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Protein

Regulator of G-protein signaling 1

Gene

RGS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • calmodulin binding Source: ProtInc
  • GTPase activator activity Source: ProtInc

GO - Biological processi

  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: ProtInc
  • immune response Source: ProtInc
  • positive regulation of GTPase activity Source: GOC
  • signal transduction Source: ProtInc
  • termination of G-protein coupled receptor signaling pathway Source: InterPro
Complete GO annotation...

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9991. RGS1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • plasma membrane Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34361.

Polymorphism and mutation databases

BioMutaiRGS1.
DMDMi229470360.

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.
ExpressionAtlasiQ08116. baseline and differential.
GenevisibleiQ08116. HS.

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 – 754Combined sources
Helixi76 – 816Combined sources
Turni82 – 843Combined sources
Helixi86 – 916Combined sources
Helixi93 – 10513Combined sources
Helixi110 – 12213Combined sources
Helixi126 – 1283Combined sources
Helixi129 – 14012Combined sources
Helixi153 – 16311Combined sources
Turni168 – 1714Combined sources
Helixi172 – 18413Combined sources
Helixi186 – 1916Combined sources
Helixi194 – 2029Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiQ08116.
KOiK16449.
OMAiKIYKAFV.
OrthoDBiEOG7VHSZ5.
PhylomeDBiQ08116.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
InterProiIPR016137. RGS.
IPR030409. RGS1.
IPR024066. RGS_subdom1.
[Graphical view]
PANTHERiPTHR10845:SF34. PTHR10845:SF34. 1 hit.
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. AlignAdd to basket

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

        10         20         30         40         50
MRAAAISTPK LDKMPGMFFS ANPKELKGTT HSLLDDKMQK RRPKTFGMDM
60 70 80 90 100
KAYLRSMIPH LESGMKSSKS KDVLSAAEVM QWSQSLEKLL ANQTGQNVFG
110 120 130 140 150
SFLKSEFSEE NIEFWLACED YKKTESDLLP CKAEEIYKAF VHSDAAKQIN
160 170 180 190 200
IDFRTRESTA KKIKAPTPTC FDEAQKVIYT LMEKDSYPRF LKSDIYLNLL

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

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:
EMBLi
GenBanki
DDBJi
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.
ENST00000469578; ENSP00000464323; ENSG00000090104. [Q08116-2]
GeneIDi5996.
KEGGihsa:5996.
UCSCiuc001gsi.1. human. [Q08116-1]
uc010pou.1. human. [Q08116-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ08116.

Polymorphism and mutation databases

BioMutaiRGS1.
DMDMi229470360.

Proteomic databases

PaxDbiQ08116.
PRIDEiQ08116.

Protocols and materials databases

DNASUi5996.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5996.
GeneCardsiGC01P192544.
H-InvDBHIX0001431.
HGNCiHGNC:9991. RGS1.
MIMi600323. gene.
neXtProtiNX_Q08116.
PharmGKBiPA34361.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG312555.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiQ08116.
KOiK16449.
OMAiKIYKAFV.
OrthoDBiEOG7VHSZ5.
PhylomeDBiQ08116.
TreeFamiTF315837.

Enzyme and pathway databases

ReactomeiREACT_19231. G alpha (i) signalling events.

Miscellaneous databases

ChiTaRSiRGS1. human.
EvolutionaryTraceiQ08116.
GeneWikiiRGS1.
GenomeRNAii5996.
NextBioi23367.
PROiQ08116.
SOURCEiSearch...

Gene expression databases

BgeeiQ08116.
CleanExiHS_RGS1.
ExpressionAtlasiQ08116. baseline and differential.
GenevisibleiQ08116. HS.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
InterProiIPR016137. RGS.
IPR030409. RGS1.
IPR024066. RGS_subdom1.
[Graphical view]
PANTHERiPTHR10845:SF34. PTHR10845:SF34. 1 hit.
PfamiPF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
PROSITEiPS50132. RGS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 146 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.