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P41220

- RGS2_HUMAN

UniProt

P41220 - RGS2_HUMAN

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
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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
    3. protein binding Source: UniProtKB

    GO - Biological processi

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

    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-SubCell
    5. neuron projection Source: Ensembl
    6. nucleolus Source: UniProtKB-SubCell
    7. plasma membrane Source: RefGenome

    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

    ArrayExpressiP41220.
    BgeeiP41220.
    CleanExiHS_RGS2.
    GenevestigatoriP41220.

    Organism-specific databases

    HPAiHPA013385.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi111929. 55 interactions.
    DIPiDIP-44289N.
    IntActiP41220. 44 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.
    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: P41220-1) [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

    MQSAMFLAVQ HDCRPMDKSA GSGHKSEEKR EKMKRTLLKD WKTRLSYFLQ    50
    NSSTPGKPKT GKKSKQQAFI KPSPEEAQLW SEAFDELLAS KYGLAAFRAF 100
    LKSEFCEENI EFWLACEDFK KTKSPQKLSS KARKIYTDFI EKEAPKEINI 150
    DFQTKTLIAQ NIQEATSGCF TTAQKRVYSL MENNSYPRFL ESEFYQDLCK 200
    KPQITTEPHA T 211
    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. 44 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.
    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

    ArrayExpressi P41220.
    Bgeei P41220.
    CleanExi HS_RGS2.
    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

    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 1, 2014
    This is version 141 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