O15492 (RGS16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Regulator of G-protein signaling 16
Short name=RGS16

Alternative name(s):
A28-RGS14P
Retinal-specific RGS
Short name=RGS-r
Short name=hRGS-r
Retinally abundant regulator of G-protein signaling

Gene names

Name:	RGS16
Synonyms:	RGSR

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	202 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. Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha. May play a role in regulating the kinetics of signaling in the phototransduction cascade.
Enzyme regulation	Phosphorylation at Tyr-168 by EGFR enhances GTPase accelerating (GAP) activity toward GNAI1.
Tissue specificity	Abundantly expressed in retina with lower levels of expression in most other tissues.
Post-translational modification	Palmitoylated on Cys-2 and/or Cys-12 By similarity. Phosphorylated. Regulated by phosphorylation at Tyr-168 by EGFR upon stimulation by EGF. Ref.9
Sequence similarities	Contains 1 RGS domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Molecular function	Signal transduction inhibitor
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of signal transduction Inferred from electronic annotation. Source: UniProtKB-KW regulation of G-protein coupled receptor protein signaling pathway Traceable author statement. Source: ProtInc visual perception Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome plasma membrane Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	GTPase activator activity Inferred from Biological aspect of Ancestor. Source: RefGenome calmodulin binding Traceable author statement. Source: ProtInc signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 202

202

Regulator of G-protein signaling 16

PRO_0000204221

Regions

Domain

65 – 181

117

RGS

Amino acid modifications

Modified residue

168

1

Phosphotyrosine; by EGFR Ref.9

Modified residue

177

1

Phosphotyrosine Ref.9

Lipidation

2

1

S-palmitoyl cysteine By similarity

Lipidation

12

1

S-palmitoyl cysteine By similarity

Natural variations

Natural variant

137

1

H → R. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8
Corresponds to variant rs1144566 [ dbSNP | Ensembl ].

VAR_046528

Experimental info

Mutagenesis

168

1

Y → F: 30% decrease in GAP activity. Ref.9

Mutagenesis

177

1

Y → F: No effect on GAP activity. Ref.9

Sequence conflict

42

1

F → S in AAC16912. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

202

Helix Strand Turn

Details...

Helix

53 – 62

10

Helix

66 – 70

5

Helix

73 – 85

13

Helix

89 – 101

13

Helix

107 – 121

15

Helix

134 – 143

10

Helix

144 – 146

3

Turn

149 – 152

4

Helix

153 – 165

13

Helix

167 – 173

7

Helix

175 – 186

12

Sequences

	Sequence		Length	Mass (Da)
	O15492 [UniParc]. Last modified January 11, 2011. Version 2. Checksum: 19B384E935F3E5D1	FASTA	202	22,749
	10 20 30 40 50 60 MCRTLAAFPT TCLERAKEFK TRLGIFLHKS ELGCDTGSTG KFEWGSKHSK ENRNFSEDVL 70 80 90 100 110 120 GWRESFDLLL SSKNGVAAFH AFLKTEFSEE NLEFWLACEE FKKIRSATKL ASRAHQIFEE 130 140 150 160 170 180 FICSEAPKEV NIDHETHELT RMNLQTATAT CFDAAQGKTR TLMEKDSYPR FLKSPAYRDL 190 200 AAQASAASAT LSSCSLDEPS HT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The p53 tumor suppressor targets a novel regulator of G protein signaling." Buckbinder L., Velasco-Miguel S., Chen Y., Xu N., Talbott R., Gelbert L., Gao J., Seizinger B.R., Gutkind J.S., Kley N. Proc. Natl. Acad. Sci. U.S.A. 94:7868-7872(1997) [PubMed: 9223279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-137. Tissue: Brain.
[2]	"Cloning of a retinally abundant regulator of G-protein signaling (RGS-r/RGS16): genomic structure and chromosomal localization of the human gene." Snow B.E., Antonio L., Suggs S., Siderovski D.P. Gene 206:247-253(1998) [PubMed: 9469939] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT ARG-137. Tissue: Retina.
[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], VARIANT ARG-137.
[4]	"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], VARIANT ARG-137.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-137.
[6]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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], VARIANT ARG-137.
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-137. Tissue: Lung.
[9]	"RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation." Derrien A., Druey K.M. J. Biol. Chem. 276:48532-48538(2001) [PubMed: 11602604] [Abstract] Cited for: PHOSPHORYLATION AT TYR-168 BY EGFR, PHOSPHORYLATION AT TYR-177, MUTAGENESIS OF TYR-168 AND TYR-177.
[10]	"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: 18434541] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-190.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U70426 mRNA. Translation: AAC16912.1.
U94829 mRNA. Translation: AAC52040.1.
AF009356 Genomic DNA. Translation: AAC39642.1.
AF493937 mRNA. Translation: AAM12651.1.
BT006638 mRNA. Translation: AAP35284.1.
AK311880 mRNA. Translation: BAG34821.1.
AL353778 Genomic DNA. Translation: CAH72419.1.
CH471067 Genomic DNA. Translation: EAW91129.1.
BC006243 mRNA. Translation: AAH06243.1.

IPI

IPI00289948.

RefSeq

NP_002919.3. NM_002928.3.

UniGene

Hs.413297.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BT2	X-ray	1.90	A/B/C/D/E	53-190	[»]
2IK8	X-ray	2.71	B/D	53-190	[»]

ProteinModelPortal

O15492.

SMR

O15492. Positions 6-188.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59094N.

IntAct

O15492. 2 interactions.

STRING

O15492.

PTM databases

PhosphoSite

O15492.

Proteomic databases

PRIDE

O15492.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000367558; ENSP00000356529; ENSG00000143333.

GeneID

6004.

KEGG

hsa:6004.

Organism-specific databases

CTD

6004.

GeneCards

GC01M182567.

H-InvDB

HIX0001402.

HGNC

HGNC:9997. RGS16.

MIM

602514. gene.

neXtProt

NX_O15492.

PharmGKB

PA34367.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19939.

GeneTree

ENSGT00600000084096.

HOGENOM

HBG713967.

HOVERGEN

HBG013233.

InParanoid

O15492.

OMA

PAEPSHT.

OrthoDB

EOG4STS5S.

PhylomeDB

O15492.

Gene expression databases

ArrayExpress

O15492.

Bgee

O15492.

CleanEx

HS_RGS16.

Genevestigator

O15492.

GermOnline

ENSG00000143333. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:1.10.196.10. G3DSA:1.10.196.10. 1 hit.

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

NextBio

23419.

SOURCE

Search...

Entry information

Entry name

RGS16_HUMAN

Accession

Primary (citable) accession number: O15492
Secondary accession number(s): B2R4M4, Q5VYN9, Q99701

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 11, 2011
Last modified:	January 25, 2012
This is version 100 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.