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O00178

- GTPB1_HUMAN

UniProt

O00178 - GTPB1_HUMAN

Protein

GTP-binding protein 1

Gene

GTPBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 3 (10 Jul 2007)
      Previous versions | rss
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    Functioni

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

    Regions

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

    GO - Molecular functioni

    1. GTPase activity Source: UniProtKB
    2. GTP binding Source: ProtInc
    3. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. GTP catabolic process Source: UniProtKB
    2. immune response Source: ProtInc
    3. positive regulation of mRNA catabolic process Source: UniProtKB
    4. signal transduction Source: ProtInc

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTP-binding protein 1
    Short name:
    G-protein 1
    Short name:
    GP-1
    Short name:
    GP1
    Gene namesi
    Name:GTPBP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:4669. GTPBP1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasmic exosome (RNase complex) Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29057.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 669669GTP-binding protein 1PRO_0000122469Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei6 – 61PhosphoserineBy similarity
    Modified residuei12 – 121PhosphoserineBy similarity
    Modified residuei25 – 251Phosphoserine1 Publication
    Modified residuei44 – 441Phosphoserine2 Publications
    Modified residuei47 – 471Phosphoserine2 Publications
    Modified residuei580 – 5801Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO00178.
    PaxDbiO00178.
    PRIDEiO00178.

    PTM databases

    PhosphoSiteiO00178.

    Expressioni

    Gene expression databases

    ArrayExpressiO00178.
    BgeeiO00178.
    CleanExiHS_GTPBP1.
    GenevestigatoriO00178.

    Organism-specific databases

    HPAiHPA003166.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi114937. 8 interactions.
    IntActiO00178. 3 interactions.
    MINTiMINT-7944705.
    STRINGi9606.ENSP00000216044.

    Structurei

    3D structure databases

    ProteinModelPortaliO00178.
    SMRiO00178. Positions 161-574.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi28 – 369Poly-Ala

    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

    eggNOGiCOG5258.
    HOGENOMiHOG000176635.
    HOVERGENiHBG004471.
    InParanoidiO00178.
    OMAiPPGDEAC.
    OrthoDBiEOG70KGPM.
    PhylomeDBiO00178.
    TreeFamiTF350446.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR000795. 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]
    PfamiPF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    PF03143. GTP_EFTU_D3. 1 hit.
    [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.

    O00178-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATERSRSAM DSPVPASMFA PEPSSPGAAR AAAAAARLHG GFDSDCSEDG    50
    EALNGEPELD LTSKLVLVSP TSEQYDSLLR QMWERMDEGC GETIYVIGQG 100
    SDGTEYGLSE ADMEASYATV KSMAEQIEAD VILLRERQEA GGRVRDYLVR 150
    KRVGDNDFLE VRVAVVGNVD AGKSTLLGVL THGELDNGRG FARQKLFRHK 200
    HEIESGRTSS VGNDILGFDS EGNVVNKPDS HGGSLEWTKI CEKSTKVITF 250
    IDLAGHEKYL KTTVFGMTGH LPDFCMLMVG SNAGIVGMTK EHLGLALALN 300
    VPVFVVVTKI DMCPANILQE TLKLLQRLLK SPGCRKIPVL VQSKDDVIVT 350
    ASNFSSERMC PIFQISNVTG ENLDLLKMFL NLLSPRTSYR EEEPAEFQID 400
    DTYSVPGVGT VVSGTTLRGL IKLNDTLLLG PDPLGNFLSI AVKSIHRKRM 450
    PVKEVRGGQT ASFALKKIKR SSIRKGMVMV SPRLNPQASW EFEAEILVLH 500
    HPTTISPRYQ AMVHCGSIRQ TATILSMDKD CLRTGDKATV HFRFIKTPEY 550
    LHIDQRLVFR EGRTKAVGTI TKLLQTTNNS PMNSKPQQIK MQSTKKGPLT 600
    KRDEGGPSGG PAVGAPPPGD EASSVGAGQP AASSNLQPQP KPSSGGRRRG 650
    GQRHKVKSQG ACVTPASGC 669
    Length:669
    Mass (Da):72,454
    Last modified:July 10, 2007 - v3
    Checksum:i0814F4DC03740ABE
    GO

    Sequence cautioni

    The sequence AAB51273.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAG30387.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti91 – 911G → R.
    Corresponds to variant rs11547402 [ dbSNP | Ensembl ].
    VAR_049496

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13977.2.
    PIRiJC5291.
    RefSeqiNP_004277.2. NM_004286.4.
    UniGeneiHs.276925.

    Genome annotation databases

    EnsembliENST00000216044; ENSP00000216044; ENSG00000100226.
    GeneIDi9567.
    KEGGihsa:9567.
    UCSCiuc003awg.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS13977.2.
    PIRi JC5291.
    RefSeqi NP_004277.2. NM_004286.4.
    UniGenei Hs.276925.

    3D structure databases

    ProteinModelPortali O00178.
    SMRi O00178. Positions 161-574.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114937. 8 interactions.
    IntActi O00178. 3 interactions.
    MINTi MINT-7944705.
    STRINGi 9606.ENSP00000216044.

    PTM databases

    PhosphoSitei O00178.

    Proteomic databases

    MaxQBi O00178.
    PaxDbi O00178.
    PRIDEi O00178.

    Protocols and materials databases

    DNASUi 9567.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216044 ; ENSP00000216044 ; ENSG00000100226 .
    GeneIDi 9567.
    KEGGi hsa:9567.
    UCSCi uc003awg.3. human.

    Organism-specific databases

    CTDi 9567.
    GeneCardsi GC22P039101.
    H-InvDB HIX0016477.
    HGNCi HGNC:4669. GTPBP1.
    HPAi HPA003166.
    MIMi 602245. gene.
    neXtProti NX_O00178.
    PharmGKBi PA29057.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5258.
    HOGENOMi HOG000176635.
    HOVERGENi HBG004471.
    InParanoidi O00178.
    OMAi PPGDEAC.
    OrthoDBi EOG70KGPM.
    PhylomeDBi O00178.
    TreeFami TF350446.

    Miscellaneous databases

    ChiTaRSi GTPBP1. human.
    GeneWikii GTPBP1.
    GenomeRNAii 9567.
    NextBioi 35877.
    PROi O00178.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00178.
    Bgeei O00178.
    CleanExi HS_GTPBP1.
    Genevestigatori O00178.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR000795. 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 ]
    Pfami PF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    PF03143. GTP_EFTU_D3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50447. SSF50447. 1 hit.
    SSF50465. SSF50465. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS51722. G_TR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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].

    Entry informationi

    Entry nameiGTPB1_HUMAN
    AccessioniPrimary (citable) accession number: O00178
    Secondary accession number(s): Q6IC67
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 125 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3