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Ras GTPase-activating protein-binding protein 1 (G3BP-1) (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent DNA/RNA helicase G3BP)

 G3BP1_BOVIN             Reviewed;         465 AA.
Q32LC7;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 1.
22-NOV-2017, entry version 93.
RecName: Full=Ras GTPase-activating protein-binding protein 1;
Short=G3BP-1;
EC=3.6.4.12;
EC=3.6.4.13;
AltName: Full=ATP-dependent DNA/RNA helicase G3BP;
Name=G3BP; Synonyms=G3BP1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: 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 (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Mg(2+) is required for helicase activity. {ECO:0000250};
-!- SUBUNIT: 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. Component of a TAU mRNP complex, at least composed of
IGF2BP1, ELAVL4 and G3BP. Interacts with RPTOR and SPAG5; this
complex is increased by oxidative stress. Interacts with ATXN2L.
{ECO:0000250|UniProtKB:P97855, ECO:0000250|UniProtKB:Q13283}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytosol
{ECO:0000250}. Cell membrane {ECO:0000250}. Nucleus {ECO:0000250}.
Cytoplasmic granule {ECO:0000250}. 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).
{ECO:0000250}.
-!- DOMAIN: The NTF2 domain mediates multimerization. {ECO:0000250}.
-!- PTM: 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).
{ECO:0000250}.
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EMBL; BC109645; AAI09646.1; -; mRNA.
RefSeq; NP_001032700.1; NM_001037611.2.
UniGene; Bt.5197; -.
ProteinModelPortal; Q32LC7; -.
SMR; Q32LC7; -.
STRING; 9913.ENSBTAP00000027067; -.
PaxDb; Q32LC7; -.
PeptideAtlas; Q32LC7; -.
PRIDE; Q32LC7; -.
Ensembl; ENSBTAT00000027067; ENSBTAP00000027067; ENSBTAG00000020309.
GeneID; 534214; -.
KEGG; bta:534214; -.
CTD; 10146; -.
eggNOG; KOG0116; Eukaryota.
eggNOG; ENOG410YV57; LUCA.
GeneTree; ENSGT00390000011365; -.
HOGENOM; HOG000220838; -.
HOVERGEN; HBG007211; -.
InParanoid; Q32LC7; -.
KO; K17265; -.
OMA; PKDEVGW; -.
OrthoDB; EOG091G0GAN; -.
TreeFam; TF325464; -.
Proteomes; UP000009136; Chromosome 7.
Bgee; ENSBTAG00000020309; -.
GO; GO:0010494; C:cytoplasmic stress granule; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
CDD; cd00780; NTF2; 1.
CDD; cd12463; RRM_G3BP1; 1.
InterPro; IPR034375; G3BP1.
InterPro; IPR034374; G3BP1_RRM.
InterPro; IPR002075; NTF2.
InterPro; IPR032710; NTF2-like_dom_sf.
InterPro; IPR018222; Nuclear_transport_factor_2_euk.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR10693:SF21; PTHR10693:SF21; 1.
Pfam; PF02136; NTF2; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54427; SSF54427; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50177; NTF2_DOMAIN; 1.
PROSITE; PS50102; RRM; 1.
2: Evidence at transcript level;
Acetylation; ATP-binding; Cell membrane; Complete proteome; Cytoplasm;
DNA-binding; Endonuclease; Helicase; Hydrolase; Isopeptide bond;
Membrane; Methylation; Nuclease; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; RNA-binding; Transport;
Ubl conjugation.
CHAIN 1 465 Ras GTPase-activating protein-binding
protein 1.
/FTId=PRO_0000271370.
DOMAIN 11 133 NTF2. {ECO:0000255|PROSITE-
ProRule:PRU00137}.
DOMAIN 339 414 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 144 224 Glu-rich.
COMPBIAS 429 460 Gly-rich.
MOD_RES 143 143 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 230 230 Phosphoserine.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 375 375 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 428 428 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 434 434 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 434 434 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 434 434 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 446 446 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P97855}.
MOD_RES 446 446 Omega-N-methylated arginine; alternate.
{ECO:0000250}.
MOD_RES 459 459 Dimethylated arginine; alternate.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 459 459 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 459 459 Omega-N-methylated arginine; alternate.
{ECO:0000250}.
MOD_RES 464 464 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q13283}.
MOD_RES 464 464 Omega-N-methylated arginine; alternate.
{ECO:0000250}.
CROSSLNK 375 375 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q13283}.
SEQUENCE 465 AA; 52122 MW; DFD85B9BDD9F7307 CRC64;
MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY VHGGLDSNGK PADAVYGQKE
IHRKVMSQNF TNCHTKIRHV DAHATLNDGV VVQVMGLLSN NNQALRRFMQ TFVLAPEGSV
ANKFYVHNDI FRYQDEVFGG FITEPQEESE EEVEEPEERQ QTPEVVPDDS GTFYDQTVSN
DLEEHLEEPV AEPEPEPEPE PEQEPVSEVQ EEKSEPVLEE TAPEDVQKSS SPAPADIAQT
VQEDLRTFSW ASVTSKNLPP SGAVPVTGIP PHVVKVPASQ PRPESKPESQ IPLQRPQRDQ
RVREQRINVP PQRGPRPVRE AGEQGDVEPR RIVRHPDSHQ LFIGNLPHEV DKSELKDFFQ
NYGNVVELRI NSGGKLPNFG FVVFDDSEPV QKVLSNRPIM FRGEVRLNVE EKKTRAAREG
DRRDNRLRGP GGPRGGLGGG MRGPPRGGMV QKPGFGVGRS IAPRQ


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