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O43665

- RGS10_HUMAN

UniProt

O43665 - RGS10_HUMAN

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Protein

Regulator of G-protein signaling 10

Gene

RGS10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 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. Associates specifically with the activated forms of the G protein subunits G(i)-alpha and G(z)-alpha but fails to interact with the structurally and functionally distinct G(s)-alpha subunit. Activity on G(z)-alpha is inhibited by palmitoylation of the G-protein.

GO - Molecular functioni

  1. GTPase activator activity Source: RefGenome

GO - Biological processi

  1. positive regulation of GTPase activity Source: GOC
  2. 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.
SignaLinkiO43665.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 10
Short name:
RGS10
Gene namesi
Name:RGS10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:9992. RGS10.

Subcellular locationi

GO - Cellular componenti

  1. axon terminus Source: Ensembl
  2. cytoplasm Source: RefGenome
  3. dendritic spine Source: Ensembl
  4. neuronal cell body Source: Ensembl
  5. nucleus Source: HPA
  6. plasma membrane Source: RefGenome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34362.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 173173Regulator of G-protein signaling 10PRO_0000204207Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi66 – 661S-palmitoyl cysteine1 Publication

Post-translational modificationi

Isoform 3 is phosphorylated on Ser-16.

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiO43665.
PaxDbiO43665.
PRIDEiO43665.

2D gel databases

OGPiO43665.

Miscellaneous databases

PMAP-CutDBO43665.

Expressioni

Gene expression databases

BgeeiO43665.
CleanExiHS_RGS10.
GenevestigatoriO43665.

Organism-specific databases

HPAiCAB004559.
HPA021305.

Interactioni

Protein-protein interaction databases

BioGridi111933. 9 interactions.
DIPiDIP-50368N.
STRINGi9606.ENSP00000358099.

Structurei

Secondary structure

1
173
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 328Combined sources
Helixi34 – 396Combined sources
Helixi41 – 5313Combined sources
Helixi58 – 7114Combined sources
Helixi75 – 8915Combined sources
Helixi94 – 963Combined sources
Helixi103 – 1053Combined sources
Helixi108 – 1125Combined sources
Turni116 – 1194Combined sources
Helixi120 – 13213Combined sources
Helixi134 – 1385Combined sources
Turni142 – 1443Combined sources
Turni146 – 1505Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DLRNMR-A23-158[»]
2I59NMR-A22-157[»]
2IHBX-ray2.71B9-152[»]
ProteinModelPortaliO43665.
SMRiO43665. Positions 20-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43665.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 148116RGSPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG271158.
GeneTreeiENSGT00760000119142.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiO43665.
KOiK16449.
OMAiPKSTAKW.
OrthoDBiEOG7XDBF0.
PhylomeDBiO43665.
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: O43665-1) [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
MQSELCFADI HDSDGSSSSS HQSLKSTAKW AASLENLLED PEGVKRFREF
60 70 80 90 100
LKKEFSEENV LFWLACEDFK KMQDKTQMQE KAKEIYMTFL SSKASSQVNV
110 120 130 140 150
EGQSRLNEKI LEEPHPLMFQ KLQDQIFNLM KYDSYSRFLK SDLFLKHKRT
160 170
EEEEEDLPDA QTAAKRASRI YNT
Length:173
Mass (Da):20,236
Last modified:August 14, 2001 - v2
Checksum:iCA73D1E38F551EF1
GO
Isoform 2 (identifier: O43665-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: MQSELCFAD → MEH

Show »
Length:167
Mass (Da):19,608
Checksum:iEF36915F1AA23F3B
GO
Isoform 3 (identifier: O43665-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MQSELCFA → MFNRAVSRLSRKRPPS

Show »
Length:181
Mass (Da):21,210
Checksum:iD83CCB98A6EE2182
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941A → V.
Corresponds to variant rs1802228 [ dbSNP | Ensembl ].
VAR_011896

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 99MQSELCFAD → MEH in isoform 2. 2 PublicationsVSP_005681
Alternative sequencei1 – 88MQSELCFA → MFNRAVSRLSRKRPPS in isoform 3. 2 PublicationsVSP_027366

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF368902 mRNA. Translation: AAK52979.1.
AF045229 mRNA. Translation: AAC03783.1.
AF493934 mRNA. Translation: AAM12648.1.
AK290773 mRNA. Translation: BAF83462.1.
CR457008 mRNA. Translation: CAG33289.1.
AL355273, AC012468 Genomic DNA. Translation: CAI16486.1.
AL355273 Genomic DNA. Translation: CAI16488.1.
CH471066 Genomic DNA. Translation: EAW49389.1.
CH471066 Genomic DNA. Translation: EAW49390.1.
BC009361 mRNA. Translation: AAH09361.1.
CCDSiCCDS31294.1. [O43665-3]
CCDS41572.1. [O43665-2]
PIRiS71812.
RefSeqiNP_001005339.1. NM_001005339.1. [O43665-3]
NP_002916.1. NM_002925.3. [O43665-2]
UniGeneiHs.501200.

Genome annotation databases

EnsembliENST00000369101; ENSP00000358097; ENSG00000148908. [O43665-1]
ENST00000369103; ENSP00000358099; ENSG00000148908. [O43665-3]
ENST00000392865; ENSP00000376605; ENSG00000148908. [O43665-2]
GeneIDi6001.
KEGGihsa:6001.
UCSCiuc001lee.3. human. [O43665-1]
uc001lef.3. human. [O43665-2]
uc001leg.3. human. [O43665-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF368902 mRNA. Translation: AAK52979.1 .
AF045229 mRNA. Translation: AAC03783.1 .
AF493934 mRNA. Translation: AAM12648.1 .
AK290773 mRNA. Translation: BAF83462.1 .
CR457008 mRNA. Translation: CAG33289.1 .
AL355273 , AC012468 Genomic DNA. Translation: CAI16486.1 .
AL355273 Genomic DNA. Translation: CAI16488.1 .
CH471066 Genomic DNA. Translation: EAW49389.1 .
CH471066 Genomic DNA. Translation: EAW49390.1 .
BC009361 mRNA. Translation: AAH09361.1 .
CCDSi CCDS31294.1. [O43665-3 ]
CCDS41572.1. [O43665-2 ]
PIRi S71812.
RefSeqi NP_001005339.1. NM_001005339.1. [O43665-3 ]
NP_002916.1. NM_002925.3. [O43665-2 ]
UniGenei Hs.501200.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DLR NMR - A 23-158 [» ]
2I59 NMR - A 22-157 [» ]
2IHB X-ray 2.71 B 9-152 [» ]
ProteinModelPortali O43665.
SMRi O43665. Positions 20-157.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111933. 9 interactions.
DIPi DIP-50368N.
STRINGi 9606.ENSP00000358099.

2D gel databases

OGPi O43665.

Proteomic databases

MaxQBi O43665.
PaxDbi O43665.
PRIDEi O43665.

Protocols and materials databases

DNASUi 6001.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369101 ; ENSP00000358097 ; ENSG00000148908 . [O43665-1 ]
ENST00000369103 ; ENSP00000358099 ; ENSG00000148908 . [O43665-3 ]
ENST00000392865 ; ENSP00000376605 ; ENSG00000148908 . [O43665-2 ]
GeneIDi 6001.
KEGGi hsa:6001.
UCSCi uc001lee.3. human. [O43665-1 ]
uc001lef.3. human. [O43665-2 ]
uc001leg.3. human. [O43665-3 ]

Organism-specific databases

CTDi 6001.
GeneCardsi GC10M121249.
HGNCi HGNC:9992. RGS10.
HPAi CAB004559.
HPA021305.
MIMi 602856. gene.
neXtProti NX_O43665.
PharmGKBi PA34362.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271158.
GeneTreei ENSGT00760000119142.
HOGENOMi HOG000233512.
HOVERGENi HBG013233.
InParanoidi O43665.
KOi K16449.
OMAi PKSTAKW.
OrthoDBi EOG7XDBF0.
PhylomeDBi O43665.
TreeFami TF315837.

Enzyme and pathway databases

Reactomei REACT_19231. G alpha (i) signalling events.
SignaLinki O43665.

Miscellaneous databases

ChiTaRSi RGS10. human.
EvolutionaryTracei O43665.
GeneWikii RGS10.
GenomeRNAii 6001.
NextBioi 23399.
PMAP-CutDB O43665.
PROi O43665.
SOURCEi Search...

Gene expression databases

Bgeei O43665.
CleanExi HS_RGS10.
Genevestigatori O43665.

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. "RGS10 is a selective activator of G alpha i GTPase activity."
    Hunt T.W., Fields T.A., Casey P.J., Peralta E.G.
    Nature 383:175-177(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cytoplasmic, nuclear, and Golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs."
    Chatterjee T.K., Fisher R.A.
    J. Biol. Chem. 275:24013-24021(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "Phosphorylation and nuclear translocation of a regulator of G protein signaling (RGS10)."
    Burgon P.G., Lee W.L., Nixon A.B., Peralta E.G., Casey P.J.
    J. Biol. Chem. 276:32828-32834(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "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).
  5. "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 3).
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  7. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [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] (ISOFORM 3).
    Tissue: Uterus.
  10. "Palmitoylation of a conserved cysteine in the regulator of G protein signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and RGS10."
    Tu Y., Popov S., Slaughter C., Ross E.M.
    J. Biol. Chem. 274:38260-38267(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-66.
  11. "Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G protein alpha subunits."
    Tu Y., Wang J., Ross E.M.
    Science 278:1132-1135(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Solution structure of the RGS domain of human regulator of G-protein signaling 10."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 23-158.

Entry informationi

Entry nameiRGS10_HUMAN
AccessioniPrimary (citable) accession number: O43665
Secondary accession number(s): A8K408
, B1AMR8, Q6IAZ6, Q96GN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 14, 2001
Last modified: November 26, 2014
This is version 132 of the entry and version 2 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 10
    Human chromosome 10: 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