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P49795

- RGS19_HUMAN

UniProt

P49795 - RGS19_HUMAN

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Protein

Regulator of G-protein signaling 19

Gene

RGS19

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-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

  1. GTPase activator activity Source: RefGenome

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. G-protein coupled receptor signaling pathway Source: ProtInc
  3. positive regulation of GTPase activity Source: GOC
  4. small GTPase mediated signal transduction Source: ProtInc
  5. termination of G-protein coupled receptor signaling pathway Source: InterPro
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: Chromosome 20

Organism-specific databases

HGNCiHGNC:13735. RGS19.

Subcellular locationi

GO - Cellular componenti

  1. brush border Source: Ensembl
  2. clathrin-coated vesicle Source: Ensembl
  3. cytoplasm Source: RefGenome
  4. Golgi apparatus Source: ProtInc
  5. membrane Source: ProtInc
  6. plasma membrane Source: RefGenome
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.

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.2 Publications

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.
ExpressionAtlasiP49795. baseline and differential.
GenevestigatoriP49795.

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. 12 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:
PDBe
RCSB PDB
PDBj
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.
OMAiFDKLMHS.
OrthoDBiEOG7SN8DQ.
PhylomeDBiP49795.
TreeFamiTF315837.

Family and domain databases

Gene3Di1.10.196.10. 1 hit.
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.

P49795 [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. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UniGeneiHs.422336.

Genome annotation databases

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

Polymorphism databases

DMDMi1730186.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS13555.1.
RefSeqi NP_001034556.1. NM_001039467.1.
NP_005864.1. NM_005873.2.
UniGenei Hs.422336.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CMZ NMR - A 76-217 [» ]
ProteinModelPortali P49795.
SMRi P49795. Positions 79-206.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115576. 12 interactions.
IntActi P49795. 4 interactions.
MINTi MINT-3017930.
STRINGi 9606.ENSP00000333194.

Chemistry

BindingDBi P49795.

PTM databases

PhosphoSitei P49795.

Polymorphism databases

DMDMi 1730186.

Proteomic databases

MaxQBi P49795.
PaxDbi P49795.
PRIDEi P49795.

Protocols and materials databases

DNASUi 10287.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000332298 ; ENSP00000333194 ; ENSG00000171700 .
ENST00000395042 ; ENSP00000378483 ; ENSG00000171700 .
GeneIDi 10287.
KEGGi hsa:10287.
UCSCi uc002yhy.3. human.

Organism-specific databases

CTDi 10287.
GeneCardsi GC20M062704.
HGNCi HGNC:13735. RGS19.
HPAi CAB031925.
MIMi 605071. gene.
neXtProti NX_P49795.
PharmGKBi PA34370.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG258376.
GeneTreei ENSGT00760000118903.
HOGENOMi HOG000233513.
HOVERGENi HBG013233.
InParanoidi P49795.
KOi K16449.
OMAi FDKLMHS.
OrthoDBi EOG7SN8DQ.
PhylomeDBi P49795.
TreeFami TF315837.

Enzyme and pathway databases

Reactomei REACT_18283. G alpha (q) signalling events.
REACT_19231. G alpha (i) signalling events.
REACT_19333. G alpha (z) signalling events.
SignaLinki P49795.

Miscellaneous databases

ChiTaRSi RGS19. human.
EvolutionaryTracei P49795.
GeneWikii RGS19.
GenomeRNAii 10287.
NextBioi 38976.
PROi P49795.
SOURCEi Search...

Gene expression databases

Bgeei P49795.
CleanExi HS_RGS19.
ExpressionAtlasi P49795. baseline and differential.
Genevestigatori P49795.

Family and domain databases

Gene3Di 1.10.196.10. 1 hit.
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. "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. "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.
  11. "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.
  12. "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: October 29, 2014
This is version 146 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