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P49758 (RGS6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of G-protein signaling 6

Short name=RGS6
Alternative name(s):
S914
Gene names
Name:RGS6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length472 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/Gbeta5 dimer. Ref.3

Subunit structure

Heterodimer with Gbeta5. Interacts with RGS7BP, leading to regulate the subcellular location of the heterodimer formed with Gbeta5 By similarity.

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein.

Domain

The RGS domain interacts avidly with Galpha and mediates the acceleration of Galpha-mediated GTP hydrolysis. Ref.6

Sequence similarities

Contains 1 DEP domain.

Contains 1 G protein gamma domain.

Contains 1 RGS domain.

Sequence caution

The sequence AAC42001.1 differs from that shown. Reason: Frameshift at several positions.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSP90AB1P082382EBI-6426927,EBI-352572

Alternative products

This entry describes 15 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49758-4)

Also known as: RGS6Lalpha2;

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: P49758-2)

Also known as: RGS6Lgamma1;

The sequence of this isoform differs from the canonical sequence as follows:
     457-472: GKSLAGKRLTGLMQSS → PESEQGRRTSLEKFTRSVLYSNTPLAKRP
Isoform 3 (identifier: P49758-3)

Also known as: RGS6Lalpha1;

The sequence of this isoform differs from the canonical sequence as follows:
     456-456: K → KPESEQGRRTSLEKFTRSV
Isoform 5 (identifier: P49758-5)

Also known as: RGS6Lbeta;

The sequence of this isoform differs from the canonical sequence as follows:
     457-472: GKSLAGKRLTGLMQSS → KVSKVVELP
Isoform 6 (identifier: P49758-6)

Also known as: RGS6Lbeta-GGL;

The sequence of this isoform differs from the canonical sequence as follows:
     285-321: Missing.
     457-472: GKSLAGKRLTGLMQSS → KVSKVVELP
Isoform 7 (identifier: P49758-7)

Also known as: RGS6Lalpha2-GGL;

The sequence of this isoform differs from the canonical sequence as follows:
     285-321: Missing.
Isoform 8 (identifier: P49758-8)

Also known as: RGS6Lgamma2;

The sequence of this isoform differs from the canonical sequence as follows:
     457-472: GKSLAGKRLTGLMQSS → LYSNTPLAKRP
Isoform 9 (identifier: P49758-9)

Also known as: RGS6Lalpha1-GGL;

The sequence of this isoform differs from the canonical sequence as follows:
     285-321: Missing.
     456-456: K → KPESEQGRRTSLEKFTRSV
Isoform 10 (identifier: P49758-10)

Also known as: RGS6Lgamma1-GGL;

The sequence of this isoform differs from the canonical sequence as follows:
     285-321: Missing.
     457-472: GKSLAGKRLTGLMQSS → PESEQGRRTSLEKFTRSVLYSNTPLAKRP
Isoform 11 (identifier: P49758-11)

Also known as: RGS6Lgamma2-GGL;

The sequence of this isoform differs from the canonical sequence as follows:
     285-321: Missing.
     457-472: GKSLAGKRLTGLMQSS → LYSNTPLAKRP
Isoform 12 (identifier: P49758-12)

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: Missing.
     457-472: GKSLAGKRLTGLMQSS → PESEQGRRTSLEKFTRSVLYSNTPLAKRP
Isoform 13 (identifier: P49758-13)

Also known as: RGS6Lepsilon;

The sequence of this isoform differs from the canonical sequence as follows:
     457-472: GKSLAGKRLTGLMQSS → PESEQGRRTSLEKFTRSVG
Isoform 14 (identifier: P49758-14)

Also known as: RGS6Ldelta;

The sequence of this isoform differs from the canonical sequence as follows:
     457-472: GKSLAGKRLTGLMQSS → PESEQGRRTSLEKFTRSVLLF
Isoform 15 (identifier: P49758-15)

Also known as: RGS6Lgamma;

The sequence of this isoform differs from the canonical sequence as follows:
     457-472: GKSLAGKRLTGLMQSS → PESEQGRRTSLEKFTRSVCLQLLF
Isoform 16 (identifier: P49758-16)

Also known as: RGS6Leta;

The sequence of this isoform differs from the canonical sequence as follows:
     457-472: GKSLAGKRLTGLMQSS → VWLL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Regulator of G-protein signaling 6
PRO_0000204192

Regions

Domain40 – 11576DEP
Domain261 – 33070G protein gamma
Domain336 – 441106RGS

Natural variations

Alternative sequence1 – 139139Missing in isoform 12.
VSP_035845
Alternative sequence285 – 32137Missing in isoform 6, isoform 7, isoform 9, isoform 10 and isoform 11.
VSP_035846
Alternative sequence4561K → KPESEQGRRTSLEKFTRSV in isoform 3 and isoform 9.
VSP_035847
Alternative sequence457 – 47216GKSLA…LMQSS → PESEQGRRTSLEKFTRSVG in isoform 13.
VSP_047806
Alternative sequence457 – 47216GKSLA…LMQSS → PESEQGRRTSLEKFTRSVLL F in isoform 14.
VSP_047807
Alternative sequence457 – 47216GKSLA…LMQSS → PESEQGRRTSLEKFTRSVCL QLLF in isoform 15.
VSP_047808
Alternative sequence457 – 47216GKSLA…LMQSS → VWLL in isoform 16.
VSP_047809
Alternative sequence457 – 47216GKSLA…LMQSS → PESEQGRRTSLEKFTRSVLY SNTPLAKRP in isoform 2, isoform 10 and isoform 12.
VSP_035848
Alternative sequence457 – 47216GKSLA…LMQSS → KVSKVVELP in isoform 5 and isoform 6.
VSP_035849
Alternative sequence457 – 47216GKSLA…LMQSS → LYSNTPLAKRP in isoform 8 and isoform 11.
VSP_035850

Experimental info

Mutagenesis2971D → A: Loss of interaction with Gbeta5. Ref.2
Mutagenesis3091W → F: Diminishes interaction with Gbeta5. Ref.2
Sequence conflict1651R → K in AAC26049. Ref.1
Sequence conflict1651R → K in AAM03004. Ref.1
Sequence conflict1651R → K in AAM03005. Ref.1
Sequence conflict1651R → K in AAM03006. Ref.1
Sequence conflict1651R → K in AAM03007. Ref.1
Sequence conflict1651R → K in AAM03008. Ref.1
Sequence conflict1651R → K in AAM03009. Ref.1
Sequence conflict1651R → K in AAM03010. Ref.1
Sequence conflict1651R → K in AAM03011. Ref.1
Sequence conflict1651R → K in AAM03012. Ref.1
Sequence conflict1651R → K in AAM03013. Ref.1
Sequence conflict2101V → L in AAC26049. Ref.1
Sequence conflict2101V → L in AAM03004. Ref.1
Sequence conflict2101V → L in AAM03005. Ref.1
Sequence conflict2101V → L in AAM03006. Ref.1
Sequence conflict2101V → L in AAM03007. Ref.1
Sequence conflict2101V → L in AAM03008. Ref.1
Sequence conflict2101V → L in AAM03009. Ref.1
Sequence conflict2101V → L in AAM03010. Ref.1
Sequence conflict2101V → L in AAM03011. Ref.1
Sequence conflict2101V → L in AAM03012. Ref.1
Sequence conflict2101V → L in AAM03013. Ref.1
Sequence conflict312 – 3132DD → EE in AAC26049. Ref.1
Sequence conflict312 – 3132DD → EE in AAM03004. Ref.1
Sequence conflict312 – 3132DD → EE in AAM03005. Ref.1
Sequence conflict312 – 3132DD → EE in AAM03006. Ref.1
Sequence conflict312 – 3132DD → EE in AAM03009. Ref.1
Sequence conflict312 – 3132DD → EE in AAM03010. Ref.1
Sequence conflict3241E → D in AAC26049. Ref.1
Sequence conflict3241E → D in AAM03004. Ref.1
Sequence conflict3241E → D in AAM03005. Ref.1
Sequence conflict3241E → D in AAM03006. Ref.1
Sequence conflict3241E → D in AAM03007. Ref.1
Sequence conflict3241E → D in AAM03008. Ref.1
Sequence conflict3241E → D in AAM03009. Ref.1
Sequence conflict3241E → D in AAM03010. Ref.1
Sequence conflict3241E → D in AAM03011. Ref.1
Sequence conflict3241E → D in AAM03012. Ref.1
Sequence conflict3241E → D in AAM03013. Ref.1
Sequence conflict4651L → C in AAC42001. Ref.5

Secondary structure

..................... 472
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (RGS6Lalpha2) [UniParc].

Last modified November 25, 2008. Version 5.
Checksum: 1424518EA697CD76

FASTA47254,423
        10         20         30         40         50         60 
MAQGSGDQRA VGVADPEESS PNMIVYCKIE DIITKMQDDK TGGVPIRTVK SFLSKIPSVV 

        70         80         90        100        110        120 
TGTDIVQWLM KNLSIEDPVE AIHLGSLIAA QGYIFPISDH VLTMKDDGTF YRFQAPYFWP 

       130        140        150        160        170        180 
SNCWEPENTD YAIYLCKRTM QNKARLELAD YEAENLARLQ RAFARKWEFI FMQAEAQVKI 

       190        200        210        220        230        240 
DRKKDKTERK ILDSQERAFW DVHRPVPGCV NTTEMDIRKC RRLKNPQKVK KSVYGVTEES 

       250        260        270        280        290        300 
QAQSPVHVLS QPIRKTTKED IRKQITFLNA QIDRHCLKMS KVAESLIAYT EQYVEYDPLI 

       310        320        330        340        350        360 
TPAEPSNPWI SDDVALWDIE MSKEPSQQRV KRWGFSFDEI LKDQVGRDQF LRFLESEFSS 

       370        380        390        400        410        420 
ENLRFWLAVQ DLKKQPLQDV AKRVEEIWQE FLAPGAPSAI NLDSHSYEIT SQNVKDGGRY 

       430        440        450        460        470 
TFEDAQEHIY KLMKSDSYAR FLRSNAYQDL LLAKKKGKSL AGKRLTGLMQ SS 

« Hide

Isoform 2 (RGS6Lgamma1) [UniParc].

Checksum: 06D282213979376C
Show »

FASTA48556,138
Isoform 3 (RGS6Lalpha1) [UniParc].

Checksum: C8BD1254D593D1F5
Show »

FASTA49056,512
Isoform 5 (RGS6Lbeta) [UniParc].

Checksum: 2027294E5EF69596
Show »

FASTA46553,787
Isoform 6 (RGS6Lbeta-GGL) [UniParc].

Checksum: A2C52E54E4569178
Show »

FASTA42849,520
Isoform 7 (RGS6Lalpha2-GGL) [UniParc].

Checksum: 95405495A89187D4
Show »

FASTA43550,155
Isoform 8 (RGS6Lgamma2) [UniParc].

Checksum: F2CE01A6D57BFD91
Show »

FASTA46754,049
Isoform 9 (RGS6Lalpha1-GGL) [UniParc].

Checksum: 78F9B10D25DF6B44
Show »

FASTA45352,245
Isoform 10 (RGS6Lgamma1-GGL) [UniParc].

Checksum: 5A6833E6530ADBAB
Show »

FASTA44851,870
Isoform 11 (RGS6Lgamma2-GGL) [UniParc].

Checksum: F484A344D2614731
Show »

FASTA43049,781
Isoform 12 [UniParc].

Checksum: A0462F5A1DBDC9EA
Show »

FASTA34640,588
Isoform 13 (RGS6Lepsilon) [UniParc].

Checksum: DBD7BC0ADF638F51
Show »

FASTA47554,953
Isoform 14 (RGS6Ldelta) [UniParc].

Checksum: B8212487BC0ADF63
Show »

FASTA47755,270
Isoform 15 (RGS6Lgamma) [UniParc].

Checksum: 6781EF37312D17BC
Show »

FASTA48055,614
Isoform 16 (RGS6Leta) [UniParc].

Checksum: 829707C9624AD2A3
Show »

FASTA46053,319

References

« Hide 'large scale' references
[1]"Human RGS6 gene structure, complex alternative splicing, and role of N terminus and G protein gamma-subunit-like (GGL) domain in subcellular localization of RGS6 splice variants."
Chatterjee T.K., Liu Z., Fisher R.A.
J. Biol. Chem. 278:30261-30271(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 5; 6; 7; 8; 9; 10; 11; 12; 13; 14; 15 AND 16).
[2]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), MUTAGENESIS OF ASP-297 AND TRP-309.
Tissue: Brain.
[3]"Regulators of G protein signaling 6 and 7. Purification of complexes with gbeta5 and assessment of their effects on g protein-mediated signaling pathways."
Posner B.A., Gilman A.G., Harris B.A.
J. Biol. Chem. 274:31087-31093(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[4]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease."
Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., Ikeda M., Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F., Bruni A.C., Montesi M.P., Sorbi S., Rainero I., Pinessi L. expand/collapse author list , Nee L., Chumakov I., Pollen D., Brookes A., Sanseau P., Polinsky R.J., Wasco W., da Silva H.A.R., Haines J.L., Pericak-Vance M.A., Tanzi R.E., Roses A.D., Fraser P.E., Rommens J.M., St George-Hyslop P.H.
Nature 375:754-760(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 362-472 (ISOFORM 1).
Tissue: Brain.
[6]"Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits."
Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J., Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A., Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P.
Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 325-470, DOMAIN RGS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF073920 mRNA. Translation: AAC26049.2.
AF073921 mRNA. Translation: AAC26050.1.
AY309097 mRNA. Translation: AAP74386.1.
AY309098 mRNA. Translation: AAP74387.1.
AY309099 mRNA. Translation: AAP74388.1.
AY309100 mRNA. Translation: AAP74389.1.
AF465727 expand/collapse EMBL AC list , AF465711, AF465712, AF465713, AF465714, AF465715, AF465716, AF465717, AF465718, AF465719, AF465720, AF465721, AF465722, AF465723, AF465724, AF465725, AF465726 Genomic DNA. Translation: AAM03004.1.
AF465727 expand/collapse EMBL AC list , AF465711, AF465712, AF465713, AF465714, AF465715, AF465716, AF465717, AF465718, AF465719, AF465720, AF465721, AF465722, AF465723, AF465724, AF465725, AF465726 Genomic DNA. Translation: AAM03005.1.
AF465726 expand/collapse EMBL AC list , AF465711, AF465712, AF465713, AF465714, AF465715, AF465716, AF465717, AF465718, AF465719, AF465720, AF465721, AF465722, AF465723, AF465724, AF465725 Genomic DNA. Translation: AAM03006.1.
AF465727 expand/collapse EMBL AC list , AF465711, AF465712, AF465713, AF465714, AF465715, AF465716, AF465717, AF465718, AF465719, AF465720, AF465721, AF465723, AF465724, AF465725, AF465726 Genomic DNA. Translation: AAM03007.1.
AF465727 expand/collapse EMBL AC list , AF465711, AF465712, AF465713, AF465714, AF465715, AF465716, AF465717, AF465718, AF465719, AF465720, AF465721, AF465723, AF465724, AF465725, AF465726 Genomic DNA. Translation: AAM03008.1.
AF465727 expand/collapse EMBL AC list , AF465711, AF465712, AF465713, AF465714, AF465715, AF465716, AF465717, AF465718, AF465719, AF465720, AF465721, AF465722, AF465723, AF465724, AF465725 Genomic DNA. Translation: AAM03009.1.
AF465727 expand/collapse EMBL AC list , AF465711, AF465712, AF465713, AF465714, AF465715, AF465716, AF465717, AF465718, AF465719, AF465720, AF465721, AF465722, AF465723, AF465724, AF465725 Genomic DNA. Translation: AAM03010.1.
AF465727 expand/collapse EMBL AC list , AF465711, AF465712, AF465713, AF465714, AF465715, AF465716, AF465717, AF465718, AF465719, AF465720, AF465721, AF465723, AF465724, AF465725 Genomic DNA. Translation: AAM03011.1.
AF465727 expand/collapse EMBL AC list , AF465711, AF465712, AF465713, AF465714, AF465715, AF465716, AF465717, AF465718, AF465719, AF465720, AF465721, AF465723, AF465724, AF465725 Genomic DNA. Translation: AAM03012.1.
AF465726 expand/collapse EMBL AC list , AF465711, AF465712, AF465713, AF465714, AF465715, AF465716, AF465717, AF465718, AF465719, AF465720, AF465721, AF465723, AF465724, AF465725 Genomic DNA. Translation: AAM03013.1.
AF107619 mRNA. Translation: AAD34717.1.
AF107620 mRNA. Translation: AAD34718.1.
AF156932 mRNA. Translation: AAD40183.1.
AC004828 Genomic DNA. No translation available.
AC005157 Genomic DNA. Translation: AAC83180.1.
AC005226 Genomic DNA. No translation available.
AC005227 Genomic DNA. No translation available.
AC005477 Genomic DNA. Translation: AAD05031.1.
AC005533 Genomic DNA. No translation available.
AC005857 Genomic DNA. No translation available.
AC005993 Genomic DNA. No translation available.
L40394 mRNA. Translation: AAC42001.1. Frameshift.
RefSeqNP_001191345.1. NM_001204416.1.
NP_001191346.1. NM_001204417.1.
NP_001191347.1. NM_001204418.1.
NP_001191348.1. NM_001204419.1.
NP_001191349.1. NM_001204420.1.
NP_001191350.1. NM_001204421.1.
NP_001191351.1. NM_001204422.1.
NP_001191352.1. NM_001204423.1.
NP_001191353.1. NM_001204424.1.
NP_004287.3. NM_004296.5.
XP_005268291.1. XM_005268234.1.
XP_005268292.1. XM_005268235.2.
XP_005268293.1. XM_005268236.1.
UniGeneHs.509872.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ES0X-ray2.10A325-470[»]
ProteinModelPortalP49758.
SMRP49758. Positions 17-452.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114987. 9 interactions.
IntActP49758. 1 interaction.
MINTMINT-242744.

PTM databases

PhosphoSiteP49758.

Polymorphism databases

DMDM215274268.

Proteomic databases

PaxDbP49758.
PRIDEP49758.

Protocols and materials databases

DNASU9628.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343854; ENSP00000341199; ENSG00000182732. [P49758-9]
ENST00000355512; ENSP00000347699; ENSG00000182732. [P49758-16]
ENST00000402788; ENSP00000383953; ENSG00000182732. [P49758-4]
ENST00000404301; ENSP00000385243; ENSG00000182732. [P49758-15]
ENST00000406236; ENSP00000384218; ENSG00000182732. [P49758-13]
ENST00000407322; ENSP00000384612; ENSG00000182732. [P49758-14]
ENST00000553525; ENSP00000451030; ENSG00000182732. [P49758-3]
ENST00000553530; ENSP00000452331; ENSG00000182732. [P49758-4]
ENST00000554474; ENSP00000450858; ENSG00000182732. [P49758-5]
ENST00000554782; ENSP00000451912; ENSG00000182732. [P49758-12]
ENST00000555571; ENSP00000450936; ENSG00000182732. [P49758-4]
ENST00000556437; ENSP00000451855; ENSG00000182732. [P49758-3]
GeneID9628.
KEGGhsa:9628.
UCSCuc001xmx.4. human. [P49758-4]
uc001xmy.4. human. [P49758-3]
uc021rvw.1. human. [P49758-2]
uc021rvx.1. human. [P49758-8]
uc021rvy.1. human. [P49758-10]
uc021rvz.1. human. [P49758-11]
uc021rwa.1. human. [P49758-9]
uc021rwb.1. human. [P49758-7]
uc021rwc.1. human. [P49758-12]

Organism-specific databases

CTD9628.
GeneCardsGC14P072399.
HGNCHGNC:10002. RGS6.
HPAHPA003067.
MIM603894. gene.
neXtProtNX_P49758.
PharmGKBPA34377.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327614.
HOVERGENHBG007404.
InParanoidP49758.
KOK16449.
OMAEDAQDHI.
OrthoDBEOG7BZVS5.
PhylomeDBP49758.
TreeFamTF351956.

Gene expression databases

ArrayExpressP49758.
BgeeP49758.
GenevestigatorP49758.

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

EvolutionaryTraceP49758.
GeneWikiRGS6.
GenomeRNAi9628.
NextBio36131.
PROP49758.
SOURCESearch...

Entry information

Entry nameRGS6_HUMAN
AccessionPrimary (citable) accession number: P49758
Secondary accession number(s): C9JE95 expand/collapse secondary AC list , F8W7W5, O75576, O75577, Q7Z4K3, Q7Z4K4, Q7Z4K5, Q7Z4K6, Q8TE13, Q8TE14, Q8TE15, Q8TE16, Q8TE17, Q8TE18, Q8TE19, Q8TE20, Q8TE21, Q8TE22, Q9UDS8, Q9UDT0, Q9Y245, Q9Y647
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 137 of the entry and version 5 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 chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM