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P41220

- RGS2_HUMAN

UniProt

P41220 - RGS2_HUMAN

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Protein

Regulator of G-protein signaling 2

Gene

RGS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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. 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.4 Publications

GO - Molecular functioni

  1. calmodulin binding Source: ProtInc
  2. GTPase activator activity Source: RefGenome

GO - Biological processi

  1. brown fat cell differentiation Source: Ensembl
  2. cell cycle Source: UniProtKB-KW
  3. negative regulation of cAMP-mediated signaling Source: Ensembl
  4. negative regulation of cardiac muscle hypertrophy Source: BHF-UCL
  5. negative regulation of G-protein coupled receptor protein signaling pathway Source: BHF-UCL
  6. negative regulation of MAP kinase activity Source: BHF-UCL
  7. negative regulation of phospholipase activity Source: BHF-UCL
  8. positive regulation of cardiac muscle contraction Source: BHF-UCL
  9. positive regulation of microtubule polymerization Source: Ensembl
  10. regulation of adrenergic receptor signaling pathway Source: BHF-UCL
  11. regulation of G-protein coupled receptor protein signaling pathway Source: ProtInc
  12. regulation of translation Source: UniProtKB-KW
  13. relaxation of cardiac muscle Source: BHF-UCL
  14. relaxation of vascular smooth muscle Source: Ensembl
  15. spermatogenesis Source: Ensembl
  16. termination of G-protein coupled receptor signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Keywords - Biological processi

Cell cycle, Translation regulation

Enzyme and pathway databases

ReactomeiREACT_18283. G alpha (q) signalling events.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RGS2
Synonyms:G0S8
ORF Names:GIG31
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9998. RGS2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. cytoplasmic side of plasma membrane Source: BHF-UCL
  3. cytosol Source: BHF-UCL
  4. mitochondrion Source: UniProtKB-KW
  5. neuron projection Source: Ensembl
  6. nucleus Source: UniProtKB-KW
  7. plasma membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 11M → L: Loss of isoform 1 expression. 1 Publication
Mutagenesisi5 – 51M → L: Loss of isoform 2 expression. 1 Publication
Mutagenesisi16 – 161M → L: Loss of isoform 3 expression. 1 Publication
Mutagenesisi33 – 331M → L: Loss of isoform 4 expression. 1 Publication
Mutagenesisi37 – 371L → D: Impairs association with plasma membrane. 1 Publication
Mutagenesisi38 – 381L → D: Impairs association with plasma membrane. 1 Publication
Mutagenesisi41 – 411W → D: Impairs association with plasma membrane. 1 Publication
Mutagenesisi45 – 451L → D: Impairs association with plasma membrane. 1 Publication
Mutagenesisi48 – 481F → D: Impairs association with plasma membrane. 1 Publication
Mutagenesisi49 – 491L → D: Impairs association with plasma membrane. 1 Publication
Mutagenesisi79 – 791L → 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. 1 Publication
Mutagenesisi86 – 861E → 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. 1 Publication
Mutagenesisi87 – 871L → 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. 1 Publication
Mutagenesisi90 – 901S → 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. 1 Publication
Mutagenesisi102 – 1021K → 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. 1 Publication
Mutagenesisi105 – 1051F → 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. 1 Publication
Mutagenesisi110 – 1101I → 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. 1 Publication
Mutagenesisi111 – 1111E → 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. 1 Publication
Mutagenesisi114 – 1141L → 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. 1 Publication
Mutagenesisi149 – 1491N → 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. 1 Publication

Organism-specific databases

PharmGKBiPA34372.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Regulator of G-protein signaling 2PRO_0000204178Add
BLAST

Post-translational modificationi

Phosphorylated by protein kinase C. Phosphorylation by PRKG1 leads to activation of RGS2 activity.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41220.
PaxDbiP41220.
PRIDEiP41220.

PTM databases

PhosphoSiteiP41220.

Expressioni

Tissue specificityi

Expressed in acute myelogenous leukemia (AML) and in acute lymphoblastic leukemia (ALL).1 Publication

Gene expression databases

BgeeiP41220.
CleanExiHS_RGS2.
ExpressionAtlasiP41220. baseline and differential.
GenevestigatoriP41220.

Organism-specific databases

HPAiHPA013385.

Interactioni

Subunit structurei

Interacts with EIF2B5. Interacts with PRKG1 (isoform alpha).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0076EBI-712388,EBI-5323863
PPP1R9AQ9ULJ83EBI-712388,EBI-2515561

Protein-protein interaction databases

BioGridi111929. 55 interactions.
DIPiDIP-44289N.
IntActiP41220. 46 interactions.
MINTiMINT-1380095.
STRINGi9606.ENSP00000235382.

Structurei

Secondary structure

1
211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi74 – 796
Turni80 – 823
Helixi84 – 896
Helixi91 – 10313
Helixi108 – 12013
Helixi125 – 13915
Helixi152 – 16110
Helixi162 – 1643
Turni167 – 1704
Helixi171 – 18313
Helixi185 – 1917
Helixi193 – 1997

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AF0X-ray2.30A71-203[»]
2V4ZX-ray2.80B71-209[»]
4EKCX-ray7.40B/D72-203[»]
4EKDX-ray2.71B72-203[»]
ProteinModelPortaliP41220.
SMRiP41220. Positions 73-200.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41220.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini83 – 199117RGSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 6635Necessary for membrane associationAdd
BLAST
Regioni79 – 11638Necessary to inhibit protein synthesisAdd
BLAST

Sequence similaritiesi

Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG252352.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiP41220.
KOiK18154.
OMAiQQAFIKP.
OrthoDBiEOG7VHSZ5.
PhylomeDBiP41220.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
InterProiIPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
[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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative initiation. Align

Isoform 1 (identifier: P41220) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MQSAMFLAVQ HDCRPMDKSA GSGHKSEEKR EKMKRTLLKD WKTRLSYFLQ
60 70 80 90 100
NSSTPGKPKT GKKSKQQAFI KPSPEEAQLW SEAFDELLAS KYGLAAFRAF
110 120 130 140 150
LKSEFCEENI EFWLACEDFK KTKSPQKLSS KARKIYTDFI EKEAPKEINI
160 170 180 190 200
DFQTKTLIAQ NIQEATSGCF TTAQKRVYSL MENNSYPRFL ESEFYQDLCK
210
KPQITTEPHA T
Length:211
Mass (Da):24,382
Last modified:February 1, 1995 - v1
Checksum:iEFFE4AE47EF9AD8F
GO
Isoform 2 (identifier: P41220-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: Missing.

Show »
Length:207
Mass (Da):23,964
Checksum:iE5DCCB2F18E09F51
GO
Isoform 3 (identifier: P41220-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: Missing.

Note: Lacks type V adenylyl cyclase (AC) inhibitory function.

Show »
Length:196
Mass (Da):22,666
Checksum:i2F5BF7609CD4172A
GO
Isoform 4 (identifier: P41220-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.

Note: Lacks type V adenylyl cyclase (AC) inhibitory function.

Show »
Length:179
Mass (Da):20,780
Checksum:i6CF0306689DC7A54
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3232Missing in isoform 4. 1 PublicationVSP_041298Add
BLAST
Alternative sequencei1 – 1515Missing in isoform 3. 1 PublicationVSP_041297Add
BLAST
Alternative sequencei1 – 44Missing in isoform 2. 1 PublicationVSP_041296

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1377.1. [P41220-1]
PIRiI53020.
RefSeqiNP_002914.1. NM_002923.3. [P41220-1]
UniGeneiHs.78944.

Genome annotation databases

EnsembliENST00000235382; ENSP00000235382; ENSG00000116741. [P41220-1]
GeneIDi5997.
KEGGihsa:5997.
UCSCiuc001gsl.3. human. [P41220-1]

Polymorphism databases

DMDMi729545.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1377.1. [P41220-1 ]
PIRi I53020.
RefSeqi NP_002914.1. NM_002923.3. [P41220-1 ]
UniGenei Hs.78944.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AF0 X-ray 2.30 A 71-203 [» ]
2V4Z X-ray 2.80 B 71-209 [» ]
4EKC X-ray 7.40 B/D 72-203 [» ]
4EKD X-ray 2.71 B 72-203 [» ]
ProteinModelPortali P41220.
SMRi P41220. Positions 73-200.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111929. 55 interactions.
DIPi DIP-44289N.
IntActi P41220. 46 interactions.
MINTi MINT-1380095.
STRINGi 9606.ENSP00000235382.

PTM databases

PhosphoSitei P41220.

Polymorphism databases

DMDMi 729545.

Proteomic databases

MaxQBi P41220.
PaxDbi P41220.
PRIDEi P41220.

Protocols and materials databases

DNASUi 5997.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000235382 ; ENSP00000235382 ; ENSG00000116741 . [P41220-1 ]
GeneIDi 5997.
KEGGi hsa:5997.
UCSCi uc001gsl.3. human. [P41220-1 ]

Organism-specific databases

CTDi 5997.
GeneCardsi GC01P192778.
HGNCi HGNC:9998. RGS2.
HPAi HPA013385.
MIMi 600861. gene.
neXtProti NX_P41220.
PharmGKBi PA34372.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG252352.
GeneTreei ENSGT00760000118903.
HOGENOMi HOG000233512.
HOVERGENi HBG013233.
InParanoidi P41220.
KOi K18154.
OMAi QQAFIKP.
OrthoDBi EOG7VHSZ5.
PhylomeDBi P41220.
TreeFami TF315837.

Enzyme and pathway databases

Reactomei REACT_18283. G alpha (q) signalling events.

Miscellaneous databases

ChiTaRSi RGS2. human.
EvolutionaryTracei P41220.
GeneWikii RGS2.
GenomeRNAii 5997.
NextBioi 23371.
PROi P41220.
SOURCEi Search...

Gene expression databases

Bgeei P41220.
CleanExi HS_RGS2.
ExpressionAtlasi P41220. baseline and differential.
Genevestigatori P41220.

Family and domain databases

Gene3Di 1.10.196.10. 2 hits.
InterProi IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
[Graphical view ]
Pfami PF00615. RGS. 1 hit.
[Graphical view ]
PRINTSi PR01301. RGSPROTEIN.
SMARTi SM00315. RGS. 1 hit.
[Graphical view ]
SUPFAMi SSF48097. SSF48097. 1 hit.
PROSITEi PS50132. RGS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 71-203.

Entry informationi

Entry nameiRGS2_HUMAN
AccessioniPrimary (citable) accession number: P41220
Secondary accession number(s): Q6I9U5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3