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O00178

- GTPB1_HUMAN

UniProt

O00178 - GTPB1_HUMAN

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Protein

GTP-binding protein 1

Gene

GTPBP1

Organism
Homo sapiens (Human)
Status
Reviewed - 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 (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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiO00178.
CleanExiHS_GTPBP1.
ExpressionAtlasiO00178. baseline.
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. 12 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.
GeneTreeiENSGT00730000110829.
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

        10         20         30         40         50
MATERSRSAM DSPVPASMFA PEPSSPGAAR AAAAAARLHG GFDSDCSEDG
60 70 80 90 100
EALNGEPELD LTSKLVLVSP TSEQYDSLLR QMWERMDEGC GETIYVIGQG
110 120 130 140 150
SDGTEYGLSE ADMEASYATV KSMAEQIEAD VILLRERQEA GGRVRDYLVR
160 170 180 190 200
KRVGDNDFLE VRVAVVGNVD AGKSTLLGVL THGELDNGRG FARQKLFRHK
210 220 230 240 250
HEIESGRTSS VGNDILGFDS EGNVVNKPDS HGGSLEWTKI CEKSTKVITF
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 MQSTKKGPLT
610 620 630 640 650
KRDEGGPSGG PAVGAPPPGD EASSVGAGQP AASSNLQPQP KPSSGGRRRG
660
GQRHKVKSQG ACVTPASGC
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. 12 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.
GeneTreei ENSGT00730000110829.
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

Bgeei O00178.
CleanExi HS_GTPBP1.
ExpressionAtlasi O00178. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 126 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