Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q08116

- RGS1_HUMAN

UniProt

Q08116 - RGS1_HUMAN

Protein

Regulator of G-protein signaling 1

Gene

RGS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (24 Mar 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. This protein may be involved in the regulation of B-cell activation and proliferation.

    GO - Molecular functioni

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

    GO - Biological processi

    1. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: ProtInc
    2. immune response Source: ProtInc
    3. positive regulation of GTPase activity Source: GOC
    4. signal transduction Source: ProtInc
    5. 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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulator of G-protein signaling 1
    Short name:
    RGS1
    Alternative name(s):
    B-cell activation protein BL34
    Early response protein 1R20
    Gene namesi
    Name:RGS1
    Synonyms:1R20, BL34, IER1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9991. RGS1.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34361.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 209209Regulator of G-protein signaling 1PRO_0000204175Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei32 – 321Phosphoserine; by CK2Sequence Analysis
    Modified residuei67 – 671Phosphoserine; by PKCSequence Analysis
    Modified residuei75 – 751Phosphoserine; by CK2Sequence Analysis
    Modified residuei159 – 1591Phosphothreonine; by PKCSequence Analysis
    Modified residuei169 – 1691Phosphothreonine; by CK2Sequence Analysis
    Modified residuei180 – 1801Phosphothreonine; by CK2Sequence Analysis
    Modified residuei207 – 2071Phosphoserine; by PKCSequence Analysis

    Post-translational modificationi

    Could be phosphorylated. Might be functionally regulated by protein kinase(s).

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ08116.
    PRIDEiQ08116.

    PTM databases

    PhosphoSiteiQ08116.

    Expressioni

    Tissue specificityi

    B-cell specific. Expression is relatively low in B-cells and chronic lymphocytic leukemia B-cells; however, in other types of malignant B-cell such as non-Hodgkin lymphoma and hairy cell leukemia, expression is constitutively high.

    Inductioni

    In response to several B-cell activation signals.

    Gene expression databases

    BgeeiQ08116.
    CleanExiHS_RGS1.
    GenevestigatoriQ08116.

    Interactioni

    Protein-protein interaction databases

    BioGridi111928. 6 interactions.
    DIPiDIP-59091N.
    IntActiQ08116. 5 interactions.
    MINTiMINT-1367963.
    STRINGi9606.ENSP00000356429.

    Structurei

    Secondary structure

    1
    209
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi72 – 754
    Helixi76 – 816
    Turni82 – 843
    Helixi86 – 916
    Helixi93 – 10513
    Helixi110 – 12213
    Helixi126 – 1283
    Helixi129 – 14012
    Helixi153 – 16311
    Turni168 – 1714
    Helixi172 – 18413
    Helixi186 – 1916
    Helixi194 – 2029

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BV1X-ray2.00A/B63-205[»]
    2GTPX-ray2.55C/D63-205[»]
    ProteinModelPortaliQ08116.
    SMRiQ08116. Positions 71-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ08116.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini85 – 200116RGSPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RGS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG312555.
    HOGENOMiHOG000233512.
    HOVERGENiHBG013233.
    InParanoidiQ08116.
    KOiK16449.
    OMAiEVIQWSQ.
    OrthoDBiEOG7VHSZ5.
    PhylomeDBiQ08116.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q08116-1) [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

    MRAAAISTPK LDKMPGMFFS ANPKELKGTT HSLLDDKMQK RRPKTFGMDM    50
    KAYLRSMIPH LESGMKSSKS KDVLSAAEVM QWSQSLEKLL ANQTGQNVFG 100
    SFLKSEFSEE NIEFWLACED YKKTESDLLP CKAEEIYKAF VHSDAAKQIN 150
    IDFRTRESTA KKIKAPTPTC FDEAQKVIYT LMEKDSYPRF LKSDIYLNLL 200
    NDLQANSLK 209
    Length:209
    Mass (Da):23,858
    Last modified:March 24, 2009 - v3
    Checksum:iD8D7D8E80819496A
    GO
    Isoform 2 (identifier: Q08116-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         149-209: INIDFRTRES...LNDLQANSLK → VSIKLIIISFSIKDPICRNNI

    Show »
    Length:169
    Mass (Da):19,134
    Checksum:i96E56F3B53747867
    GO

    Sequence cautioni

    The sequence AAB26289.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH15510.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAG37976.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAG64242.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA51826.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti177 – 1771V → A in BAG37976. (PubMed:14702039)Curated
    Sequence conflicti194 – 1941D → H in CAA51826. (PubMed:8241276)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei149 – 20961INIDF…ANSLK → VSIKLIIISFSIKDPICRNN I in isoform 2. 1 PublicationVSP_036422Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK303138 mRNA. Translation: BAG64242.1. Different initiation.
    AK315607 mRNA. Translation: BAG37976.1. Different initiation.
    AL136987 Genomic DNA. Translation: CAC19805.1.
    BC015510 mRNA. Translation: AAH15510.1. Different initiation.
    S59049 mRNA. Translation: AAB26289.1. Different initiation.
    X73427 mRNA. Translation: CAA51826.1. Different initiation.
    AF493925 mRNA. Translation: AAM12639.1.
    BT006668 mRNA. Translation: AAP35314.1.
    CCDSiCCDS1375.2. [Q08116-1]
    PIRiS43436.
    RefSeqiNP_002913.3. NM_002922.3. [Q08116-1]
    UniGeneiHs.75256.

    Genome annotation databases

    EnsembliENST00000367459; ENSP00000356429; ENSG00000090104. [Q08116-1]
    ENST00000469578; ENSP00000464323; ENSG00000090104. [Q08116-2]
    GeneIDi5996.
    KEGGihsa:5996.
    UCSCiuc001gsi.1. human. [Q08116-1]
    uc010pou.1. human. [Q08116-2]

    Polymorphism databases

    DMDMi229470360.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK303138 mRNA. Translation: BAG64242.1 . Different initiation.
    AK315607 mRNA. Translation: BAG37976.1 . Different initiation.
    AL136987 Genomic DNA. Translation: CAC19805.1 .
    BC015510 mRNA. Translation: AAH15510.1 . Different initiation.
    S59049 mRNA. Translation: AAB26289.1 . Different initiation.
    X73427 mRNA. Translation: CAA51826.1 . Different initiation.
    AF493925 mRNA. Translation: AAM12639.1 .
    BT006668 mRNA. Translation: AAP35314.1 .
    CCDSi CCDS1375.2. [Q08116-1 ]
    PIRi S43436.
    RefSeqi NP_002913.3. NM_002922.3. [Q08116-1 ]
    UniGenei Hs.75256.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BV1 X-ray 2.00 A/B 63-205 [» ]
    2GTP X-ray 2.55 C/D 63-205 [» ]
    ProteinModelPortali Q08116.
    SMRi Q08116. Positions 71-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111928. 6 interactions.
    DIPi DIP-59091N.
    IntActi Q08116. 5 interactions.
    MINTi MINT-1367963.
    STRINGi 9606.ENSP00000356429.

    PTM databases

    PhosphoSitei Q08116.

    Polymorphism databases

    DMDMi 229470360.

    Proteomic databases

    PaxDbi Q08116.
    PRIDEi Q08116.

    Protocols and materials databases

    DNASUi 5996.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367459 ; ENSP00000356429 ; ENSG00000090104 . [Q08116-1 ]
    ENST00000469578 ; ENSP00000464323 ; ENSG00000090104 . [Q08116-2 ]
    GeneIDi 5996.
    KEGGi hsa:5996.
    UCSCi uc001gsi.1. human. [Q08116-1 ]
    uc010pou.1. human. [Q08116-2 ]

    Organism-specific databases

    CTDi 5996.
    GeneCardsi GC01P192544.
    H-InvDB HIX0001431.
    HGNCi HGNC:9991. RGS1.
    MIMi 600323. gene.
    neXtProti NX_Q08116.
    PharmGKBi PA34361.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG312555.
    HOGENOMi HOG000233512.
    HOVERGENi HBG013233.
    InParanoidi Q08116.
    KOi K16449.
    OMAi EVIQWSQ.
    OrthoDBi EOG7VHSZ5.
    PhylomeDBi Q08116.
    TreeFami TF315837.

    Enzyme and pathway databases

    Reactomei REACT_19231. G alpha (i) signalling events.

    Miscellaneous databases

    EvolutionaryTracei Q08116.
    GeneWikii RGS1.
    GenomeRNAii 5996.
    NextBioi 23367.
    PROi Q08116.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q08116.
    CleanExi HS_RGS1.
    Genevestigatori Q08116.

    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. "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] (ISOFORMS 1 AND 2).
      Tissue: Skeletal muscle and Thymus.
    2. "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].
    3. "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] OF 2-209 (ISOFORM 1).
      Tissue: Skin.
    4. "Isolation and characterization of a novel B cell activation gene."
      Hong J.X., Wilson G.L., Fox C.H., Kehrl J.H.
      J. Immunol. 150:3895-3904(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-209 (ISOFORM 1).
      Tissue: B-cell.
    5. "A B cell specific immediate early human gene is located on chromosome band 1q31 and encodes an alpha helical basic phosphoprotein."
      Newton J.S., Deed R.W., Mitchell E.L.D., Murphy J.J., Norton J.D.
      Biochim. Biophys. Acta 1216:314-316(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-209 (ISOFORM 1).
      Tissue: B-cell.
    6. "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] OF 14-209 (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] OF 14-209 (ISOFORM 1).

    Entry informationi

    Entry nameiRGS1_HUMAN
    AccessioniPrimary (citable) accession number: Q08116
    Secondary accession number(s): B2RDM9
    , B4DZY0, Q07918, Q9H1W2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 139 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. 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