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P41220 (RGS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of G-protein signaling 2

Short name=RGS2
Alternative name(s):
Cell growth-inhibiting gene 31 protein
G0/G1 switch regulatory protein 8
Gene names
Name:RGS2
Synonyms:G0S8
ORF Names:GIG31
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length211 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. May play a role in leukemogenesis. Plays a role in negative feedback control pathway for adenylyl cyclase signaling. Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein. Ref.2 Ref.3 Ref.12 Ref.15

Subunit structure

Interacts with EIF2B5. Interacts with PRKG1 (isoform alpha) Ref.14 Ref.15

Subcellular location

Isoform 1: Cell membrane. Cytoplasm. Nucleusnucleolus Ref.2 Ref.3.

Isoform 2: Cell membrane. Cytoplasm. Nucleusnucleolus Ref.2 Ref.3.

Isoform 3: Cell membrane. Cytoplasm. Nucleusnucleolus Ref.2 Ref.3.

Isoform 4: Cell membrane. Mitochondrion Ref.2 Ref.3.

Tissue specificity

Expressed in acute myelogenous leukemia (AML) and in acute lymphoblastic leukemia (ALL). Ref.12

Post-translational modification

Phosphorylated by protein kinase C. Phosphorylation by PRKG1 leads to activation of RGS2 activity. Ref.13 Ref.14

Sequence similarities

Contains 1 RGS domain.

Ontologies

Keywords
   Biological processCell cycle
Translation regulation
   Cellular componentCell membrane
Cytoplasm
Membrane
Mitochondrion
Nucleus
   Coding sequence diversityAlternative initiation
   Molecular functionSignal transduction inhibitor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrown fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of G-protein coupled receptor protein signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of cardiac muscle hypertrophy

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of phospholipase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cardiac muscle contraction

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of microtubule polymerization

Inferred from electronic annotation. Source: Ensembl

regulation of G-protein coupled receptor protein signaling pathway

Traceable author statement PubMed 10747990. Source: ProtInc

regulation of adrenergic receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

relaxation of cardiac muscle

Inferred from sequence or structural similarity. Source: BHF-UCL

relaxation of vascular smooth muscle

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

termination of G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Inferred from sequence or structural similarity. Source: BHF-UCL

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionGTPase activator activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

calmodulin binding

Traceable author statement PubMed 10747990. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PPP1R9AQ9ULJ83EBI-712388,EBI-2515561

Alternative products

This entry describes 4 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P41220-1)

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: P41220-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: Missing.
Isoform 3 (identifier: P41220-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: Missing.
Note: Lacks type V adenylyl cyclase (AC) inhibitory function.
Isoform 4 (identifier: P41220-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.
Note: Lacks type V adenylyl cyclase (AC) inhibitory function.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Regulator of G-protein signaling 2
PRO_0000204178

Regions

Domain83 – 199117RGS
Region32 – 6635Necessary for membrane association
Region79 – 11638Necessary to inhibit protein synthesis

Natural variations

Alternative sequence1 – 3232Missing in isoform 4.
VSP_041298
Alternative sequence1 – 1515Missing in isoform 3.
VSP_041297
Alternative sequence1 – 44Missing in isoform 2.
VSP_041296

Experimental info

Mutagenesis11M → L: Loss of isoform 1 expression. Ref.3
Mutagenesis51M → L: Loss of isoform 2 expression. Ref.3
Mutagenesis161M → L: Loss of isoform 3 expression. Ref.3
Mutagenesis331M → L: Loss of isoform 4 expression. Ref.3
Mutagenesis371L → D: Impairs association with plasma membrane. Ref.2
Mutagenesis381L → D: Impairs association with plasma membrane. Ref.2
Mutagenesis411W → D: Impairs association with plasma membrane. Ref.2
Mutagenesis451L → D: Impairs association with plasma membrane. Ref.2
Mutagenesis481F → D: Impairs association with plasma membrane. Ref.2
Mutagenesis491L → D: Impairs association with plasma membrane. Ref.2
Mutagenesis791L → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with E-86; L-87; S-90; K-102; F-105; I-110; E-111 and L-114. Ref.15
Mutagenesis861E → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; L-87; S-90; K-102; F-105; I-110; E-111 and L-114. Ref.15
Mutagenesis871L → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; S-90; K-102; F-105; I-110; E-111 and L-114. Ref.15
Mutagenesis901S → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; K-102; F-105; I-110; E-111 and L-114. Ref.15
Mutagenesis1021K → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; F-105; I-110; E-111 and L-114. Ref.15
Mutagenesis1051F → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; I-110; E-111 and L-114. Ref.15
Mutagenesis1101I → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; E-111 and L-114. Ref.15
Mutagenesis1111E → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; I-110 and L-114. Ref.15
Mutagenesis1141L → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; I-110 and E-111. Ref.15
Mutagenesis1491N → A: Decreases GTPase accelerating function but has no effect on translation inhibitory activity, suggesting that its role in translation is independent of its effects on G proteins. Ref.15

Secondary structure

...................... 211
Helix Strand Turn

Details...

Sequences

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

Last modified February 1, 1995. Version 1.
Checksum: EFFE4AE47EF9AD8F

FASTA21124,382
        10         20         30         40         50         60 
MQSAMFLAVQ HDCRPMDKSA GSGHKSEEKR EKMKRTLLKD WKTRLSYFLQ NSSTPGKPKT 

        70         80         90        100        110        120 
GKKSKQQAFI KPSPEEAQLW SEAFDELLAS KYGLAAFRAF LKSEFCEENI EFWLACEDFK 

       130        140        150        160        170        180 
KTKSPQKLSS KARKIYTDFI EKEAPKEINI DFQTKTLIAQ NIQEATSGCF TTAQKRVYSL 

       190        200        210 
MENNSYPRFL ESEFYQDLCK KPQITTEPHA T 

« Hide

Isoform 2 [UniParc].

Checksum: E5DCCB2F18E09F51
Show »

FASTA20723,964
Isoform 3 [UniParc].

Checksum: 2F5BF7609CD4172A
Show »

FASTA19622,666
Isoform 4 [UniParc].

Checksum: 6CF0306689DC7A54
Show »

FASTA17920,780

References

« Hide 'large scale' references
[1]"A human gene encoding a putative basic helix-loop-helix phosphoprotein whose mRNA increases rapidly in cycloheximide-treated blood mononuclear cells."
Siderovski D.P., Heximer S.P., Forsdyke D.R.
DNA Cell Biol. 13:125-147(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"Mechanisms governing subcellular localization and function of human RGS2."
Heximer S.P., Lim H., Bernard J.L., Blumer K.J.
J. Biol. Chem. 276:14195-14203(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-37; LEU-38; TRP-41; LEU-45; PHE-48 AND LEU-49.
[3]"Alternative translation initiation of human regulators of G-protein signaling-2 yields a set of functionally distinct proteins."
Gu S., Anton A., Salim S., Blumer K.J., Dessauer C.W., Heximer S.P.
Mol. Pharmacol. 73:1-11(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, MUTAGENESIS OF MET-1; MET-5; MET-16 AND MET-33.
[4]"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] (ISOFORM 1).
[5]"Identification of a human cell growth-inhibiting gene."
Kim J.W., Kim H.K., Shin S.M.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[9]"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].
[10]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].
[11]"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 1).
Tissue: Urinary bladder.
[12]"Differential expression of a basic helix-loop-helix phosphoprotein gene, G0S8, in acute leukemia and localization to human chromosome 1q31."
Wu H.-K., Heng H.H.Q., Shi X.-M., Forsdyke D.R., Tsui L.-C., Mak T.W., Minden M.D., Siderovski D.P.
Leukemia 9:1291-1298(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[13]"Protein kinase C phosphorylates RGS2 and modulates its capacity for negative regulation of Galpha 11 signaling."
Cunningham M.L., Waldo G.L., Hollinger S., Hepler J.R., Harden T.K.
J. Biol. Chem. 276:5438-5444(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[14]"Regulator of G-protein signaling-2 mediates vascular smooth muscle relaxation and blood pressure."
Tang K.M., Wang G.R., Lu P., Karas R.H., Aronovitz M., Heximer S.P., Kaltenbronn K.M., Blumer K.J., Siderovski D.P., Zhu Y., Mendelsohn M.E.
Nat. Med. 9:1506-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY PRKG1, INTERACTION WITH PRKG1.
[15]"Translational control by RGS2."
Nguyen C.H., Ming H., Zhao P., Hugendubler L., Gros R., Kimball S.R., Chidiac P.
J. Cell Biol. 186:755-765(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EIF2B5, MUTAGENESIS OF LEU-79; GLU-86; LEU-87; SER-90; LYS-102; PHE-105; ILE-110; GLU-111; LEU-114 AND ASN-149.
[16]"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 (2.3 ANGSTROMS) OF 71-203.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13391 Genomic DNA. Translation: AAA20680.1.
L13463 mRNA. Translation: AAC37587.1.
AF493926 mRNA. Translation: AAM12640.1.
AY971351 mRNA. Translation: AAY40361.1.
AK313668 mRNA. Translation: BAG36420.1.
BT007065 mRNA. Translation: AAP35728.1.
CR457410 mRNA. Translation: CAG33691.1.
AL035407 Genomic DNA. Translation: CAB62512.1.
CH471067 Genomic DNA. Translation: EAW91231.1.
BC007049 mRNA. Translation: AAH07049.1.
PIRI53020.
RefSeqNP_002914.1. NM_002923.3.
UniGeneHs.78944.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AF0X-ray2.30A71-203[»]
2V4ZX-ray2.80B71-209[»]
4EKCX-ray7.40B/D72-203[»]
4EKDX-ray2.71B72-203[»]
ProteinModelPortalP41220.
SMRP41220. Positions 73-200.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111929. 54 interactions.
DIPDIP-44289N.
IntActP41220. 44 interactions.
MINTMINT-1380095.
STRING9606.ENSP00000235382.

PTM databases

PhosphoSiteP41220.

Polymorphism databases

DMDM729545.

Proteomic databases

PaxDbP41220.
PRIDEP41220.

Protocols and materials databases

DNASU5997.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000235382; ENSP00000235382; ENSG00000116741. [P41220-1]
GeneID5997.
KEGGhsa:5997.
UCSCuc001gsl.3. human. [P41220-1]

Organism-specific databases

CTD5997.
GeneCardsGC01P192778.
HGNCHGNC:9998. RGS2.
HPAHPA013385.
MIM600861. gene.
neXtProtNX_P41220.
PharmGKBPA34372.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG252352.
HOGENOMHOG000233512.
HOVERGENHBG013233.
InParanoidP41220.
KOK16449.
OMAKSKQQAF.
OrthoDBEOG7VHSZ5.
PhylomeDBP41220.
TreeFamTF315837.

Gene expression databases

ArrayExpressP41220.
BgeeP41220.
CleanExHS_RGS2.
GenevestigatorP41220.

Family and domain databases

Gene3D1.10.196.10. 2 hits.
InterProIPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
[Graphical view]
PfamPF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR01301. RGSPROTEIN.
SMARTSM00315. RGS. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
PROSITEPS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRGS2. human.
EvolutionaryTraceP41220.
GeneWikiRGS2.
GenomeRNAi5997.
NextBio23371.
PROP41220.
SOURCESearch...

Entry information

Entry nameRGS2_HUMAN
AccessionPrimary (citable) accession number: P41220
Secondary accession number(s): Q6I9U5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 136 of the entry and version 1 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 1

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