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Protein

Ras GTPase-activating protein-binding protein 1

Gene

G3bp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be a regulated effector of stress granule assembly. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-dependent helicase. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Mg2+By similarityNote: Mg2+ is required for helicase activity.By similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB-KW
  • endonuclease activity Source: UniProtKB-KW
  • helicase activity Source: UniProtKB-KW
  • mRNA binding Source: MGI
  • poly(A) RNA binding Source: MGI

GO - Biological processi

  • negative regulation of canonical Wnt signaling pathway Source: MGI
  • transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Helicase, Hydrolase, Nuclease

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras GTPase-activating protein-binding protein 1 (EC:3.6.4.12, EC:3.6.4.13)
Short name:
G3BP-1
Alternative name(s):
ATP-dependent DNA helicase VIII
GAP SH3 domain-binding protein 1
HDH-VIII
Gene namesi
Name:G3bp1
Synonyms:G3bp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1351465. G3bp1.

Subcellular locationi

  • Cytoplasm By similarity
  • Cytoplasmcytosol By similarity
  • Cytoplasmic granule By similarity
  • Cell membrane By similarity
  • Nucleus By similarity

  • Note: Cytoplasmic in proliferating cells, can be recruited to the plasma membrane in exponentially growing cells (By similarity). Cytosolic and partially nuclear in resting cells. Recruited to stress granules (SGs) upon either arsenite or high temperature treatment. Recruitment to SGs is influenced by HRAS (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytoplasmic stress granule Source: MGI
  • cytosol Source: UniProtKB-SubCell
  • focal adhesion Source: MGI
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 465464Ras GTPase-activating protein-binding protein 1PRO_0000194799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei143 – 1431PhosphothreonineBy similarity
Modified residuei149 – 1491PhosphoserineCombined sources1 Publication
Modified residuei231 – 2311PhosphoserineCombined sources1 Publication
Modified residuei371 – 3711PhosphoserineBy similarity
Modified residuei374 – 3741N6-acetyllysineBy similarity
Modified residuei433 – 4331Dimethylated arginine; alternateBy similarity
Modified residuei433 – 4331Omega-N-methylarginine; alternateBy similarity
Modified residuei445 – 4451Omega-N-methylated arginineBy similarity
Modified residuei458 – 4581Dimethylated arginine; alternateBy similarity
Modified residuei458 – 4581Omega-N-methylated arginine; alternateBy similarity
Modified residuei464 – 4641Omega-N-methylated arginineBy similarity

Post-translational modificationi

Phosphorylated exclusively on serine residues. Hyperphosphorylated in quiescent fibroblasts. Hypophosphorylation leads to a decrease in endoribonuclease activity. RASA1-dependent phosphorylation of Ser-149 induces a conformational change that prevents self-association. Dephosphorylation after HRAS activation is required for stress granule assembly. Ser-149 phosphorylation induces partial nuclear localization (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiP97855.
PaxDbiP97855.
PRIDEiP97855.

PTM databases

iPTMnetiP97855.
PhosphoSiteiP97855.
SwissPalmiP97855.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP97855.
GenevisibleiP97855. MM.

Interactioni

Subunit structurei

Binds to the SH3 domain of Ras GTPase-activating protein (RASA1) in proliferating cells. No interaction in quiescent cells. Interacts with USP10, and may regulate it. Forms homodimers and oligomers (By similarity). Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP1 (PubMed:15086518). Interacts with RPTOR and SPAG5; this complex is increased by oxidative stress (By similarity). Interacts with ATXN2L (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi205102. 4 interactions.
IntActiP97855. 8 interactions.
MINTiMINT-1857867.
STRINGi10090.ENSMUSP00000018727.

Structurei

3D structure databases

ProteinModelPortaliP97855.
SMRiP97855. Positions 7-138, 339-404.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 133123NTF2PROSITE-ProRule annotationAdd
BLAST
Domaini338 – 41376RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi144 – 22582Glu-richAdd
BLAST
Compositional biasi428 – 45932Gly-richAdd
BLAST

Domaini

The NTF2 domain mediates multimerization.By similarity

Sequence similaritiesi

Contains 1 NTF2 domain.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0116. Eukaryota.
ENOG410YV57. LUCA.
GeneTreeiENSGT00390000011365.
HOVERGENiHBG007211.
InParanoidiP97855.
KOiK17265.
OMAiGYARGEY.
OrthoDBiEOG77Q4ZC.
TreeFamiTF325464.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR002075. NTF2.
IPR032710. NTF2-like_dom.
IPR018222. Nuclear_transport_factor_2_euk.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF02136. NTF2. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS50177. NTF2_DOMAIN. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P97855-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY AHGGLDSNGK
60 70 80 90 100
PADAVYGQKE IHRKVMSQNF TNCHTKIRHV DAHATLNDGV VVQVMGLLSN
110 120 130 140 150
NNQALRRFMQ TFVLAPEGSV ANKFYVHNDI FRYQDEVFGG FVTEPQEESE
160 170 180 190 200
EEVEEPEERQ QTPEVVPDDS GTFYDQTVSN DLEEHLEEPV VEPEPEPEPE
210 220 230 240 250
PEPEPVSDIQ EDKPEAALEE AAPDDVQKST SPAPADVAPA QEDLRTFSWA
260 270 280 290 300
SVTSKNLPPS GAVPVTGTPP HVVKVPASQP RPESKPDSQI PPQRPQRDQR
310 320 330 340 350
VREQRINIPP QRGPRPIREA GEPGDVEPRR MVRHPDSHQL FIGNLPHEVD
360 370 380 390 400
KSELKDFFQN FGNVVELRIN SGGKLPNFGF VVFDDSEPVQ KVLSNRPIMF
410 420 430 440 450
RGAVRLNVEE KKTRAAREGD RRDNRLRGPG GPRGGPSGGM RGPPRGGMVQ
460
KPGFGVGRGI TTPRQ
Length:465
Mass (Da):51,829
Last modified:May 1, 1997 - v1
Checksum:iEB213303D21B1D57
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001927 mRNA. Translation: BAA19469.1.
BC021156 mRNA. Translation: AAH21156.1.
CCDSiCCDS24714.1.
RefSeqiNP_038744.1. NM_013716.2.
UniGeneiMm.380129.
Mm.39631.
Mm.405739.

Genome annotation databases

EnsembliENSMUST00000018727; ENSMUSP00000018727; ENSMUSG00000018583.
GeneIDi27041.
KEGGimmu:27041.
UCSCiuc007izl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001927 mRNA. Translation: BAA19469.1.
BC021156 mRNA. Translation: AAH21156.1.
CCDSiCCDS24714.1.
RefSeqiNP_038744.1. NM_013716.2.
UniGeneiMm.380129.
Mm.39631.
Mm.405739.

3D structure databases

ProteinModelPortaliP97855.
SMRiP97855. Positions 7-138, 339-404.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205102. 4 interactions.
IntActiP97855. 8 interactions.
MINTiMINT-1857867.
STRINGi10090.ENSMUSP00000018727.

PTM databases

iPTMnetiP97855.
PhosphoSiteiP97855.
SwissPalmiP97855.

Proteomic databases

EPDiP97855.
PaxDbiP97855.
PRIDEiP97855.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018727; ENSMUSP00000018727; ENSMUSG00000018583.
GeneIDi27041.
KEGGimmu:27041.
UCSCiuc007izl.1. mouse.

Organism-specific databases

CTDi10146.
MGIiMGI:1351465. G3bp1.

Phylogenomic databases

eggNOGiKOG0116. Eukaryota.
ENOG410YV57. LUCA.
GeneTreeiENSGT00390000011365.
HOVERGENiHBG007211.
InParanoidiP97855.
KOiK17265.
OMAiGYARGEY.
OrthoDBiEOG77Q4ZC.
TreeFamiTF325464.

Miscellaneous databases

ChiTaRSiG3bp1. mouse.
PROiP97855.
SOURCEiSearch...

Gene expression databases

BgeeiP97855.
GenevisibleiP97855. MM.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR002075. NTF2.
IPR032710. NTF2-like_dom.
IPR018222. Nuclear_transport_factor_2_euk.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF02136. NTF2. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
SSF54928. SSF54928. 1 hit.
PROSITEiPS50177. NTF2_DOMAIN. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of GAP SH3 binding protein from mouse brain."
    Saitoh H., Abe T.K., Masuko M., Tanaka H., Watanabe Y.G., Odani S., Kuwano R.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  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: Czech II.
    Tissue: Mammary gland.
  3. Lubec G., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 124-132; 334-351 AND 375-391, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Brain and Hippocampus.
  4. "A Ras-GTPase-activating protein SH3-domain-binding protein."
    Parker F., Maurier F., Delumeau I., Duchesne M., Faucher D., Debussche L., Dugue A., Schweighoffer F., Tocque B.
    Mol. Cell. Biol. 16:2561-2569(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "RasGAP-associated endoribonuclease G3Bp: selective RNA degradation and phosphorylation-dependent localization."
    Tourriere H., Gallouzi I.-E., Chebli K., Capony J.-P., Mouaikel J., van der Geer P., Tazi J.
    Mol. Cell. Biol. 21:7747-7760(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENDORIBONUCLEASE ACTIVITY, PHOSPHORYLATION AT SER-149 AND SER-231.
  6. "The insulin-like growth factor mRNA binding-protein IMP-1 and the Ras-regulatory protein G3BP associate with tau mRNA and HuD protein in differentiated P19 neuronal cells."
    Atlas R., Behar L., Elliott E., Ginzburg I.
    J. Neurochem. 89:613-626(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP1 AND ELAVL4.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiG3BP1_MOUSE
AccessioniPrimary (citable) accession number: P97855
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: May 1, 1997
Last modified: June 8, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.