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Protein

Regulator of G-protein signaling 17

Gene

RGS17

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 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. Binds selectively to G(z)-alpha and G(alpha)-i2 subunits, accelerates their GTPase activity and regulates their signaling activities. The G(z)-alpha activity is inhibited by the phosphorylation and palmitoylation of the G-protein. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins (By similarity).By similarity

GO - Molecular functioni

  1. GTPase activator activity Source: GO_Central

GO - Biological processi

  1. positive regulation of GTPase activity Source: GOC
  2. termination of G-protein coupled receptor signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Enzyme and pathway databases

ReactomeiREACT_19333. G alpha (z) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 17
Short name:
RGS17
Gene namesi
Name:RGS17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:14088. RGS17.

Subcellular locationi

Membrane; Lipid-anchor. Nucleus. Cytoplasm
Note: Shuttles between the cytoplasm/cell membrane and the nucleus. Anchored to the membrane through palmitoylation (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. nucleus Source: UniProtKB-SubCell
  3. plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34368.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210Regulator of G-protein signaling 17PRO_0000204224Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei137 – 1371PhosphotyrosineBy similarity

Post-translational modificationi

Fatty acylated. Heavily palmitoylated in the cysteine string motif (By similarity).By similarity
N- and O-glycosylated in synapsomal membranes.By similarity
Serine phosphorylated in synapsomal membranes.By similarity
Sumoylated with SUMO1 and SUM02 in synaptosomes. The sumoylated forms act as a scaffold for sequestering mu-opioid receptor-activated G(alpha) subunits (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9UGC6.
PRIDEiQ9UGC6.

PTM databases

PhosphoSiteiQ9UGC6.

Expressioni

Tissue specificityi

Predominantly expressed in the cerebellum. Also expressed in the cortex and medulla. Weakly expressed in a number of peripheral tissues notably spleen, lung and leukocytes.1 Publication

Gene expression databases

BgeeiQ9UGC6.
CleanExiHS_RGS17.
GenevestigatoriQ9UGC6.

Organism-specific databases

HPAiHPA022276.

Interactioni

Protein-protein interaction databases

BioGridi117744. 20 interactions.
DIPiDIP-59095N.
IntActiQ9UGC6. 3 interactions.
STRINGi9606.ENSP00000206262.

Structurei

Secondary structure

1
210
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi75 – 806Combined sources
Helixi85 – 895Combined sources
Helixi92 – 10413Combined sources
Helixi108 – 12215Combined sources
Helixi126 – 14015Combined sources
Helixi153 – 1619Combined sources
Turni168 – 1714Combined sources
Helixi172 – 18413Combined sources
Helixi187 – 1904Combined sources
Helixi194 – 20310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZV4X-ray2.40X72-206[»]
ProteinModelPortaliQ9UGC6.
SMRiQ9UGC6. Positions 69-204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UGC6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 200117RGSPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi28 – 4013Poly-CysAdd
BLAST

Sequence similaritiesi

Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG258376.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233513.
HOVERGENiHBG013233.
InParanoidiQ9UGC6.
KOiK16449.
OMAiQQSQNEE.
OrthoDBiEOG7SN8DQ.
PhylomeDBiQ9UGC6.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 1 hit.
InterProiIPR016137. RGS.
IPR024066. RGS_subdom1.
[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.

Q9UGC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKRQQSQNE GTPAVSQAPG NQRPNNTCCF CWCCCCSCSC LTVRNEERGE
60 70 80 90 100
NAGRPTHTTK MESIQVLEEC QNPTAEEVLS WSQNFDKMMK APAGRNLFRE
110 120 130 140 150
FLRTEYSEEN LLFWLACEDL KKEQNKKVIE EKARMIYEDY ISILSPKEVS
160 170 180 190 200
LDSRVREVIN RNLLDPNPHM YEDAQLQIYT LMHRDSFPRF LNSQIYKSFV
210
ESTAGSSSES
Length:210
Mass (Da):24,359
Last modified:August 14, 2001 - v2
Checksum:i0AFA22A43BF5E481
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF202257 mRNA. Translation: AAF08978.3.
BT006997 mRNA. Translation: AAP35643.1.
AL080276 Genomic DNA. Translation: CAI18900.1.
BC013117 mRNA. Translation: AAH13117.1.
AF493938 mRNA. Translation: AAM12652.1.
CCDSiCCDS5244.1.
RefSeqiNP_036551.3. NM_012419.4.
UniGeneiHs.166313.

Genome annotation databases

EnsembliENST00000206262; ENSP00000206262; ENSG00000091844.
ENST00000367225; ENSP00000356194; ENSG00000091844.
GeneIDi26575.
KEGGihsa:26575.
UCSCiuc003qpm.3. human.

Polymorphism databases

DMDMi15214238.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF202257 mRNA. Translation: AAF08978.3.
BT006997 mRNA. Translation: AAP35643.1.
AL080276 Genomic DNA. Translation: CAI18900.1.
BC013117 mRNA. Translation: AAH13117.1.
AF493938 mRNA. Translation: AAM12652.1.
CCDSiCCDS5244.1.
RefSeqiNP_036551.3. NM_012419.4.
UniGeneiHs.166313.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZV4X-ray2.40X72-206[»]
ProteinModelPortaliQ9UGC6.
SMRiQ9UGC6. Positions 69-204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117744. 20 interactions.
DIPiDIP-59095N.
IntActiQ9UGC6. 3 interactions.
STRINGi9606.ENSP00000206262.

PTM databases

PhosphoSiteiQ9UGC6.

Polymorphism databases

DMDMi15214238.

Proteomic databases

PaxDbiQ9UGC6.
PRIDEiQ9UGC6.

Protocols and materials databases

DNASUi26575.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000206262; ENSP00000206262; ENSG00000091844.
ENST00000367225; ENSP00000356194; ENSG00000091844.
GeneIDi26575.
KEGGihsa:26575.
UCSCiuc003qpm.3. human.

Organism-specific databases

CTDi26575.
GeneCardsiGC06M153331.
HGNCiHGNC:14088. RGS17.
HPAiHPA022276.
MIMi607191. gene.
neXtProtiNX_Q9UGC6.
PharmGKBiPA34368.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG258376.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233513.
HOVERGENiHBG013233.
InParanoidiQ9UGC6.
KOiK16449.
OMAiQQSQNEE.
OrthoDBiEOG7SN8DQ.
PhylomeDBiQ9UGC6.
TreeFamiTF315837.

Enzyme and pathway databases

ReactomeiREACT_19333. G alpha (z) signalling events.

Miscellaneous databases

ChiTaRSiRGS17. human.
EvolutionaryTraceiQ9UGC6.
GeneWikiiRGS17.
GenomeRNAii26575.
NextBioi48914.
PROiQ9UGC6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UGC6.
CleanExiHS_RGS17.
GenevestigatoriQ9UGC6.

Family and domain databases

Gene3Di1.10.196.10. 1 hit.
InterProiIPR016137. RGS.
IPR024066. RGS_subdom1.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Ghahremani M.H., Daigle M., Albert P.R.
    Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "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].
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Lung.
  5. "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 61-210.
    Tissue: Brain.
  6. "RGS17/RGSZ2, a novel regulator of Gi/o, Gz, and Gq signaling."
    Mao H., Zhao Q., Daigle M., Ghahremani M.H., Chidiac P., Albert P.R.
    J. Biol. Chem. 279:26314-26322(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiRGS17_HUMAN
AccessioniPrimary (citable) accession number: Q9UGC6
Secondary accession number(s): Q5TF49, Q8TD61, Q9UJS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: August 14, 2001
Last modified: March 4, 2015
This is version 127 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 6
    Human chromosome 6: 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.