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P49795 (RGS19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulator of G-protein signaling 19

Short name=RGS19
Alternative name(s):
G-alpha-interacting protein
Short name=GAIP
Gene names
Name:RGS19
Synonyms:GAIP, GNAI3IP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceEvidence 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-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.

Subunit structure

Interacts with GIPC PDZ domain.

Subcellular location

Membrane; Lipid-anchor.

Tissue specificity

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

Post-translational modification

Fatty acylated. Heavily palmitoylated in the cysteine string motif. Ref.8

Phosphorylated, mainly on serine residues. Ref.12

Sequence similarities

Contains 1 RGS domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Gnai3P087534EBI-874907,EBI-874897From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Regulator of G-protein signaling 19
PRO_0000204229

Regions

Domain90 – 206117RGS
Region207 – 21711Interaction with GIPC
Compositional bias39 – 4911Poly-Cys

Amino acid modifications

Modified residue241Phosphoserine By similarity
Modified residue971Phosphoserine Ref.9
Modified residue1511Phosphoserine; by MAPK1 and MAPK3 Ref.12

Experimental info

Mutagenesis1511S → A: Diminishes gap activity towards G(i)-alpha3 and autophagy in colon cancer cells. Ref.12
Sequence conflict2041A → V in AAM12653. Ref.2

Secondary structure

........................ 217
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49795 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 925A5687DC222CBD

FASTA21724,636
        10         20         30         40         50         60 
MPTPHEAEKQ ITGPEEADRP PSMSSHDTAS PAAPSRNPCC LCWCCCCSCS WNQERRRAWQ 

        70         80         90        100        110        120 
ASRESKLQPL PSCEVCATPS PEEVQSWAQS FDKLMHSPAG RSVFRAFLRT EYSEENMLFW 

       130        140        150        160        170        180 
LACEELKAEA NQHVVDEKAR LIYEDYVSIL SPKEVSLDSR VREGINKKMQ EPSAHTFDDA 

       190        200        210 
QLQIYTLMHR DSYPRFLSSP TYRALLLQGP SQSSSEA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13555.1.
RefSeqNP_001034556.1. NM_001039467.1.
NP_005864.1. NM_005873.2.
UniGeneHs.422336.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CMZNMR-A76-217[»]
ProteinModelPortalP49795.
SMRP49795. Positions 79-206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115576. 12 interactions.
IntActP49795. 4 interactions.
MINTMINT-3017930.
STRING9606.ENSP00000333194.

Chemistry

BindingDBP49795.

PTM databases

PhosphoSiteP49795.

Polymorphism databases

DMDM1730186.

Proteomic databases

MaxQBP49795.
PaxDbP49795.
PRIDEP49795.

Protocols and materials databases

DNASU10287.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332298; ENSP00000333194; ENSG00000171700.
ENST00000395042; ENSP00000378483; ENSG00000171700.
GeneID10287.
KEGGhsa:10287.
UCSCuc002yhy.3. human.

Organism-specific databases

CTD10287.
GeneCardsGC20M062704.
HGNCHGNC:13735. RGS19.
HPACAB031925.
MIM605071. gene.
neXtProtNX_P49795.
PharmGKBPA34370.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258376.
HOGENOMHOG000233513.
HOVERGENHBG013233.
InParanoidP49795.
KOK16449.
OMAFDKLMHS.
OrthoDBEOG7SN8DQ.
PhylomeDBP49795.
TreeFamTF315837.

Enzyme and pathway databases

SignaLinkP49795.

Gene expression databases

ArrayExpressP49795.
BgeeP49795.
CleanExHS_RGS19.
GenevestigatorP49795.

Family and domain databases

Gene3D1.10.196.10. 1 hit.
InterProIPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
[Graphical view]
PfamPF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR01301. RGSPROTEIN.
SMARTSM00315. RGS. 1 hit.
[Graphical view]
SUPFAMSSF48097. SSF48097. 1 hit.
PROSITEPS50132. RGS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRGS19. human.
EvolutionaryTraceP49795.
GeneWikiRGS19.
GenomeRNAi10287.
NextBio38976.
PROP49795.
SOURCESearch...

Entry information

Entry nameRGS19_HUMAN
AccessionPrimary (citable) accession number: P49795
Secondary accession number(s): A8K216 expand/collapse secondary AC list , E1P5G9, Q53XN0, Q8TD60
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM