GTP-binding protein 1 - Mus musculus (Mouse)

Contribute

Send feedback

Read comments (?) or add your own

O08582 (GTPB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 102. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
GTP-binding protein 1
Short name=G-protein 1
Short name=GP-1
Short name=GP1

Gene names

Name:	Gtpbp1
Synonyms:	Gtpbp

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	668 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity By similarity.
Subunit structure	Interacts with EXOSC2/RRP4, EXOSC3/RRP40, EXOSC5/RRP46, HNRNPD, HNRNPR and SYNCRIP. Identified in a complex with AANAT mRNA, but does not bind mRNA by itself By similarity.
Subcellular location	Cytoplasm Ref.4.
Tissue specificity	Detected in some neurons in the brain cortex. Detected in small arteries, dendritic cells and macrophages in the thymus. Detected in lung bronchi, in bronchial epithelial cells and in bronchial smooth muscle cells. Detected in smooth muscle cells in a broad range of organs (at protein level). Expressed in brain, thymus, lung, and kidney. Ref.3 Ref.4
Disruption phenotype	No visible phenotype. Mice are born at the expected Mendelian ratio, develop normally and are fertile. They exhibit increased stability of some mRNA species. Ref.4 Ref.8
Sequence similarities	Belongs to the GTPBP1 GTP-binding protein family.
Sequence caution	The sequence AAB51274.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB23409.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE28091.1 differs from that shown. Reason: Frameshift at position 631. The sequence BAE29280.1 differs from that shown. Reason: Frameshift at position 666. The sequence BAE29365.1 differs from that shown. Reason: Frameshift at position 666.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of mRNA catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasmic exosome (RNase complex) Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 668

668

GTP-binding protein 1

PRO_0000122470

Regions

Nucleotide binding

167 – 174

GTP Potential

Nucleotide binding

252 – 256

GTP Potential

Nucleotide binding

308 – 311

GTP Potential

Compositional bias

28 – 36

Poly-Ala

Amino acid modifications

Modified residue

Phosphoserine Ref.6

Modified residue

Phosphoserine Ref.6

Modified residue

Phosphoserine Ref.6

Modified residue

Phosphoserine Ref.5

Modified residue

Phosphoserine Ref.6 Ref.7

Modified residue

Phosphoserine Ref.6 Ref.7

Modified residue

580

Phosphoserine By similarity

Experimental info

Sequence conflict

121

K → E in BAE28091. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O08582 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: E77C2148D6B237F8
Show »

FASTA

668

72,301

        10         20         30         40         50         60 
MAAERSRSPV DSPVPASMFA PEPSSPGAAR AAAAAARLHG GFDSDCSEDG EALNGEPELD 

        70         80         90        100        110        120 
LTSKLVLVSP TSEQYDSLLR QMWERMDEGC GETIYVIGQG SDGTEYGLSE ADMEASYATV 

       130        140        150        160        170        180 
KSMAEQIEAD VILLRERQEA GGRVRDYLVR KRVGDNDFLE VRVAVVGNVD AGKSTLLGVL 

       190        200        210        220        230        240 
THGELDNGRG FARQKLFRHK HEIESGRTSS VGNDILGFDS EGNVVNKPDS HGGSLEWTKI 

       250        260        270        280        290        300 
CEKSSKVITF IDLAGHEKYL KTTVFGMTGH LPDFCMLMVG SNAGIVGMTK EHLGLALALN 

       310        320        330        340        350        360 
VPVFVVVTKI DMCPANILQE TLKLLQRLLK SPGCRKIPVL VQSKDDVIVT ASNFSSERMC 

       370        380        390        400        410        420 
PIFQISNVTG ENLDLLKMFL NLLSPRTSYR EEEPAEFQID DTYSVPGVGT VVSGTTLRGL 

       430        440        450        460        470        480 
IKLNDTLLLG PDPLGNFLSI AVKSIHRKRM PVKEVRGGQT ASFALKKIKR SSIRKGMVMV 

       490        500        510        520        530        540 
SPRLNPQASW EFEAEILVLH HPTTISPRYQ AMVHCGSIRQ TATILSMDKD CLRTGDKATV 

       550        560        570        580        590        600 
HFRFIKTPEY LHIDQRLVFR EGRTKAVGTI TKLLQTTNNS PMNSKPQQIK MQSTKKGPLS 

       610        620        630        640        650        660 
KREEGGPCGV PAAGGPPTGD EASSLGTAQA ASTSGLQPQP KPSSGGRRRG GQRHKVKSGA 


CVTPASGC

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Dendritic cell, Lung and Melanocyte.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[3]	"Identification of human and mouse GP-1, a putative member of a novel G-protein family." Senju S., Nishimura Y. Biochem. Biophys. Res. Commun. 231:360-364(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-668, TISSUE SPECIFICITY.
[4]	"Immunocytochemical analyses and targeted gene disruption of GTPBP1." Senju S., Iyama K., Kudo H., Aizawa S., Nishimura Y. Mol. Cell. Biol. 20:6195-6200(2000) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, MASS SPECTROMETRY. Tissue: Brain cortex.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-8; SER-12; SER-44 AND SER-47, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-47, MASS SPECTROMETRY. Tissue: Melanoma.
[8]	"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: DISRUPTION PHENOTYPE.
[9]	"A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex." Reiser J.B., Gregoire C., Darnault C., Mosser T., Guimezanes A., Schmitt-Verhulst A.M., Fontecilla-Camps J.C., Mazza G., Malissen B., Housset D. Immunity 16:345-354(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 246-253 IN COMPLEX WITH MHC.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK004612 mRNA. Translation: BAB23409.1. Different initiation.
AK147717 mRNA. Translation: BAE28091.1. Frameshift.
AK150068 mRNA. Translation: BAE29280.1. Frameshift.
AK150185 mRNA. Translation: BAE29365.1. Frameshift.
AK170091 mRNA. Translation: BAE41557.1.
BC046228 mRNA. Translation: AAH46228.1.
U87965 mRNA. Translation: AAB51274.1. Different initiation.

IPI

IPI00761677.

PIR

JC5292.

RefSeq

NP_038846.2. NM_013818.2.

UniGene

Mm.19080.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KJ2	X-ray	2.71	P/Q	246-253	[»]
1KJ3	X-ray	2.30	P/Q	246-253	[»]

ProteinModelPortal

O08582.

SMR

O08582. Positions 161-574.

ModBase

Search...

PTM databases

PhosphoSite

O08582.

Proteomic databases

PaxDb

O08582.

PRIDE

O08582.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000046463; ENSMUSP00000043575; ENSMUSG00000042535.

GeneID

14904.

KEGG

mmu:14904.

UCSC

uc007wuf.1. mouse.

Organism-specific databases

CTD

9567.

MGI

MGI:109443. Gtpbp1.

Phylogenomic databases

eggNOG

COG5258.

GeneTree

ENSGT00670000097839.

HOGENOM

HOG000176635.

HOVERGEN

HBG004471.

InParanoid

O08582.

OMA

REHQEAG.

OrthoDB

EOG4CJVGS.

Gene expression databases

Bgee

O08582.

CleanEx

MM_GTPBP1.

Genevestigator

O08582.

GermOnline

ENSMUSG00000042535. Mus musculus.

Family and domain databases

InterPro

IPR000795. EF_GTP-bd_dom.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]

Pfam

PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]

SUPFAM

SSF50465. Elong_init_C. 1 hit.
SSF50447. Translat_factor. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

GTPBP1. mouse.

EvolutionaryTrace

O08582.

NextBio

287191.

SOURCE

Search...

Entry information

Entry name

GTPB1_MOUSE

Accession

Primary (citable) accession number: O08582
Secondary accession number(s): Q3UD96

Q80ZY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents