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P49802

- RGS7_HUMAN

UniProt

P49802 - RGS7_HUMAN

Protein

Regulator of G-protein signaling 7

Gene

RGS7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (18 Oct 2001)
      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. Activity on G(o)-alpha is specifically enhanced by the RGS6/GNG5 dimer. May play a role in synaptic vesicle exocytosis. May play important role in the rapid regulation of neuronal excitability and the cellular responses to short-lived stimulations By similarity.By similarity

    GO - Molecular functioni

    1. G-protein beta-subunit binding Source: UniProt
    2. GTPase activator activity Source: RefGenome
    3. signal transducer activity Source: InterPro

    GO - Biological processi

    1. G-protein coupled receptor signaling pathway Source: InterPro
    2. intracellular signal transduction Source: InterPro
    3. positive regulation of GTPase activity Source: GOC
    4. termination of G-protein coupled receptor signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Signal transduction inhibitor

    Enzyme and pathway databases

    ReactomeiREACT_19231. G alpha (i) signalling events.
    SignaLinkiP49802.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulator of G-protein signaling 7
    Short name:
    RGS7
    Gene namesi
    Name:RGS7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10003. RGS7.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. cytosol Source: Ensembl
    3. dendrite terminus Source: Ensembl
    4. heterotrimeric G-protein complex Source: InterPro
    5. nucleus Source: Ensembl
    6. plasma membrane Source: RefGenome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi306 – 3061W → F: Diminishes interaction with Gbeta5. 1 Publication

    Organism-specific databases

    PharmGKBiPA34378.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 495495Regulator of G-protein signaling 7PRO_0000204196Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei434 – 4341Phosphoserine1 Publication

    Post-translational modificationi

    Palmitoylated.By similarity
    Phosphorylation and subsequent interaction with 14-3-3 proteins inhibits GAP activity.1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP49802.
    PaxDbiP49802.
    PRIDEiP49802.

    PTM databases

    PhosphoSiteiP49802.

    Expressioni

    Gene expression databases

    ArrayExpressiP49802.
    BgeeiP49802.
    CleanExiHS_RGS7.
    GenevestigatoriP49802.

    Organism-specific databases

    HPAiCAB017561.
    HPA000688.

    Interactioni

    Subunit structurei

    Heterodimer with GNG5. Interacts with RGS7BP, leading to regulate the subcellular location of the heterodimer formed with Gbeta5 By similarity. Interacts with 14-3-3 protein Tau and SNAPIN.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi111932. 8 interactions.
    DIPiDIP-40869N.
    IntActiP49802. 5 interactions.
    MINTiMINT-136910.
    STRINGi9606.ENSP00000355520.

    Structurei

    Secondary structure

    1
    495
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi324 – 3296
    Helixi330 – 3323
    Helixi334 – 3396
    Helixi341 – 35313
    Helixi358 – 36912
    Helixi374 – 3763
    Helixi377 – 38812
    Helixi401 – 41212
    Turni414 – 4196
    Helixi420 – 43213
    Helixi434 – 4407
    Helixi442 – 4498

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A72X-ray2.00A/B320-463[»]
    2D9JNMR-A323-448[»]
    ProteinModelPortaliP49802.
    SMRiP49802. Positions 19-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49802.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini37 – 11276DEPPROSITE-ProRule annotationAdd
    BLAST
    Domaini255 – 31662G protein gammaAdd
    BLAST
    Domaini333 – 448116RGSPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 DEP domain.PROSITE-ProRule annotation
    Contains 1 G protein gamma domain.Curated
    Contains 1 RGS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG327614.
    HOVERGENiHBG007404.
    InParanoidiP49802.
    KOiK16449.
    OMAiWIMKNLD.
    PhylomeDBiP49802.
    TreeFamiTF351956.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    1.10.196.10. 1 hit.
    4.10.260.10. 1 hit.
    InterProiIPR000591. 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]
    PfamiPF00610. DEP. 1 hit.
    PF00631. G-gamma. 1 hit.
    PF00615. RGS. 1 hit.
    [Graphical view]
    PRINTSiPR01301. RGSPROTEIN.
    SMARTiSM00049. DEP. 1 hit.
    SM00224. GGL. 1 hit.
    SM00315. RGS. 1 hit.
    [Graphical view]
    SUPFAMiSSF48097. SSF48097. 1 hit.
    SSF48670. SSF48670. 1 hit.
    PROSITEiPS50186. DEP. 1 hit.
    PS50132. RGS. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49802-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAQGNNYGQT SNGVADESPN MLVYRKMEDV IARMQDEKNG IPIRTVKSFL    50
    SKIPSVFSGS DIVQWLIKNL TIEDPVEALH LGTLMAAHGY FFPISDHVLT 100
    LKDDGTFYRF QTPYFWPSNC WEPENTDYAV YLCKRTMQNK ARLELADYEA 150
    ESLARLQRAF ARKWEFIFMQ AEAQAKVDKK RDKIERKILD SQERAFWDVH 200
    RPVPGCVNTT EVDIKKSSRM RNPHKTRKSV YGLQNDIRSH SPTHTPTPET 250
    KPPTEDELQQ QIKYWQIQLD RHRLKMSKVA DSLLSYTEQY LEYDPFLLPP 300
    DPSNPWLSDD TTFWELEASK EPSQQRVKRW GFGMDEALKD PVGREQFLKF 350
    LESEFSSENL RFWLAVEDLK KRPIKEVPSR VQEIWQEFLA PGAPSAINLD 400
    SKSYDKTTQN VKEPGRYTFE DAQEHIYKLM KSDSYPRFIR SSAYQELLQA 450
    KKKSGNSMDR RTSFEKFAQN VGRNIPIFPC HKNCTPTLRA STNLL 495
    Length:495
    Mass (Da):57,668
    Last modified:October 18, 2001 - v3
    Checksum:i1FCC2D60622675DE
    GO
    Isoform 2 (identifier: P49802-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         454-495: SGNSMDRRTSFEKFAQNVGRNIPIFPCHKNCTPTLRASTNLL → GKSLTSKRLTSLAQSY

    Show »
    Length:469
    Mass (Da):54,685
    Checksum:i993C1209EDD884EC
    GO
    Isoform 3 (identifier: P49802-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         454-471: Missing.

    Show »
    Length:477
    Mass (Da):55,612
    Checksum:iA7252A838E1881A9
    GO
    Isoform 4 (identifier: P49802-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         76-128: Missing.
         454-471: Missing.

    Show »
    Length:424
    Mass (Da):49,387
    Checksum:i25A8A2F507C07E87
    GO
    Isoform 5 (identifier: P49802-5) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:487
    Mass (Da):56,741
    Checksum:i50BDD0E8896444BC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261K → R in AAM12645. 1 PublicationCurated
    Sequence conflicti234 – 2341Q → R in AAM12644. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti137 – 1371M → L.
    Corresponds to variant rs12746550 [ dbSNP | Ensembl ].
    VAR_057153
    Natural varianti409 – 4091Q → H.1 Publication
    Corresponds to variant rs17851953 [ dbSNP | Ensembl ].
    VAR_060604

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei76 – 12853Missing in isoform 4. 1 PublicationVSP_005671Add
    BLAST
    Alternative sequencei454 – 49542SGNSM…STNLL → GKSLTSKRLTSLAQSY in isoform 2. 2 PublicationsVSP_005672Add
    BLAST
    Alternative sequencei454 – 47118Missing in isoform 3 and isoform 4. 1 PublicationVSP_005673Add
    BLAST
    Alternative sequencei473 – 49523RNIPI…STNLL → KSLTSKRLTSLAQSY in isoform 5. 1 PublicationVSP_038388Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090116 mRNA. Translation: AAD34290.1.
    AF090117 mRNA. Translation: AAD34291.1.
    U32439 mRNA. Translation: AAC50351.1.
    AF493930 mRNA. Translation: AAM12644.1.
    AF493931 mRNA. Translation: AAM12645.1.
    AY587875 mRNA. Translation: AAT52231.1.
    AL512307
    , AL359764, AL365184, AL590682 Genomic DNA. Translation: CAH71987.1.
    AL512307
    , AL359764, AL365184, AL590682 Genomic DNA. Translation: CAH71988.1.
    AL512307
    , AL359764, AL365184, AL590682 Genomic DNA. Translation: CAH71989.1.
    AL512307
    , AL359764, AL365184, AL590682 Genomic DNA. Translation: CAH71990.1.
    AL590682
    , AL359764, AL365184, AL512307 Genomic DNA. Translation: CAH73809.1.
    AL590682
    , AL359764, AL365184, AL512307 Genomic DNA. Translation: CAH73810.1.
    AL590682
    , AL359764, AL365184, AL512307 Genomic DNA. Translation: CAH73811.1.
    AL590682
    , AL359764, AL365184, AL512307 Genomic DNA. Translation: CAH73812.1.
    AL359764
    , AL365184, AL512307, AL590682 Genomic DNA. Translation: CAI15140.1.
    AL359764
    , AL365184, AL512307, AL590682 Genomic DNA. Translation: CAI15141.1.
    AL359764
    , AL365184, AL512307, AL590682 Genomic DNA. Translation: CAI15142.1.
    AL359764
    , AL365184, AL512307, AL590682 Genomic DNA. Translation: CAI15143.1.
    AL365184
    , AL359764, AL512307, AL590682 Genomic DNA. Translation: CAI16818.1.
    AL365184
    , AL359764, AL512307, AL590682 Genomic DNA. Translation: CAI16819.1.
    AL365184
    , AL359764, AL512307, AL590682 Genomic DNA. Translation: CAI16820.1.
    AL365184
    , AL359764, AL512307, AL590682 Genomic DNA. Translation: CAI16821.1.
    CH471098 Genomic DNA. Translation: EAW70086.1.
    BC022009 mRNA. Translation: AAH22009.1.
    CCDSiCCDS31071.1. [P49802-5]
    CCDS60457.1. [P49802-4]
    CCDS60458.1. [P49802-2]
    CCDS60459.1. [P49802-3]
    RefSeqiNP_001269702.1. NM_001282773.1. [P49802-4]
    NP_001269704.1. NM_001282775.1. [P49802-3]
    NP_001269707.1. NM_001282778.1. [P49802-2]
    NP_002915.3. NM_002924.5. [P49802-5]
    XP_005273275.1. XM_005273218.1. [P49802-1]
    UniGeneiHs.655739.

    Genome annotation databases

    EnsembliENST00000348120; ENSP00000341242; ENSG00000182901. [P49802-4]
    ENST00000366562; ENSP00000355520; ENSG00000182901. [P49802-2]
    ENST00000366563; ENSP00000355521; ENSG00000182901. [P49802-3]
    ENST00000366564; ENSP00000355522; ENSG00000182901. [P49802-2]
    ENST00000366565; ENSP00000355523; ENSG00000182901. [P49802-5]
    ENST00000401882; ENSP00000385508; ENSG00000182901. [P49802-4]
    GeneIDi6000.
    KEGGihsa:6000.
    UCSCiuc001hyt.2. human. [P49802-1]
    uc001hyu.2. human. [P49802-3]
    uc001hyv.2. human. [P49802-5]
    uc001hyw.2. human. [P49802-2]
    uc009xgn.1. human. [P49802-4]

    Polymorphism databases

    DMDMi17380284.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090116 mRNA. Translation: AAD34290.1 .
    AF090117 mRNA. Translation: AAD34291.1 .
    U32439 mRNA. Translation: AAC50351.1 .
    AF493930 mRNA. Translation: AAM12644.1 .
    AF493931 mRNA. Translation: AAM12645.1 .
    AY587875 mRNA. Translation: AAT52231.1 .
    AL512307
    , AL359764 , AL365184 , AL590682 Genomic DNA. Translation: CAH71987.1 .
    AL512307
    , AL359764 , AL365184 , AL590682 Genomic DNA. Translation: CAH71988.1 .
    AL512307
    , AL359764 , AL365184 , AL590682 Genomic DNA. Translation: CAH71989.1 .
    AL512307
    , AL359764 , AL365184 , AL590682 Genomic DNA. Translation: CAH71990.1 .
    AL590682
    , AL359764 , AL365184 , AL512307 Genomic DNA. Translation: CAH73809.1 .
    AL590682
    , AL359764 , AL365184 , AL512307 Genomic DNA. Translation: CAH73810.1 .
    AL590682
    , AL359764 , AL365184 , AL512307 Genomic DNA. Translation: CAH73811.1 .
    AL590682
    , AL359764 , AL365184 , AL512307 Genomic DNA. Translation: CAH73812.1 .
    AL359764
    , AL365184 , AL512307 , AL590682 Genomic DNA. Translation: CAI15140.1 .
    AL359764
    , AL365184 , AL512307 , AL590682 Genomic DNA. Translation: CAI15141.1 .
    AL359764
    , AL365184 , AL512307 , AL590682 Genomic DNA. Translation: CAI15142.1 .
    AL359764
    , AL365184 , AL512307 , AL590682 Genomic DNA. Translation: CAI15143.1 .
    AL365184
    , AL359764 , AL512307 , AL590682 Genomic DNA. Translation: CAI16818.1 .
    AL365184
    , AL359764 , AL512307 , AL590682 Genomic DNA. Translation: CAI16819.1 .
    AL365184
    , AL359764 , AL512307 , AL590682 Genomic DNA. Translation: CAI16820.1 .
    AL365184
    , AL359764 , AL512307 , AL590682 Genomic DNA. Translation: CAI16821.1 .
    CH471098 Genomic DNA. Translation: EAW70086.1 .
    BC022009 mRNA. Translation: AAH22009.1 .
    CCDSi CCDS31071.1. [P49802-5 ]
    CCDS60457.1. [P49802-4 ]
    CCDS60458.1. [P49802-2 ]
    CCDS60459.1. [P49802-3 ]
    RefSeqi NP_001269702.1. NM_001282773.1. [P49802-4 ]
    NP_001269704.1. NM_001282775.1. [P49802-3 ]
    NP_001269707.1. NM_001282778.1. [P49802-2 ]
    NP_002915.3. NM_002924.5. [P49802-5 ]
    XP_005273275.1. XM_005273218.1. [P49802-1 ]
    UniGenei Hs.655739.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2A72 X-ray 2.00 A/B 320-463 [» ]
    2D9J NMR - A 323-448 [» ]
    ProteinModelPortali P49802.
    SMRi P49802. Positions 19-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111932. 8 interactions.
    DIPi DIP-40869N.
    IntActi P49802. 5 interactions.
    MINTi MINT-136910.
    STRINGi 9606.ENSP00000355520.

    PTM databases

    PhosphoSitei P49802.

    Polymorphism databases

    DMDMi 17380284.

    Proteomic databases

    MaxQBi P49802.
    PaxDbi P49802.
    PRIDEi P49802.

    Protocols and materials databases

    DNASUi 6000.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000348120 ; ENSP00000341242 ; ENSG00000182901 . [P49802-4 ]
    ENST00000366562 ; ENSP00000355520 ; ENSG00000182901 . [P49802-2 ]
    ENST00000366563 ; ENSP00000355521 ; ENSG00000182901 . [P49802-3 ]
    ENST00000366564 ; ENSP00000355522 ; ENSG00000182901 . [P49802-2 ]
    ENST00000366565 ; ENSP00000355523 ; ENSG00000182901 . [P49802-5 ]
    ENST00000401882 ; ENSP00000385508 ; ENSG00000182901 . [P49802-4 ]
    GeneIDi 6000.
    KEGGi hsa:6000.
    UCSCi uc001hyt.2. human. [P49802-1 ]
    uc001hyu.2. human. [P49802-3 ]
    uc001hyv.2. human. [P49802-5 ]
    uc001hyw.2. human. [P49802-2 ]
    uc009xgn.1. human. [P49802-4 ]

    Organism-specific databases

    CTDi 6000.
    GeneCardsi GC01M240938.
    HGNCi HGNC:10003. RGS7.
    HPAi CAB017561.
    HPA000688.
    MIMi 602517. gene.
    neXtProti NX_P49802.
    PharmGKBi PA34378.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327614.
    HOVERGENi HBG007404.
    InParanoidi P49802.
    KOi K16449.
    OMAi WIMKNLD.
    PhylomeDBi P49802.
    TreeFami TF351956.

    Enzyme and pathway databases

    Reactomei REACT_19231. G alpha (i) signalling events.
    SignaLinki P49802.

    Miscellaneous databases

    ChiTaRSi RGS7. human.
    EvolutionaryTracei P49802.
    GeneWikii RGS7.
    GenomeRNAii 6000.
    NextBioi 23395.
    PROi P49802.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49802.
    Bgeei P49802.
    CleanExi HS_RGS7.
    Genevestigatori P49802.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    1.10.196.10. 1 hit.
    4.10.260.10. 1 hit.
    InterProi IPR000591. 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 ]
    Pfami PF00610. DEP. 1 hit.
    PF00631. G-gamma. 1 hit.
    PF00615. RGS. 1 hit.
    [Graphical view ]
    PRINTSi PR01301. RGSPROTEIN.
    SMARTi SM00049. DEP. 1 hit.
    SM00224. GGL. 1 hit.
    SM00315. RGS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48097. SSF48097. 1 hit.
    SSF48670. SSF48670. 1 hit.
    PROSITEi PS50186. DEP. 1 hit.
    PS50132. RGS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    2. "EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins."
      Koelle M.R., Horvitz H.R.
      Cell 84:115-125(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
      Tissue: Brain.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), VARIANT HIS-409.
      Tissue: Testis.
    7. "Fidelity of G protein beta-subunit association by the G protein gamma-subunit-like domains of RGS6, RGS7, and RGS11."
      Snow B.E., Betts L., Mangion J., Sondek J., Siderovski D.P.
      Proc. Natl. Acad. Sci. U.S.A. 96:6489-6494(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GBETA5, MUTAGENESIS OF TRP-306.
      Tissue: Brain.
    8. "14-3-3 interacts with regulator of G protein signaling proteins and modulates their activity."
      Benzing T., Yaffe M.B., Arnould T., Sellin L., Schermer B., Schilling B., Schreiber R., Kunzelmann K., Leparc G.G., Kim E., Walz G.
      J. Biol. Chem. 275:28167-28172(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-434, INTERACTION WITH 14-3-3 PROTEINS.
    9. "Snapin interacts with the N-terminus of regulator of G protein signaling 7."
      Hunt R.A., Edris W., Chanda P.K., Nieuwenhuijsen B., Young K.H.
      Biochem. Biophys. Res. Commun. 303:594-599(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNAPIN.
    10. "Solution structure of the RGS domain of regulator of G-protein signaling 7."
      RIKEN structural genomics initiative (RSGI)
      Submitted (DEC-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 323-448.

    Entry informationi

    Entry nameiRGS7_HUMAN
    AccessioniPrimary (citable) accession number: P49802
    Secondary accession number(s): Q5T3H4
    , Q8TD66, Q8TD67, Q8WW09, Q9UNU7, Q9Y6B9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 18, 2001
    Last modified: October 1, 2014
    This is version 148 of the entry and version 3 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. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3