Primary Information |
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| BoMiProt ID | Bomi6156 |
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| Protein Name | GTP-binding protein 1 |
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| Organism | Bos taurus |
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| Uniprot ID | Q58DC5 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001017938.1 |
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| Aminoacid Length | 669 |
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| Molecular Weight | 72585 |
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| FASTA Sequence |
Download |
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| Gene Name | GTPBP1 |
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| Gene ID | 513922 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| 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. |
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| 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. |
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| PTMs | Phosphorylation on Ser |
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| Additional Comments | GTPBP2 lacked elongation activity and did not stimulate exosomal degradation, indicating that GTPBP1 and GTPBP2 have different functions. |
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| Linking IDs | Bomi6156 |
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| 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. |
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| 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. |
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| PTMs | Phosphorylation on Ser |
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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 |
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| Predicted Disorder Regions | 2 disordered segments; (1-57), (584-669) |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Additional Comments | GTPBP2 lacked elongation activity and did not stimulate exosomal degradation, indicating that GTPBP1 and GTPBP2 have different functions. |
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| Linking IDs | |
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| 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. |
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