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Q9NS28

- RGS18_HUMAN

UniProt

Q9NS28 - RGS18_HUMAN

Protein

Regulator of G-protein signaling 18

Gene

RGS18

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      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. Binds to G(i) alpha-1, G(i) alpha-2, G(i) alpha-3 and G(q) alpha.2 Publications

    GO - Molecular functioni

    1. GTPase activator activity Source: RefGenome

    GO - Biological processi

    1. G-protein coupled receptor signaling pathway Source: Ensembl
    2. termination of G-protein coupled receptor signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Signal transduction inhibitor

    Enzyme and pathway databases

    ReactomeiREACT_18283. G alpha (q) signalling events.
    REACT_19231. G alpha (i) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulator of G-protein signaling 18
    Short name:
    RGS18
    Gene namesi
    Name:RGS18
    Synonyms:RGS13
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:14261. RGS18.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. plasma membrane Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34369.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 235235Regulator of G-protein signaling 18PRO_0000204227Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei49 – 491Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9NS28.
    PRIDEiQ9NS28.

    2D gel databases

    OGPiQ9NS28.

    PTM databases

    PhosphoSiteiQ9NS28.

    Expressioni

    Tissue specificityi

    Expressed in peripheral leukocytes, bone marrow, platelet, spleen and fetal liver.2 Publications

    Gene expression databases

    BgeeiQ9NS28.
    CleanExiHS_RGS13.
    HS_RGS18.
    GenevestigatoriQ9NS28.

    Organism-specific databases

    HPAiHPA045780.

    Interactioni

    Protein-protein interaction databases

    BioGridi122160. 5 interactions.
    DIPiDIP-59096N.
    STRINGi9606.ENSP00000356430.

    Structurei

    Secondary structure

    1
    235
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi77 – 837
    Helixi87 – 926
    Helixi94 – 10613
    Helixi111 – 12212
    Helixi127 – 14115
    Beta strandi144 – 1474
    Helixi155 – 1639
    Helixi164 – 1663
    Turni170 – 1734
    Helixi174 – 18613
    Helixi188 – 1936
    Helixi196 – 2027

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DLVNMR-A76-202[»]
    2JM5NMR-A75-223[»]
    2OWINMR-A75-223[»]
    ProteinModelPortaliQ9NS28.
    SMRiQ9NS28. Positions 77-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NS28.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini86 – 202117RGSPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RGS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG278594.
    HOGENOMiHOG000233512.
    HOVERGENiHBG013233.
    InParanoidiQ9NS28.
    KOiK16449.
    OMAiLDFHTKE.
    OrthoDBiEOG7VHSZ5.
    PhylomeDBiQ9NS28.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9NS28-1 [UniParc]FASTAAdd to Basket

    « Hide

    METTLLFFSQ INMCESKEKT FFKLIHGSGK EETSKEAKIR AKEKRNRLSL    50
    LVQKPEFHED TRSSRSGHLA KETRVSPEEA VKWGESFDKL LSHRDGLEAF 100
    TRFLKTEFSE ENIEFWIACE DFKKSKGPQQ IHLKAKAIYE KFIQTDAPKE 150
    VNLDFHTKEV ITNSITQPTL HSFDAAQSRV YQLMEQDSYT RFLKSDIYLD 200
    LMEGRPQRPT NLRRRSRSFT CNEFQDVQSD VAIWL 235
    Length:235
    Mass (Da):27,582
    Last modified:October 1, 2000 - v1
    Checksum:i973ABDE8EC7DE3D5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti226 – 2272DV → ML(PubMed:11042171)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076642 mRNA. Translation: AAF80227.1.
    AF268036 mRNA. Translation: AAK58589.1.
    AL596342, AL513175 Genomic DNA. Translation: CAH71160.1.
    AK315377 mRNA. Translation: BAG37770.1.
    AL513175, AL596342 Genomic DNA. Translation: CAH70529.1.
    CH471067 Genomic DNA. Translation: EAW91223.1.
    BC020632 mRNA. Translation: AAH20632.1.
    CCDSiCCDS1374.1.
    RefSeqiNP_570138.1. NM_130782.2.
    UniGeneiHs.440890.

    Genome annotation databases

    EnsembliENST00000367460; ENSP00000356430; ENSG00000150681.
    GeneIDi64407.
    KEGGihsa:64407.
    UCSCiuc001gsg.3. human.

    Polymorphism databases

    DMDMi15214228.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF076642 mRNA. Translation: AAF80227.1 .
    AF268036 mRNA. Translation: AAK58589.1 .
    AL596342 , AL513175 Genomic DNA. Translation: CAH71160.1 .
    AK315377 mRNA. Translation: BAG37770.1 .
    AL513175 , AL596342 Genomic DNA. Translation: CAH70529.1 .
    CH471067 Genomic DNA. Translation: EAW91223.1 .
    BC020632 mRNA. Translation: AAH20632.1 .
    CCDSi CCDS1374.1.
    RefSeqi NP_570138.1. NM_130782.2.
    UniGenei Hs.440890.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DLV NMR - A 76-202 [» ]
    2JM5 NMR - A 75-223 [» ]
    2OWI NMR - A 75-223 [» ]
    ProteinModelPortali Q9NS28.
    SMRi Q9NS28. Positions 77-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122160. 5 interactions.
    DIPi DIP-59096N.
    STRINGi 9606.ENSP00000356430.

    PTM databases

    PhosphoSitei Q9NS28.

    Polymorphism databases

    DMDMi 15214228.

    2D gel databases

    OGPi Q9NS28.

    Proteomic databases

    PaxDbi Q9NS28.
    PRIDEi Q9NS28.

    Protocols and materials databases

    DNASUi 64407.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367460 ; ENSP00000356430 ; ENSG00000150681 .
    GeneIDi 64407.
    KEGGi hsa:64407.
    UCSCi uc001gsg.3. human.

    Organism-specific databases

    CTDi 64407.
    GeneCardsi GC01P192127.
    HGNCi HGNC:14261. RGS18.
    HPAi HPA045780.
    MIMi 607192. gene.
    neXtProti NX_Q9NS28.
    PharmGKBi PA34369.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG278594.
    HOGENOMi HOG000233512.
    HOVERGENi HBG013233.
    InParanoidi Q9NS28.
    KOi K16449.
    OMAi LDFHTKE.
    OrthoDBi EOG7VHSZ5.
    PhylomeDBi Q9NS28.
    TreeFami TF315837.

    Enzyme and pathway databases

    Reactomei REACT_18283. G alpha (q) signalling events.
    REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    EvolutionaryTracei Q9NS28.
    GeneWikii RGS18.
    GenomeRNAii 64407.
    NextBioi 66362.
    PROi Q9NS28.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NS28.
    CleanExi HS_RGS13.
    HS_RGS18.
    Genevestigatori Q9NS28.

    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 novel regulator of G-protein signaling."
      Zhang W., Wan T., Yuan Z., He L., Cao X.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular cloning and characterization of a novel regulator of G-protein signaling from mouse hematopoietic stem cells."
      Park I.K., Klug C.A., Li K., Jerabek L., Li L., Nanamori M., Neubig R.R., Hood L., Weissman I.L., Clarke M.F.
      J. Biol. Chem. 276:915-923(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    3. "Cloning and characterization of a novel regulator of G protein signalling in human platelets."
      Gagnon A.W., Murray D.L., Leadley R.J. Jr.
      Cell. Signal. 14:595-606(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Platelet.
    4. "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].
      Tissue: Amygdala.
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Liver.
    8. "Differential proteome analysis of TRAP-activated platelets: involvement of DOK-2 and phosphorylation of RGS proteins."
      Garcia A., Prabhakar S., Hughan S., Anderson T.W., Brock C.J., Pearce A.C., Dwek R.A., Watson S.P., Hebestreit H.F., Zitzmann N.
      Blood 103:2088-2095(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-49.
    9. "Solution structure of the RGS domain of human regulator of G-protein signaling 18."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 76-204.

    Entry informationi

    Entry nameiRGS18_HUMAN
    AccessioniPrimary (citable) accession number: Q9NS28
    Secondary accession number(s): B2RD23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 14, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 110 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