Overview
| Uniprot ID | O00178 |
|---|
| Protein Name | GTP-binding protein 1 |
|---|
| Gene Name | GTPBP1 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 590 |
NSKPQQIKMQSTKKG |
| 657 |
GGQRHKVKSQGACVT |
Function
GTPase that plays a role in the elongation phase of protein synthesis by forming ternary complexes with GTP and aminoacyl-transfer RNAs (aa-tRNAs), and delivering aa-tRNAs to the ribosomal A site in a GTP-dependent manner (PubMed:30108131). Is also able to deliver deacylated tRNA to the A site (PubMed:30108131). Additionally, it is involved in RNA quality control; after GTP hydrolysis, which is not immediately followed by rapid peptide bond formation, GTPBP1 likely retains aa-tRNA in the A site and promotes exosomal degradation of faulty mRNAs engaged in 80S elongation complexes (PubMed:30108131). Plays a role in the regulation of circadian mRNA stability (By similarity)
Protein Sequence
10
MATERSRSAM
20
DSPVPASMFA
30
PEPSSPGAAR
40
AAAAAARLHG
50
GFDSDCSEDG
60
EALNGEPELD
70
LTSKLVLVSP
80
TSEQYDSLLR
90
QMWERMDEGC
100
GETIYVIGQG
110
SDGTEYGLSE
120
ADMEASYATV
130
KSMAEQIEAD
140
VILLRERQEA
150
GGRVRDYLVR
160
KRVGDNDFLE
170
VRVAVVGNVD
180
AGKSTLLGVL
190
THGELDNGRG
200
FARQKLFRHK
210
HEIESGRTSS
220
VGNDILGFDS
230
EGNVVNKPDS
240
HGGSLEWTKI
250
CEKSTKVITF
260
IDLAGHEKYL
270
KTTVFGMTGH
280
LPDFCMLMVG
290
SNAGIVGMTK
300
EHLGLALALN
310
VPVFVVVTKI
320
DMCPANILQE
330
TLKLLQRLLK
340
SPGCRKIPVL
350
VQSKDDVIVT
360
ASNFSSERMC
370
PIFQISNVTG
380
ENLDLLKMFL
390
NLLSPRTSYR
400
EEEPAEFQID
410
DTYSVPGVGT
420
VVSGTTLRGL
430
IKLNDTLLLG
440
PDPLGNFLSI
450
AVKSIHRKRM
460
PVKEVRGGQT
470
ASFALKKIKR
480
SSIRKGMVMV
490
SPRLNPQASW
500
EFEAEILVLH
510
HPTTISPRYQ
520
AMVHCGSIRQ
530
TATILSMDKD
540
CLRTGDKATV
550
HFRFIKTPEY
560
LHIDQRLVFR
570
EGRTKAVGTI
580
TKLLQTTNNS
590
PMNSKPQQIK
600
MQSTKKGPLT
610
KRDEGGPSGG
620
PAVGAPPPGD
630
EASSVGAGQP
640
AASSNLQPQP
650
KPSSGGRRRG
660
GQRHKVKSQG
ACVTPASGC
Gene Ontology
| Classification |
GO ID |
Description |
| Biological Process |
GO:0046039 |
GTP metabolic process |
| Cellular Component |
GO:0000177 |
cytoplasmic exosome (RNase complex) |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0016020 |
membrane |
| Molecular Function |
GO:1904678 |
alpha-aminoacyl-tRNA binding |
| Molecular Function |
GO:0005525 |
GTP binding |
| Molecular Function |
GO:0003924 |
GTPase activity |
| Molecular Function |
GO:0003723 |
RNA binding |
| Molecular Function |
GO:0003746 |
translation elongation factor activity |
| Molecular Function |
GO:0000049 |
tRNA binding |
| Biological Process |
GO:0002181 |
cytoplasmic translation |
| Biological Process |
GO:0006955 |
immune response |
| Biological Process |
GO:0061014 |
positive regulation of mRNA catabolic process |
| Biological Process |
GO:0071025 |
RNA surveillance |
| Biological Process |
GO:0007165 |
signal transduction |
| Biological Process |
GO:0006414 |
translational elongation |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.