G3BP2_HUMAN
ID G3BP2_HUMAN Reviewed; 482 AA.
AC Q9UN86; A8K6X1; O60606; O75149; Q9UPA1;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 206.
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; Synonyms=KIAA0660;
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] (ISOFORMS A AND B).
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC TISSUE=Brain;
RA Guitard E.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC TISSUE=Brain;
RA Kennedy D., Ru K., Mattick J.S.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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] (ISOFORM B).
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 PROTEIN SEQUENCE OF 2-13; 18-32; 124-132; 206-224; 243-252; 278-290;
RP 371-397 AND 439-447, CLEAVAGE OF INITIATOR METHIONINE, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma, Lung carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Vousden K.H.,
RA Lukashchuk N., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP INTERACTION WITH NFKBIA.
RX PubMed=10969074; DOI=10.1074/jbc.m004751200;
RA Prigent M., Barlat I., Langen H., Dargemont C.;
RT "IkappaBalpha and IkappaBalpha /NF-kappa B complexes are retained in the
RT cytoplasm through interaction with a novel partner, RasGAP SH3-binding
RT protein 2.";
RL J. Biol. Chem. 275:36441-36449(2000).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP INTERACTION WITH SINBIS VIRUS NON-STRUCTURAL PROTEIN 3 (MICROBIAL
RP INFECTION).
RX PubMed=18684830; DOI=10.1128/jvi.01011-08;
RA Gorchakov R., Garmashova N., Frolova E., Frolov I.;
RT "Different types of nsP3-containing protein complexes in Sindbis virus-
RT infected cells.";
RL J. Virol. 82:10088-10101(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-149,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227 AND SER-235 (ISOFORM B),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-149 AND THR-227, AND
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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227 AND SER-466, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [20]
RP FUNCTION, INTERACTION WITH USP10; PABPC1 AND G3BP1, SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=23279204; DOI=10.1111/gtc.12023;
RA Matsuki H., Takahashi M., Higuchi M., Makokha G.N., Oie M., Fujii M.;
RT "Both G3BP1 and G3BP2 contribute to stress granule formation.";
RL Genes Cells 18:135-146(2013).
RN [21]
RP 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).
RN [22]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-457 AND ARG-468, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-281, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-281, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [26]
RP SUBCELLULAR LOCATION, AND CLEAVAGE BY FOOT-AND-MOUTH DISEASE VIRUS LEADER
RP PROTEASE (MICROBIAL INFECTION).
RX PubMed=30404792; DOI=10.1128/jvi.00922-18;
RA Visser L.J., Medina G.N., Rabouw H.H., de Groot R.J., Langereis M.A.,
RA de Los Santos T., van Kuppeveld F.J.M.;
RT "Foot-and-Mouth Disease Virus Leader Protease Cleaves G3BP1 and G3BP2 and
RT Inhibits Stress Granule Formation.";
RL J. Virol. 93:0-0(2019).
RN [27]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-434.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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:0000269|PubMed:23279204}.
CC -!- SUBUNIT: Forms homooligomers (PubMed:23279204). Forms heterodimers with
CC G3BP1 (PubMed:23279204). Interacts with NFKBIA (via N-terminus)
CC (PubMed:10969074). Interacts with USP10 (PubMed:23279204). Interacts
CC with PABPC1 (PubMed:23279204). {ECO:0000269|PubMed:10969074,
CC ECO:0000269|PubMed:23279204}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Sindbis virus non-
CC structural protein 3 (via C-terminus); this interaction inhibits the
CC formation of host stress granules on viral mRNAs and the nsp3-G3BP2
CC complexes bind viral RNAs and probably orchestrate the assembly of
CC viral replication complexes. {ECO:0000269|PubMed:18684830}.
CC -!- INTERACTION:
CC Q9UN86; Q15672: TWIST1; NbExp=2; IntAct=EBI-1044298, EBI-1797287;
CC Q9UN86; Q14694: USP10; NbExp=9; IntAct=EBI-1044298, EBI-2510389;
CC Q9UN86; P0DTC9: N; Xeno; NbExp=32; IntAct=EBI-1044298, EBI-25475856;
CC Q9UN86; P26687: Twist1; Xeno; NbExp=2; IntAct=EBI-1044298, EBI-6123119;
CC Q9UN86-2; Q7Z417: NUFIP2; NbExp=4; IntAct=EBI-11035716, EBI-1210753;
CC Q9UN86-2; Q14694: USP10; NbExp=3; IntAct=EBI-11035716, EBI-2510389;
CC Q9UN86-2; Q5T7W0: ZNF618; NbExp=3; IntAct=EBI-11035716, EBI-6255994;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23279204,
CC ECO:0000269|PubMed:30404792}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:23279204, ECO:0000269|PubMed:30404792}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9UN86-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9UN86-2; Sequence=VSP_003605;
CC -!- PTM: Arg-457 and Arg-468 are dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- PTM: (Microbial infection) Cleaved by foot-and-mouth disease virus
CC leader protease; this cleavage suppresses the formation of cytoplasmic
CC stress granules. {ECO:0000269|PubMed:30404792}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31635.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF145284; AAD51932.1; -; mRNA.
DR EMBL; AB014560; BAA31635.2; ALT_INIT; mRNA.
DR EMBL; AF051311; AAC15705.1; -; mRNA.
DR EMBL; AF053535; AAC95292.1; -; mRNA.
DR EMBL; AK291786; BAF84475.1; -; mRNA.
DR EMBL; CH471057; EAX05742.1; -; Genomic_DNA.
DR EMBL; BC011731; AAH11731.1; -; mRNA.
DR CCDS; CCDS3571.1; -. [Q9UN86-1]
DR CCDS; CCDS3572.1; -. [Q9UN86-2]
DR RefSeq; NP_036429.2; NM_012297.4. [Q9UN86-1]
DR RefSeq; NP_987100.1; NM_203504.2. [Q9UN86-2]
DR RefSeq; NP_987101.1; NM_203505.2. [Q9UN86-1]
DR RefSeq; XP_005263439.1; XM_005263382.2. [Q9UN86-1]
DR RefSeq; XP_005263440.1; XM_005263383.3. [Q9UN86-1]
DR RefSeq; XP_011530743.1; XM_011532441.2. [Q9UN86-1]
DR RefSeq; XP_016864365.1; XM_017008876.1. [Q9UN86-1]
DR RefSeq; XP_016864366.1; XM_017008877.1.
DR RefSeq; XP_016864367.1; XM_017008878.1. [Q9UN86-2]
DR RefSeq; XP_016864368.1; XM_017008879.1. [Q9UN86-2]
DR PDB; 5DRV; X-ray; 2.75 A; A=1-139.
DR PDBsum; 5DRV; -.
DR AlphaFoldDB; Q9UN86; -.
DR SMR; Q9UN86; -.
DR BioGRID; 115237; 254.
DR CORUM; Q9UN86; -.
DR DIP; DIP-50299N; -.
DR ELM; Q9UN86; -.
DR IntAct; Q9UN86; 89.
DR MINT; Q9UN86; -.
DR STRING; 9606.ENSP00000352738; -.
DR GlyGen; Q9UN86; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9UN86; -.
DR MetOSite; Q9UN86; -.
DR PhosphoSitePlus; Q9UN86; -.
DR SwissPalm; Q9UN86; -.
DR BioMuta; G3BP2; -.
DR DMDM; 116242482; -.
DR EPD; Q9UN86; -.
DR jPOST; Q9UN86; -.
DR MassIVE; Q9UN86; -.
DR MaxQB; Q9UN86; -.
DR PaxDb; Q9UN86; -.
DR PeptideAtlas; Q9UN86; -.
DR PRIDE; Q9UN86; -.
DR ProteomicsDB; 85270; -. [Q9UN86-1]
DR ProteomicsDB; 85271; -. [Q9UN86-2]
DR Antibodypedia; 13391; 162 antibodies from 26 providers.
DR DNASU; 9908; -.
DR Ensembl; ENST00000357854.7; ENSP00000350518.3; ENSG00000138757.15. [Q9UN86-2]
DR Ensembl; ENST00000359707.9; ENSP00000352738.4; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000395719.7; ENSP00000379069.3; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000676470.1; ENSP00000503688.1; ENSG00000138757.15. [Q9UN86-2]
DR Ensembl; ENST00000676584.1; ENSP00000504496.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000676666.1; ENSP00000503496.1; ENSG00000138757.15. [Q9UN86-2]
DR Ensembl; ENST00000676839.1; ENSP00000503442.1; ENSG00000138757.15. [Q9UN86-2]
DR Ensembl; ENST00000676974.1; ENSP00000503669.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000677125.1; ENSP00000503209.1; ENSG00000138757.15. [Q9UN86-2]
DR Ensembl; ENST00000677162.1; ENSP00000504101.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000677171.1; ENSP00000503911.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000677201.1; ENSP00000504523.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000677265.1; ENSP00000504591.1; ENSG00000138757.15. [Q9UN86-2]
DR Ensembl; ENST00000677333.1; ENSP00000503355.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000677566.1; ENSP00000504361.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000677583.1; ENSP00000504564.1; ENSG00000138757.15. [Q9UN86-2]
DR Ensembl; ENST00000677606.1; ENSP00000503228.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000677620.1; ENSP00000504316.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000677876.1; ENSP00000504206.1; ENSG00000138757.15. [Q9UN86-2]
DR Ensembl; ENST00000678062.1; ENSP00000503239.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000678100.1; ENSP00000504698.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000678122.1; ENSP00000504363.1; ENSG00000138757.15. [Q9UN86-2]
DR Ensembl; ENST00000678123.1; ENSP00000503504.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000678265.1; ENSP00000504159.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000678273.1; ENSP00000502996.1; ENSG00000138757.15. [Q9UN86-2]
DR Ensembl; ENST00000678552.1; ENSP00000504588.1; ENSG00000138757.15. [Q9UN86-2]
DR Ensembl; ENST00000678578.1; ENSP00000503943.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000678798.1; ENSP00000504585.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000678971.1; ENSP00000504371.1; ENSG00000138757.15. [Q9UN86-1]
DR Ensembl; ENST00000679281.1; ENSP00000504025.1; ENSG00000138757.15. [Q9UN86-2]
DR GeneID; 9908; -.
DR KEGG; hsa:9908; -.
DR MANE-Select; ENST00000359707.9; ENSP00000352738.4; NM_203505.3; NP_987101.1.
DR UCSC; uc003hir.4; human. [Q9UN86-1]
DR CTD; 9908; -.
DR DisGeNET; 9908; -.
DR GeneCards; G3BP2; -.
DR HGNC; HGNC:30291; G3BP2.
DR HPA; ENSG00000138757; Low tissue specificity.
DR neXtProt; NX_Q9UN86; -.
DR OpenTargets; ENSG00000138757; -.
DR PharmGKB; PA162389134; -.
DR VEuPathDB; HostDB:ENSG00000138757; -.
DR eggNOG; KOG0116; Eukaryota.
DR GeneTree; ENSGT00390000011365; -.
DR HOGENOM; CLU_022209_0_2_1; -.
DR InParanoid; Q9UN86; -.
DR OMA; XSEDEVE; -.
DR PhylomeDB; Q9UN86; -.
DR TreeFam; TF325464; -.
DR PathwayCommons; Q9UN86; -.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; Q9UN86; -.
DR SIGNOR; Q9UN86; -.
DR BioGRID-ORCS; 9908; 28 hits in 1097 CRISPR screens.
DR ChiTaRS; G3BP2; human.
DR GeneWiki; G3BP2; -.
DR GenomeRNAi; 9908; -.
DR Pharos; Q9UN86; Tbio.
DR PRO; PR:Q9UN86; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9UN86; protein.
DR Bgee; ENSG00000138757; Expressed in cortical plate and 204 other tissues.
DR ExpressionAtlas; Q9UN86; baseline and differential.
DR Genevisible; Q9UN86; HS.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IMP:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; NAS:UniProtKB.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; NAS:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IMP:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; NAS:UniProtKB.
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 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Immunity; Innate immunity; Isopeptide bond;
KW Methylation; mRNA transport; Phosphoprotein; Reference proteome;
KW RNA-binding; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8"
FT CHAIN 2..482
FT /note="Ras GTPase-activating protein-binding protein 2"
FT /id="PRO_0000194800"
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..172
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:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97379"
FT MOD_RES 227
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 392
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97379"
FT MOD_RES 457
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
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:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 243..275
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT /id="VSP_003605"
FT VARIANT 434
FT /note="P -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036128"
FT CONFLICT 267
FT /note="P -> S (in Ref. 1; AAD51932)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="E -> V (in Ref. 3; AAC15705)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="M -> I (in Ref. 3; AAC15705)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:5DRV"
FT HELIX 8..25
FT /evidence="ECO:0007829|PDB:5DRV"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:5DRV"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:5DRV"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:5DRV"
FT STRAND 74..84
FT /evidence="ECO:0007829|PDB:5DRV"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5DRV"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:5DRV"
FT STRAND 106..116
FT /evidence="ECO:0007829|PDB:5DRV"
FT STRAND 118..133
FT /evidence="ECO:0007829|PDB:5DRV"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:5DRV"
FT MOD_RES Q9UN86-2:227
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES Q9UN86-2:235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
SQ SEQUENCE 482 AA; 54121 MW; 74B8EA43C0560229 CRC64;
MVMEKPSPLL VGREFVRQYY TLLNKAPEYL HRFYGRNSSY VHGGVDASGK PQEAVYGQND
IHHKVLSLNF SECHTKIRHV DAHATLSDGV VVQVMGLLSN SGQPERKFMQ TFVLAPEGSV
PNKFYVHNDM FRYEDEVFGD SEPELDEESE DEVEEEQEER QPSPEPVQEN ANSGYYEAHP
VTNGIEEPLE ESSHEPEPEP ESETKTEELK PQVEEKNLEE LEEKSTTPPP AEPVSLPQEP
PKAFSWASVT SKNLPPSGTV SSSGIPPHVK APVSQPRVEA KPEVQSQPPR VREQRPRERP
GFPPRGPRPG RGDMEQNDSD NRRIIRYPDS HQLFVGNLPH DIDENELKEF FMSFGNVVEL
RINTKGVGGK LPNFGFVVFD DSEPVQRILI AKPIMFRGEV RLNVEEKKTR AARERETRGG
GDDRRDIRRN DRGPGGPRGI VGGGMMRDRD GRGPPPRGGM AQKLGSGRGT GQMEGRFTGQ
RR
