SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O00178

- GTPB1_HUMAN

UniProt

O00178 - GTPB1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

GTP-binding protein 1

Gene
GTPBP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi167 – 1748GTP Reviewed prediction
Nucleotide bindingi252 – 2565GTP Reviewed prediction
Nucleotide bindingi308 – 3114GTP Reviewed prediction

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
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 – 61Phosphoserine By similarity
Modified residuei12 – 121Phosphoserine By 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.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliO00178.
SMRiO00178. Positions 161-574.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini158 – 389232tr-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni167 – 1748G1 By similarity
Regioni206 – 2105G2 By similarity
Regioni252 – 2554G3 By similarity
Regioni308 – 3114G4 By similarity
Regioni366 – 3683G5 By similarity

Compositional bias

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

Sequence similaritiesi

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

« 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: September 3, 2014
This is version 124 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

Similar proteinsi