P41220 (RGS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Regulator of G-protein signaling 2
Short name=RGS2

Alternative name(s):
Cell growth-inhibiting gene 31 protein
G0/G1 switch regulatory protein 8

Gene names

Name:	RGS2
Synonyms:	G0S8
ORF Names:	GIG31

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	211 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. May play a role in leukemogenesis. Plays a role in negative feedback control pathway for adenylyl cyclase signaling. Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein. Ref.2 Ref.3 Ref.12 Ref.15
Subunit structure	Interacts with EIF2B5. Interacts with PRKG1 (isoform alpha). Ref.14 Ref.15
Subcellular location	Isoform 1: Cell membrane. Cytoplasm. Nucleus › nucleolus Ref.2 Ref.3. Isoform 2: Cell membrane. Cytoplasm. Nucleus › nucleolus Ref.2 Ref.3. Isoform 3: Cell membrane. Cytoplasm. Nucleus › nucleolus Ref.2 Ref.3. Isoform 4: Cell membrane. Mitochondrion Ref.2 Ref.3.
Tissue specificity	Expressed in acute myelogenous leukemia (AML) and in acute lymphoblastic leukemia (ALL). Ref.12
Post-translational modification	Phosphorylated by protein kinase C. Phosphorylation by PRKG1 leads to activation of RGS2 activity. Ref.13 Ref.14
Sequence similarities	Contains 1 RGS domain.

Ontologies

Keywords
Biological process	Cell cycle Translation regulation
Cellular component	Cell membrane Cytoplasm Membrane Mitochondrion Nucleus
Coding sequence diversity	Alternative initiation
Molecular function	Signal transduction inhibitor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	brown fat cell differentiation Inferred from electronic annotation. Source: Compara cell cycle Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of G-protein coupled receptor protein signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of MAP kinase activity Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of cardiac muscle hypertrophy Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of phospholipase activity Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of cardiac muscle contraction Inferred from sequence or structural similarity. Source: BHF-UCL regulation of adrenergic receptor signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW relaxation of cardiac muscle Inferred from sequence or structural similarity. Source: BHF-UCL relaxation of vascular smooth muscle Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from electronic annotation. Source: Compara termination of G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: BHF-UCL internal side of plasma membrane Inferred from sequence or structural similarity. Source: BHF-UCL mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTPase activator activity Inferred from Biological aspect of Ancestor. Source: RefGenome calmodulin binding Traceable author statement PubMed 10747990. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative initiation. [Align] [Select]

Isoform 1 (identifier: P41220-1)

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: P41220-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: Missing.

Isoform 3 (identifier: P41220-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: Missing.

Note: Lacks type V adenylyl cyclase (AC) inhibitory function.

Isoform 4 (identifier: P41220-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.

Note: Lacks type V adenylyl cyclase (AC) inhibitory function.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 211

211

Regulator of G-protein signaling 2

PRO_0000204178

Regions

Domain

83 – 199

117

RGS

Region

32 – 66

35

Necessary for membrane association

Region

79 – 116

38

Necessary to inhibit protein synthesis

Natural variations

Alternative sequence

1 – 32

32

Missing in isoform 4.

VSP_041298

Alternative sequence

1 – 15

15

Missing in isoform 3.

VSP_041297

Alternative sequence

1 – 4

4

Missing in isoform 2.

VSP_041296

Experimental info

Mutagenesis

1

1

M → L: Loss of isoform 1 expression. Ref.3

Mutagenesis

5

1

M → L: Loss of isoform 2 expression. Ref.3

Mutagenesis

16

1

M → L: Loss of isoform 3 expression. Ref.3

Mutagenesis

33

1

M → L: Loss of isoform 4 expression. Ref.3

Mutagenesis

37

1

L → D: Impairs association with plasma membrane. Ref.2

Mutagenesis

38

1

L → D: Impairs association with plasma membrane. Ref.2

Mutagenesis

41

1

W → D: Impairs association with plasma membrane. Ref.2

Mutagenesis

45

1

L → D: Impairs association with plasma membrane. Ref.2

Mutagenesis

48

1

F → D: Impairs association with plasma membrane. Ref.2

Mutagenesis

49

1

L → D: Impairs association with plasma membrane. Ref.2

Mutagenesis

79

1

L → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with E-86; L-87; S-90; K-102; F-105; I-110; E-111 and L-114. Ref.15

Mutagenesis

86

1

E → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; L-87; S-90; K-102; F-105; I-110; E-111 and L-114. Ref.15

Mutagenesis

87

1

L → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; S-90; K-102; F-105; I-110; E-111 and L-114. Ref.15

Mutagenesis

90

1

S → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; K-102; F-105; I-110; E-111 and L-114. Ref.15

Mutagenesis

102

1

K → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; F-105; I-110; E-111 and L-114. Ref.15

Mutagenesis

105

1

F → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; I-110; E-111 and L-114. Ref.15

Mutagenesis

110

1

I → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; E-111 and L-114. Ref.15

Mutagenesis

111

1

E → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; I-110 and L-114. Ref.15

Mutagenesis

114

1

L → A: Near loss of EIF2B5 binding and inhibition of in vitro translation; when associated with L-79; E-86; L-87; S-90; K-102; F-105; I-110 and E-111. Ref.15

Mutagenesis

149

1

N → A: Decreases GTPase accelerating function but has no effect on translation inhibitory activity, suggesting that its role in translation is independent of its effects on G proteins. Ref.15

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

211

Helix Strand Turn

Details...

Helix

74 – 79

6

Turn

80 – 82

3

Helix

84 – 89

6

Helix

91 – 103

13

Helix

108 – 120

13

Helix

125 – 139

15

Helix

152 – 161

10

Helix

162 – 164

3

Turn

167 – 170

4

Helix

171 – 183

13

Helix

185 – 191

7

Helix

193 – 199

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: EFFE4AE47EF9AD8F	FASTA	211	24,382
	10 20 30 40 50 60 MQSAMFLAVQ HDCRPMDKSA GSGHKSEEKR EKMKRTLLKD WKTRLSYFLQ NSSTPGKPKT 70 80 90 100 110 120 GKKSKQQAFI KPSPEEAQLW SEAFDELLAS KYGLAAFRAF LKSEFCEENI EFWLACEDFK 130 140 150 160 170 180 KTKSPQKLSS KARKIYTDFI EKEAPKEINI DFQTKTLIAQ NIQEATSGCF TTAQKRVYSL 190 200 210 MENNSYPRFL ESEFYQDLCK KPQITTEPHA T
	Isoform 2 [UniParc]. Checksum: E5DCCB2F18E09F51	FASTA	207	23,964
	10 20 30 40 50 60 MFLAVQHDCR PMDKSAGSGH KSEEKREKMK RTLLKDWKTR LSYFLQNSST PGKPKTGKKS 70 80 90 100 110 120 KQQAFIKPSP EEAQLWSEAF DELLASKYGL AAFRAFLKSE FCEENIEFWL ACEDFKKTKS 130 140 150 160 170 180 PQKLSSKARK IYTDFIEKEA PKEINIDFQT KTLIAQNIQE ATSGCFTTAQ KRVYSLMENN 190 200 SYPRFLESEF YQDLCKKPQI TTEPHAT
	Isoform 3 [UniParc]. Checksum: 2F5BF7609CD4172A	FASTA	196	22,666
	10 20 30 40 50 60 MDKSAGSGHK SEEKREKMKR TLLKDWKTRL SYFLQNSSTP GKPKTGKKSK QQAFIKPSPE 70 80 90 100 110 120 EAQLWSEAFD ELLASKYGLA AFRAFLKSEF CEENIEFWLA CEDFKKTKSP QKLSSKARKI 130 140 150 160 170 180 YTDFIEKEAP KEINIDFQTK TLIAQNIQEA TSGCFTTAQK RVYSLMENNS YPRFLESEFY 190 QDLCKKPQIT TEPHAT
	Isoform 4 [UniParc]. Checksum: 6CF0306689DC7A54	FASTA	179	20,780
	10 20 30 40 50 60 MKRTLLKDWK TRLSYFLQNS STPGKPKTGK KSKQQAFIKP SPEEAQLWSE AFDELLASKY 70 80 90 100 110 120 GLAAFRAFLK SEFCEENIEF WLACEDFKKT KSPQKLSSKA RKIYTDFIEK EAPKEINIDF 130 140 150 160 170 QTKTLIAQNI QEATSGCFTT AQKRVYSLME NNSYPRFLES EFYQDLCKKP QITTEPHAT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A human gene encoding a putative basic helix-loop-helix phosphoprotein whose mRNA increases rapidly in cycloheximide-treated blood mononuclear cells." Siderovski D.P., Heximer S.P., Forsdyke D.R. DNA Cell Biol. 13:125-147(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). Tissue: Placenta.
[2]	"Mechanisms governing subcellular localization and function of human RGS2." Heximer S.P., Lim H., Bernard J.L., Blumer K.J. J. Biol. Chem. 276:14195-14203(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-37; LEU-38; TRP-41; LEU-45; PHE-48 AND LEU-49.
[3]	"Alternative translation initiation of human regulators of G-protein signaling-2 yields a set of functionally distinct proteins." Gu S., Anton A., Salim S., Blumer K.J., Dessauer C.W., Heximer S.P. Mol. Pharmacol. 73:1-11(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, MUTAGENESIS OF MET-1; MET-5; MET-16 AND MET-33.
[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]	"Identification of a human cell growth-inhibiting gene." Kim J.W., Kim H.K., Shin S.M. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	"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 1).
[7]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]	"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 1).
[9]	"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].
[10]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	"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 1). Tissue: Urinary bladder.
[12]	"Differential expression of a basic helix-loop-helix phosphoprotein gene, G0S8, in acute leukemia and localization to human chromosome 1q31." Wu H.-K., Heng H.H.Q., Shi X.-M., Forsdyke D.R., Tsui L.-C., Mak T.W., Minden M.D., Siderovski D.P. Leukemia 9:1291-1298(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[13]	"Protein kinase C phosphorylates RGS2 and modulates its capacity for negative regulation of Galpha 11 signaling." Cunningham M.L., Waldo G.L., Hollinger S., Hepler J.R., Harden T.K. J. Biol. Chem. 276:5438-5444(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION.
[14]	"Regulator of G-protein signaling-2 mediates vascular smooth muscle relaxation and blood pressure." Tang K.M., Wang G.R., Lu P., Karas R.H., Aronovitz M., Heximer S.P., Kaltenbronn K.M., Blumer K.J., Siderovski D.P., Zhu Y., Mendelsohn M.E. Nat. Med. 9:1506-1512(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY PRKG1, INTERACTION WITH PRKG1.
[15]	"Translational control by RGS2." Nguyen C.H., Ming H., Zhao P., Hugendubler L., Gros R., Kimball S.R., Chidiac P. J. Cell Biol. 186:755-765(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EIF2B5, MUTAGENESIS OF LEU-79; GLU-86; LEU-87; SER-90; LYS-102; PHE-105; ILE-110; GLU-111; LEU-114 AND ASN-149.
[16]	"Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits." Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J., Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A., Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P. Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 71-203.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L13391 Genomic DNA. Translation: AAA20680.1.
L13463 mRNA. Translation: AAC37587.1.
AF493926 mRNA. Translation: AAM12640.1.
AY971351 mRNA. Translation: AAY40361.1.
AK313668 mRNA. Translation: BAG36420.1.
BT007065 mRNA. Translation: AAP35728.1.
CR457410 mRNA. Translation: CAG33691.1.
AL035407 Genomic DNA. Translation: CAB62512.1.
CH471067 Genomic DNA. Translation: EAW91231.1.
BC007049 mRNA. Translation: AAH07049.1.

IPI

IPI00013177.
IPI01017891.
IPI01017975.
IPI01018248.

PIR

I53020.

RefSeq

NP_002914.1. NM_002923.3.

UniGene

Hs.78944.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AF0	X-ray	2.30	A	71-203	[»]
2V4Z	X-ray	2.80	B	71-209	[»]
4EKC	X-ray	7.40	B/D	72-203	[»]
4EKD	X-ray	2.71	B	72-203	[»]

ProteinModelPortal

P41220.

ModBase

Search...

Protein-protein interaction databases

IntAct

P41220. 18 interactions.

MINT

MINT-1380095.

STRING

9606.ENSP00000235382.

PTM databases

PhosphoSite

P41220.

Polymorphism databases

DMDM

729545.

Proteomic databases

PaxDb

P41220.

PRIDE

P41220.

Protocols and materials databases

DNASU

5997.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000235382; ENSP00000235382; ENSG00000116741.

GeneID

5997.

KEGG

hsa:5997.

UCSC

uc001gsl.3. human.

Organism-specific databases

CTD

5997.

GeneCards

GC01P192778.

HGNC

HGNC:9998. RGS2.

MIM

600861. gene.

neXtProt

NX_P41220.

PharmGKB

PA34372.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG252352.

HOGENOM

HOG000233512.

HOVERGEN

HBG013233.

InParanoid

P41220.

KO

K16449.

OMA

KSKQQAF.

OrthoDB

EOG4ZGPD8.

PhylomeDB

P41220.

Gene expression databases

ArrayExpress

P41220.

Bgee

P41220.

CleanEx

HS_RGS2.

Genevestigator

P41220.

GermOnline

ENSG00000116741. Homo sapiens.

Family and domain databases

Gene3D

1.10.196.10. 2 hits.

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

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Other

ChiTaRS

RGS2. human.

EvolutionaryTrace

P41220.

GenomeRNAi

5997.

NextBio

23371.

SOURCE

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Entry information

Entry name

RGS2_HUMAN

Accession

Primary (citable) accession number: P41220
Secondary accession number(s): Q6I9U5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 128 of the entry and version 1 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.