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Protein

GTP-binding protein 1

Gene

Gtpbp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi167 – 1748GTPSequence analysis
Nucleotide bindingi252 – 2565GTPSequence analysis
Nucleotide bindingi308 – 3114GTPSequence analysis

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: Ensembl

GO - Biological processi

  • positive regulation of mRNA catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding protein 1
Gene namesi
Name:Gtpbp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi1306758. Gtpbp1.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasmic exosome (RNase complex) Source: UniProtKB
  • cytosol Source: UniProtKB
  • membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi173 – 1742KS → AA: Reduced decay of target mRNA. Slightly reduced GTPase activity. No effect on GTP binding. 1 Publication
Mutagenesisi173 – 1731K → A: Reduced decay of target mRNA. No effect on GTP binding. 1 Publication
Mutagenesisi173 – 1731K → E: Reduced decay of target mRNA. Reduced GTPase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 669669GTP-binding protein 1PRO_0000412470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei8 – 81PhosphoserineBy similarity
Modified residuei12 – 121PhosphoserineCombined sources
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei25 – 251PhosphoserineBy similarity
Modified residuei44 – 441PhosphoserineCombined sources
Modified residuei47 – 471PhosphoserineCombined sources
Modified residuei69 – 691PhosphoserineCombined sources
Modified residuei580 – 5801PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiD2XV59.
PRIDEiD2XV59.

PTM databases

iPTMnetiD2XV59.

Expressioni

Tissue specificityi

Detected in pineal gland (at protein level).1 Publication

Gene expression databases

GenevisibleiD2XV59. RN.

Interactioni

Subunit structurei

Interacts with EXOSC2/RRP4, EXOSC3/RRP40, EXOSC5/RRP46, HNRNPD, HNRNPR and SYNCRIP. Identified in a complex with HNRNPD, HNRNPL, HNRNPQ, HNRNPR, HNRNPU and AANAT mRNA, but does not bind mRNA by itself.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000039165.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini158 – 389232tr-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni167 – 1748G1PROSITE-ProRule annotation
Regioni206 – 2105G2PROSITE-ProRule annotation
Regioni252 – 2554G3PROSITE-ProRule annotation
Regioni308 – 3114G4PROSITE-ProRule annotation
Regioni366 – 3683G5PROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. GTPBP1 subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0463. Eukaryota.
COG5258. LUCA.
GeneTreeiENSGT00730000110829.
HOGENOMiHOG000176635.
InParanoidiD2XV59.
OMAiPPGDEAC.
OrthoDBiEOG70KGPM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D2XV59-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAERSRSPV DSPVPASMFA PEPSSPGAAR AAAAAARLHG GFDSDCSEDG
60 70 80 90 100
EALNGEPELD LTSKLVLVSP TSEQYDSLLR QMWERMDEGC GETIYVIGQG
110 120 130 140 150
SDGTEYGLSE ADMEASYATV KSMAEQIEAD VILLRERQES GGRVRDYLVR
160 170 180 190 200
KRVGDNDFLE VRVAVVGNVD AGKSTLLGVL THGELDNGRG FARQKLFRHK
210 220 230 240 250
HEIESGRTSS VGNDILGFDS EGNVVNKPDS HGGSLEWTKI CEKSSKVITF
260 270 280 290 300
IDLAGHEKYL KTTVFGMTGH LPDFCMLMVG SNAGIVGMTK EHLGLALALN
310 320 330 340 350
VPVFVVVTKI DMCPANILQE TLKLLQRLLK SPGCRKIPVL VQSKDDVIVT
360 370 380 390 400
ASNFSSERMC PIFQISNVTG ENLDLLKMFL NLLSPRTSYR EEEPAEFQID
410 420 430 440 450
DTYSVPGVGT VVSGTTLRGL IKLNDTLLLG PDPLGNFLSI AVKSIHRKRM
460 470 480 490 500
PVKEVRGGQT ASFALKKIKR SSIRKGMVMV SPRLNPQASW EFEAEILVLH
510 520 530 540 550
HPTTISPRYQ AMVHCGSIRQ TATILSMDKD CLRTGDKATV HFRFIKTPEY
560 570 580 590 600
LHIDQRLVFR EGRTKAVGTI TKLLQTTNNS PMNSKPQQIK MQSTKKGPLS
610 620 630 640 650
KREEGGPSGV PAAGPPSTGD EASSLGTTQA ATSSGLQPQP KPSSGGRRRG
660
GQRHKVKSQG ACVTPASGC
Length:669
Mass (Da):72,489
Last modified:March 2, 2010 - v1
Checksum:i8A244D3E408E0197
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GU256773 mRNA. Translation: ADB22435.1.
CH473950 Genomic DNA. Translation: EDM15787.1.
RefSeqiNP_001186244.1. NM_001199315.1.
UniGeneiRn.97210.

Genome annotation databases

EnsembliENSRNOT00000049247; ENSRNOP00000039165; ENSRNOG00000014634.
GeneIDi300077.
KEGGirno:300077.
UCSCiRGD:1306758. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GU256773 mRNA. Translation: ADB22435.1.
CH473950 Genomic DNA. Translation: EDM15787.1.
RefSeqiNP_001186244.1. NM_001199315.1.
UniGeneiRn.97210.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000039165.

PTM databases

iPTMnetiD2XV59.

Proteomic databases

PaxDbiD2XV59.
PRIDEiD2XV59.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000049247; ENSRNOP00000039165; ENSRNOG00000014634.
GeneIDi300077.
KEGGirno:300077.
UCSCiRGD:1306758. rat.

Organism-specific databases

CTDi9567.
RGDi1306758. Gtpbp1.

Phylogenomic databases

eggNOGiKOG0463. Eukaryota.
COG5258. LUCA.
GeneTreeiENSGT00730000110829.
HOGENOMiHOG000176635.
InParanoidiD2XV59.
OMAiPPGDEAC.
OrthoDBiEOG70KGPM.

Miscellaneous databases

PROiD2XV59.

Gene expression databases

GenevisibleiD2XV59. RN.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Kim T.-D., Kim K.-T.
    Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "Modulation of exosome-mediated mRNA turnover by interaction of GTP-binding protein 1 (GTPBP1) with its target mRNAs."
    Woo K.C., Kim T.D., Lee K.H., Kim D.Y., Kim S., Lee H.R., Kang H.J., Chung S.J., Senju S., Nishimura Y., Kim K.T.
    FASEB J. 25:2757-2769(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HNRNPD; HNRNPR; SYNCRIP; EXOSC2; EXOSC3 AND EXOSC5, IDENTIFICATION IN A COMPLEX WITH HNRNPD; HNRNPL; HNRNPQ; HNRNPR; HNRNPU AND MRNA, GTP BINDING, GTPASE ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-173 AND 173-LYS-SER-174, TISSUE SPECIFICITY.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-44; SER-47; SER-69 AND SER-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGTPB1_RAT
AccessioniPrimary (citable) accession number: D2XV59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: March 2, 2010
Last modified: June 8, 2016
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.