Full text data of G3BP2
G3BP2
(KIAA0660)
[Confidence: low (only semi-automatic identification from reviews)]
Ras GTPase-activating protein-binding protein 2; G3BP-2 (GAP SH3 domain-binding protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ras GTPase-activating protein-binding protein 2; G3BP-2 (GAP SH3 domain-binding protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UN86
ID G3BP2_HUMAN Reviewed; 482 AA.
AC Q9UN86; A8K6X1; O60606; O75149; Q9UPA1;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 134.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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,
RT members of a novel SH3 domain-binding and RNA-binding protein family
RT implicated in 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.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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, LACK OF
RP N-TERMINAL ACETYLATION, AND 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 IKAPPABALPHA.
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
RT the cytoplasm through interaction with a novel partner, RasGAP SH3-
RT binding 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-149, AND
RP MASS SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-149,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227 AND SER-235 (ISOFORM
RP B), AND MASS SPECTROMETRY.
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 [13]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-149 AND
RP THR-227, AND MASS SPECTROMETRY.
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 [15]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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.,
RA Buerckstuemmer T., 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-149, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Probable scaffold protein that may be involved in mRNA
CC transport (Potential).
CC -!- SUBUNIT: Binds to the N-terminal domain of I-kappa-B-alpha.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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 Note=Contains a phosphothreonine at position 227. Contains a
CC phosphoserine at position 235;
CC -!- PTM: Arg-457 and Arg-468 are dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- SIMILARITY: Contains 1 NTF2 domain.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31635.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_036429.2; NM_012297.4.
DR RefSeq; NP_987100.1; NM_203504.2.
DR RefSeq; NP_987101.1; NM_203505.2.
DR RefSeq; XP_005263439.1; XM_005263382.1.
DR RefSeq; XP_005263440.1; XM_005263383.1.
DR RefSeq; XP_005263441.1; XM_005263384.1.
DR RefSeq; XP_005263442.1; XM_005263385.1.
DR RefSeq; XP_005263443.1; XM_005263386.1.
DR UniGene; Hs.303676; -.
DR ProteinModelPortal; Q9UN86; -.
DR SMR; Q9UN86; 1-138, 332-392.
DR IntAct; Q9UN86; 28.
DR MINT; MINT-3082700; -.
DR STRING; 9606.ENSP00000352738; -.
DR PhosphoSite; Q9UN86; -.
DR DMDM; 116242482; -.
DR PaxDb; Q9UN86; -.
DR PRIDE; Q9UN86; -.
DR Ensembl; ENST00000357854; ENSP00000350518; ENSG00000138757.
DR Ensembl; ENST00000359707; ENSP00000352738; ENSG00000138757.
DR Ensembl; ENST00000395719; ENSP00000379069; ENSG00000138757.
DR GeneID; 9908; -.
DR KEGG; hsa:9908; -.
DR UCSC; uc003hir.3; human.
DR CTD; 9908; -.
DR GeneCards; GC04M076567; -.
DR HGNC; HGNC:30291; G3BP2.
DR HPA; HPA018304; -.
DR HPA; HPA018425; -.
DR neXtProt; NX_Q9UN86; -.
DR PharmGKB; PA162389134; -.
DR eggNOG; NOG324333; -.
DR HOGENOM; HOG000220838; -.
DR HOVERGEN; HBG007211; -.
DR InParanoid; Q9UN86; -.
DR OMA; SHPVTNG; -.
DR OrthoDB; EOG77Q4ZC; -.
DR PhylomeDB; Q9UN86; -.
DR GeneWiki; G3BP2; -.
DR GenomeRNAi; 9908; -.
DR NextBio; 37365; -.
DR PRO; PR:Q9UN86; -.
DR ArrayExpress; Q9UN86; -.
DR Bgee; Q9UN86; -.
DR CleanEx; HS_G3BP2; -.
DR Genevestigator; Q9UN86; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; NAS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0007265; P:Ras protein signal transduction; NAS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR002075; NTF2.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF02136; NTF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; mRNA transport; Phosphoprotein;
KW Polymorphism; Reference proteome; RNA-binding; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 482 Ras GTPase-activating protein-binding
FT protein 2.
FT /FTId=PRO_0000194800.
FT DOMAIN 11 133 NTF2.
FT DOMAIN 331 409 RRM.
FT COMPBIAS 134 223 Glu-rich.
FT COMPBIAS 419 479 Gly-rich.
FT SITE 2 2 Not acetylated.
FT MOD_RES 141 141 Phosphoserine.
FT MOD_RES 149 149 Phosphoserine.
FT MOD_RES 227 227 Phosphothreonine.
FT VAR_SEQ 243 275 Missing (in isoform B).
FT /FTId=VSP_003605.
FT VARIANT 434 434 P -> L (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036128.
FT CONFLICT 267 267 P -> S (in Ref. 1; AAD51932).
FT CONFLICT 359 359 E -> V (in Ref. 3; AAC15705).
FT CONFLICT 460 460 M -> I (in Ref. 3; AAC15705).
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
//
ID G3BP2_HUMAN Reviewed; 482 AA.
AC Q9UN86; A8K6X1; O60606; O75149; Q9UPA1;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 134.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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,
RT members of a novel SH3 domain-binding and RNA-binding protein family
RT implicated in 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.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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, LACK OF
RP N-TERMINAL ACETYLATION, AND 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 IKAPPABALPHA.
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
RT the cytoplasm through interaction with a novel partner, RasGAP SH3-
RT binding 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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-149, AND
RP MASS SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-149,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227 AND SER-235 (ISOFORM
RP B), AND MASS SPECTROMETRY.
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 [13]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-149 AND
RP THR-227, AND MASS SPECTROMETRY.
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 [15]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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.,
RA Buerckstuemmer T., 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-149, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
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.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Probable scaffold protein that may be involved in mRNA
CC transport (Potential).
CC -!- SUBUNIT: Binds to the N-terminal domain of I-kappa-B-alpha.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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 Note=Contains a phosphothreonine at position 227. Contains a
CC phosphoserine at position 235;
CC -!- PTM: Arg-457 and Arg-468 are dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- SIMILARITY: Contains 1 NTF2 domain.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31635.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_036429.2; NM_012297.4.
DR RefSeq; NP_987100.1; NM_203504.2.
DR RefSeq; NP_987101.1; NM_203505.2.
DR RefSeq; XP_005263439.1; XM_005263382.1.
DR RefSeq; XP_005263440.1; XM_005263383.1.
DR RefSeq; XP_005263441.1; XM_005263384.1.
DR RefSeq; XP_005263442.1; XM_005263385.1.
DR RefSeq; XP_005263443.1; XM_005263386.1.
DR UniGene; Hs.303676; -.
DR ProteinModelPortal; Q9UN86; -.
DR SMR; Q9UN86; 1-138, 332-392.
DR IntAct; Q9UN86; 28.
DR MINT; MINT-3082700; -.
DR STRING; 9606.ENSP00000352738; -.
DR PhosphoSite; Q9UN86; -.
DR DMDM; 116242482; -.
DR PaxDb; Q9UN86; -.
DR PRIDE; Q9UN86; -.
DR Ensembl; ENST00000357854; ENSP00000350518; ENSG00000138757.
DR Ensembl; ENST00000359707; ENSP00000352738; ENSG00000138757.
DR Ensembl; ENST00000395719; ENSP00000379069; ENSG00000138757.
DR GeneID; 9908; -.
DR KEGG; hsa:9908; -.
DR UCSC; uc003hir.3; human.
DR CTD; 9908; -.
DR GeneCards; GC04M076567; -.
DR HGNC; HGNC:30291; G3BP2.
DR HPA; HPA018304; -.
DR HPA; HPA018425; -.
DR neXtProt; NX_Q9UN86; -.
DR PharmGKB; PA162389134; -.
DR eggNOG; NOG324333; -.
DR HOGENOM; HOG000220838; -.
DR HOVERGEN; HBG007211; -.
DR InParanoid; Q9UN86; -.
DR OMA; SHPVTNG; -.
DR OrthoDB; EOG77Q4ZC; -.
DR PhylomeDB; Q9UN86; -.
DR GeneWiki; G3BP2; -.
DR GenomeRNAi; 9908; -.
DR NextBio; 37365; -.
DR PRO; PR:Q9UN86; -.
DR ArrayExpress; Q9UN86; -.
DR Bgee; Q9UN86; -.
DR CleanEx; HS_G3BP2; -.
DR Genevestigator; Q9UN86; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; NAS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0007265; P:Ras protein signal transduction; NAS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR002075; NTF2.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF02136; NTF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; mRNA transport; Phosphoprotein;
KW Polymorphism; Reference proteome; RNA-binding; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 482 Ras GTPase-activating protein-binding
FT protein 2.
FT /FTId=PRO_0000194800.
FT DOMAIN 11 133 NTF2.
FT DOMAIN 331 409 RRM.
FT COMPBIAS 134 223 Glu-rich.
FT COMPBIAS 419 479 Gly-rich.
FT SITE 2 2 Not acetylated.
FT MOD_RES 141 141 Phosphoserine.
FT MOD_RES 149 149 Phosphoserine.
FT MOD_RES 227 227 Phosphothreonine.
FT VAR_SEQ 243 275 Missing (in isoform B).
FT /FTId=VSP_003605.
FT VARIANT 434 434 P -> L (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036128.
FT CONFLICT 267 267 P -> S (in Ref. 1; AAD51932).
FT CONFLICT 359 359 E -> V (in Ref. 3; AAC15705).
FT CONFLICT 460 460 M -> I (in Ref. 3; AAC15705).
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
//