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P49802

- RGS7_HUMAN

UniProt

P49802 - RGS7_HUMAN

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Protein

Regulator of G-protein signaling 7

Gene

RGS7

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Activity on G(o)-alpha is specifically enhanced by the RGS6/GNG5 dimer. May play a role in synaptic vesicle exocytosis. May play important role in the rapid regulation of neuronal excitability and the cellular responses to short-lived stimulations (By similarity).By similarity

GO - Molecular functioni

  1. G-protein beta-subunit binding Source: UniProt
  2. GTPase activator activity Source: RefGenome
  3. signal transducer activity Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Signal transduction inhibitor

Enzyme and pathway databases

ReactomeiREACT_19231. G alpha (i) signalling events.
SignaLinkiP49802.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 7
Short name:
RGS7
Gene namesi
Name:RGS7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10003. RGS7.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. cytosol Source: Ensembl
  3. dendrite terminus Source: Ensembl
  4. heterotrimeric G-protein complex Source: InterPro
  5. nucleus Source: Ensembl
  6. plasma membrane Source: RefGenome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi306 – 3061W → F: Diminishes interaction with Gbeta5. 1 Publication

Organism-specific databases

PharmGKBiPA34378.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Regulator of G-protein signaling 7PRO_0000204196Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei434 – 4341Phosphoserine1 Publication

Post-translational modificationi

Palmitoylated.By similarity
Phosphorylation and subsequent interaction with 14-3-3 proteins inhibits GAP activity.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP49802.
PaxDbiP49802.
PRIDEiP49802.

PTM databases

PhosphoSiteiP49802.

Expressioni

Gene expression databases

BgeeiP49802.
CleanExiHS_RGS7.
ExpressionAtlasiP49802. baseline and differential.
GenevestigatoriP49802.

Organism-specific databases

HPAiCAB017561.
HPA000688.

Interactioni

Subunit structurei

Heterodimer with GNG5. Interacts with RGS7BP, leading to regulate the subcellular location of the heterodimer formed with Gbeta5 (By similarity). Interacts with 14-3-3 protein Tau and SNAPIN.By similarity3 Publications

Protein-protein interaction databases

BioGridi111932. 8 interactions.
DIPiDIP-40869N.
IntActiP49802. 5 interactions.
MINTiMINT-136910.
STRINGi9606.ENSP00000355520.

Structurei

Secondary structure

1
495
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi324 – 3296Combined sources
Helixi330 – 3323Combined sources
Helixi334 – 3396Combined sources
Helixi341 – 35313Combined sources
Helixi358 – 36912Combined sources
Helixi374 – 3763Combined sources
Helixi377 – 38812Combined sources
Helixi401 – 41212Combined sources
Turni414 – 4196Combined sources
Helixi420 – 43213Combined sources
Helixi434 – 4407Combined sources
Helixi442 – 4498Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A72X-ray2.00A/B320-463[»]
2D9JNMR-A323-448[»]
ProteinModelPortaliP49802.
SMRiP49802. Positions 19-450.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49802.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 11276DEPPROSITE-ProRule annotationAdd
BLAST
Domaini255 – 31662G protein gammaAdd
BLAST
Domaini333 – 448116RGSPROSITE-ProRule annotationAdd
BLAST

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.
InParanoidiP49802.
KOiK16449.
OMAiWIMKNLD.
PhylomeDBiP49802.
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.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
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. Align

Isoform 1 (identifier: P49802-1) [UniParc]FASTAAdd to Basket

Also known as: A

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
MAQGNNYGQT SNGVADESPN MLVYRKMEDV IARMQDEKNG IPIRTVKSFL
60 70 80 90 100
SKIPSVFSGS DIVQWLIKNL TIEDPVEALH LGTLMAAHGY FFPISDHVLT
110 120 130 140 150
LKDDGTFYRF QTPYFWPSNC WEPENTDYAV YLCKRTMQNK ARLELADYEA
160 170 180 190 200
ESLARLQRAF ARKWEFIFMQ AEAQAKVDKK RDKIERKILD SQERAFWDVH
210 220 230 240 250
RPVPGCVNTT EVDIKKSSRM RNPHKTRKSV YGLQNDIRSH SPTHTPTPET
260 270 280 290 300
KPPTEDELQQ QIKYWQIQLD RHRLKMSKVA DSLLSYTEQY LEYDPFLLPP
310 320 330 340 350
DPSNPWLSDD TTFWELEASK EPSQQRVKRW GFGMDEALKD PVGREQFLKF
360 370 380 390 400
LESEFSSENL RFWLAVEDLK KRPIKEVPSR VQEIWQEFLA PGAPSAINLD
410 420 430 440 450
SKSYDKTTQN VKEPGRYTFE DAQEHIYKLM KSDSYPRFIR SSAYQELLQA
460 470 480 490
KKKSGNSMDR RTSFEKFAQN VGRNIPIFPC HKNCTPTLRA STNLL
Length:495
Mass (Da):57,668
Last modified:October 18, 2001 - v3
Checksum:i1FCC2D60622675DE
GO
Isoform 2 (identifier: P49802-2) [UniParc]FASTAAdd to Basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     454-495: SGNSMDRRTSFEKFAQNVGRNIPIFPCHKNCTPTLRASTNLL → GKSLTSKRLTSLAQSY

Show »
Length:469
Mass (Da):54,685
Checksum:i993C1209EDD884EC
GO
Isoform 3 (identifier: P49802-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     454-471: Missing.

Show »
Length:477
Mass (Da):55,612
Checksum:iA7252A838E1881A9
GO
Isoform 4 (identifier: P49802-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     76-128: Missing.
     454-471: Missing.

Show »
Length:424
Mass (Da):49,387
Checksum:i25A8A2F507C07E87
GO
Isoform 5 (identifier: P49802-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     473-495: RNIPIFPCHKNCTPTLRASTNLL → KSLTSKRLTSLAQSY

Show »
Length:487
Mass (Da):56,741
Checksum:i50BDD0E8896444BC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261K → R in AAM12645. 1 PublicationCurated
Sequence conflicti234 – 2341Q → R in AAM12644. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371M → L.
Corresponds to variant rs12746550 [ dbSNP | Ensembl ].
VAR_057153
Natural varianti409 – 4091Q → H.1 Publication
Corresponds to variant rs17851953 [ dbSNP | Ensembl ].
VAR_060604

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei76 – 12853Missing in isoform 4. 1 PublicationVSP_005671Add
BLAST
Alternative sequencei454 – 49542SGNSM…STNLL → GKSLTSKRLTSLAQSY in isoform 2. 2 PublicationsVSP_005672Add
BLAST
Alternative sequencei454 – 47118Missing in isoform 3 and isoform 4. 1 PublicationVSP_005673Add
BLAST
Alternative sequencei473 – 49523RNIPI…STNLL → KSLTSKRLTSLAQSY in isoform 5. 1 PublicationVSP_038388Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF090116 mRNA. Translation: AAD34290.1.
AF090117 mRNA. Translation: AAD34291.1.
U32439 mRNA. Translation: AAC50351.1.
AF493930 mRNA. Translation: AAM12644.1.
AF493931 mRNA. Translation: AAM12645.1.
AY587875 mRNA. Translation: AAT52231.1.
AL512307
, AL359764, AL365184, AL590682 Genomic DNA. Translation: CAH71987.1.
AL512307
, AL359764, AL365184, AL590682 Genomic DNA. Translation: CAH71988.1.
AL512307
, AL359764, AL365184, AL590682 Genomic DNA. Translation: CAH71989.1.
AL512307
, AL359764, AL365184, AL590682 Genomic DNA. Translation: CAH71990.1.
AL590682
, AL359764, AL365184, AL512307 Genomic DNA. Translation: CAH73809.1.
AL590682
, AL359764, AL365184, AL512307 Genomic DNA. Translation: CAH73810.1.
AL590682
, AL359764, AL365184, AL512307 Genomic DNA. Translation: CAH73811.1.
AL590682
, AL359764, AL365184, AL512307 Genomic DNA. Translation: CAH73812.1.
AL359764
, AL365184, AL512307, AL590682 Genomic DNA. Translation: CAI15140.1.
AL359764
, AL365184, AL512307, AL590682 Genomic DNA. Translation: CAI15141.1.
AL359764
, AL365184, AL512307, AL590682 Genomic DNA. Translation: CAI15142.1.
AL359764
, AL365184, AL512307, AL590682 Genomic DNA. Translation: CAI15143.1.
AL365184
, AL359764, AL512307, AL590682 Genomic DNA. Translation: CAI16818.1.
AL365184
, AL359764, AL512307, AL590682 Genomic DNA. Translation: CAI16819.1.
AL365184
, AL359764, AL512307, AL590682 Genomic DNA. Translation: CAI16820.1.
AL365184
, AL359764, AL512307, AL590682 Genomic DNA. Translation: CAI16821.1.
CH471098 Genomic DNA. Translation: EAW70086.1.
BC022009 mRNA. Translation: AAH22009.1.
CCDSiCCDS31071.1. [P49802-5]
CCDS60457.1. [P49802-4]
CCDS60458.1. [P49802-2]
CCDS60459.1. [P49802-3]
RefSeqiNP_001269702.1. NM_001282773.1. [P49802-4]
NP_001269704.1. NM_001282775.1. [P49802-3]
NP_001269707.1. NM_001282778.1. [P49802-2]
NP_002915.3. NM_002924.5. [P49802-5]
XP_005273275.1. XM_005273218.1. [P49802-1]
UniGeneiHs.655739.

Genome annotation databases

EnsembliENST00000348120; ENSP00000341242; ENSG00000182901. [P49802-4]
ENST00000366563; ENSP00000355521; ENSG00000182901. [P49802-3]
ENST00000366564; ENSP00000355522; ENSG00000182901. [P49802-2]
ENST00000366565; ENSP00000355523; ENSG00000182901. [P49802-5]
GeneIDi6000.
KEGGihsa:6000.
UCSCiuc001hyt.2. human. [P49802-1]
uc001hyu.2. human. [P49802-3]
uc001hyv.2. human. [P49802-5]
uc001hyw.2. human. [P49802-2]
uc009xgn.1. human. [P49802-4]

Polymorphism databases

DMDMi17380284.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF090116 mRNA. Translation: AAD34290.1 .
AF090117 mRNA. Translation: AAD34291.1 .
U32439 mRNA. Translation: AAC50351.1 .
AF493930 mRNA. Translation: AAM12644.1 .
AF493931 mRNA. Translation: AAM12645.1 .
AY587875 mRNA. Translation: AAT52231.1 .
AL512307
, AL359764 , AL365184 , AL590682 Genomic DNA. Translation: CAH71987.1 .
AL512307
, AL359764 , AL365184 , AL590682 Genomic DNA. Translation: CAH71988.1 .
AL512307
, AL359764 , AL365184 , AL590682 Genomic DNA. Translation: CAH71989.1 .
AL512307
, AL359764 , AL365184 , AL590682 Genomic DNA. Translation: CAH71990.1 .
AL590682
, AL359764 , AL365184 , AL512307 Genomic DNA. Translation: CAH73809.1 .
AL590682
, AL359764 , AL365184 , AL512307 Genomic DNA. Translation: CAH73810.1 .
AL590682
, AL359764 , AL365184 , AL512307 Genomic DNA. Translation: CAH73811.1 .
AL590682
, AL359764 , AL365184 , AL512307 Genomic DNA. Translation: CAH73812.1 .
AL359764
, AL365184 , AL512307 , AL590682 Genomic DNA. Translation: CAI15140.1 .
AL359764
, AL365184 , AL512307 , AL590682 Genomic DNA. Translation: CAI15141.1 .
AL359764
, AL365184 , AL512307 , AL590682 Genomic DNA. Translation: CAI15142.1 .
AL359764
, AL365184 , AL512307 , AL590682 Genomic DNA. Translation: CAI15143.1 .
AL365184
, AL359764 , AL512307 , AL590682 Genomic DNA. Translation: CAI16818.1 .
AL365184
, AL359764 , AL512307 , AL590682 Genomic DNA. Translation: CAI16819.1 .
AL365184
, AL359764 , AL512307 , AL590682 Genomic DNA. Translation: CAI16820.1 .
AL365184
, AL359764 , AL512307 , AL590682 Genomic DNA. Translation: CAI16821.1 .
CH471098 Genomic DNA. Translation: EAW70086.1 .
BC022009 mRNA. Translation: AAH22009.1 .
CCDSi CCDS31071.1. [P49802-5 ]
CCDS60457.1. [P49802-4 ]
CCDS60458.1. [P49802-2 ]
CCDS60459.1. [P49802-3 ]
RefSeqi NP_001269702.1. NM_001282773.1. [P49802-4 ]
NP_001269704.1. NM_001282775.1. [P49802-3 ]
NP_001269707.1. NM_001282778.1. [P49802-2 ]
NP_002915.3. NM_002924.5. [P49802-5 ]
XP_005273275.1. XM_005273218.1. [P49802-1 ]
UniGenei Hs.655739.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2A72 X-ray 2.00 A/B 320-463 [» ]
2D9J NMR - A 323-448 [» ]
ProteinModelPortali P49802.
SMRi P49802. Positions 19-450.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111932. 8 interactions.
DIPi DIP-40869N.
IntActi P49802. 5 interactions.
MINTi MINT-136910.
STRINGi 9606.ENSP00000355520.

PTM databases

PhosphoSitei P49802.

Polymorphism databases

DMDMi 17380284.

Proteomic databases

MaxQBi P49802.
PaxDbi P49802.
PRIDEi P49802.

Protocols and materials databases

DNASUi 6000.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000348120 ; ENSP00000341242 ; ENSG00000182901 . [P49802-4 ]
ENST00000366563 ; ENSP00000355521 ; ENSG00000182901 . [P49802-3 ]
ENST00000366564 ; ENSP00000355522 ; ENSG00000182901 . [P49802-2 ]
ENST00000366565 ; ENSP00000355523 ; ENSG00000182901 . [P49802-5 ]
GeneIDi 6000.
KEGGi hsa:6000.
UCSCi uc001hyt.2. human. [P49802-1 ]
uc001hyu.2. human. [P49802-3 ]
uc001hyv.2. human. [P49802-5 ]
uc001hyw.2. human. [P49802-2 ]
uc009xgn.1. human. [P49802-4 ]

Organism-specific databases

CTDi 6000.
GeneCardsi GC01M240938.
HGNCi HGNC:10003. RGS7.
HPAi CAB017561.
HPA000688.
MIMi 602517. gene.
neXtProti NX_P49802.
PharmGKBi PA34378.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG327614.
GeneTreei ENSGT00760000119142.
HOVERGENi HBG007404.
InParanoidi P49802.
KOi K16449.
OMAi WIMKNLD.
PhylomeDBi P49802.
TreeFami TF351956.

Enzyme and pathway databases

Reactomei REACT_19231. G alpha (i) signalling events.
SignaLinki P49802.

Miscellaneous databases

ChiTaRSi RGS7. human.
EvolutionaryTracei P49802.
GeneWikii RGS7.
GenomeRNAii 6000.
NextBioi 23395.
PROi P49802.
SOURCEi Search...

Gene expression databases

Bgeei P49802.
CleanExi HS_RGS7.
ExpressionAtlasi P49802. baseline and differential.
Genevestigatori P49802.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
1.10.196.10. 1 hit.
4.10.260.10. 1 hit.
InterProi IPR000591. 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 ]
Pfami PF00610. DEP. 1 hit.
PF00631. G-gamma. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view ]
PRINTSi PR01301. RGSPROTEIN.
SMARTi SM00049. DEP. 1 hit.
SM00224. GGL. 1 hit.
SM00315. RGS. 1 hit.
[Graphical view ]
SUPFAMi SSF48097. SSF48097. 1 hit.
SSF48670. SSF48670. 1 hit.
PROSITEi PS50186. DEP. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  2. "EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins."
    Koelle M.R., Horvitz H.R.
    Cell 84:115-125(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  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-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
    Tissue: Brain.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 5), VARIANT HIS-409.
    Tissue: Testis.
  7. "Fidelity of G protein beta-subunit association by the G protein gamma-subunit-like domains of RGS6, RGS7, and RGS11."
    Snow B.E., Betts L., Mangion J., Sondek J., Siderovski D.P.
    Proc. Natl. Acad. Sci. U.S.A. 96:6489-6494(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GBETA5, MUTAGENESIS OF TRP-306.
    Tissue: Brain.
  8. "14-3-3 interacts with regulator of G protein signaling proteins and modulates their activity."
    Benzing T., Yaffe M.B., Arnould T., Sellin L., Schermer B., Schilling B., Schreiber R., Kunzelmann K., Leparc G.G., Kim E., Walz G.
    J. Biol. Chem. 275:28167-28172(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-434, INTERACTION WITH 14-3-3 PROTEINS.
  9. "Snapin interacts with the N-terminus of regulator of G protein signaling 7."
    Hunt R.A., Edris W., Chanda P.K., Nieuwenhuijsen B., Young K.H.
    Biochem. Biophys. Res. Commun. 303:594-599(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNAPIN.
  10. "Solution structure of the RGS domain of regulator of G-protein signaling 7."
    RIKEN structural genomics initiative (RSGI)
    Submitted (DEC-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 323-448.

Entry informationi

Entry nameiRGS7_HUMAN
AccessioniPrimary (citable) accession number: P49802
Secondary accession number(s): Q5T3H4
, Q8TD66, Q8TD67, Q8WW09, Q9UNU7, Q9Y6B9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 18, 2001
Last modified: October 29, 2014
This is version 149 of the entry and version 3 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. 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3