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O15492

- RGS16_HUMAN

UniProt

O15492 - RGS16_HUMAN

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Protein

Regulator of G-protein signaling 16

Gene

RGS16

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. 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 regulationi

Phosphorylation at Tyr-168 by EGFR enhances GTPase accelerating (GAP) activity toward GNAI1.

GO - Molecular functioni

  1. calmodulin binding Source: ProtInc
  2. GTPase activator activity Source: RefGenome

GO - Biological processi

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

Keywords - Molecular functioni

Signal transduction inhibitor

Names & Taxonomyi

Protein namesi
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 namesi
Name:RGS16
Synonyms:RGSR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9997. RGS16.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. plasma membrane Source: RefGenome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi168 – 1681Y → F: 30% decrease in GAP activity. 1 Publication
Mutagenesisi177 – 1771Y → F: No effect on GAP activity. 1 Publication

Organism-specific databases

PharmGKBiPA34367.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 202202Regulator of G-protein signaling 16PRO_0000204221Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21S-palmitoyl cysteineBy similarity
Lipidationi12 – 121S-palmitoyl cysteineBy similarity
Modified residuei168 – 1681Phosphotyrosine; by EGFR1 Publication
Modified residuei177 – 1771Phosphotyrosine1 Publication

Post-translational modificationi

Palmitoylated on Cys-2 and/or Cys-12.By similarity
Phosphorylated. Regulated by phosphorylation at Tyr-168 by EGFR upon stimulation by EGF.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiO15492.
PRIDEiO15492.

PTM databases

PhosphoSiteiO15492.

Expressioni

Tissue specificityi

Abundantly expressed in retina with lower levels of expression in most other tissues.

Gene expression databases

BgeeiO15492.
CleanExiHS_RGS16.
GenevestigatoriO15492.

Organism-specific databases

HPAiHPA053250.
HPA055824.

Interactioni

Protein-protein interaction databases

BioGridi111936. 13 interactions.
DIPiDIP-59094N.
IntActiO15492. 2 interactions.
STRINGi9606.ENSP00000356529.

Structurei

Secondary structure

1
202
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi53 – 6210Combined sources
Helixi66 – 705Combined sources
Helixi73 – 8513Combined sources
Helixi89 – 10113Combined sources
Helixi107 – 12115Combined sources
Helixi134 – 14310Combined sources
Helixi144 – 1463Combined sources
Turni149 – 1524Combined sources
Helixi153 – 16513Combined sources
Helixi167 – 1737Combined sources
Helixi175 – 18612Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BT2X-ray1.90A/B/C/D/E53-190[»]
2IK8X-ray2.71B/D53-190[»]
ProteinModelPortaliO15492.
SMRiO15492. Positions 53-188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15492.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 181117RGSPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG269229.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233512.
HOVERGENiHBG013233.
InParanoidiO15492.
KOiK16449.
OMAiSRAQRIF.
OrthoDBiEOG7VHSZ5.
PhylomeDBiO15492.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 2 hits.
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]

Sequencei

Sequence statusi: Complete.

O15492 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MCRTLAAFPT TCLERAKEFK TRLGIFLHKS ELGCDTGSTG KFEWGSKHSK
60 70 80 90 100
ENRNFSEDVL GWRESFDLLL SSKNGVAAFH AFLKTEFSEE NLEFWLACEE
110 120 130 140 150
FKKIRSATKL ASRAHQIFEE FICSEAPKEV NIDHETHELT RMNLQTATAT
160 170 180 190 200
CFDAAQGKTR TLMEKDSYPR FLKSPAYRDL AAQASAASAT LSSCSLDEPS

HT
Length:202
Mass (Da):22,749
Last modified:January 11, 2011 - v2
Checksum:i19B384E935F3E5D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421F → S in AAC16912. (PubMed:9223279)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371H → R.7 Publications
Corresponds to variant rs1144566 [ dbSNP | Ensembl ].
VAR_046528

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1348.1.
RefSeqiNP_002919.3. NM_002928.3.
UniGeneiHs.413297.

Genome annotation databases

EnsembliENST00000367558; ENSP00000356529; ENSG00000143333.
GeneIDi6004.
KEGGihsa:6004.
UCSCiuc001gpl.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1348.1.
RefSeqi NP_002919.3. NM_002928.3.
UniGenei Hs.413297.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali O15492.
SMRi O15492. Positions 53-188.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111936. 13 interactions.
DIPi DIP-59094N.
IntActi O15492. 2 interactions.
STRINGi 9606.ENSP00000356529.

Chemistry

BindingDBi O15492.

PTM databases

PhosphoSitei O15492.

Proteomic databases

PaxDbi O15492.
PRIDEi O15492.

Protocols and materials databases

DNASUi 6004.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367558 ; ENSP00000356529 ; ENSG00000143333 .
GeneIDi 6004.
KEGGi hsa:6004.
UCSCi uc001gpl.4. human.

Organism-specific databases

CTDi 6004.
GeneCardsi GC01M182567.
H-InvDB HIX0001402.
HGNCi HGNC:9997. RGS16.
HPAi HPA053250.
HPA055824.
MIMi 602514. gene.
neXtProti NX_O15492.
PharmGKBi PA34367.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG269229.
GeneTreei ENSGT00760000118903.
HOGENOMi HOG000233512.
HOVERGENi HBG013233.
InParanoidi O15492.
KOi K16449.
OMAi SRAQRIF.
OrthoDBi EOG7VHSZ5.
PhylomeDBi O15492.
TreeFami TF315837.

Miscellaneous databases

EvolutionaryTracei O15492.
GeneWikii RGS16.
GenomeRNAii 6004.
NextBioi 23419.
PROi O15492.
SOURCEi Search...

Gene expression databases

Bgeei O15492.
CleanExi HS_RGS16.
Genevestigatori O15492.

Family and domain databases

Gene3Di 1.10.196.10. 2 hits.
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. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-168 BY EGFR, PHOSPHORYLATION AT TYR-177, MUTAGENESIS OF TYR-168 AND TYR-177.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 53-190.

Entry informationi

Entry nameiRGS16_HUMAN
AccessioniPrimary (citable) accession number: O15492
Secondary accession number(s): B2R4M4, Q5VYN9, Q99701
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 126 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 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