AL512307 Genomic DNA. Translation: CAH73810.1.
AL590682 expand/collapse EMBL AC list , AL359764, AL365184, AL512307 Genomic DNA. Translation: CAH73811.1.
AL590682 expand/collapse EMBL AC list , AL359764, AL365184, AL512307 Genomic DNA. Translation: CAH73812.1.
AL359764 expand/collapse EMBL AC list , AL365184, AL512307, AL590682 Genomic DNA. Translation: CAI15140.1.
AL359764 expand/collapse EMBL AC list , AL365184, AL512307, AL590682 Genomic DNA. Translation: CAI15141.1.
AL359764 expand/collapse EMBL AC list , AL365184, AL512307, AL590682 Genomic DNA. Translation: CAI15142.1.
AL359764 expand/collapse EMBL AC list , AL365184, AL512307, AL590682 Genomic DNA. Translation: CAI15143.1.
AL365184 expand/collapse EMBL AC list , AL359764, AL512307, AL590682 Genomic DNA. Translation: CAI16818.1.
AL365184 expand/collapse EMBL AC list , AL359764, AL512307, AL590682 Genomic DNA. Translation: CAI16819.1.
AL365184 expand/collapse EMBL AC list , AL359764, AL512307, AL590682 Genomic DNA. Translation: CAI16820.1.
AL365184 expand/collapse EMBL AC list , AL359764, AL512307, AL590682 Genomic DNA. Translation: CAI16821.1.
CH471098 Genomic DNA. Translation: EAW70086.1.
BC022009 mRNA. Translation: AAH22009.1.
CCDSCCDS31071.1. [P49802-5]
CCDS60457.1. [P49802-4]
CCDS60458.1. [P49802-2]
CCDS60459.1. [P49802-3]
RefSeqNP_001269702.1. NM_001282773.1. [P49802-4]
NP_001269704.1. NM_001282775.1. [P49802-3]
NP_001269707.1. NM_001282778.1. [P49802-2]
NP_002915.3. NM_002924.5. [P49802-5]
XP_005273275.1. XM_005273218.1. [P49802-1]
UniGeneHs.655739.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A72X-ray2.00A/B320-463[»]
2D9JNMR-A323-448[»]
ProteinModelPortalP49802.
SMRP49802. Positions 19-450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111932. 8 interactions.
DIPDIP-40869N.
IntActP49802. 5 interactions.
MINTMINT-136910.
STRING9606.ENSP00000355520.

PTM databases

PhosphoSiteP49802.

Polymorphism databases

DMDM17380284.

Proteomic databases

MaxQBP49802.
PaxDbP49802.
PRIDEP49802.

Protocols and materials databases

DNASU6000.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000348120; ENSP00000341242; ENSG00000182901. [P49802-4]
ENST00000366562; ENSP00000355520; ENSG00000182901. [P49802-2]
ENST00000366563; ENSP00000355521; ENSG00000182901. [P49802-3]
ENST00000366564; ENSP00000355522; ENSG00000182901. [P49802-2]
ENST00000366565; ENSP00000355523; ENSG00000182901. [P49802-5]
ENST00000401882; ENSP00000385508; ENSG00000182901. [P49802-4]
ENST00000407727; ENSP00000384428; ENSG00000182901. [P49802-1]
GeneID6000.
KEGGhsa:6000.
UCSCuc001hyt.2. human. [P49802-1]
uc001hyu.2. human. [P49802-3]
uc001hyv.2. human. [P49802-5]
uc001hyw.2. human. [P49802-2]
uc009xgn.1. human. [P49802-4]

Organism-specific databases

CTD6000.
GeneCardsGC01M240938.
HGNCHGNC:10003. RGS7.
HPACAB017561.
HPA000688.
MIM602517. gene.
neXtProtNX_P49802.
PharmGKBPA34378.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327614.
HOVERGENHBG007404.
InParanoidP49802.
KOK16449.
OMAWIMKNLD.
PhylomeDBP49802.
TreeFamTF351956.

Enzyme and pathway databases

SignaLinkP49802.

Gene expression databases

ArrayExpressP49802.
BgeeP49802.
CleanExHS_RGS7.
GenevestigatorP49802.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
1.10.196.10. 1 hit.
4.10.260.10. 1 hit.
InterProIPR000591. DEP_dom.
IPR015898. G-protein_gamma-like_dom.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00610. DEP. 1 hit.
PF00631. G-gamma. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR01301. RGSPROTEIN.
SMARTSM00049. DEP. 1 hit.
SM00224. GGL. 1 hit.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
SSF48670. SSF48670. 1 hit.
PROSITEPS50186. DEP. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRGS7. human.
EvolutionaryTraceP49802.
GeneWikiRGS7.
GenomeRNAi6000.
NextBio23395.
PROP49802.
SOURCESearch...

Entry information

Entry nameRGS7_HUMAN
AccessionPrimary (citable) accession number: P49802
Secondary accession number(s): Q5T3H4 expand/collapse secondary AC list , Q8TD66, Q8TD67, Q8WW09, Q9UNU7, Q9Y6B9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 18, 2001
Last modified: July 9, 2014
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM