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O00178 (GTPB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTP-binding protein 1

Short name=G-protein 1
Short name=GP-1
Short name=GP1
Gene names
Name:GTPBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length669 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity.

Sequence similarities

Belongs to the GTPBP1 GTP-binding protein family.

Sequence caution

The sequence AAB51273.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAG30387.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 669669GTP-binding protein 1
PRO_0000122469

Regions

Nucleotide binding167 – 1748GTP Potential
Nucleotide binding252 – 2565GTP Potential
Nucleotide binding308 – 3114GTP Potential
Compositional bias28 – 369Poly-Ala

Amino acid modifications

Modified residue61Phosphoserine By similarity
Modified residue121Phosphoserine By similarity
Modified residue251Phosphoserine Ref.5
Modified residue441Phosphoserine Ref.5 Ref.7
Modified residue471Phosphoserine Ref.5 Ref.7
Modified residue5801Phosphoserine Ref.5 Ref.8 Ref.10

Natural variations

Natural variant911G → R.
Corresponds to variant rs11547402 [ dbSNP | Ensembl ].
VAR_049496

Sequences

Sequence LengthMass (Da)Tools
O00178 [UniParc].

Last modified July 10, 2007. Version 3.
Checksum: 0814F4DC03740ABE

FASTA66972,454
        10         20         30         40         50         60 
MATERSRSAM 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 
CEKSTKVITF 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 MQSTKKGPLT 

       610        620        630        640        650        660 
KRDEGGPSGG PAVGAPPPGD EASSVGAGQP AASSNLQPQP KPSSGGRRRG GQRHKVKSQG 


ACVTPASGC 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] OF 4-669.
Tissue: Brain.
[3]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-669.
[4]"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 35-669.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-44; SER-47 AND SER-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL021707 Genomic DNA. Translation: CAI21603.2.
BC014075 mRNA. Translation: AAH14075.3.
CR456501 mRNA. Translation: CAG30387.1. Different initiation.
U87964 mRNA. Translation: AAB51273.1. Different initiation.
CCDSCCDS13977.2.
PIRJC5291.
RefSeqNP_004277.2. NM_004286.4.
UniGeneHs.276925.

3D structure databases

ProteinModelPortalO00178.
SMRO00178. Positions 161-574.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114937. 8 interactions.
IntActO00178. 3 interactions.
MINTMINT-7944705.
STRING9606.ENSP00000216044.

PTM databases

PhosphoSiteO00178.

Proteomic databases

MaxQBO00178.
PaxDbO00178.
PRIDEO00178.

Protocols and materials databases

DNASU9567.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216044; ENSP00000216044; ENSG00000100226.
GeneID9567.
KEGGhsa:9567.
UCSCuc003awg.3. human.

Organism-specific databases

CTD9567.
GeneCardsGC22P039101.
H-InvDBHIX0016477.
HGNCHGNC:4669. GTPBP1.
HPAHPA003166.
MIM602245. gene.
neXtProtNX_O00178.
PharmGKBPA29057.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5258.
HOGENOMHOG000176635.
HOVERGENHBG004471.
InParanoidO00178.
OMAPPGDEAC.
OrthoDBEOG70KGPM.
PhylomeDBO00178.
TreeFamTF350446.

Gene expression databases

ArrayExpressO00178.
BgeeO00178.
CleanExHS_GTPBP1.
GenevestigatorO00178.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000795. EF_GTP-bd_dom.
IPR027417. P-loop_NTPase.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
SUPFAMSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGTPBP1. human.
GeneWikiGTPBP1.
GenomeRNAi9567.
NextBio35877.
PROO00178.
SOURCESearch...

Entry information

Entry nameGTPB1_HUMAN
AccessionPrimary (citable) accession number: O00178
Secondary accession number(s): Q6IC67
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 10, 2007
Last modified: July 9, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM