Skip Header

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

Q13283

- G3BP1_HUMAN

UniProt

Q13283 - G3BP1_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

Ras GTPase-activating protein-binding protein 1

Gene

G3BP1

Organism
Homo sapiens (Human)
Status
Reviewed - 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.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Magnesium. Required for helicase activity.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent DNA helicase activity Source: ProtInc
  3. ATP-dependent RNA helicase activity Source: ProtInc
  4. DNA binding Source: UniProtKB-KW
  5. endonuclease activity Source: UniProtKB-KW
  6. mRNA binding Source: Ensembl
  7. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA duplex unwinding Source: GOC
  3. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  4. Ras protein signal transduction Source: ProtInc
  5. 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
Short name:
hDH VIII
GAP SH3 domain-binding protein 1
Gene namesi
Name:G3BP1
Synonyms:G3BP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:30292. G3BP1.

Subcellular locationi

Cytoplasm. Cytoplasmcytosol. Cytoplasmic granule. Cell membrane. Nucleus
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

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytoplasmic stress granule Source: Ensembl
  3. focal adhesion Source: UniProtKB
  4. nucleus Source: ProtInc
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi149 – 1491S → A: Cytoplasmic; no effect on stress granule assembly. 2 Publications
Mutagenesisi149 – 1491S → E: Cytoplasmic and nuclear; no assembly of stress granules; no homo-oligomerization. 2 Publications
Mutagenesisi232 – 2321S → A: Cytoplasmic. Partially nuclear; when associated with E-149. 1 Publication
Mutagenesisi232 – 2321S → E: Cytoplasmic. Partially nuclear; when associated with E-149. 1 Publication

Organism-specific databases

PharmGKBiPA162389105.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 466465Ras GTPase-activating protein-binding protein 1PRO_0000194798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei143 – 1431Phosphothreonine1 Publication
Modified residuei149 – 1491Phosphoserine9 Publications
Modified residuei231 – 2311Phosphoserine1 Publication
Modified residuei232 – 2321Phosphoserine6 Publications
Modified residuei373 – 3731Phosphoserine2 Publications
Modified residuei376 – 3761N6-acetyllysine1 Publication
Modified residuei435 – 4351Dimethylated arginine; alternate1 Publication
Modified residuei435 – 4351Omega-N-methylarginine; alternate1 Publication
Modified residuei460 – 4601Dimethylated arginine; alternate1 Publication
Modified residuei460 – 4601Omega-N-methylated arginine; alternate1 Publication

Post-translational modificationi

Phosphorylated exclusively on serine residues. Hyperphosphorylated in quiescent fibroblasts. Hypophosphorylation leads to a decrease in endoribonuclease activity (By similarity). 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 similarity12 Publications
Arg-435 is dimethylated, probably to asymmetric dimethylarginine.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ13283.
PaxDbiQ13283.
PeptideAtlasiQ13283.
PRIDEiQ13283.

PTM databases

PhosphoSiteiQ13283.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ13283.
CleanExiHS_G3BP1.
ExpressionAtlasiQ13283. baseline and differential.
GenevestigatoriQ13283.

Organism-specific databases

HPAiHPA004052.

Interactioni

Subunit structurei

Binds to the SH3 domain of Ras GTPase-activating protein (RASA1) in proliferating cells. No interaction in quiescent cells Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP1 (By similarity). Interacts with USP10, and may regulate it. Forms homodimers and oligomers. Interacts with RPTOR and SPAG5; this complex is increased by oxidative stress.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATXN2Q997004EBI-1047359,EBI-697691
ATXN2LQ8WWM75EBI-1047359,EBI-948363
RPTORQ8N1224EBI-1047359,EBI-1567928
SND1Q7KZF43EBI-1047359,EBI-1044112

Protein-protein interaction databases

BioGridi115448. 89 interactions.
IntActiQ13283. 55 interactions.
MINTiMINT-5002789.
STRINGi9606.ENSP00000348578.

Structurei

Secondary structure

1
466
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2518
Helixi27 – 337
Beta strandi34 – 418
Beta strandi47 – 515
Helixi57 – 6711
Beta strandi74 – 8411
Helixi86 – 883
Beta strandi90 – 9910
Helixi100 – 1023
Beta strandi106 – 11611
Beta strandi118 – 1203
Beta strandi124 – 13411
Turni135 – 1373

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q90X-ray1.70A/B1-139[»]
4FCJX-ray1.62A/B1-139[»]
4FCMX-ray2.69A/B1-139[»]
4IIAX-ray3.30A11-139[»]
ProteinModelPortaliQ13283.
SMRiQ13283. Positions 7-138, 341-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 133123NTF2PROSITE-ProRule annotationAdd
BLAST
Domaini340 – 41576RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi144 – 22582Glu-richAdd
BLAST
Compositional biasi430 – 46132Gly-richAdd
BLAST

Domaini

The NTF2 domain mediates multimerization.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG324333.
GeneTreeiENSGT00390000011365.
HOGENOMiHOG000220838.
HOVERGENiHBG007211.
InParanoidiQ13283.
KOiK17265.
OMAiRVREQRI.
PhylomeDBiQ13283.
TreeFamiTF325464.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR002075. NTF2.
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]
PROSITEiPS50177. NTF2_DOMAIN. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13283-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY VHGGLDSNGK
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 GTFYDQAVVS NDMEEHLEEP VAEPEPDPEP
210 220 230 240 250
EPEQEPVSEI QEEKPEPVLE ETAPEDAQKS SSPAPADIAQ TVQEDLRTFS
260 270 280 290 300
WASVTSKNLP PSGAVPVTGI PPHVVKVPAS QPRPESKPES QIPPQRPQRD
310 320 330 340 350
QRVREQRINI PPQRGPRPIR EAGEQGDIEP RRMVRHPDSH QLFIGNLPHE
360 370 380 390 400
VDKSELKDFF QSYGNVVELR INSGGKLPNF GFVVFDDSEP VQKVLSNRPI
410 420 430 440 450
MFRGEVRLNV EEKKTRAARE GDRRDNRLRG PGGPRGGLGG GMRGPPRGGM
460
VQKPGFGVGR GLAPRQ
Length:466
Mass (Da):52,164
Last modified:November 1, 1996 - v1
Checksum:i0F9429D78E0C7F59
GO
Isoform 2 (identifier: Q13283-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     118-122: GSVAN → SLKKK
     123-466: Missing.

Show »
Length:122
Mass (Da):13,874
Checksum:iBC791D59A75533DB
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei118 – 1225GSVAN → SLKKK in isoform 2. 2 PublicationsVSP_056280
Alternative sequencei123 – 466344Missing in isoform 2. 2 PublicationsVSP_056281Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U32519 mRNA. Translation: AAB07787.1.
AK300098 mRNA. Translation: BAG61899.1.
BX647869 mRNA. Translation: CAI46065.1.
AC091982 Genomic DNA. No translation available.
BC006997 mRNA. Translation: AAH06997.1.
CCDSiCCDS4319.1. [Q13283-1]
RefSeqiNP_005745.1. NM_005754.2.
NP_938405.1. NM_198395.1.
XP_006714812.1. XM_006714749.1.
XP_006714813.1. XM_006714750.1.
UniGeneiHs.3353.
Hs.587054.

Genome annotation databases

EnsembliENST00000356245; ENSP00000348578; ENSG00000145907. [Q13283-1]
ENST00000394123; ENSP00000377681; ENSG00000145907. [Q13283-1]
ENST00000520177; ENSP00000427810; ENSG00000145907. [Q13283-2]
ENST00000522367; ENSP00000428926; ENSG00000145907. [Q13283-2]
GeneIDi10146.
KEGGihsa:10146.
UCSCiuc003lum.3. human. [Q13283-1]

Polymorphism databases

DMDMi14916572.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U32519 mRNA. Translation: AAB07787.1 .
AK300098 mRNA. Translation: BAG61899.1 .
BX647869 mRNA. Translation: CAI46065.1 .
AC091982 Genomic DNA. No translation available.
BC006997 mRNA. Translation: AAH06997.1 .
CCDSi CCDS4319.1. [Q13283-1 ]
RefSeqi NP_005745.1. NM_005754.2.
NP_938405.1. NM_198395.1.
XP_006714812.1. XM_006714749.1.
XP_006714813.1. XM_006714750.1.
UniGenei Hs.3353.
Hs.587054.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3Q90 X-ray 1.70 A/B 1-139 [» ]
4FCJ X-ray 1.62 A/B 1-139 [» ]
4FCM X-ray 2.69 A/B 1-139 [» ]
4IIA X-ray 3.30 A 11-139 [» ]
ProteinModelPortali Q13283.
SMRi Q13283. Positions 7-138, 341-406.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115448. 89 interactions.
IntActi Q13283. 55 interactions.
MINTi MINT-5002789.
STRINGi 9606.ENSP00000348578.

PTM databases

PhosphoSitei Q13283.

Polymorphism databases

DMDMi 14916572.

Proteomic databases

MaxQBi Q13283.
PaxDbi Q13283.
PeptideAtlasi Q13283.
PRIDEi Q13283.

Protocols and materials databases

DNASUi 10146.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356245 ; ENSP00000348578 ; ENSG00000145907 . [Q13283-1 ]
ENST00000394123 ; ENSP00000377681 ; ENSG00000145907 . [Q13283-1 ]
ENST00000520177 ; ENSP00000427810 ; ENSG00000145907 . [Q13283-2 ]
ENST00000522367 ; ENSP00000428926 ; ENSG00000145907 . [Q13283-2 ]
GeneIDi 10146.
KEGGi hsa:10146.
UCSCi uc003lum.3. human. [Q13283-1 ]

Organism-specific databases

CTDi 10146.
GeneCardsi GC05P151151.
HGNCi HGNC:30292. G3BP1.
HPAi HPA004052.
MIMi 608431. gene.
neXtProti NX_Q13283.
PharmGKBi PA162389105.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG324333.
GeneTreei ENSGT00390000011365.
HOGENOMi HOG000220838.
HOVERGENi HBG007211.
InParanoidi Q13283.
KOi K17265.
OMAi RVREQRI.
PhylomeDBi Q13283.
TreeFami TF325464.

Miscellaneous databases

ChiTaRSi G3BP1. human.
GeneWikii G3BP1.
GenomeRNAii 10146.
NextBioi 38391.
PROi Q13283.
SOURCEi Search...

Gene expression databases

Bgeei Q13283.
CleanExi HS_G3BP1.
ExpressionAtlasi Q13283. baseline and differential.
Genevestigatori Q13283.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR002075. NTF2.
IPR018222. Nuclear_transport_factor_2_euk.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF02136. NTF2. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50177. NTF2_DOMAIN. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Pericardium.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Adipose tissue.
  4. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Prostate.
  6. Cited for: PROTEIN SEQUENCE OF 2-13; 18-32; 37-59; 65-76; 108-132; 230-276; 308-314; 321-331; 336-370; 377-403; 430-443 AND 448-465, CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT ARG-435 AND ARG-460, PHOSPHORYLATION AT SER-231 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma, Colon carcinoma and Ovarian carcinoma.
  7. "Human DNA helicase VIII: a DNA and RNA helicase corresponding to the G3BP protein, an element of the ras transduction pathway."
    Costa M., Ochem A., Staub A., Falaschi A.
    Nucleic Acids Res. 27:817-821(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 248-257; 336-353; 394-403 AND 444-463, FUNCTION AS A HELICASE.
  8. "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: FUNCTION AS AN ENDORIBONUCLEASE, PHOSPHORYLATION AT SER-149 AND SER-232, MUTAGENESIS OF SER-149 AND SER-232.
  9. "Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific protease."
    Soncini C., Berdo I., Draetta G.
    Oncogene 20:3869-3879(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USP10.
  10. "The RasGAP-associated endoribonuclease G3BP assembles stress granules."
    Tourriere H., Chebli K., Zekri L., Courselaud B., Blanchard J.-M., Bertrand E., Tazi J.
    J. Cell Biol. 160:823-831(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECRUITMENT TO STRESS GRANULES, DIMERIZATION, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF SER-149.
  11. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  15. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  16. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  18. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143; SER-149; SER-232 AND SER-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "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].
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  24. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-376, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "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-149; SER-232 AND SER-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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-149 AND SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. Cited for: INTERACTION WITH RPTOR ANS SPAG5, SUBCELLULAR LOCATION.
  29. "Crystal structure of the NTF2 domain of ras GTPase-activating protein-binding protein 1."
    Structural genomics consortium (SGC)
    Submitted (FEB-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-139.

Entry informationi

Entry nameiG3BP1_HUMAN
AccessioniPrimary (citable) accession number: Q13283
Secondary accession number(s): Q5HYE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 155 of the entry and version 1 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3