GTPB2_MOUSE
ID GTPB2_MOUSE Reviewed; 602 AA.
AC Q3UJK4; Q9EST7; Q9JIX7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=GTP-binding protein 2;
DE AltName: Full=GTP-binding-like protein 2;
GN Name=Gtpbp2 {ECO:0000312|MGI:MGI:1860138};
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] {ECO:0000305, ECO:0000312|EMBL:AAF78885.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC TISSUE=Brain {ECO:0000312|EMBL:AAF78885.1};
RX PubMed=10833435; DOI=10.1006/bbrc.2000.2763;
RA Kudo H., Senju S., Mitsuya H., Nishimura Y.;
RT "Mouse and human GTPBP2, newly identified members of the GP-1 family of
RT GTPase.";
RL Biochem. Biophys. Res. Commun. 272:456-465(2000).
RN [2] {ECO:0000312|EMBL:BAE27151.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=DBA/2J {ECO:0000312|EMBL:BAE27151.1};
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 [3] {ECO:0000312|EMBL:AAH49089.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH49089.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH49089.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAB12430.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 86-602, AND TISSUE SPECIFICITY.
RX PubMed=11054535; DOI=10.1016/s0378-1119(00)00346-2;
RA Watanabe M., Yoshida K., Hida M., Kato H., Uchida K., Yamaguchi R.,
RA Tateyama S., Sugano S.;
RT "Cloning, expression analysis, and chromosomal mapping of GTPBP2, a novel
RT member of the G protein family.";
RL Gene 256:51-58(2000).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
CC -!- INTERACTION:
CC Q3UJK4; Q80X73: Pelo; NbExp=3; IntAct=EBI-16114877, EBI-16114899;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in thymus, spleen, and
CC testis. Expressed at lower levels in brain, heart, lung, kidney, and
CC skeletal muscle. In testis, specifically expressed in spermatocytes and
CC round spermatids. {ECO:0000269|PubMed:11054535}.
CC -!- INDUCTION: Up-regulated in thioglycolate-elicited mouse peritoneal
CC macrophages. {ECO:0000269|PubMed:10833435}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. GTPBP1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF78885.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH49089.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH51958.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB12430.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF168991; AAF78885.1; ALT_INIT; mRNA.
DR EMBL; AK146415; BAE27151.1; -; mRNA.
DR EMBL; BC049089; AAH49089.1; ALT_INIT; mRNA.
DR EMBL; BC051958; AAH51958.1; ALT_INIT; mRNA.
DR EMBL; AB024573; BAB12430.1; ALT_INIT; mRNA.
DR CCDS; CCDS50122.1; -.
DR PIR; JC7285; JC7285.
DR RefSeq; NP_001139451.1; NM_001145979.1.
DR RefSeq; NP_062527.2; NM_019581.3.
DR AlphaFoldDB; Q3UJK4; -.
DR SMR; Q3UJK4; -.
DR DIP; DIP-61685N; -.
DR IntAct; Q3UJK4; 1.
DR STRING; 10090.ENSMUSP00000024748; -.
DR iPTMnet; Q3UJK4; -.
DR PhosphoSitePlus; Q3UJK4; -.
DR EPD; Q3UJK4; -.
DR MaxQB; Q3UJK4; -.
DR PaxDb; Q3UJK4; -.
DR PRIDE; Q3UJK4; -.
DR ProteomicsDB; 271346; -.
DR Antibodypedia; 30525; 187 antibodies from 27 providers.
DR Ensembl; ENSMUST00000024748; ENSMUSP00000024748; ENSMUSG00000023952.
DR GeneID; 56055; -.
DR KEGG; mmu:56055; -.
DR UCSC; uc008crw.2; mouse.
DR CTD; 54676; -.
DR MGI; MGI:1860138; Gtpbp2.
DR VEuPathDB; HostDB:ENSMUSG00000023952; -.
DR eggNOG; KOG1143; Eukaryota.
DR GeneTree; ENSGT00940000155636; -.
DR HOGENOM; CLU_012821_1_1_1; -.
DR InParanoid; Q3UJK4; -.
DR OMA; ENMPMKI; -.
DR OrthoDB; 682656at2759; -.
DR PhylomeDB; Q3UJK4; -.
DR TreeFam; TF350446; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 56055; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q3UJK4; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3UJK4; protein.
DR Bgee; ENSMUSG00000023952; Expressed in retinal neural layer and 263 other tissues.
DR ExpressionAtlas; Q3UJK4; baseline and differential.
DR Genevisible; Q3UJK4; MM.
DR GO; GO:0005525; F:GTP binding; ISS:MGI.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IMP:MGI.
DR GO; GO:0072344; P:rescue of stalled ribosome; IMP:MGI.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd04165; GTPBP1_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR035531; GTPBP1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..602
FT /note="GTP-binding protein 2"
FT /id="PRO_0000248501"
FT DOMAIN 170..398
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 18..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179..186
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O08582"
FT BINDING 260..264
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O08582"
FT BINDING 316..319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O08582"
FT CONFLICT 215
FT /note="I -> V (in Ref. 4; BAB12430)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="P -> S (in Ref. 4; BAB12430)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="Missing (in Ref. 4; BAB12430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 65754 MW; 018D8BBB4F05151D CRC64;
MDSRVSELFG GCCRPGGGPA MGGNLKARGA GGSSSCGGPK GKKKNGRNRG GKANNPPYLP
PEAEDGNIEY KLKLVNPSQY RFEHLVTQMK WRLQEGRGEA VYQIGVEDNG LLVGLAEEEM
RASLKTLHRM AEKVGADITV LREREVDYDS DVPRKITEVL VRKVPDNQQF LDLRVAVLGN
VDSGKSTLLG VLTQGELDNG RGRARLNLFR HLHEIQSGRT SSISFEILGF NSKGEVVNYS
DSRTAEEICE SSSKMITFID LAGHHKYLHT TIFGLTSYCP DCALLLVSAN TGIAGTTREH
LGLALALKVP FFIVVSKVDL CAKTTVERTV RQLERVLKQP GCHKVPMLVT SEDDAVTAAQ
QFAQSPNVTP IFTLSSVSGE SLDLLKVFLN ILPPLTNSKE QEELMQQLTE FQVDEIYTVP
EVGTVVGGTL SSGICREGDQ LVVGPTDDGC FLELRVCSIQ RNRSACRVLR AGQAATLALG
DFDRALLRKG MVMVSPEMNP TICSVFEAEI VLLFHATTFR RGFQVTVHVG NVRQTAVVEK
IHAKDKLRTG EKAVVRFRFL KHPEYLKVGA KLLFREGVTK GIGHVTDVQA ITAGEAQATM
GF
