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O75916 (RGS9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of G-protein signaling 9

Short name=RGS9
Gene names
Name:RGS9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length674 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 to G(t)-alpha. Involved in phototransduction; key element in the recovery phase of visual transduction By similarity. Ref.8

Subunit structure

Heterodimer with Gbeta5. Interacts with RGS7BP, leading to regulate the subcellular location of the heterodimer formed with Gbeta5. Component of the RGS9-1-Gbeta5 complex composed of isoform 3 of RGS9 (RGS9-1), Gbeta5 (GNB5) and RGS9BP Probable.

Subcellular location

Isoform 3: Membrane; Peripheral membrane protein. Note: Isoform 3 is targeted to the membrane via its interaction with RGS9BP By similarity.

Tissue specificity

Highly expressed in the caudate and putamen, lower levels found in the hypothalamus and nucleus accumbens and very low levels in cerebellum. Not expressed in globus pallidus or cingulate cortex. Isoform 2 is expressed predominantly in pineal gland and retina. Isoform 3 is expressed in retina (abundant in photoreceptors).

Domain

In photoreceptor cells the DEP domain is essential for targeting RGS9 to the outer rod segments. Ref.8

Post-translational modification

Retinal isoform 3 is light-dependent phosphorylated at 'Ser-478'. Phosphorylation is decreased by light exposition By similarity.

Involvement in disease

Prolonged electroretinal response suppression (PERRS) [MIM:608415]: Characterized by difficulty adjusting to sudden changes in luminance levels mediated by cones.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Contains 1 DEP domain.

Contains 1 G protein gamma domain.

Contains 1 RGS domain.

Sequence caution

The sequence AAC25430.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processSensory transduction
Vision
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   Molecular functionSignal transduction inhibitor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdopamine receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

nervous system development

Inferred from electronic annotation. Source: Ensembl

phototransduction, visible light

Traceable author statement. Source: Reactome

regulation of G-protein coupled receptor protein signaling pathway

Traceable author statement Ref.1. Source: ProtInc

regulation of rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

response to estrogen

Inferred from electronic annotation. Source: Ensembl

rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

termination of G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

heterotrimeric G-protein complex

Inferred from electronic annotation. Source: InterPro

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionGTPase activator activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75916-1)

Also known as: RGS9L;

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.
Isoform 2 (identifier: O75916-2)

Also known as: RGS9S;

The sequence of this isoform differs from the canonical sequence as follows:
     470-674: Missing.
Isoform 3 (identifier: O75916-3)

Also known as: RGS9-1;

The sequence of this isoform differs from the canonical sequence as follows:
     216-218: Missing.
     470-487: PGQHMAPSPHLTVYTGTC → VMSKLDRRSQLKKELPPK
     488-674: Missing.
Isoform 4 (identifier: O75916-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-229: Missing.
Isoform 5 (identifier: O75916-5)

The sequence of this isoform differs from the canonical sequence as follows:
     216-218: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 674674Regulator of G-protein signaling 9
PRO_0000204203

Regions

Domain30 – 10576DEP
Domain219 – 28062G protein gamma
Domain298 – 413116RGS

Natural variations

Alternative sequence1 – 229229Missing in isoform 4.
VSP_005674
Alternative sequence216 – 2183Missing in isoform 3 and isoform 5.
VSP_038381
Alternative sequence470 – 674205Missing in isoform 2.
VSP_005675
Alternative sequence470 – 48718PGQHM…YTGTC → VMSKLDRRSQLKKELPPK in isoform 3.
VSP_038382
Alternative sequence488 – 674187Missing in isoform 3.
VSP_038383
Natural variant2581S → L.
Corresponds to variant rs12452285 [ dbSNP | Ensembl ].
VAR_051796
Natural variant2991W → R in PERRS. Ref.9
VAR_017912

Experimental info

Sequence conflict1121Q → R in AAG09311. Ref.2
Sequence conflict1121Q → R in AAG09312. Ref.2
Sequence conflict1421E → G in AAM12647. Ref.3
Sequence conflict3061L → S in AAM12646. Ref.3
Sequence conflict3191F → S in AAM12647. Ref.3
Sequence conflict3361E → G in AAM12647. Ref.3
Sequence conflict3921Q → R in AAM12647. Ref.3
Sequence conflict4171L → Q in AAC25430. Ref.7
Sequence conflict4221E → D in AAC25430. Ref.7
Sequence conflict4281K → R in AAM12647. Ref.3
Sequence conflict4541E → G in AAM12646. Ref.3
Sequence conflict4601E → K in AAG09311. Ref.2
Sequence conflict4601E → K in AAG09312. Ref.2
Sequence conflict518 – 5192Missing in AAC25430. Ref.7
Sequence conflict527 – 5315RVALE → LVVLD in AAC25430. Ref.7
Sequence conflict544 – 5496GSMAPR → WSGANP in AAC25430. Ref.7
Sequence conflict5551E → D in AAC25430. Ref.7
Sequence conflict5611L → R in AAC25430. Ref.7
Sequence conflict5641S → P in AAM12647. Ref.3
Sequence conflict5661P → T in AAC25430. Ref.7
Sequence conflict5741P → L in AAC25430. Ref.7
Sequence conflict5991L → V in AAC25430. Ref.7
Sequence conflict6681I → T in AAM12646. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (RGS9L) [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 8E2B11104B448364

FASTA67476,966
        10         20         30         40         50         60 
MTIRHQGQQY RPRMAFLQKI EALVKDMQNP ETGVRMQNQR VLVTSVPHAM TGSDVLQWIV 

        70         80         90        100        110        120 
QRLWISSLEA QNLGNFIVRY GYIYPLQDPK NLILKPDGSL YRFQTPYFWP TQQWPAEDTD 

       130        140        150        160        170        180 
YAIYLAKRNI KKKGILEEYE KENYNFLNQK MNYKWDFVIM QAKEQYRAGK ERNKADRYAL 

       190        200        210        220        230        240 
DCQEKAYWLV HRCPPGMDNV LDYGLDRVTN PNEVKVNQKQ TVVAVKKEIM YYQQALMRST 

       250        260        270        280        290        300 
VKSSVSLGGI VKYSEQFSSN DAIMSGCLPS NPWITDDTQF WDLNAKLVEI PTKMRVERWA 

       310        320        330        340        350        360 
FNFSELIRDP KGRQSFQYFL KKEFSGENLG FWEACEDLKY GDQSKVKEKA EEIYKLFLAP 

       370        380        390        400        410        420 
GARRWINIDG KTMDITVKGL KHPHRYVLDA AQTHIYMLMK KDSYARYLKS PIYKDMLAKA 

       430        440        450        460        470        480 
IEPQETTKKS STLPFMRRHL RSSPSPVILR QLEEEAKARE AANTVDITQP GQHMAPSPHL 

       490        500        510        520        530        540 
TVYTGTCMPP SPSSPFSSSC RSPRKPFASP SRFIRRPSTT ICPSPIRVAL ESSSGLEQKG 

       550        560        570        580        590        600 
ECSGSMAPRG PSVTESSEAS LDTSWPRSRP RAPPKARMAL SFSRFLRRGC LASPVFARLS 

       610        620        630        640        650        660 
PKCPAVSHGR VQPLGDVGQQ LPRLKSKRVA NFFQIKMDVP TGSGTCLMDS EDAGTGESGD 

       670 
RATEKEVICP WESL 

« Hide

Isoform 2 (RGS9S) [UniParc].

Checksum: 04A5CF08AE73AEAC
Show »

FASTA46954,982
Isoform 3 (RGS9-1) [UniParc].

Checksum: 9E7C2371DF3BE3B5
Show »

FASTA48456,776
Isoform 4 [UniParc].

Checksum: A30CF34166481356
Show »

FASTA44549,810
Isoform 5 [UniParc].

Checksum: 3866AC4C0DBB9B6A
Show »

FASTA67176,625

References

« Hide 'large scale' references
[1]"Molecular characterization of human and rat RGS9L, a novel splice variant enriched in dopamine target regions, and chromosomal localization of the RGS9 gene."
Granneman J.G., Zhai Y., Zhu Z., Bannon M.J., Burchett S.A., Schmidt C.J., Andrade R., Cooper J.
Mol. Pharmacol. 54:687-694(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Kidney and Retina.
[2]"Structure, alternative splicing, and expression of the human RGS9 gene."
Zhang K., Howes K.A., He W., Pettenati M.J., Palczewski K., Wensel T.G., Baehr W.
Gene 240:23-34(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 3 AND 5).
[3]"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-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
Tissue: Brain.
[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. expand/collapse author list , 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] (ISOFORM 5).
Tissue: Brain.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Homo sapiens regulator of G protein signaling 9."
Chatterjee T.K., Fisher R.A.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 218-674 (ISOFORM 1).
[8]"The DEP domain determines subcellular targeting of the GTPase activating protein RGS9 in vivo."
Martemyanov K.A., Lishko P.V., Calero N., Keresztes G., Sokolov M., Strissel K.J., Leskov I.B., Hopp J.A., Kolesnikov A.V., Chen C.-K., Lem J., Heller S., Burns M.E., Arshavsky V.Y.
J. Neurosci. 23:10175-10181(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DEP DOMAIN TARGETING FUNCTION.
[9]"Defects in RGS9 or its anchor protein R9AP in patients with slow photoreceptor deactivation."
Nishiguchi K.M., Sandberg M.A., Kooijman A.C., Martemyanov K.A., Pott J.W.R., Hagstrom S.A., Arshavsky V.Y., Berson E.L., Dryja T.P.
Nature 427:75-78(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PERRS ARG-299.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF071476 mRNA. Translation: AAC64040.1.
AF178070 expand/collapse EMBL AC list , AF178056, AF178057, AF178058, AF178059, AF178060, AF178061, AF178062, AF178063, AF178064, AF178065, AF178066, AF178067, AF178068, AF178069 Genomic DNA. Translation: AAG09311.1.
AF178072 expand/collapse EMBL AC list , AF178056, AF178057, AF178058, AF178059, AF178060, AF178061, AF178062, AF178063, AF178064, AF178065, AF178066, AF178067, AF178068, AF178069, AF178070, AF178071 Genomic DNA. Translation: AAG09312.1.
AF493932 mRNA. Translation: AAM12646.1.
AF493933 mRNA. Translation: AAM12647.1.
AY585190 mRNA. Translation: AAT79493.1.
AY585191 mRNA. Translation: AAT79494.1.
AK290535 mRNA. Translation: BAF83224.1.
AC015821 Genomic DNA. No translation available.
AC060771 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW88998.1.
AF073710 mRNA. Translation: AAC25430.1. Different initiation.
CCDSCCDS42373.1. [O75916-1]
CCDS45764.1. [O75916-5]
RefSeqNP_001075424.1. NM_001081955.2. [O75916-5]
NP_003826.2. NM_003835.3. [O75916-1]
UniGeneHs.664380.

3D structure databases

ProteinModelPortalO75916.
SMRO75916. Positions 7-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114315. 6 interactions.
IntActO75916. 2 interactions.
MINTMINT-3001991.
STRING9606.ENSP00000262406.

PTM databases

PhosphoSiteO75916.

Proteomic databases

PaxDbO75916.
PRIDEO75916.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262406; ENSP00000262406; ENSG00000108370. [O75916-1]
ENST00000449996; ENSP00000396329; ENSG00000108370. [O75916-5]
GeneID8787.
KEGGhsa:8787.
UCSCuc002jfd.3. human. [O75916-5]
uc002jfe.3. human. [O75916-1]

Organism-specific databases

CTD8787.
GeneCardsGC17P063133.
HGNCHGNC:10004. RGS9.
MIM604067. gene.
608415. phenotype.
neXtProtNX_O75916.
Orphanet75374. Bradyopsia.
PharmGKBPA34380.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327614.
HOVERGENHBG007404.
InParanoidO75916.
KOK13765.
OMALVKDMQN.
PhylomeDBO75916.
TreeFamTF351956.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressO75916.
BgeeO75916.
CleanExHS_RGS9.
GenevestigatorO75916.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
1.10.196.10. 1 hit.
4.10.260.10. 1 hit.
InterProIPR000591. DEP_dom.
IPR015898. G-protein_gamma-like_dom.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00610. DEP. 1 hit.
PF00631. G-gamma. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR01301. RGSPROTEIN.
SMARTSM00049. DEP. 1 hit.
SM00224. GGL. 1 hit.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
SSF48670. SSF48670. 1 hit.
PROSITEPS50186. DEP. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRGS9.
GenomeRNAi8787.
NextBio32954.
PROO75916.
SOURCESearch...

Entry information

Entry nameRGS9_HUMAN
AccessionPrimary (citable) accession number: O75916
Secondary accession number(s): A8K3C0 expand/collapse secondary AC list , O75573, Q696R2, Q8TD64, Q8TD65, Q9HC32, Q9HC33
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 143 of the entry and version 1 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM