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Protein

Regulator of G-protein signaling 19

Gene

RGS19

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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-alpha subfamily 1 members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Keywords - Biological processi

Autophagy

Enzyme and pathway databases

ReactomeiREACT_18283. G alpha (q) signalling events.
REACT_19231. G alpha (i) signalling events.
REACT_19333. G alpha (z) signalling events.
SignaLinkiP49795.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of G-protein signaling 19
Short name:
RGS19
Alternative name(s):
G-alpha-interacting protein
Short name:
GAIP
Gene namesi
Name:RGS19
Synonyms:GAIP, GNAI3IP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:13735. RGS19.

Subcellular locationi

GO - Cellular componenti

  • brush border Source: Ensembl
  • clathrin-coated vesicle Source: Ensembl
  • cytoplasm Source: GO_Central
  • Golgi apparatus Source: ProtInc
  • membrane Source: ProtInc
  • membrane raft Source: Ensembl
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi151 – 1511S → A: Diminishes gap activity towards G(i)-alpha3 and autophagy in colon cancer cells. 1 Publication

Organism-specific databases

PharmGKBiPA34370.

Polymorphism and mutation databases

BioMutaiRGS19.
DMDMi1730186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 217217Regulator of G-protein signaling 19PRO_0000204229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei97 – 971Phosphoserine1 Publication
Modified residuei151 – 1511Phosphoserine; by MAPK1 and MAPK31 Publication

Post-translational modificationi

Fatty acylated. Heavily palmitoylated in the cysteine string motif.1 Publication
Phosphorylated, mainly on serine residues.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP49795.
PaxDbiP49795.
PRIDEiP49795.

PTM databases

PhosphoSiteiP49795.

Expressioni

Tissue specificityi

Highest expression in lung. Placenta, liver and heart also express high levels of GAIP.

Gene expression databases

BgeeiP49795.
CleanExiHS_RGS19.
GenevisibleiP49795. HS.

Organism-specific databases

HPAiCAB031925.

Interactioni

Subunit structurei

Interacts with GIPC PDZ domain.

Binary interactionsi

WithEntry#Exp.IntActNotes
Gnai3P087534EBI-874907,EBI-874897From a different organism.

Protein-protein interaction databases

BioGridi115576. 10 interactions.
IntActiP49795. 4 interactions.
MINTiMINT-3017930.
STRINGi9606.ENSP00000333194.

Structurei

Secondary structure

1
217
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi81 – 877Combined sources
Helixi92 – 954Combined sources
Helixi98 – 11114Combined sources
Helixi115 – 12511Combined sources
Helixi126 – 1283Combined sources
Helixi133 – 14513Combined sources
Turni146 – 1483Combined sources
Beta strandi150 – 1523Combined sources
Helixi160 – 1689Combined sources
Beta strandi169 – 1713Combined sources
Helixi178 – 19114Combined sources
Helixi193 – 1964Combined sources
Helixi200 – 2034Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CMZNMR-A76-217[»]
ProteinModelPortaliP49795.
SMRiP49795. Positions 79-206.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49795.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini90 – 206117RGSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni207 – 21711Interaction with GIPCAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi39 – 4911Poly-CysAdd
BLAST

Sequence similaritiesi

Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG258376.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233513.
HOVERGENiHBG013233.
InParanoidiP49795.
KOiK16449.
OMAiGINKKMQ.
OrthoDBiEOG7SN8DQ.
PhylomeDBiP49795.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 1 hit.
InterProiIPR016137. RGS.
IPR024066. RGS_subdom1.
[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.

P49795-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTPHEAEKQ ITGPEEADRP PSMSSHDTAS PAAPSRNPCC LCWCCCCSCS
60 70 80 90 100
WNQERRRAWQ ASRESKLQPL PSCEVCATPS PEEVQSWAQS FDKLMHSPAG
110 120 130 140 150
RSVFRAFLRT EYSEENMLFW LACEELKAEA NQHVVDEKAR LIYEDYVSIL
160 170 180 190 200
SPKEVSLDSR VREGINKKMQ EPSAHTFDDA QLQIYTLMHR DSYPRFLSSP
210
TYRALLLQGP SQSSSEA
Length:217
Mass (Da):24,636
Last modified:October 1, 1996 - v1
Checksum:i925A5687DC222CBD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041A → V in AAM12653 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91809 mRNA. Translation: CAA62919.1.
AF493939 mRNA. Translation: AAM12653.1.
AY585188 mRNA. Translation: AAS94232.1.
BT009804 mRNA. Translation: AAP88806.1.
AK290081 mRNA. Translation: BAF82770.1.
AL590548 Genomic DNA. Translation: CAD11902.1.
CH471077 Genomic DNA. Translation: EAW75166.1.
CH471077 Genomic DNA. Translation: EAW75167.1.
BC001318 mRNA. Translation: AAH01318.1.
BC054337 mRNA. Translation: AAH54337.1.
BC063010 mRNA. Translation: AAH63010.1.
CCDSiCCDS13555.1.
RefSeqiNP_001034556.1. NM_001039467.1.
NP_005864.1. NM_005873.2.
XP_011526787.1. XM_011528485.1.
XP_011526788.1. XM_011528486.1.
UniGeneiHs.422336.

Genome annotation databases

EnsembliENST00000332298; ENSP00000333194; ENSG00000171700.
ENST00000395042; ENSP00000378483; ENSG00000171700.
GeneIDi10287.
KEGGihsa:10287.
UCSCiuc002yhy.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91809 mRNA. Translation: CAA62919.1.
AF493939 mRNA. Translation: AAM12653.1.
AY585188 mRNA. Translation: AAS94232.1.
BT009804 mRNA. Translation: AAP88806.1.
AK290081 mRNA. Translation: BAF82770.1.
AL590548 Genomic DNA. Translation: CAD11902.1.
CH471077 Genomic DNA. Translation: EAW75166.1.
CH471077 Genomic DNA. Translation: EAW75167.1.
BC001318 mRNA. Translation: AAH01318.1.
BC054337 mRNA. Translation: AAH54337.1.
BC063010 mRNA. Translation: AAH63010.1.
CCDSiCCDS13555.1.
RefSeqiNP_001034556.1. NM_001039467.1.
NP_005864.1. NM_005873.2.
XP_011526787.1. XM_011528485.1.
XP_011526788.1. XM_011528486.1.
UniGeneiHs.422336.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CMZNMR-A76-217[»]
ProteinModelPortaliP49795.
SMRiP49795. Positions 79-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115576. 10 interactions.
IntActiP49795. 4 interactions.
MINTiMINT-3017930.
STRINGi9606.ENSP00000333194.

Chemistry

BindingDBiP49795.

PTM databases

PhosphoSiteiP49795.

Polymorphism and mutation databases

BioMutaiRGS19.
DMDMi1730186.

Proteomic databases

MaxQBiP49795.
PaxDbiP49795.
PRIDEiP49795.

Protocols and materials databases

DNASUi10287.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000332298; ENSP00000333194; ENSG00000171700.
ENST00000395042; ENSP00000378483; ENSG00000171700.
GeneIDi10287.
KEGGihsa:10287.
UCSCiuc002yhy.3. human.

Organism-specific databases

CTDi10287.
GeneCardsiGC20M062704.
HGNCiHGNC:13735. RGS19.
HPAiCAB031925.
MIMi605071. gene.
neXtProtiNX_P49795.
PharmGKBiPA34370.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG258376.
GeneTreeiENSGT00760000118903.
HOGENOMiHOG000233513.
HOVERGENiHBG013233.
InParanoidiP49795.
KOiK16449.
OMAiGINKKMQ.
OrthoDBiEOG7SN8DQ.
PhylomeDBiP49795.
TreeFamiTF315837.

Enzyme and pathway databases

ReactomeiREACT_18283. G alpha (q) signalling events.
REACT_19231. G alpha (i) signalling events.
REACT_19333. G alpha (z) signalling events.
SignaLinkiP49795.

Miscellaneous databases

ChiTaRSiRGS19. human.
EvolutionaryTraceiP49795.
GeneWikiiRGS19.
GenomeRNAii10287.
NextBioi38976.
PROiP49795.
SOURCEiSearch...

Gene expression databases

BgeeiP49795.
CleanExiHS_RGS19.
GenevisibleiP49795. HS.

Family and domain databases

Gene3Di1.10.196.10. 1 hit.
InterProiIPR016137. RGS.
IPR024066. RGS_subdom1.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain."
    de Vries L., Mousli M., Wurmser A., Farquhar M.G.
    Proc. Natl. Acad. Sci. U.S.A. 92:11916-11920(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "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 (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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].
    Tissue: Subthalamic nucleus.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Blood, Placenta and Testis.
  8. "GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits."
    de Vries L., Elenko E., Hubler L., Jones T.L.Z., Farquhar M.G.
    Proc. Natl. Acad. Sci. U.S.A. 93:15203-15208(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Solution structure of human GAIP (Galpha interacting protein): a regulator of G protein signaling."
    de Alba E., De Vries L., Farquhar M.G., Tjandra N.
    J. Mol. Biol. 291:927-939(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 79-206.
  12. "RGSZ1, a Gz-selective RGS protein in brain. Structure, membrane association, regulation by Galphaz phosphorylation, and relationship to a Gz GTPase-activating protein subfamily."
    Wang J., Ducret A., Tu Y., Kozasa T., Aebersold R., Ross E.M.
    J. Biol. Chem. 273:26014-26025(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION.
  13. "Erk1/2-dependent phosphorylation of Galpha-interacting protein stimulates its GTPase accelerating activity and autophagy in human colon cancer cells."
    Ogier-Denis E., Pattingre S., El Benna J., Codogno P.
    J. Biol. Chem. 275:39090-39095(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-151, MUTAGENESIS OF SER-151.

Entry informationi

Entry nameiRGS19_HUMAN
AccessioniPrimary (citable) accession number: P49795
Secondary accession number(s): A8K216
, E1P5G9, Q53XN0, Q8TD60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 153 of the entry and version 1 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 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.