Search by BoMiProt ID - Bomi6156


Primary Information

BoMiProt ID Bomi6156
Protein Name GTP-binding protein 1
Organism Bos taurus
Uniprot IdQ58DC5
Milk FractionWhey
Ref Sequence Id NP_001017938.1
Aminoacid Length 669
Molecular Weight 72585
Fasta Sequence https://www.uniprot.org/uniprot/Q58DC5.fasta
Gene Name GTPBP1
Gene Id 513922
Protein Existence Status reviewed

Secondary Information

Protein Function exosomal degradation of mRNAs in elongation complexes. GTP hydrolysis by GTPBP1 is not followed by rapid peptide bond formation, suggesting that after hydrolysis, GTPBP1 retains aa-tRNA, delaying its accommodation in the A site.
Biochemical Properties GTPBP1 possesses eEF1A-like elongation activity, delivering cognate aminoacyl-transfer RNA (aa-tRNA) to the ribosomal A site in a GTP-dependent manner.
PTMs Phosphorylation on Ser
Additional Comments GTPBP2 lacked elongation activity and did not stimulate exosomal degradation, indicating that GTPBP1 and GTPBP2 have different functions.
Linking IDs Bomi6156
Bibliography Zinoviev A, Goyal A, Jindal S, LaCava J, Komar AA, Rodnina MV, Hellen CUT, Pestova TV. Functions of unconventional mammalian translational GTPases GTPBP1 and GTPBP2. Genes Dev. 2018 Sep 1;32(17-18):1226-1241. doi: 10.1101/gad.314724.118. Epub 2018 Aug 14. PMID: 30108131; PMCID: PMC6120710.
Protein Function exosomal degradation of mRNAs in elongation complexes. GTP hydrolysis by GTPBP1 is not followed by rapid peptide bond formation, suggesting that after hydrolysis, GTPBP1 retains aa-tRNA, delaying its accommodation in the A site.
Biochemical Properties GTPBP1 possesses eEF1A-like elongation activity, delivering cognate aminoacyl-transfer RNA (aa-tRNA) to the ribosomal A site in a GTP-dependent manner.
PTMs Phosphorylation on Ser
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q58DC5|GTPB1_BOVIN GTP-binding protein 1 OS=Bos taurus OX=9913 GN=GTPBP1 PE=2 SV=2 MAAERS*6RS*8PMES*12PVPASMFAPEPS*24S*25PGAARAAAAAARLHGGFDS*44DCS*47EDGEALNGEPELDLTSKLVLVS*69PTSEQYDSLLRQMWERMDEGCGETIYVIGQGSDGTEYGLSEADMEASYATV KSMAEQIEADVILLRERQEAGGRVRDYLVRKRVGDNDFLEVRVAVVGNVDAGKSTLLGVL THGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGNVVNKPDSHGGSLEWTKI CEKSTKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALN VPVFVVVTKIDMCPANILQETLKLLQRLLKSPGCRKIPVLVQSKDDVIVTASNFSSERMC PIFQISNVTGENLDLLKMFLNLLSPRTSYREEEPAEFQIDDTYSVPGVGTVVSGTTLRGL IKLNDTLLLGPDPLGNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMVMV SPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATV HFRFIKTPEYLHIDQRLVFREGRTKAVGTITKLLQTTNNS*580PMNSKPQQIKMQSTKKGPLP KREEGGPSGGPTVGGPPPGDEACSLGATQLAASSSLQPQPKPSSGGRRRGGQRHKVKSQG ACMTPASGC
Predicted Disorder Regions 2 disordered segments; (1-57), (584-669)
DisProt Annotation
TM Helix Prediction No TM helices
Additional Comments GTPBP2 lacked elongation activity and did not stimulate exosomal degradation, indicating that GTPBP1 and GTPBP2 have different functions.
Linking IDs
Bibliography Zinoviev A, Goyal A, Jindal S, LaCava J, Komar AA, Rodnina MV, Hellen CUT, Pestova TV. Functions of unconventional mammalian translational GTPases GTPBP1 and GTPBP2. Genes Dev. 2018 Sep 1;32(17-18):1226-1241. doi: 10.1101/gad.314724.118. Epub 2018 Aug 14. PMID: 30108131; PMCID: PMC6120710.