O43665 (RGS10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Regulator of G-protein signaling 10
Short name=RGS10

Gene names

Name:

RGS10

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	173 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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.
Post-translational modification	Isoform 3 is phosphorylated on Ser-16.
Sequence similarities	Contains 1 RGS domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Signal transduction inhibitor
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	termination of G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular_component	axon terminus Inferred from electronic annotation. Source: Compara cytoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome dendritic spine Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	GTPase activator activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O43665-1)

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: O43665-2)

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

Isoform 3 (identifier: O43665-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 173

173

Regulator of G-protein signaling 10

PRO_0000204207

Regions

Domain

33 – 148

116

RGS

Amino acid modifications

Lipidation

66

1

S-palmitoyl cysteine Ref.10

Natural variations

Alternative sequence

1 – 9

9

MQSELCFAD → MEH in isoform 2.

VSP_005681

Alternative sequence

1 – 8

8

MQSELCFA → MFNRAVSRLSRKRPPS in isoform 3.

VSP_027366

Natural variant

94

1

A → V.
Corresponds to variant rs1802228 [ dbSNP | Ensembl ].

VAR_011896

Secondary structure

1

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173

Helix Strand Turn

Details...

Helix

25 – 32

8

Helix

34 – 39

6

Helix

41 – 53

13

Helix

58 – 71

14

Helix

75 – 89

15

Helix

94 – 96

3

Helix

103 – 105

3

Helix

108 – 112

5

Turn

116 – 119

4

Helix

120 – 132

13

Helix

134 – 138

5

Turn

142 – 144

3

Turn

146 – 150

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: CA73D1E38F551EF1	FASTA	173	20,236
	10 20 30 40 50 60 MQSELCFADI HDSDGSSSSS HQSLKSTAKW AASLENLLED PEGVKRFREF LKKEFSEENV 70 80 90 100 110 120 LFWLACEDFK KMQDKTQMQE KAKEIYMTFL SSKASSQVNV EGQSRLNEKI LEEPHPLMFQ 130 140 150 160 170 KLQDQIFNLM KYDSYSRFLK SDLFLKHKRT EEEEEDLPDA QTAAKRASRI YNT
	Isoform 2 [UniParc]. Checksum: EF36915F1AA23F3B	FASTA	167	19,608
	10 20 30 40 50 60 MEHIHDSDGS SSSSHQSLKS TAKWAASLEN LLEDPEGVKR FREFLKKEFS EENVLFWLAC 70 80 90 100 110 120 EDFKKMQDKT QMQEKAKEIY MTFLSSKASS QVNVEGQSRL NEKILEEPHP LMFQKLQDQI 130 140 150 160 FNLMKYDSYS RFLKSDLFLK HKRTEEEEED LPDAQTAAKR ASRIYNT
	Isoform 3 [UniParc]. Checksum: D83CCB98A6EE2182	FASTA	181	21,210
	10 20 30 40 50 60 MFNRAVSRLS RKRPPSDIHD SDGSSSSSHQ SLKSTAKWAA SLENLLEDPE GVKRFREFLK 70 80 90 100 110 120 KEFSEENVLF WLACEDFKKM QDKTQMQEKA KEIYMTFLSS KASSQVNVEG QSRLNEKILE 130 140 150 160 170 180 EPHPLMFQKL QDQIFNLMKY DSYSRFLKSD LFLKHKRTEE EEEDLPDAQT AAKRASRIYN T

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	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. , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00013454.
IPI00216532.
IPI00643554.

PIR

S71812.

RefSeq

NP_001005339.1. NM_001005339.1.
NP_002916.1. NM_002925.3.

UniGene

Hs.501200.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O43665.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-50368N.

STRING

9606.ENSP00000358099.

2D gel databases

OGP

O43665.

Proteomic databases

PaxDb

O43665.

PRIDE

O43665.

Protocols and materials databases

DNASU

6001.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369101; ENSP00000358097; ENSG00000148908.
ENST00000369103; ENSP00000358099; ENSG00000148908.
ENST00000392865; ENSP00000376605; ENSG00000148908.

GeneID

6001.

KEGG

hsa:6001.

UCSC

uc001lee.3. human.
uc001lef.3. human.
uc001leg.3. human.

Organism-specific databases

CTD

6001.

GeneCards

GC10M121249.

HGNC

HGNC:9992. RGS10.

HPA

CAB004559.
HPA021305.

MIM

602856. gene.

neXtProt

NX_O43665.

PharmGKB

PA34362.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG271158.

HOGENOM

HOG000233512.

HOVERGEN

HBG013233.

KO

K16449.

OMA

PKSTAKW.

Gene expression databases

Bgee

O43665.

CleanEx

HS_RGS10.

Genevestigator

O43665.

GermOnline

ENSG00000148908. Homo sapiens.

Family and domain databases

Gene3D

1.10.196.10. 1 hit.

InterPro

IPR000342. Regulat_G_prot_signal.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
[Graphical view]

Pfam

PF00615. RGS. 1 hit.
[Graphical view]

PRINTS

PR01301. RGSPROTEIN.

SMART

SM00315. RGS. 1 hit.
[Graphical view]

SUPFAM

SSF48097. Regulat_G_prot_signal_superfam. 1 hit.

PROSITE

PS50132. RGS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O43665.

GenomeRNAi

6001.

NextBio

23399.

PMAP-CutDB

O43665.

SOURCE

Search...

Entry information

Entry name

RGS10_HUMAN

Accession

Primary (citable) accession number: O43665
Secondary accession number(s): A8K408 , B1AMR8, Q6IAZ6, Q96GN0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 14, 2001
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.