G3BP2_MOUSE
ID G3BP2_MOUSE Reviewed; 482 AA.
AC P97379; Q3UL55; Q9R1B8;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Ras GTPase-activating protein-binding protein 2;
DE Short=G3BP-2;
DE AltName: Full=GAP SH3 domain-binding protein 2;
GN Name=G3bp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RX PubMed=9575347;
RA Kennedy D., Wood S.A., Ramsdale T., Tam P.P., Steiner K.A., Mattick J.S.;
RT "Identification of a mouse orthologue of the human ras-GAP-SH3-domain
RT binding protein and structural confirmation that these proteins contain an
RT RNA recognition motif.";
RL Biomed. Pept. Proteins Nucleic Acids 2:93-99(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RA Kennedy D., Mattick J.S.;
RT "Characterisation and chromosomal location of G3BP-1 and G3BP-2a/b, members
RT of a novel SH3 domain-binding and RNA-binding protein family implicated in
RT signal transduction.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND THR-227 (ISOFORM B),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-149; SER-225 AND
RP THR-227, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-392, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-468, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Scaffold protein that plays an essential role in cytoplasmic
CC stress granule formation which acts as a platform for antiviral
CC signaling. {ECO:0000250|UniProtKB:Q9UN86}.
CC -!- SUBUNIT: Forms homooligomers. Forms heterodimers with G3BP1. Interacts
CC with NFKBIA (via N-terminus). Interacts with USP10. Interacts with
CC PABPC1. {ECO:0000250|UniProtKB:Q9UN86}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UN86}.
CC Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9UN86}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P97379-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P97379-2; Sequence=VSP_003606;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE26595.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U65313; AAC53553.1; -; mRNA.
DR EMBL; AF145285; AAD51933.1; -; mRNA.
DR EMBL; AK145697; BAE26595.1; ALT_INIT; mRNA.
DR CCDS; CCDS19427.1; -. [P97379-1]
DR CCDS; CCDS39149.1; -. [P97379-2]
DR RefSeq; NP_001074263.1; NM_001080794.2. [P97379-1]
DR RefSeq; NP_001074266.1; NM_001080797.2. [P97379-1]
DR RefSeq; NP_035946.2; NM_011816.4. [P97379-1]
DR RefSeq; XP_006534990.1; XM_006534927.3.
DR RefSeq; XP_006534991.1; XM_006534928.3.
DR AlphaFoldDB; P97379; -.
DR SMR; P97379; -.
DR BioGRID; 204773; 30.
DR IntAct; P97379; 6.
DR MINT; P97379; -.
DR STRING; 10090.ENSMUSP00000128244; -.
DR iPTMnet; P97379; -.
DR PhosphoSitePlus; P97379; -.
DR SwissPalm; P97379; -.
DR EPD; P97379; -.
DR jPOST; P97379; -.
DR PaxDb; P97379; -.
DR PeptideAtlas; P97379; -.
DR PRIDE; P97379; -.
DR ProteomicsDB; 273018; -. [P97379-1]
DR ProteomicsDB; 273019; -. [P97379-2]
DR Antibodypedia; 13391; 162 antibodies from 26 providers.
DR DNASU; 23881; -.
DR Ensembl; ENSMUST00000113127; ENSMUSP00000108752; ENSMUSG00000029405. [P97379-2]
DR Ensembl; ENSMUST00000164378; ENSMUSP00000128353; ENSMUSG00000029405. [P97379-1]
DR Ensembl; ENSMUST00000167918; ENSMUSP00000132469; ENSMUSG00000029405. [P97379-2]
DR Ensembl; ENSMUST00000169094; ENSMUSP00000128244; ENSMUSG00000029405. [P97379-1]
DR Ensembl; ENSMUST00000202258; ENSMUSP00000144456; ENSMUSG00000029405. [P97379-1]
DR GeneID; 23881; -.
DR KEGG; mmu:23881; -.
DR UCSC; uc008ycg.2; mouse. [P97379-1]
DR CTD; 9908; -.
DR MGI; MGI:2442040; G3bp2.
DR VEuPathDB; HostDB:ENSMUSG00000029405; -.
DR eggNOG; KOG0116; Eukaryota.
DR GeneTree; ENSGT00390000011365; -.
DR HOGENOM; CLU_022209_0_2_1; -.
DR InParanoid; P97379; -.
DR OMA; PHQIGSE; -.
DR PhylomeDB; P97379; -.
DR TreeFam; TF325464; -.
DR BioGRID-ORCS; 23881; 2 hits in 72 CRISPR screens.
DR ChiTaRS; G3bp2; mouse.
DR PRO; PR:P97379; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P97379; protein.
DR Bgee; ENSMUSG00000029405; Expressed in animal zygote and 268 other tissues.
DR ExpressionAtlas; P97379; baseline and differential.
DR Genevisible; P97379; MM.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0062029; P:positive regulation of stress granule assembly; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:MGI.
DR GO; GO:0034063; P:stress granule assembly; IEA:InterPro.
DR CDD; cd00780; NTF2; 1.
DR CDD; cd12464; RRM_G3BP2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034377; G3BP2.
DR InterPro; IPR034376; G3BP2_RRM.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR039539; Ras_GTPase_bind_prot.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR10693; PTHR10693; 1.
DR PANTHER; PTHR10693:SF10; PTHR10693:SF10; 1.
DR Pfam; PF02136; NTF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Immunity; Innate immunity;
KW Isopeptide bond; Methylation; mRNA transport; Phosphoprotein;
KW Reference proteome; RNA-binding; Transport; Ubl conjugation.
FT CHAIN 1..482
FT /note="Ras GTPase-activating protein-binding protein 2"
FT /id="PRO_0000194801"
FT DOMAIN 11..133
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 331..409
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 140..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..159
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 227
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 392
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 457
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN86"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UN86"
FT MOD_RES 468
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 281
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UN86"
FT VAR_SEQ 243..275
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:9575347, ECO:0000303|Ref.2"
FT /id="VSP_003606"
FT CONFLICT 476..482
FT /note="RFTGQRR -> TLHRTASLKSHCWQFWQWYLTHRVCILVKFFWLWNVTQPF
FT (in Ref. 1; AAC53553)"
FT /evidence="ECO:0000305"
FT MOD_RES P97379-2:225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES P97379-2:227
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
SQ SEQUENCE 482 AA; 54088 MW; FB8BC2086123A5CE CRC64;
MVMEKPSPLL VGREFVRQYY TLLNKAPEYL HRFYGRNSSY VHGGVDASGK PQEAVYGQND
IHHKVLSLNF SECHTKIRHV DAHATLSDGV VVQVMGLLSN SGQPERKFMQ TFVLAPEGSV
PNKFYVHNDM FRYEDEVFGD SEPELDEESE DEVEEEQEDR QPSPEPVQEN ANSAYYDAHP
VTNGIEEPLE ESSHEPEPEP ESETKTEELK PQVEEKHLEE LEEKSATPPP AEPASLPQEP
PKAFSWASVT SKNLPPSGTV SSSGIPPHVK APVSQPRVDA KPEVQSQPPR VREQRPRERP
GFPPRGPRPG RGDMEQNDSD NRRIIRYPDS HQLFVGNLPH DIDENELKEF FMSFGNVVEL
RINTKGVGGK LPNFGFVVFD DSEPVQRILI AKPIMFRGEV RLNVEEKKTR AARERETRGG
GDDRRDIRRN DRGPGGPRGI VGGGMMRDRD GRGPPPRGGM TQKLGSGRGT GQMEGRFTGQ
RR
