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Protein

Regulator of G-protein signaling 18

Gene

RGS18

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 to G(i) alpha-1, G(i) alpha-2, G(i) alpha-3 and G(q) alpha.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Enzyme and pathway databases

ReactomeiREACT_18283. G alpha (q) signalling events.
REACT_19231. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 18
Short name:
RGS18
Gene namesi
Name:RGS18
Synonyms:RGS13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:14261. RGS18.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34369.

Polymorphism and mutation databases

BioMutaiRGS18.
DMDMi15214228.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 235235Regulator of G-protein signaling 18PRO_0000204227Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9NS28.
PRIDEiQ9NS28.

2D gel databases

OGPiQ9NS28.

PTM databases

PhosphoSiteiQ9NS28.

Expressioni

Tissue specificityi

Expressed in peripheral leukocytes, bone marrow, platelet, spleen and fetal liver.2 Publications

Gene expression databases

BgeeiQ9NS28.
CleanExiHS_RGS13.
HS_RGS18.
GenevestigatoriQ9NS28.

Organism-specific databases

HPAiHPA045780.

Interactioni

Protein-protein interaction databases

BioGridi122160. 5 interactions.
DIPiDIP-59096N.
STRINGi9606.ENSP00000356430.

Structurei

Secondary structure

1
235
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi77 – 837Combined sources
Helixi87 – 926Combined sources
Helixi94 – 10613Combined sources
Helixi111 – 12212Combined sources
Helixi127 – 14115Combined sources
Beta strandi144 – 1474Combined sources
Helixi155 – 1639Combined sources
Helixi164 – 1663Combined sources
Turni170 – 1734Combined sources
Helixi174 – 18613Combined sources
Helixi188 – 1936Combined sources
Helixi196 – 2027Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DLVNMR-A76-202[»]
2JM5NMR-A75-223[»]
2OWINMR-A75-223[»]
ProteinModelPortaliQ9NS28.
SMRiQ9NS28. Positions 77-204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NS28.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 202117RGSPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG278594.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiQ9NS28.
KOiK16449.
OMAiLDFHTKE.
OrthoDBiEOG7VHSZ5.
PhylomeDBiQ9NS28.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
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.

Q9NS28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METTLLFFSQ INMCESKEKT FFKLIHGSGK EETSKEAKIR AKEKRNRLSL
60 70 80 90 100
LVQKPEFHED TRSSRSGHLA KETRVSPEEA VKWGESFDKL LSHRDGLEAF
110 120 130 140 150
TRFLKTEFSE ENIEFWIACE DFKKSKGPQQ IHLKAKAIYE KFIQTDAPKE
160 170 180 190 200
VNLDFHTKEV ITNSITQPTL HSFDAAQSRV YQLMEQDSYT RFLKSDIYLD
210 220 230
LMEGRPQRPT NLRRRSRSFT CNEFQDVQSD VAIWL
Length:235
Mass (Da):27,582
Last modified:October 1, 2000 - v1
Checksum:i973ABDE8EC7DE3D5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti226 – 2272DV → ML (PubMed:11042171).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076642 mRNA. Translation: AAF80227.1.
AF268036 mRNA. Translation: AAK58589.1.
AL596342, AL513175 Genomic DNA. Translation: CAH71160.1.
AK315377 mRNA. Translation: BAG37770.1.
AL513175, AL596342 Genomic DNA. Translation: CAH70529.1.
CH471067 Genomic DNA. Translation: EAW91223.1.
BC020632 mRNA. Translation: AAH20632.1.
CCDSiCCDS1374.1.
RefSeqiNP_570138.1. NM_130782.2.
UniGeneiHs.440890.

Genome annotation databases

EnsembliENST00000367460; ENSP00000356430; ENSG00000150681.
GeneIDi64407.
KEGGihsa:64407.
UCSCiuc001gsg.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076642 mRNA. Translation: AAF80227.1.
AF268036 mRNA. Translation: AAK58589.1.
AL596342, AL513175 Genomic DNA. Translation: CAH71160.1.
AK315377 mRNA. Translation: BAG37770.1.
AL513175, AL596342 Genomic DNA. Translation: CAH70529.1.
CH471067 Genomic DNA. Translation: EAW91223.1.
BC020632 mRNA. Translation: AAH20632.1.
CCDSiCCDS1374.1.
RefSeqiNP_570138.1. NM_130782.2.
UniGeneiHs.440890.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DLVNMR-A76-202[»]
2JM5NMR-A75-223[»]
2OWINMR-A75-223[»]
ProteinModelPortaliQ9NS28.
SMRiQ9NS28. Positions 77-204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122160. 5 interactions.
DIPiDIP-59096N.
STRINGi9606.ENSP00000356430.

PTM databases

PhosphoSiteiQ9NS28.

Polymorphism and mutation databases

BioMutaiRGS18.
DMDMi15214228.

2D gel databases

OGPiQ9NS28.

Proteomic databases

PaxDbiQ9NS28.
PRIDEiQ9NS28.

Protocols and materials databases

DNASUi64407.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367460; ENSP00000356430; ENSG00000150681.
GeneIDi64407.
KEGGihsa:64407.
UCSCiuc001gsg.3. human.

Organism-specific databases

CTDi64407.
GeneCardsiGC01P192127.
HGNCiHGNC:14261. RGS18.
HPAiHPA045780.
MIMi607192. gene.
neXtProtiNX_Q9NS28.
PharmGKBiPA34369.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG278594.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiQ9NS28.
KOiK16449.
OMAiLDFHTKE.
OrthoDBiEOG7VHSZ5.
PhylomeDBiQ9NS28.
TreeFamiTF315837.

Enzyme and pathway databases

ReactomeiREACT_18283. G alpha (q) signalling events.
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

EvolutionaryTraceiQ9NS28.
GeneWikiiRGS18.
GenomeRNAii64407.
NextBioi66362.
PROiQ9NS28.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NS28.
CleanExiHS_RGS13.
HS_RGS18.
GenevestigatoriQ9NS28.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
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. "A novel regulator of G-protein signaling."
    Zhang W., Wan T., Yuan Z., He L., Cao X.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning and characterization of a novel regulator of G-protein signaling from mouse hematopoietic stem cells."
    Park I.K., Klug C.A., Li K., Jerabek L., Li L., Nanamori M., Neubig R.R., Hood L., Weissman I.L., Clarke M.F.
    J. Biol. Chem. 276:915-923(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  3. "Cloning and characterization of a novel regulator of G protein signalling in human platelets."
    Gagnon A.W., Murray D.L., Leadley R.J. Jr.
    Cell. Signal. 14:595-606(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Platelet.
  4. "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].
    Tissue: Amygdala.
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Liver.
  8. "Differential proteome analysis of TRAP-activated platelets: involvement of DOK-2 and phosphorylation of RGS proteins."
    Garcia A., Prabhakar S., Hughan S., Anderson T.W., Brock C.J., Pearce A.C., Dwek R.A., Watson S.P., Hebestreit H.F., Zitzmann N.
    Blood 103:2088-2095(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-49.
  9. "Solution structure of the RGS domain of human regulator of G-protein signaling 18."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 76-204.

Entry informationi

Entry nameiRGS18_HUMAN
AccessioniPrimary (citable) accession number: Q9NS28
Secondary accession number(s): B2RD23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: October 1, 2000
Last modified: April 29, 2015
This is version 115 of the entry and version 1 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.