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P49795

- RGS19_HUMAN

UniProt

P49795 - RGS19_HUMAN

Protein

Regulator of G-protein signaling 19

Gene

RGS19

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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-alpha subfamily 1 members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein.

    GO - Molecular functioni

    1. GTPase activator activity Source: RefGenome
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. autophagy Source: UniProtKB-KW
    2. G-protein coupled receptor signaling pathway Source: ProtInc
    3. positive regulation of GTPase activity Source: GOC
    4. small GTPase mediated signal transduction Source: ProtInc
    5. termination of G-protein coupled receptor signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Signal transduction inhibitor

    Keywords - Biological processi

    Autophagy

    Enzyme and pathway databases

    ReactomeiREACT_18283. G alpha (q) signalling events.
    REACT_19231. G alpha (i) signalling events.
    REACT_19333. G alpha (z) signalling events.
    SignaLinkiP49795.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulator of G-protein signaling 19
    Short name:
    RGS19
    Alternative name(s):
    G-alpha-interacting protein
    Short name:
    GAIP
    Gene namesi
    Name:RGS19
    Synonyms:GAIP, GNAI3IP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:13735. RGS19.

    Subcellular locationi

    GO - Cellular componenti

    1. brush border Source: Ensembl
    2. clathrin-coated vesicle Source: Ensembl
    3. cytoplasm Source: RefGenome
    4. Golgi apparatus Source: ProtInc
    5. membrane Source: ProtInc
    6. plasma membrane Source: RefGenome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi151 – 1511S → A: Diminishes gap activity towards G(i)-alpha3 and autophagy in colon cancer cells. 1 Publication

    Organism-specific databases

    PharmGKBiPA34370.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 217217Regulator of G-protein signaling 19PRO_0000204229Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei24 – 241PhosphoserineBy similarity
    Modified residuei97 – 971Phosphoserine1 Publication
    Modified residuei151 – 1511Phosphoserine; by MAPK1 and MAPK31 Publication

    Post-translational modificationi

    Fatty acylated. Heavily palmitoylated in the cysteine string motif.1 Publication
    Phosphorylated, mainly on serine residues.2 Publications

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP49795.
    PaxDbiP49795.
    PRIDEiP49795.

    PTM databases

    PhosphoSiteiP49795.

    Expressioni

    Tissue specificityi

    Highest expression in lung. Placenta, liver and heart also express high levels of GAIP.

    Gene expression databases

    ArrayExpressiP49795.
    BgeeiP49795.
    CleanExiHS_RGS19.
    GenevestigatoriP49795.

    Organism-specific databases

    HPAiCAB031925.

    Interactioni

    Subunit structurei

    Interacts with GIPC PDZ domain.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Gnai3P087534EBI-874907,EBI-874897From a different organism.

    Protein-protein interaction databases

    BioGridi115576. 12 interactions.
    IntActiP49795. 4 interactions.
    MINTiMINT-3017930.
    STRINGi9606.ENSP00000333194.

    Structurei

    Secondary structure

    1
    217
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi81 – 877
    Helixi92 – 954
    Helixi98 – 11114
    Helixi115 – 12511
    Helixi126 – 1283
    Helixi133 – 14513
    Turni146 – 1483
    Beta strandi150 – 1523
    Helixi160 – 1689
    Beta strandi169 – 1713
    Helixi178 – 19114
    Helixi193 – 1964
    Helixi200 – 2034

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CMZNMR-A76-217[»]
    ProteinModelPortaliP49795.
    SMRiP49795. Positions 79-206.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49795.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini90 – 206117RGSPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni207 – 21711Interaction with GIPCAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi39 – 4911Poly-CysAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RGS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG258376.
    HOGENOMiHOG000233513.
    HOVERGENiHBG013233.
    InParanoidiP49795.
    KOiK16449.
    OMAiFDKLMHS.
    OrthoDBiEOG7SN8DQ.
    PhylomeDBiP49795.
    TreeFamiTF315837.

    Family and domain databases

    Gene3Di1.10.196.10. 1 hit.
    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.

    P49795-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPTPHEAEKQ ITGPEEADRP PSMSSHDTAS PAAPSRNPCC LCWCCCCSCS    50
    WNQERRRAWQ ASRESKLQPL PSCEVCATPS PEEVQSWAQS FDKLMHSPAG 100
    RSVFRAFLRT EYSEENMLFW LACEELKAEA NQHVVDEKAR LIYEDYVSIL 150
    SPKEVSLDSR VREGINKKMQ EPSAHTFDDA QLQIYTLMHR DSYPRFLSSP 200
    TYRALLLQGP SQSSSEA 217
    Length:217
    Mass (Da):24,636
    Last modified:October 1, 1996 - v1
    Checksum:i925A5687DC222CBD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti204 – 2041A → V in AAM12653. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91809 mRNA. Translation: CAA62919.1.
    AF493939 mRNA. Translation: AAM12653.1.
    AY585188 mRNA. Translation: AAS94232.1.
    BT009804 mRNA. Translation: AAP88806.1.
    AK290081 mRNA. Translation: BAF82770.1.
    AL590548 Genomic DNA. Translation: CAD11902.1.
    CH471077 Genomic DNA. Translation: EAW75166.1.
    CH471077 Genomic DNA. Translation: EAW75167.1.
    BC001318 mRNA. Translation: AAH01318.1.
    BC054337 mRNA. Translation: AAH54337.1.
    BC063010 mRNA. Translation: AAH63010.1.
    CCDSiCCDS13555.1.
    RefSeqiNP_001034556.1. NM_001039467.1.
    NP_005864.1. NM_005873.2.
    UniGeneiHs.422336.

    Genome annotation databases

    EnsembliENST00000332298; ENSP00000333194; ENSG00000171700.
    ENST00000395042; ENSP00000378483; ENSG00000171700.
    GeneIDi10287.
    KEGGihsa:10287.
    UCSCiuc002yhy.3. human.

    Polymorphism databases

    DMDMi1730186.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91809 mRNA. Translation: CAA62919.1 .
    AF493939 mRNA. Translation: AAM12653.1 .
    AY585188 mRNA. Translation: AAS94232.1 .
    BT009804 mRNA. Translation: AAP88806.1 .
    AK290081 mRNA. Translation: BAF82770.1 .
    AL590548 Genomic DNA. Translation: CAD11902.1 .
    CH471077 Genomic DNA. Translation: EAW75166.1 .
    CH471077 Genomic DNA. Translation: EAW75167.1 .
    BC001318 mRNA. Translation: AAH01318.1 .
    BC054337 mRNA. Translation: AAH54337.1 .
    BC063010 mRNA. Translation: AAH63010.1 .
    CCDSi CCDS13555.1.
    RefSeqi NP_001034556.1. NM_001039467.1.
    NP_005864.1. NM_005873.2.
    UniGenei Hs.422336.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CMZ NMR - A 76-217 [» ]
    ProteinModelPortali P49795.
    SMRi P49795. Positions 79-206.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115576. 12 interactions.
    IntActi P49795. 4 interactions.
    MINTi MINT-3017930.
    STRINGi 9606.ENSP00000333194.

    Chemistry

    BindingDBi P49795.

    PTM databases

    PhosphoSitei P49795.

    Polymorphism databases

    DMDMi 1730186.

    Proteomic databases

    MaxQBi P49795.
    PaxDbi P49795.
    PRIDEi P49795.

    Protocols and materials databases

    DNASUi 10287.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000332298 ; ENSP00000333194 ; ENSG00000171700 .
    ENST00000395042 ; ENSP00000378483 ; ENSG00000171700 .
    GeneIDi 10287.
    KEGGi hsa:10287.
    UCSCi uc002yhy.3. human.

    Organism-specific databases

    CTDi 10287.
    GeneCardsi GC20M062704.
    HGNCi HGNC:13735. RGS19.
    HPAi CAB031925.
    MIMi 605071. gene.
    neXtProti NX_P49795.
    PharmGKBi PA34370.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258376.
    HOGENOMi HOG000233513.
    HOVERGENi HBG013233.
    InParanoidi P49795.
    KOi K16449.
    OMAi FDKLMHS.
    OrthoDBi EOG7SN8DQ.
    PhylomeDBi P49795.
    TreeFami TF315837.

    Enzyme and pathway databases

    Reactomei REACT_18283. G alpha (q) signalling events.
    REACT_19231. G alpha (i) signalling events.
    REACT_19333. G alpha (z) signalling events.
    SignaLinki P49795.

    Miscellaneous databases

    ChiTaRSi RGS19. human.
    EvolutionaryTracei P49795.
    GeneWikii RGS19.
    GenomeRNAii 10287.
    NextBioi 38976.
    PROi P49795.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49795.
    Bgeei P49795.
    CleanExi HS_RGS19.
    Genevestigatori P49795.

    Family and domain databases

    Gene3Di 1.10.196.10. 1 hit.
    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. "GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain."
      de Vries L., Mousli M., Wurmser A., Farquhar M.G.
      Proc. Natl. Acad. Sci. U.S.A. 92:11916-11920(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "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 (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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: Subthalamic nucleus.
    5. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [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: Blood, Placenta and Testis.
    8. "GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits."
      de Vries L., Elenko E., Hubler L., Jones T.L.Z., Farquhar M.G.
      Proc. Natl. Acad. Sci. U.S.A. 93:15203-15208(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Solution structure of human GAIP (Galpha interacting protein): a regulator of G protein signaling."
      de Alba E., De Vries L., Farquhar M.G., Tjandra N.
      J. Mol. Biol. 291:927-939(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 79-206.
    11. "RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane association, regulation by Galphaz phosphorylation, and relationship to a Gz GTPase-activating protein subfamily."
      Wang J., Ducret A., Tu Y., Kozasa T., Aebersold R., Ross E.M.
      J. Biol. Chem. 273:26014-26025(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITION.
    12. "Erk1/2-dependent phosphorylation of Galpha-interacting protein stimulates its GTPase accelerating activity and autophagy in human colon cancer cells."
      Ogier-Denis E., Pattingre S., El Benna J., Codogno P.
      J. Biol. Chem. 275:39090-39095(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-151, MUTAGENESIS OF SER-151.

    Entry informationi

    Entry nameiRGS19_HUMAN
    AccessioniPrimary (citable) accession number: P49795
    Secondary accession number(s): A8K216
    , E1P5G9, Q53XN0, Q8TD60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 145 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 20
      Human chromosome 20: 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