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O15492

- RGS16_HUMAN

UniProt

O15492 - RGS16_HUMAN

Protein

Regulator of G-protein signaling 16

Gene

RGS16

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      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 and G(o)-alpha, but not to G(s)-alpha. May play a role in regulating the kinetics of signaling in the phototransduction cascade.

    Enzyme regulationi

    Phosphorylation at Tyr-168 by EGFR enhances GTPase accelerating (GAP) activity toward GNAI1.

    GO - Molecular functioni

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

    GO - Biological processi

    1. positive regulation of GTPase activity Source: GOC
    2. regulation of G-protein coupled receptor protein signaling pathway Source: ProtInc
    3. termination of G-protein coupled receptor signaling pathway Source: InterPro
    4. visual perception Source: ProtInc

    Keywords - Molecular functioni

    Signal transduction inhibitor

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulator of G-protein signaling 16
    Short name:
    RGS16
    Alternative name(s):
    A28-RGS14P
    Retinal-specific RGS
    Short name:
    RGS-r
    Short name:
    hRGS-r
    Retinally abundant regulator of G-protein signaling
    Gene namesi
    Name:RGS16
    Synonyms:RGSR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9997. RGS16.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi168 – 1681Y → F: 30% decrease in GAP activity. 1 Publication
    Mutagenesisi177 – 1771Y → F: No effect on GAP activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA34367.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 202202Regulator of G-protein signaling 16PRO_0000204221Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21S-palmitoyl cysteineBy similarity
    Lipidationi12 – 121S-palmitoyl cysteineBy similarity
    Modified residuei168 – 1681Phosphotyrosine; by EGFR1 Publication
    Modified residuei177 – 1771Phosphotyrosine1 Publication

    Post-translational modificationi

    Palmitoylated on Cys-2 and/or Cys-12.By similarity
    Phosphorylated. Regulated by phosphorylation at Tyr-168 by EGFR upon stimulation by EGF.1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiO15492.
    PRIDEiO15492.

    PTM databases

    PhosphoSiteiO15492.

    Expressioni

    Tissue specificityi

    Abundantly expressed in retina with lower levels of expression in most other tissues.

    Gene expression databases

    BgeeiO15492.
    CleanExiHS_RGS16.
    GenevestigatoriO15492.

    Organism-specific databases

    HPAiHPA053250.
    HPA055824.

    Interactioni

    Protein-protein interaction databases

    BioGridi111936. 13 interactions.
    DIPiDIP-59094N.
    IntActiO15492. 2 interactions.
    STRINGi9606.ENSP00000356529.

    Structurei

    Secondary structure

    1
    202
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi53 – 6210
    Helixi66 – 705
    Helixi73 – 8513
    Helixi89 – 10113
    Helixi107 – 12115
    Helixi134 – 14310
    Helixi144 – 1463
    Turni149 – 1524
    Helixi153 – 16513
    Helixi167 – 1737
    Helixi175 – 18612

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BT2X-ray1.90A/B/C/D/E53-190[»]
    2IK8X-ray2.71B/D53-190[»]
    ProteinModelPortaliO15492.
    SMRiO15492. Positions 53-188.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15492.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 181117RGSPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RGS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG269229.
    HOGENOMiHOG000233512.
    HOVERGENiHBG013233.
    InParanoidiO15492.
    KOiK16449.
    OMAiSRAQRIF.
    OrthoDBiEOG7VHSZ5.
    PhylomeDBiO15492.
    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.

    O15492-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCRTLAAFPT TCLERAKEFK TRLGIFLHKS ELGCDTGSTG KFEWGSKHSK    50
    ENRNFSEDVL GWRESFDLLL SSKNGVAAFH AFLKTEFSEE NLEFWLACEE 100
    FKKIRSATKL ASRAHQIFEE FICSEAPKEV NIDHETHELT RMNLQTATAT 150
    CFDAAQGKTR TLMEKDSYPR FLKSPAYRDL AAQASAASAT LSSCSLDEPS 200
    HT 202
    Length:202
    Mass (Da):22,749
    Last modified:January 11, 2011 - v2
    Checksum:i19B384E935F3E5D1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 421F → S in AAC16912. (PubMed:9223279)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti137 – 1371H → R.7 Publications
    Corresponds to variant rs1144566 [ dbSNP | Ensembl ].
    VAR_046528

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70426 mRNA. Translation: AAC16912.1.
    U94829 mRNA. Translation: AAC52040.1.
    AF009356 Genomic DNA. Translation: AAC39642.1.
    AF493937 mRNA. Translation: AAM12651.1.
    BT006638 mRNA. Translation: AAP35284.1.
    AK311880 mRNA. Translation: BAG34821.1.
    AL353778 Genomic DNA. Translation: CAH72419.1.
    CH471067 Genomic DNA. Translation: EAW91129.1.
    BC006243 mRNA. Translation: AAH06243.1.
    CCDSiCCDS1348.1.
    RefSeqiNP_002919.3. NM_002928.3.
    UniGeneiHs.413297.

    Genome annotation databases

    EnsembliENST00000367558; ENSP00000356529; ENSG00000143333.
    GeneIDi6004.
    KEGGihsa:6004.
    UCSCiuc001gpl.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U70426 mRNA. Translation: AAC16912.1 .
    U94829 mRNA. Translation: AAC52040.1 .
    AF009356 Genomic DNA. Translation: AAC39642.1 .
    AF493937 mRNA. Translation: AAM12651.1 .
    BT006638 mRNA. Translation: AAP35284.1 .
    AK311880 mRNA. Translation: BAG34821.1 .
    AL353778 Genomic DNA. Translation: CAH72419.1 .
    CH471067 Genomic DNA. Translation: EAW91129.1 .
    BC006243 mRNA. Translation: AAH06243.1 .
    CCDSi CCDS1348.1.
    RefSeqi NP_002919.3. NM_002928.3.
    UniGenei Hs.413297.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BT2 X-ray 1.90 A/B/C/D/E 53-190 [» ]
    2IK8 X-ray 2.71 B/D 53-190 [» ]
    ProteinModelPortali O15492.
    SMRi O15492. Positions 53-188.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111936. 13 interactions.
    DIPi DIP-59094N.
    IntActi O15492. 2 interactions.
    STRINGi 9606.ENSP00000356529.

    Chemistry

    BindingDBi O15492.

    PTM databases

    PhosphoSitei O15492.

    Proteomic databases

    PaxDbi O15492.
    PRIDEi O15492.

    Protocols and materials databases

    DNASUi 6004.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367558 ; ENSP00000356529 ; ENSG00000143333 .
    GeneIDi 6004.
    KEGGi hsa:6004.
    UCSCi uc001gpl.4. human.

    Organism-specific databases

    CTDi 6004.
    GeneCardsi GC01M182567.
    H-InvDB HIX0001402.
    HGNCi HGNC:9997. RGS16.
    HPAi HPA053250.
    HPA055824.
    MIMi 602514. gene.
    neXtProti NX_O15492.
    PharmGKBi PA34367.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG269229.
    HOGENOMi HOG000233512.
    HOVERGENi HBG013233.
    InParanoidi O15492.
    KOi K16449.
    OMAi SRAQRIF.
    OrthoDBi EOG7VHSZ5.
    PhylomeDBi O15492.
    TreeFami TF315837.

    Miscellaneous databases

    EvolutionaryTracei O15492.
    GeneWikii RGS16.
    GenomeRNAii 6004.
    NextBioi 23419.
    PROi O15492.
    SOURCEi Search...

    Gene expression databases

    Bgeei O15492.
    CleanExi HS_RGS16.
    Genevestigatori O15492.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-137.
      Tissue: Brain.
    2. "Cloning of a retinally abundant regulator of G-protein signaling (RGS-r/RGS16): genomic structure and chromosomal localization of the human gene."
      Snow B.E., Antonio L., Suggs S., Siderovski D.P.
      Gene 206:247-253(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT ARG-137.
      Tissue: Retina.
    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], VARIANT ARG-137.
    4. "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], VARIANT ARG-137.
    5. "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], VARIANT ARG-137.
    6. "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].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-137.
    8. "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], VARIANT ARG-137.
      Tissue: Lung.
    9. "RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation."
      Derrien A., Druey K.M.
      J. Biol. Chem. 276:48532-48538(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-168 BY EGFR, PHOSPHORYLATION AT TYR-177, MUTAGENESIS OF TYR-168 AND TYR-177.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-190.

    Entry informationi

    Entry nameiRGS16_HUMAN
    AccessioniPrimary (citable) accession number: O15492
    Secondary accession number(s): B2R4M4, Q5VYN9, Q99701
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 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