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Protein

Regulator of G-protein signaling 9

Gene

RGS9

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

GO - Molecular functioni

  • GTPase activator activity Source: ProtInc
  • signal transducer activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Keywords - Biological processi

Sensory transduction, Vision

Enzyme and pathway databases

ReactomeiREACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_19231. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 9
Short name:
RGS9
Gene namesi
Name:RGS9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:10004. RGS9.

Subcellular locationi

Isoform 3 :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Prolonged electroretinal response suppression (PERRS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionCharacterized by difficulty adjusting to sudden changes in luminance levels mediated by cones.

See also OMIM:608415
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti299 – 2991W → R in PERRS. 1 Publication
VAR_017912

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi608415. phenotype.
Orphaneti75374. Bradyopsia.
PharmGKBiPA34380.

Polymorphism and mutation databases

BioMutaiRGS9.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 674674Regulator of G-protein signaling 9PRO_0000204203Add
BLAST

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO75916.
PRIDEiO75916.

PTM databases

PhosphoSiteiO75916.

Expressioni

Tissue specificityi

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).

Gene expression databases

BgeeiO75916.
CleanExiHS_RGS9.
ExpressionAtlasiO75916. baseline and differential.
GenevisibleiO75916. HS.

Interactioni

Subunit structurei

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).Curated

Protein-protein interaction databases

BioGridi114315. 7 interactions.
IntActiO75916. 2 interactions.
MINTiMINT-3001991.
STRINGi9606.ENSP00000262406.

Structurei

3D structure databases

ProteinModelPortaliO75916.
SMRiO75916. Positions 7-424.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 10576DEPPROSITE-ProRule annotationAdd
BLAST
Domaini219 – 28062G protein gammaAdd
BLAST
Domaini298 – 413116RGSPROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 DEP domain.PROSITE-ProRule annotation
Contains 1 G protein gamma domain.Curated
Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG327614.
GeneTreeiENSGT00760000119142.
HOVERGENiHBG007404.
InParanoidiO75916.
KOiK13765.
OMAiPRMAFLQ.
PhylomeDBiO75916.
TreeFamiTF351956.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.196.10. 1 hit.
4.10.260.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR015898. G-protein_gamma-like_dom.
IPR016137. RGS.
IPR024066. RGS_subdom1.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00610. DEP. 1 hit.
PF00631. G-gamma. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00049. DEP. 1 hit.
SM00224. GGL. 1 hit.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF48670. SSF48670. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75916-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTIRHQGQQY RPRMAFLQKI EALVKDMQNP ETGVRMQNQR VLVTSVPHAM
60 70 80 90 100
TGSDVLQWIV QRLWISSLEA QNLGNFIVRY GYIYPLQDPK NLILKPDGSL
110 120 130 140 150
YRFQTPYFWP TQQWPAEDTD YAIYLAKRNI KKKGILEEYE KENYNFLNQK
160 170 180 190 200
MNYKWDFVIM QAKEQYRAGK ERNKADRYAL DCQEKAYWLV HRCPPGMDNV
210 220 230 240 250
LDYGLDRVTN PNEVKVNQKQ TVVAVKKEIM YYQQALMRST VKSSVSLGGI
260 270 280 290 300
VKYSEQFSSN DAIMSGCLPS NPWITDDTQF WDLNAKLVEI PTKMRVERWA
310 320 330 340 350
FNFSELIRDP KGRQSFQYFL KKEFSGENLG FWEACEDLKY GDQSKVKEKA
360 370 380 390 400
EEIYKLFLAP GARRWINIDG KTMDITVKGL KHPHRYVLDA AQTHIYMLMK
410 420 430 440 450
KDSYARYLKS PIYKDMLAKA IEPQETTKKS STLPFMRRHL RSSPSPVILR
460 470 480 490 500
QLEEEAKARE AANTVDITQP GQHMAPSPHL TVYTGTCMPP SPSSPFSSSC
510 520 530 540 550
RSPRKPFASP SRFIRRPSTT ICPSPIRVAL ESSSGLEQKG ECSGSMAPRG
560 570 580 590 600
PSVTESSEAS LDTSWPRSRP RAPPKARMAL SFSRFLRRGC LASPVFARLS
610 620 630 640 650
PKCPAVSHGR VQPLGDVGQQ LPRLKSKRVA NFFQIKMDVP TGSGTCLMDS
660 670
EDAGTGESGD RATEKEVICP WESL
Length:674
Mass (Da):76,966
Last modified:November 1, 1998 - v1
Checksum:i8E2B11104B448364
GO
Isoform 2 (identifier: O75916-2) [UniParc]FASTAAdd to basket

Also known as: RGS9S

The sequence of this isoform differs from the canonical sequence as follows:
     470-674: Missing.

Show »
Length:469
Mass (Da):54,982
Checksum:i04A5CF08AE73AEAC
GO
Isoform 3 (identifier: O75916-3) [UniParc]FASTAAdd to basket

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.

Show »
Length:484
Mass (Da):56,776
Checksum:i9E7C2371DF3BE3B5
GO
Isoform 4 (identifier: O75916-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-229: Missing.

Show »
Length:445
Mass (Da):49,810
Checksum:iA30CF34166481356
GO
Isoform 5 (identifier: O75916-5) [UniParc]FASTAAdd to basket

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

Show »
Length:671
Mass (Da):76,625
Checksum:i3866AC4C0DBB9B6A
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121Q → R in AAG09311 (PubMed:10564809).Curated
Sequence conflicti112 – 1121Q → R in AAG09312 (PubMed:10564809).Curated
Sequence conflicti142 – 1421E → G in AAM12647 (Ref. 3) Curated
Sequence conflicti306 – 3061L → S in AAM12646 (Ref. 3) Curated
Sequence conflicti319 – 3191F → S in AAM12647 (Ref. 3) Curated
Sequence conflicti336 – 3361E → G in AAM12647 (Ref. 3) Curated
Sequence conflicti392 – 3921Q → R in AAM12647 (Ref. 3) Curated
Sequence conflicti417 – 4171L → Q in AAC25430 (Ref. 7) Curated
Sequence conflicti422 – 4221E → D in AAC25430 (Ref. 7) Curated
Sequence conflicti428 – 4281K → R in AAM12647 (Ref. 3) Curated
Sequence conflicti454 – 4541E → G in AAM12646 (Ref. 3) Curated
Sequence conflicti460 – 4601E → K in AAG09311 (PubMed:10564809).Curated
Sequence conflicti460 – 4601E → K in AAG09312 (PubMed:10564809).Curated
Sequence conflicti518 – 5192Missing in AAC25430 (Ref. 7) Curated
Sequence conflicti527 – 5315RVALE → LVVLD in AAC25430 (Ref. 7) Curated
Sequence conflicti544 – 5496GSMAPR → WSGANP in AAC25430 (Ref. 7) Curated
Sequence conflicti555 – 5551E → D in AAC25430 (Ref. 7) Curated
Sequence conflicti561 – 5611L → R in AAC25430 (Ref. 7) Curated
Sequence conflicti564 – 5641S → P in AAM12647 (Ref. 3) Curated
Sequence conflicti566 – 5661P → T in AAC25430 (Ref. 7) Curated
Sequence conflicti574 – 5741P → L in AAC25430 (Ref. 7) Curated
Sequence conflicti599 – 5991L → V in AAC25430 (Ref. 7) Curated
Sequence conflicti668 – 6681I → T in AAM12646 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti258 – 2581S → L.
Corresponds to variant rs12452285 [ dbSNP | Ensembl ].
VAR_051796
Natural varianti299 – 2991W → R in PERRS. 1 Publication
VAR_017912

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 229229Missing in isoform 4. 1 PublicationVSP_005674Add
BLAST
Alternative sequencei216 – 2183Missing in isoform 3 and isoform 5. 2 PublicationsVSP_038381
Alternative sequencei470 – 674205Missing in isoform 2. 1 PublicationVSP_005675Add
BLAST
Alternative sequencei470 – 48718PGQHM…YTGTC → VMSKLDRRSQLKKELPPK in isoform 3. CuratedVSP_038382Add
BLAST
Alternative sequencei488 – 674187Missing in isoform 3. CuratedVSP_038383Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071476 mRNA. Translation: AAC64040.1.
AF178070
, AF178056, AF178057, AF178058, AF178059, AF178060, AF178061, AF178062, AF178063, AF178064, AF178065, AF178066, AF178067, AF178068, AF178069 Genomic DNA. Translation: AAG09311.1.
AF178072
, 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.
CCDSiCCDS42373.1. [O75916-1]
CCDS45764.1. [O75916-5]
RefSeqiNP_001075424.1. NM_001081955.2. [O75916-5]
NP_003826.2. NM_003835.3. [O75916-1]
UniGeneiHs.664380.

Genome annotation databases

EnsembliENST00000262406; ENSP00000262406; ENSG00000108370. [O75916-1]
ENST00000449996; ENSP00000396329; ENSG00000108370. [O75916-5]
GeneIDi8787.
KEGGihsa:8787.
UCSCiuc002jfd.3. human. [O75916-5]
uc002jfe.3. human. [O75916-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071476 mRNA. Translation: AAC64040.1.
AF178070
, AF178056, AF178057, AF178058, AF178059, AF178060, AF178061, AF178062, AF178063, AF178064, AF178065, AF178066, AF178067, AF178068, AF178069 Genomic DNA. Translation: AAG09311.1.
AF178072
, 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.
CCDSiCCDS42373.1. [O75916-1]
CCDS45764.1. [O75916-5]
RefSeqiNP_001075424.1. NM_001081955.2. [O75916-5]
NP_003826.2. NM_003835.3. [O75916-1]
UniGeneiHs.664380.

3D structure databases

ProteinModelPortaliO75916.
SMRiO75916. Positions 7-424.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114315. 7 interactions.
IntActiO75916. 2 interactions.
MINTiMINT-3001991.
STRINGi9606.ENSP00000262406.

PTM databases

PhosphoSiteiO75916.

Polymorphism and mutation databases

BioMutaiRGS9.

Proteomic databases

PaxDbiO75916.
PRIDEiO75916.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262406; ENSP00000262406; ENSG00000108370. [O75916-1]
ENST00000449996; ENSP00000396329; ENSG00000108370. [O75916-5]
GeneIDi8787.
KEGGihsa:8787.
UCSCiuc002jfd.3. human. [O75916-5]
uc002jfe.3. human. [O75916-1]

Organism-specific databases

CTDi8787.
GeneCardsiGC17P063133.
HGNCiHGNC:10004. RGS9.
MIMi604067. gene.
608415. phenotype.
neXtProtiNX_O75916.
Orphaneti75374. Bradyopsia.
PharmGKBiPA34380.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG327614.
GeneTreeiENSGT00760000119142.
HOVERGENiHBG007404.
InParanoidiO75916.
KOiK13765.
OMAiPRMAFLQ.
PhylomeDBiO75916.
TreeFamiTF351956.

Enzyme and pathway databases

ReactomeiREACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

GeneWikiiRGS9.
GenomeRNAii8787.
NextBioi32954.
PROiO75916.
SOURCEiSearch...

Gene expression databases

BgeeiO75916.
CleanExiHS_RGS9.
ExpressionAtlasiO75916. baseline and differential.
GenevisibleiO75916. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
1.10.196.10. 1 hit.
4.10.260.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR015898. G-protein_gamma-like_dom.
IPR016137. RGS.
IPR024066. RGS_subdom1.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00610. DEP. 1 hit.
PF00631. G-gamma. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR01301. RGSPROTEIN.
SMARTiSM00049. DEP. 1 hit.
SM00224. GGL. 1 hit.
SM00315. RGS. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF48670. SSF48670. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiRGS9_HUMAN
AccessioniPrimary (citable) accession number: O75916
Secondary accession number(s): A8K3C0
, O75573, Q696R2, Q8TD64, Q8TD65, Q9HC32, Q9HC33
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: June 24, 2015
This is version 150 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.