Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UGC6 (RGS17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of G-protein signaling 17

Short name=RGS17
Gene names
Name:RGS17
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subcellular location

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

Tissue specificity

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. Ref.6

Post-translational modification

Fatty acylated. Heavily palmitoylated in the cysteine string motif 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.

Sequence similarities

Contains 1 RGS domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 210210Regulator of G-protein signaling 17
PRO_0000204224

Regions

Domain84 – 200117RGS
Compositional bias28 – 4013Poly-Cys

Amino acid modifications

Modified residue1371Phosphotyrosine By similarity

Secondary structure

.................... 210
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UGC6 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: 0AFA22A43BF5E481

FASTA21024,359
        10         20         30         40         50         60 
MRKRQQSQNE GTPAVSQAPG NQRPNNTCCF CWCCCCSCSC LTVRNEERGE NAGRPTHTTK 

        70         80         90        100        110        120 
MESIQVLEEC QNPTAEEVLS WSQNFDKMMK APAGRNLFRE FLRTEYSEEN LLFWLACEDL 

       130        140        150        160        170        180 
KKEQNKKVIE EKARMIYEDY ISILSPKEVS LDSRVREVIN RNLLDPNPHM YEDAQLQIYT 

       190        200        210 
LMHRDSFPRF LNSQIYKSFV ESTAGSSSES 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_036551.3. NM_012419.4.
UniGeneHs.166313.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZV4X-ray2.40X72-206[»]
ProteinModelPortalQ9UGC6.
SMRQ9UGC6. Positions 69-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117744. 6 interactions.
DIPDIP-59095N.
IntActQ9UGC6. 3 interactions.
STRING9606.ENSP00000206262.

PTM databases

PhosphoSiteQ9UGC6.

Polymorphism databases

DMDM15214238.

Proteomic databases

PaxDbQ9UGC6.
PRIDEQ9UGC6.

Protocols and materials databases

DNASU26575.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000206262; ENSP00000206262; ENSG00000091844.
ENST00000367225; ENSP00000356194; ENSG00000091844.
GeneID26575.
KEGGhsa:26575.
UCSCuc003qpm.3. human.

Organism-specific databases

CTD26575.
GeneCardsGC06M153331.
HGNCHGNC:14088. RGS17.
HPAHPA022276.
MIM607191. gene.
neXtProtNX_Q9UGC6.
PharmGKBPA34368.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258376.
HOGENOMHOG000233513.
HOVERGENHBG013233.
InParanoidQ9UGC6.
KOK16449.
OMAQQSQNEE.
OrthoDBEOG7SN8DQ.
PhylomeDBQ9UGC6.
TreeFamTF315837.

Gene expression databases

BgeeQ9UGC6.
CleanExHS_RGS17.
GenevestigatorQ9UGC6.

Family and domain databases

Gene3D1.10.196.10. 1 hit.
InterProIPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
[Graphical view]
PfamPF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR01301. RGSPROTEIN.
SMARTSM00315. RGS. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
PROSITEPS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRGS17. human.
EvolutionaryTraceQ9UGC6.
GeneWikiRGS17.
GenomeRNAi26575.
NextBio48914.
PROQ9UGC6.
SOURCESearch...

Entry information

Entry nameRGS17_HUMAN
AccessionPrimary (citable) accession number: Q9UGC6
Secondary accession number(s): Q5TF49, Q8TD61, Q9UJS8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: August 14, 2001
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM