Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O15539

- RGS5_HUMAN

UniProt

O15539 - RGS5_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Regulator of G-protein signaling 5

Gene

RGS5

Organism
Homo sapiens (Human)
Status
Reviewed - 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 and G(o)-alpha, but not to G(s)-alpha (By similarity).By similarity

GO - Molecular functioni

  1. GTPase activator activity Source: RefGenome

GO - Biological processi

  1. positive regulation of GTPase activity Source: GOC
  2. regulation of G-protein coupled receptor protein signaling pathway Source: ProtInc
  3. signal transduction Source: Ensembl
  4. termination of G-protein coupled receptor signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 5
Short name:
RGS5
Gene namesi
Name:RGS5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10001. RGS5.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. plasma membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34376.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 181181Regulator of G-protein signaling 5PRO_0000204188Add
BLAST

Proteomic databases

PaxDbiO15539.
PRIDEiO15539.

PTM databases

PhosphoSiteiO15539.

Expressioni

Gene expression databases

BgeeiO15539.
CleanExiHS_RGS5.
ExpressionAtlasiO15539. baseline and differential.
GenevestigatoriO15539.

Organism-specific databases

HPAiHPA001821.

Interactioni

Protein-protein interaction databases

BioGridi114062. 7 interactions.
STRINGi9606.ENSP00000319308.

Structurei

Secondary structure

1
181
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi55 – 584Combined sources
Helixi60 – 634Combined sources
Helixi65 – 706Combined sources
Helixi72 – 8413Combined sources
Helixi88 – 10114Combined sources
Helixi108 – 11912Combined sources
Helixi133 – 1419Combined sources
Helixi149 – 1513Combined sources
Helixi152 – 16413Combined sources
Helixi166 – 1727Combined sources
Helixi174 – 1807Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CRPNMR-A44-180[»]
ProteinModelPortaliO15539.
SMRiO15539. Positions 44-180.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15539.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 180117RGSPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG285261.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiO15539.
KOiK16449.
OMAiWRDSLEK.
OrthoDBiEOG7VHSZ5.
PhylomeDBiO15539.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 1 hit.
InterProiIPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
[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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15539-1) [UniParc]FASTAAdd to Basket

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
MCKGLAALPH SCLERAKEIK IKLGILLQKP DSVGDLVIPY NEKPEKPAKT
60 70 80 90 100
QKTSLDEALQ WRDSLDKLLQ NNYGLASFKS FLKSEFSEEN LEFWIACEDY
110 120 130 140 150
KKIKSPAKMA EKAKQIYEEF IQTEAPKEVN IDHFTKDITM KNLVEPSLSS
160 170 180
FDMAQKRIHA LMEKDSLPRF VRSEFYQELI K
Length:181
Mass (Da):20,946
Last modified:January 1, 1998 - v1
Checksum:i2E08CB0179DE7687
GO
Isoform 2 (identifier: O15539-2) [UniParc]FASTAAdd to Basket

Also known as: RGS5s

The sequence of this isoform differs from the canonical sequence as follows:
     1-108: Missing.

Note: Acts as an endogenous negative regulator of isoform 1.

Show »
Length:73
Mass (Da):8,664
Checksum:i3B9DE08FBE577E5D
GO
Isoform 3 (identifier: O15539-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     128-128: E → EVGLW

Note: No experimental confirmation available.

Show »
Length:185
Mass (Da):21,402
Checksum:i3B1840D1AB0D8DC0
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 108108Missing in isoform 2. 1 PublicationVSP_043094Add
BLAST
Alternative sequencei128 – 1281E → EVGLW in isoform 3. 1 PublicationVSP_045086

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF030108 mRNA. Translation: AAB84001.1.
AB008109 mRNA. Translation: BAA22889.1.
AF159570 mRNA. Translation: AAD40957.1.
AJ891044 mRNA. Translation: CAI76926.1.
AF493929 mRNA. Translation: AAM12643.1.
BX537427 mRNA. Translation: CAD97669.1.
AL451063, AL499616, AL583850 Genomic DNA. Translation: CAH71851.1.
AL583850, AL451063, AL499616 Genomic DNA. Translation: CAH73764.1.
AL499616, AL451063, AL583850 Genomic DNA. Translation: CAI15095.1.
CH471067 Genomic DNA. Translation: EAW90731.1.
BC030059 mRNA. Translation: AAH30059.1.
BU172751 mRNA. No translation available.
CCDSiCCDS1244.1. [O15539-1]
CCDS55652.1. [O15539-2]
CCDS58041.1. [O15539-3]
RefSeqiNP_001182232.1. NM_001195303.2. [O15539-2]
NP_001241677.1. NM_001254748.1. [O15539-2]
NP_001241678.1. NM_001254749.1. [O15539-3]
NP_003608.1. NM_003617.3. [O15539-1]
UniGeneiHs.24950.
Hs.677623.

Genome annotation databases

EnsembliENST00000313961; ENSP00000319308; ENSG00000143248. [O15539-1]
ENST00000527988; ENSP00000432313; ENSG00000143248. [O15539-2]
ENST00000530507; ENSP00000433001; ENSG00000143248. [O15539-3]
ENST00000618415; ENSP00000480891; ENSG00000143248. [O15539-2]
GeneIDi8490.
KEGGihsa:8490.
UCSCiuc001gcn.3. human. [O15539-1]
uc009wvb.3. human. [O15539-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF030108 mRNA. Translation: AAB84001.1 .
AB008109 mRNA. Translation: BAA22889.1 .
AF159570 mRNA. Translation: AAD40957.1 .
AJ891044 mRNA. Translation: CAI76926.1 .
AF493929 mRNA. Translation: AAM12643.1 .
BX537427 mRNA. Translation: CAD97669.1 .
AL451063 , AL499616 , AL583850 Genomic DNA. Translation: CAH71851.1 .
AL583850 , AL451063 , AL499616 Genomic DNA. Translation: CAH73764.1 .
AL499616 , AL451063 , AL583850 Genomic DNA. Translation: CAI15095.1 .
CH471067 Genomic DNA. Translation: EAW90731.1 .
BC030059 mRNA. Translation: AAH30059.1 .
BU172751 mRNA. No translation available.
CCDSi CCDS1244.1. [O15539-1 ]
CCDS55652.1. [O15539-2 ]
CCDS58041.1. [O15539-3 ]
RefSeqi NP_001182232.1. NM_001195303.2. [O15539-2 ]
NP_001241677.1. NM_001254748.1. [O15539-2 ]
NP_001241678.1. NM_001254749.1. [O15539-3 ]
NP_003608.1. NM_003617.3. [O15539-1 ]
UniGenei Hs.24950.
Hs.677623.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CRP NMR - A 44-180 [» ]
ProteinModelPortali O15539.
SMRi O15539. Positions 44-180.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114062. 7 interactions.
STRINGi 9606.ENSP00000319308.

PTM databases

PhosphoSitei O15539.

Proteomic databases

PaxDbi O15539.
PRIDEi O15539.

Protocols and materials databases

DNASUi 8490.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313961 ; ENSP00000319308 ; ENSG00000143248 . [O15539-1 ]
ENST00000527988 ; ENSP00000432313 ; ENSG00000143248 . [O15539-2 ]
ENST00000530507 ; ENSP00000433001 ; ENSG00000143248 . [O15539-3 ]
ENST00000618415 ; ENSP00000480891 ; ENSG00000143248 . [O15539-2 ]
GeneIDi 8490.
KEGGi hsa:8490.
UCSCi uc001gcn.3. human. [O15539-1 ]
uc009wvb.3. human. [O15539-2 ]

Organism-specific databases

CTDi 8490.
GeneCardsi GC01M163080.
HGNCi HGNC:10001. RGS5.
HPAi HPA001821.
MIMi 603276. gene.
neXtProti NX_O15539.
PharmGKBi PA34376.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG285261.
GeneTreei ENSGT00760000118903.
HOGENOMi HOG000233512.
HOVERGENi HBG013233.
InParanoidi O15539.
KOi K16449.
OMAi WRDSLEK.
OrthoDBi EOG7VHSZ5.
PhylomeDBi O15539.
TreeFami TF315837.

Miscellaneous databases

EvolutionaryTracei O15539.
GeneWikii RGS5.
GenomeRNAii 8490.
NextBioi 31763.
PROi O15539.
SOURCEi Search...

Gene expression databases

Bgeei O15539.
CleanExi HS_RGS5.
ExpressionAtlasi O15539. baseline and differential.
Genevestigatori O15539.

Family and domain databases

Gene3Di 1.10.196.10. 1 hit.
InterProi IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
[Graphical view ]
Pfami PF00615. RGS. 1 hit.
[Graphical view ]
PRINTSi PR01301. RGSPROTEIN.
SMARTi SM00315. RGS. 1 hit.
[Graphical view ]
SUPFAMi SSF48097. SSF48097. 1 hit.
PROSITEi PS50132. RGS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Chatterjee T.K., Fisher R.A.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Isolation, tissue expression, and chromosomal assignment of human RGS5, a novel G-protein signaling regulator gene."
    Seki N., Sugano S., Suzuki Y., Nakagawara A., Ohira M., Muramatsu M.-A., Saito T., Hori T.
    J. Hum. Genet. 43:202-205(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Neuroblastoma.
  3. "Genetic screens in yeast to identify mammalian nonreceptor modulators of G-protein signaling."
    Cismowski M.J., Takesono A., Ma C., Lizano J.S., Xie X., Fuernkranz H., Lanier S.M., Duzic E.
    Nat. Biotechnol. 17:878-883(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  4. "Identification of a novel alternative splicing variant of RGS5 mRNA in human ocular tissues."
    Liang Y., Li C., Gozamn V.W., Woodwrad D.F.
    FEBS J. 272:791-799(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
    Tissue: Eye.
  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] (ISOFORM 1).
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Cervix.
  7. "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].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORMS 1 AND 3).
    Tissue: Brain and Melanoma.
  10. "Solution structure of the RGS domain of regulator of G-protein signalling 5 (RGS 5)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 44-180.

Entry informationi

Entry nameiRGS5_HUMAN
AccessioniPrimary (citable) accession number: O15539
Secondary accession number(s): E9PMP5, Q53XA9, Q599J0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 126 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