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Q13283 (G3BP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras GTPase-activating protein-binding protein 1

Short name=G3BP-1
EC=3.6.4.12
EC=3.6.4.13
Alternative name(s):
ATP-dependent DNA helicase VIII
Short name=hDH VIII
GAP SH3 domain-binding protein 1
Gene names
Name:G3BP1
Synonyms:G3BP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.5

Catalytic activity

ATP + H2O = ADP + phosphate.

Cofactor

Magnesium. Required for helicase activity.

Subunit structure

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. Ref.6 Ref.7 Ref.25

Subcellular location

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. Ref.7 Ref.25

Tissue specificity

Ubiquitous.

Domain

The NTF2 domain mediates multimerization.

Post-translational modification

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. Ref.3 Ref.5 Ref.7

Arg-435 is dimethylated, probably to asymmetric dimethylarginine. Ref.3

Sequence similarities

Contains 1 NTF2 domain.

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   LigandATP-binding
DNA-binding
Nucleotide-binding
RNA-binding
   Molecular functionEndonuclease
Helicase
Hydrolase
Nuclease
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Traceable author statement Ref.4. Source: GOC

DNA duplex unwinding

Traceable author statement Ref.4. Source: GOC

Ras protein signal transduction

Traceable author statement Ref.1. Source: ProtInc

negative regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic stress granule

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Traceable author statement Ref.4. Source: ProtInc

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Traceable author statement Ref.4. Source: ProtInc

ATP-dependent RNA helicase activity

Traceable author statement Ref.4. Source: ProtInc

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

endonuclease activity

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA binding

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 466465Ras GTPase-activating protein-binding protein 1
PRO_0000194798

Regions

Domain11 – 133123NTF2
Domain340 – 41576RRM
Compositional bias144 – 22582Glu-rich
Compositional bias430 – 46132Gly-rich

Amino acid modifications

Modified residue1431Phosphothreonine Ref.16
Modified residue1491Phosphoserine Ref.5 Ref.9 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.22 Ref.24
Modified residue2311Phosphoserine Ref.3
Modified residue2321Phosphoserine Ref.3 Ref.5 Ref.16 Ref.20 Ref.22 Ref.24
Modified residue3731Phosphoserine Ref.16 Ref.22
Modified residue3761N6-acetyllysine Ref.21
Modified residue4351Dimethylated arginine; alternate Ref.3
Modified residue4351Omega-N-methylarginine; alternate Ref.3
Modified residue4601Dimethylated arginine; alternate Ref.3
Modified residue4601Omega-N-methylated arginine; alternate Ref.3

Experimental info

Mutagenesis1491S → A: Cytoplasmic; no effect on stress granule assembly. Ref.5 Ref.7
Mutagenesis1491S → E: Cytoplasmic and nuclear; no assembly of stress granules; no homo-oligomerization. Ref.5 Ref.7
Mutagenesis2321S → A: Cytoplasmic. Partially nuclear; when associated with E-149. Ref.5
Mutagenesis2321S → E: Cytoplasmic. Partially nuclear; when associated with E-149. Ref.5

Secondary structure

........................ 466
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13283 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0F9429D78E0C7F59

FASTA46652,164
        10         20         30         40         50         60 
MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY VHGGLDSNGK PADAVYGQKE 

        70         80         90        100        110        120 
IHRKVMSQNF TNCHTKIRHV DAHATLNDGV VVQVMGLLSN NNQALRRFMQ TFVLAPEGSV 

       130        140        150        160        170        180 
ANKFYVHNDI FRYQDEVFGG FVTEPQEESE EEVEEPEERQ QTPEVVPDDS GTFYDQAVVS 

       190        200        210        220        230        240 
NDMEEHLEEP VAEPEPDPEP EPEQEPVSEI QEEKPEPVLE ETAPEDAQKS SSPAPADIAQ 

       250        260        270        280        290        300 
TVQEDLRTFS WASVTSKNLP PSGAVPVTGI PPHVVKVPAS QPRPESKPES QIPPQRPQRD 

       310        320        330        340        350        360 
QRVREQRINI PPQRGPRPIR EAGEQGDIEP RRMVRHPDSH QLFIGNLPHE VDKSELKDFF 

       370        380        390        400        410        420 
QSYGNVVELR INSGGKLPNF GFVVFDDSEP VQKVLSNRPI MFRGEVRLNV EEKKTRAARE 

       430        440        450        460 
GDRRDNRLRG PGGPRGGLGG GMRGPPRGGM VQKPGFGVGR GLAPRQ 

« Hide

References

« Hide 'large scale' references
[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].
Tissue: Placenta.
[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].
Tissue: Prostate.
[3]Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Calvo F., Zebisch A., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
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.
[4]"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.
[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: FUNCTION AS AN ENDORIBONUCLEASE, PHOSPHORYLATION AT SER-149 AND SER-232, MUTAGENESIS OF SER-149 AND SER-232.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
[17]"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.
[18]"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].
[19]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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.
[21]"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].
[22]"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.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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].
[25]"Inhibition of mTORC1 by astrin and stress granules prevents apoptosis in cancer cells."
Thedieck K., Holzwarth B., Prentzell M.T., Boehlke C., Klasener K., Ruf S., Sonntag A.G., Maerz L., Grellscheid S.N., Kremmer E., Nitschke R., Kuehn E.W., Jonker J.W., Groen A.K., Reth M., Hall M.N., Baumeister R.
Cell 154:859-874(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RPTOR ANS SPAG5, SUBCELLULAR LOCATION.
[26]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U32519 mRNA. Translation: AAB07787.1.
BC006997 mRNA. Translation: AAH06997.1.
RefSeqNP_005745.1. NM_005754.2.
NP_938405.1. NM_198395.1.
UniGeneHs.587054.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q90X-ray1.70A/B1-139[»]
4FCJX-ray1.62A/B1-139[»]
4FCMX-ray2.69A/B1-139[»]
4IIAX-ray3.30A11-139[»]
ProteinModelPortalQ13283.
SMRQ13283. Positions 7-138, 341-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115448. 86 interactions.
IntActQ13283. 55 interactions.
MINTMINT-5002789.
STRING9606.ENSP00000348578.

PTM databases

PhosphoSiteQ13283.

Polymorphism databases

DMDM14916572.

Proteomic databases

PaxDbQ13283.
PeptideAtlasQ13283.
PRIDEQ13283.

Protocols and materials databases

DNASU10146.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356245; ENSP00000348578; ENSG00000145907.
ENST00000394123; ENSP00000377681; ENSG00000145907.
GeneID10146.
KEGGhsa:10146.
UCSCuc003lum.3. human.

Organism-specific databases

CTD10146.
GeneCardsGC05P151151.
HGNCHGNC:30292. G3BP1.
HPAHPA004052.
MIM608431. gene.
neXtProtNX_Q13283.
PharmGKBPA162389105.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG324333.
HOGENOMHOG000220838.
HOVERGENHBG007211.
InParanoidQ13283.
KOK17265.
OMAYDQAVVS.
PhylomeDBQ13283.
TreeFamTF325464.

Gene expression databases

ArrayExpressQ13283.
BgeeQ13283.
CleanExHS_G3BP1.
GenevestigatorQ13283.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR002075. NTF2.
IPR018222. Nuclear_transport_factor_2_euk.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF02136. NTF2. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50177. NTF2_DOMAIN. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSG3BP1. human.
GeneWikiG3BP1.
GenomeRNAi10146.
NextBio38391.
PROQ13283.
SOURCESearch...

Entry information

Entry nameG3BP1_HUMAN
AccessionPrimary (citable) accession number: Q13283
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM