GPSM3_HUMAN
ID GPSM3_HUMAN Reviewed; 160 AA.
AC Q9Y4H4; A2BFJ3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=G-protein-signaling modulator 3;
DE AltName: Full=Activator of G-protein signaling 4;
DE AltName: Full=G18.1b;
DE AltName: Full=Protein G18;
GN Name=GPSM3; Synonyms=AGS4, C6orf9, G18;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=15096500; DOI=10.1074/jbc.m312786200;
RA Cao X., Cismowski M.J., Sato M., Blumer J.B., Lanier S.M.;
RT "Identification and characterization of AGS4: a protein containing three G-
RT protein regulatory motifs that regulate the activation state of Gialpha.";
RL J. Biol. Chem. 279:27567-27574(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kendall E., Campbell R.D.;
RT "Characterisation of the novel gene G18, located in the class III region of
RT the human major histocompatibility complex.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RA Li Y., Fu S., Huang C., Jiang C., Ren S., Zhou J., Yu Y., Xu S., Wang Y.,
RA Fu G., Chen Z., Han Z.;
RT "A novel gene expressed in human adrenal gland.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, MUTAGENESIS OF ALA-121, AND DOMAIN.
RX PubMed=14656218; DOI=10.1042/bj20031686;
RA Kimple R.J., Willard F.S., Hains M.D., Jones M.B., Nweke G.K.,
RA Siderovski D.P.;
RT "Guanine nucleotide dissociation inhibitor activity of the triple GoLoco
RT motif protein G18: alanine-to-aspartate mutation restores function to an
RT inactive second GoLoco motif.";
RL Biochem. J. 378:801-808(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-39, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-39; SER-59 AND
RP THR-62, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Interacts with subunit of G(i) alpha proteins and regulates
CC the activation of G(i) alpha proteins. {ECO:0000269|PubMed:14656218,
CC ECO:0000269|PubMed:15096500}.
CC -!- INTERACTION:
CC Q9Y4H4; Q8TDX5-2: ACMSD; NbExp=3; IntAct=EBI-347538, EBI-12809094;
CC Q9Y4H4; Q7Z3H0-1: ANKRD33; NbExp=5; IntAct=EBI-347538, EBI-16746154;
CC Q9Y4H4; Q8WXK1: ASB15; NbExp=3; IntAct=EBI-347538, EBI-12809012;
CC Q9Y4H4; Q8N1L9: BATF2; NbExp=3; IntAct=EBI-347538, EBI-742695;
CC Q9Y4H4; Q96LC9: BMF; NbExp=3; IntAct=EBI-347538, EBI-3919268;
CC Q9Y4H4; Q8WW14-2: C10orf82; NbExp=3; IntAct=EBI-347538, EBI-12831628;
CC Q9Y4H4; Q8TAV5: C11orf45; NbExp=3; IntAct=EBI-347538, EBI-12810853;
CC Q9Y4H4; Q5W0N0-2: C9orf57; NbExp=3; IntAct=EBI-347538, EBI-18101667;
CC Q9Y4H4; Q6WN34-2: CHRDL2; NbExp=3; IntAct=EBI-347538, EBI-12593838;
CC Q9Y4H4; Q96BR5: COA7; NbExp=3; IntAct=EBI-347538, EBI-6269632;
CC Q9Y4H4; P78358: CTAG1B; NbExp=5; IntAct=EBI-347538, EBI-1188472;
CC Q9Y4H4; Q01658: DR1; NbExp=3; IntAct=EBI-347538, EBI-750300;
CC Q9Y4H4; Q9NVL1-2: FAM86C1P; NbExp=5; IntAct=EBI-347538, EBI-12845222;
CC Q9Y4H4; P21333-2: FLNA; NbExp=3; IntAct=EBI-347538, EBI-9641086;
CC Q9Y4H4; Q8WXI9: GATAD2B; NbExp=3; IntAct=EBI-347538, EBI-923440;
CC Q9Y4H4; P63096: GNAI1; NbExp=8; IntAct=EBI-347538, EBI-618639;
CC Q9Y4H4; P04899: GNAI2; NbExp=3; IntAct=EBI-347538, EBI-353997;
CC Q9Y4H4; P08754: GNAI3; NbExp=8; IntAct=EBI-347538, EBI-357563;
CC Q9Y4H4; P28799: GRN; NbExp=3; IntAct=EBI-347538, EBI-747754;
CC Q9Y4H4; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-347538, EBI-1054873;
CC Q9Y4H4; A0A087WSW0: HELT; NbExp=3; IntAct=EBI-347538, EBI-12057631;
CC Q9Y4H4; Q4VC39: HIGD2B; NbExp=3; IntAct=EBI-347538, EBI-12881610;
CC Q9Y4H4; O75031: HSF2BP; NbExp=3; IntAct=EBI-347538, EBI-7116203;
CC Q9Y4H4; P04792: HSPB1; NbExp=3; IntAct=EBI-347538, EBI-352682;
CC Q9Y4H4; Q6IPM2: IQCE; NbExp=3; IntAct=EBI-347538, EBI-3893098;
CC Q9Y4H4; P26440: IVD; NbExp=3; IntAct=EBI-347538, EBI-2866408;
CC Q9Y4H4; O60333-2: KIF1B; NbExp=3; IntAct=EBI-347538, EBI-10975473;
CC Q9Y4H4; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-347538, EBI-1052037;
CC Q9Y4H4; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-347538, EBI-10241252;
CC Q9Y4H4; Q3LI73: KRTAP19-4; NbExp=3; IntAct=EBI-347538, EBI-12958461;
CC Q9Y4H4; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-347538, EBI-12516603;
CC Q9Y4H4; P50222: MEOX2; NbExp=3; IntAct=EBI-347538, EBI-748397;
CC Q9Y4H4; Q15466: NR0B2; NbExp=3; IntAct=EBI-347538, EBI-3910729;
CC Q9Y4H4; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-347538, EBI-10181968;
CC Q9Y4H4; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-347538, EBI-473160;
CC Q9Y4H4; P85299-2: PRR5; NbExp=3; IntAct=EBI-347538, EBI-12944296;
CC Q9Y4H4; P57078-2: RIPK4; NbExp=3; IntAct=EBI-347538, EBI-12854608;
CC Q9Y4H4; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-347538, EBI-396669;
CC Q9Y4H4; Q2I0M5: RSPO4; NbExp=3; IntAct=EBI-347538, EBI-12821217;
CC Q9Y4H4; P00441: SOD1; NbExp=3; IntAct=EBI-347538, EBI-990792;
CC Q9Y4H4; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-347538, EBI-11959123;
CC Q9Y4H4; O43610: SPRY3; NbExp=3; IntAct=EBI-347538, EBI-12290641;
CC Q9Y4H4; Q9Y2K9: STXBP5L; NbExp=3; IntAct=EBI-347538, EBI-11294039;
CC Q9Y4H4; O75478: TADA2A; NbExp=3; IntAct=EBI-347538, EBI-742268;
CC Q9Y4H4; Q13148: TARDBP; NbExp=6; IntAct=EBI-347538, EBI-372899;
CC Q9Y4H4; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-347538, EBI-11523345;
CC Q9Y4H4; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-347538, EBI-12068150;
CC Q9Y4H4; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-347538, EBI-739895;
CC Q9Y4H4; O76024: WFS1; NbExp=3; IntAct=EBI-347538, EBI-720609;
CC Q9Y4H4; P63104: YWHAZ; NbExp=5; IntAct=EBI-347538, EBI-347088;
CC Q9Y4H4; P17024: ZNF20; NbExp=3; IntAct=EBI-347538, EBI-717634;
CC Q9Y4H4; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-347538, EBI-745520;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15096500}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, placenta, lung and liver.
CC {ECO:0000269|PubMed:15096500}.
CC -!- DOMAIN: The GoLoco 1 and/or GoLoco 3 domains exhibit GDI activity
CC towards GDP-bound G(i) alpha protein, but not the GoLoco 2 domain.
CC {ECO:0000269|PubMed:14656218}.
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DR EMBL; AJ243937; CAB51288.1; -; mRNA.
DR EMBL; AF155657; AAF67476.1; -; mRNA.
DR EMBL; AK313922; BAG36643.1; -; mRNA.
DR EMBL; AL662830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX284686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR933878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR812478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03620.1; -; Genomic_DNA.
DR EMBL; BC018724; AAH18724.1; -; mRNA.
DR CCDS; CCDS34419.1; -.
DR RefSeq; NP_001263430.1; NM_001276501.1.
DR RefSeq; NP_071390.1; NM_022107.2.
DR AlphaFoldDB; Q9Y4H4; -.
DR BioGRID; 122005; 84.
DR IntAct; Q9Y4H4; 53.
DR STRING; 9606.ENSP00000364180; -.
DR iPTMnet; Q9Y4H4; -.
DR PhosphoSitePlus; Q9Y4H4; -.
DR BioMuta; GPSM3; -.
DR DMDM; 74753502; -.
DR EPD; Q9Y4H4; -.
DR jPOST; Q9Y4H4; -.
DR MassIVE; Q9Y4H4; -.
DR MaxQB; Q9Y4H4; -.
DR PaxDb; Q9Y4H4; -.
DR PeptideAtlas; Q9Y4H4; -.
DR PRIDE; Q9Y4H4; -.
DR ProteomicsDB; 86206; -.
DR Antibodypedia; 28524; 66 antibodies from 18 providers.
DR DNASU; 63940; -.
DR Ensembl; ENST00000375040.8; ENSP00000364180.3; ENSG00000213654.10.
DR Ensembl; ENST00000375043.3; ENSP00000364183.3; ENSG00000213654.10.
DR Ensembl; ENST00000383265.8; ENSP00000372752.4; ENSG00000206314.9.
DR Ensembl; ENST00000383269.2; ENSP00000372756.2; ENSG00000206314.9.
DR Ensembl; ENST00000414839.6; ENSP00000405026.2; ENSG00000236697.7.
DR Ensembl; ENST00000420041.1; ENSP00000413975.1; ENSG00000233490.7.
DR Ensembl; ENST00000424520.6; ENSP00000413430.2; ENSG00000237052.7.
DR Ensembl; ENST00000429209.6; ENSP00000392487.2; ENSG00000234243.7.
DR Ensembl; ENST00000432871.6; ENSP00000414939.2; ENSG00000234508.7.
DR Ensembl; ENST00000441705.1; ENSP00000396786.1; ENSG00000234243.7.
DR Ensembl; ENST00000445326.1; ENSP00000407538.1; ENSG00000234508.7.
DR Ensembl; ENST00000448684.1; ENSP00000403132.1; ENSG00000236697.7.
DR Ensembl; ENST00000453667.6; ENSP00000414024.2; ENSG00000233490.7.
DR Ensembl; ENST00000457070.1; ENSP00000410087.1; ENSG00000237052.7.
DR GeneID; 63940; -.
DR KEGG; hsa:63940; -.
DR MANE-Select; ENST00000375040.8; ENSP00000364180.3; NM_001276501.2; NP_001263430.1.
DR UCSC; uc003oay.5; human.
DR CTD; 63940; -.
DR DisGeNET; 63940; -.
DR GeneCards; GPSM3; -.
DR HGNC; HGNC:13945; GPSM3.
DR HPA; ENSG00000213654; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 618558; gene.
DR neXtProt; NX_Q9Y4H4; -.
DR NIAGADS; ENSG00000213654; -.
DR OpenTargets; ENSG00000213654; -.
DR PharmGKB; PA25940; -.
DR VEuPathDB; HostDB:ENSG00000213654; -.
DR eggNOG; ENOG502STIS; Eukaryota.
DR GeneTree; ENSGT00390000002471; -.
DR HOGENOM; CLU_139851_0_0_1; -.
DR InParanoid; Q9Y4H4; -.
DR OMA; HQSQRME; -.
DR PhylomeDB; Q9Y4H4; -.
DR TreeFam; TF339136; -.
DR PathwayCommons; Q9Y4H4; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; Q9Y4H4; -.
DR SIGNOR; Q9Y4H4; -.
DR BioGRID-ORCS; 63940; 19 hits in 1071 CRISPR screens.
DR GenomeRNAi; 63940; -.
DR Pharos; Q9Y4H4; Tbio.
DR PRO; PR:Q9Y4H4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9Y4H4; protein.
DR Bgee; ENSG00000213654; Expressed in granulocyte and 95 other tissues.
DR ExpressionAtlas; Q9Y4H4; baseline and differential.
DR Genevisible; Q9Y4H4; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0030695; F:GTPase regulator activity; IEA:InterPro.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IBA:GO_Central.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR042888; GPSM3.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR47617; PTHR47617; 1.
DR Pfam; PF02188; GoLoco; 2.
DR SMART; SM00390; GoLoco; 3.
DR PROSITE; PS50877; GOLOCO; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..160
FT /note="G-protein-signaling modulator 3"
FT /id="PRO_0000233717"
FT DOMAIN 62..84
FT /note="GoLoco 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT DOMAIN 104..126
FT /note="GoLoco 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT DOMAIN 132..155
FT /note="GoLoco 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U1Z5"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MUTAGEN 121
FT /note="A->D: Restores G(i) alpha binding and GDI activity
FT of the GoLoco 2 domain."
FT /evidence="ECO:0000269|PubMed:14656218"
FT CONFLICT 14
FT /note="Q -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 160 AA; 17866 MW; 42B3D207D2C48428 CRC64;
MEAERPQEEE DGEQGPPQDE EGWPPPNSTT RPWRSAPPSP PPPGTRHTAL GPRSASLLSL
QTELLLDLVA EAQSRRLEEQ RATFYTPQNP SSLAPAPLRP LEDREQLYST ILSHQCQRME
AQRSEPPLPP GGQELLELLL RVQGGGRMEE QRSRPPTHTC
