GTPB1_MOUSE
ID GTPB1_MOUSE Reviewed; 668 AA.
AC O08582; Q3UD96; Q3UGW6; Q545R1; Q80ZY5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=GTP-binding protein 1;
DE Short=G-protein 1;
DE Short=GP-1;
DE Short=GP1;
GN Name=Gtpbp1; Synonyms=Gtpbp;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Dendritic cell, Lung, and Melanocyte;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-668, AND TISSUE SPECIFICITY.
RX PubMed=9070279; DOI=10.1006/bbrc.1997.6103;
RA Senju S., Nishimura Y.;
RT "Identification of human and mouse GP-1, a putative member of a novel G-
RT protein family.";
RL Biochem. Biophys. Res. Commun. 231:360-364(1997).
RN [4]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10938096; DOI=10.1128/mcb.20.17.6195-6200.2000;
RA Senju S., Iyama K., Kudo H., Aizawa S., Nishimura Y.;
RT "Immunocytochemical analyses and targeted gene disruption of GTPBP1.";
RL Mol. Cell. Biol. 20:6195-6200(2000).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-12; SER-44 AND SER-47,
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 [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-8; SER-12; SER-24; SER-25;
RP SER-44 AND SER-47, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 DISRUPTION PHENOTYPE.
RX PubMed=21515746; DOI=10.1096/fj.10-178715;
RA Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J.,
RA Chung S.J., Senju S., Nishimura Y., Kim K.T.;
RT "Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding
RT protein 1 (GTPBP1) with its target mRNAs.";
RL FASEB J. 25:2757-2769(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 246-253 IN COMPLEX WITH MHC.
RX PubMed=11911820; DOI=10.1016/s1074-7613(02)00288-1;
RA Reiser J.B., Gregoire C., Darnault C., Mosser T., Guimezanes A.,
RA Schmitt-Verhulst A.M., Fontecilla-Camps J.C., Mazza G., Malissen B.,
RA Housset D.;
RT "A T cell receptor CDR3beta loop undergoes conformational changes of
RT unprecedented magnitude upon binding to a peptide/MHC class I complex.";
RL Immunity 16:345-354(2002).
CC -!- FUNCTION: Promotes degradation of target mRNA species. Plays a role in
CC the regulation of circadian mRNA stability. Binds GTP and has GTPase
CC activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EXOSC2/RRP4, EXOSC3/RRP40, EXOSC5/RRP46,
CC HNRNPD, HNRNPR and SYNCRIP. Identified in a complex with AANAT mRNA,
CC but does not bind mRNA by itself (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10938096}.
CC -!- TISSUE SPECIFICITY: Detected in some neurons in the brain cortex.
CC Detected in small arteries, dendritic cells and macrophages in the
CC thymus. Detected in lung bronchi, in bronchial epithelial cells and in
CC bronchial smooth muscle cells. Detected in smooth muscle cells in a
CC broad range of organs (at protein level). Expressed in brain, thymus,
CC lung, and kidney. {ECO:0000269|PubMed:10938096,
CC ECO:0000269|PubMed:9070279}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are born at the
CC expected Mendelian ratio, develop normally and are fertile. They
CC exhibit increased stability of some mRNA species.
CC {ECO:0000269|PubMed:10938096, ECO:0000269|PubMed:21515746}.
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=AAB51274.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB23409.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE28091.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE29280.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE29365.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK004612; BAB23409.1; ALT_INIT; mRNA.
DR EMBL; AK147717; BAE28091.1; ALT_FRAME; mRNA.
DR EMBL; AK150068; BAE29280.1; ALT_FRAME; mRNA.
DR EMBL; AK150185; BAE29365.1; ALT_FRAME; mRNA.
DR EMBL; AK170091; BAE41557.1; -; mRNA.
DR EMBL; BC046228; AAH46228.1; -; mRNA.
DR EMBL; U87965; AAB51274.1; ALT_INIT; mRNA.
DR CCDS; CCDS27648.1; -.
DR PIR; JC5292; JC5292.
DR RefSeq; NP_038846.2; NM_013818.2.
DR PDB; 1KJ2; X-ray; 2.71 A; P/Q=246-253.
DR PDB; 1KJ3; X-ray; 2.30 A; P/Q=246-253.
DR PDBsum; 1KJ2; -.
DR PDBsum; 1KJ3; -.
DR AlphaFoldDB; O08582; -.
DR SMR; O08582; -.
DR BioGRID; 200118; 4.
DR IntAct; O08582; 1.
DR MINT; O08582; -.
DR STRING; 10090.ENSMUSP00000043575; -.
DR iPTMnet; O08582; -.
DR PhosphoSitePlus; O08582; -.
DR SwissPalm; O08582; -.
DR EPD; O08582; -.
DR jPOST; O08582; -.
DR MaxQB; O08582; -.
DR PaxDb; O08582; -.
DR PeptideAtlas; O08582; -.
DR PRIDE; O08582; -.
DR ProteomicsDB; 271345; -.
DR Antibodypedia; 26419; 204 antibodies from 27 providers.
DR Ensembl; ENSMUST00000046463; ENSMUSP00000043575; ENSMUSG00000042535.
DR GeneID; 14904; -.
DR KEGG; mmu:14904; -.
DR UCSC; uc007wuf.1; mouse.
DR CTD; 9567; -.
DR MGI; MGI:109443; Gtpbp1.
DR VEuPathDB; HostDB:ENSMUSG00000042535; -.
DR eggNOG; KOG0463; Eukaryota.
DR GeneTree; ENSGT00940000156054; -.
DR HOGENOM; CLU_012821_2_0_1; -.
DR InParanoid; O08582; -.
DR OMA; FRFIQRP; -.
DR OrthoDB; 682656at2759; -.
DR PhylomeDB; O08582; -.
DR TreeFam; TF350446; -.
DR BioGRID-ORCS; 14904; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Gtpbp1; mouse.
DR EvolutionaryTrace; O08582; -.
DR PRO; PR:O08582; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O08582; protein.
DR Bgee; ENSMUSG00000042535; Expressed in retinal neural layer and 248 other tissues.
DR ExpressionAtlas; O08582; baseline and differential.
DR Genevisible; O08582; MM.
DR GO; GO:0000177; C:cytoplasmic exosome (RNase complex); ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
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; IPR039263; GTPB1.
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 PANTHER; PTHR43721:SF9; PTHR43721:SF9; 1.
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 3D-structure; Cytoplasm; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..668
FT /note="GTP-binding protein 1"
FT /id="PRO_0000122470"
FT DOMAIN 158..389
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..174
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 206..210
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 252..255
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 308..311
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 366..368
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 573..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 167..174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 252..256
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 308..311
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00178"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00178"
FT CONFLICT 121
FT /note="K -> E (in Ref. 1; BAE28091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 668 AA; 72301 MW; E77C2148D6B237F8 CRC64;
MAAERSRSPV DSPVPASMFA PEPSSPGAAR AAAAAARLHG GFDSDCSEDG EALNGEPELD
LTSKLVLVSP TSEQYDSLLR QMWERMDEGC GETIYVIGQG SDGTEYGLSE ADMEASYATV
KSMAEQIEAD VILLRERQEA GGRVRDYLVR KRVGDNDFLE VRVAVVGNVD AGKSTLLGVL
THGELDNGRG FARQKLFRHK HEIESGRTSS VGNDILGFDS EGNVVNKPDS HGGSLEWTKI
CEKSSKVITF IDLAGHEKYL KTTVFGMTGH LPDFCMLMVG SNAGIVGMTK EHLGLALALN
VPVFVVVTKI DMCPANILQE TLKLLQRLLK SPGCRKIPVL VQSKDDVIVT ASNFSSERMC
PIFQISNVTG ENLDLLKMFL NLLSPRTSYR EEEPAEFQID DTYSVPGVGT VVSGTTLRGL
IKLNDTLLLG PDPLGNFLSI AVKSIHRKRM PVKEVRGGQT ASFALKKIKR SSIRKGMVMV
SPRLNPQASW EFEAEILVLH HPTTISPRYQ AMVHCGSIRQ TATILSMDKD CLRTGDKATV
HFRFIKTPEY LHIDQRLVFR EGRTKAVGTI TKLLQTTNNS PMNSKPQQIK MQSTKKGPLS
KREEGGPCGV PAAGGPPTGD EASSLGTAQA ASTSGLQPQP KPSSGGRRRG GQRHKVKSGA
CVTPASGC
