Q13283 (G3BP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 G3BP By similarity. Interacts with USP10, and may regulate it. Forms homodimers and oligomers. Ref.6 Ref.7
Subcellular location	Cytoplasm. Cytoplasm › cytosol. 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
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 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Arg-435 is dimethylated, probably to asymmetric dimethylarginine. Ref.3 Ref.8
Sequence similarities	Contains 1 NTF2 domain. Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Ligand	ATP-binding DNA-binding Nucleotide-binding RNA-binding
Molecular function	Endonuclease Helicase Hydrolase Nuclease
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	Ras protein signal transduction Traceable author statement. Source: ProtInc transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Traceable author statement. Source: ProtInc plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent DNA helicase activity Traceable author statement. Source: ProtInc ATP-dependent RNA helicase activity Traceable author statement. Source: ProtInc DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 466

465

Ras GTPase-activating protein-binding protein 1

PRO_0000194798

Regions

Domain

11 – 133

123

NTF2

Domain

340 – 415

76

RRM

Compositional bias

144 – 225

82

Glu-rich

Compositional bias

430 – 461

32

Gly-rich

Sites

Site

2

1

Not acetylated

Amino acid modifications

Modified residue

143

1

Phosphothreonine Ref.20

Modified residue

149

1

Phosphoserine Ref.5 Ref.11 Ref.12 Ref.15 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24

Modified residue

230

1

Phosphoserine Ref.16 Ref.23

Modified residue

231

1

Phosphoserine Ref.3 Ref.16 Ref.17 Ref.22

Modified residue

232

1

Phosphoserine Ref.3 Ref.5 Ref.9 Ref.10 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24

Modified residue

268

1

Phosphothreonine By similarity

Modified residue

373

1

Phosphoserine Ref.20

Modified residue

376

1

N6-acetyllysine Ref.25

Modified residue

435

1

Dimethylated arginine; alternate Ref.3 Ref.8

Modified residue

435

1

Omega-N-methylarginine; alternate Ref.3 Ref.8

Modified residue

447

1

Omega-N-methylated arginine Ref.8

Modified residue

460

1

Dimethylated arginine; alternate Ref.3 Ref.8

Modified residue

460

1

Omega-N-methylated arginine; alternate Ref.3 Ref.8

Modified residue

465

1

Omega-N-methylated arginine Ref.8

Experimental info

Mutagenesis

149

1

S → A: Cytoplasmic; no effect on stress granule assembly. Ref.5 Ref.7

Mutagenesis

149

1

S → E: Cytoplasmic and nuclear; no assembly of stress granules; no homo-oligomerization. Ref.5 Ref.7

Mutagenesis

232

1

S → A: Cytoplasmic. Partially nuclear; when associated with E-149. Ref.5

Mutagenesis

232

1

S → E: Cytoplasmic. Partially nuclear; when associated with E-149. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

466

Helix Strand Turn

Details...

Turn

8 – 10

3

Helix

14 – 25

12

Helix

27 – 33

7

Beta strand

39 – 41

3

Helix

59 – 67

9

Beta strand

74 – 83

10

Beta strand

91 – 95

5

Beta strand

97 – 99

3

Beta strand

108 – 116

9

Beta strand

124 – 134

11

Sequences

	Sequence		Length	Mass (Da)
	Q13283 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0F9429D78E0C7F59	FASTA	466	52,164
	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

References

	« Hide 'large scale' referencesShow '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: 8649363] [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: 15489334] [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, LACK OF N-TERMINAL ACETYLATION, METHYLATION AT ARG-435 AND ARG-460, PHOSPHORYLATION AT SER-231 AND SER-232, 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: 9889278] [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: 11604510] [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: 11439350] [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: 12642610] [Abstract] Cited for: RECRUITMENT TO STRESS GRANULES, DIMERIZATION, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF SER-149.
[8]	"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC." Ong S.E., Mittler G., Mann M. Nat. Methods 1:119-126(2004) [PubMed: 15782174] [Abstract] Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-435; ARG-447; ARG-460 AND ARG-465, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[13]	"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: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, MASS SPECTROMETRY. Tissue: Prostate cancer.
[14]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-231 AND SER-232, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-232, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-232, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-232, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143; SER-149; SER-232 AND SER-373, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, MASS SPECTROMETRY. Tissue: Liver.
[22]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-231 AND SER-232, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[23]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230 AND SER-232, MASS SPECTROMETRY.
[24]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-232, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-376, MASS SPECTROMETRY.
[26]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]	"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.

IPI

IPI00012442.

RefSeq

NP_005745.1. NM_005754.2.
NP_938405.1. NM_198395.1.

UniGene

Hs.587054.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3Q90	X-ray	1.70	A/B	1-139	[»]

ProteinModelPortal

Q13283.

SMR

Q13283. Positions 1-139, 339-417.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13283. 38 interactions.

MINT

MINT-5002789.

STRING

Q13283.

PTM databases

PhosphoSite

Q13283.

Polymorphism databases

DMDM

14916572.

Proteomic databases

PeptideAtlas

Q13283.

PRIDE

Q13283.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356245; ENSP00000348578; ENSG00000145907.
ENST00000394123; ENSP00000377681; ENSG00000145907.

GeneID

10146.

KEGG

hsa:10146.

UCSC

uc003lum.1. human.

Organism-specific databases

CTD

10146.

GeneCards

GC05P151151.

H-InvDB

HIX0005333.

HGNC

HGNC:30292. G3BP1.

HPA

HPA004052.

MIM

608431. gene.

neXtProt

NX_Q13283.

PharmGKB

PA162389105.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14386.

HOGENOM

HBG445300.

HOVERGEN

HBG007211.

InParanoid

Q13283.

OMA

VVSNDME.

OrthoDB

EOG4XWFZ0.

PhylomeDB

Q13283.

Gene expression databases

ArrayExpress

Q13283.

Bgee

Q13283.

CleanEx

HS_G3BP1.

Genevestigator

Q13283.

GermOnline

ENSG00000145907. Homo sapiens.

Family and domain databases

InterPro

IPR002075. NTF2.
IPR018222. Nuclear_transport_factor_2_euk.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Gene3D

G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.

Pfam

PF02136. NTF2. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50177. NTF2_DOMAIN. 1 hit.
PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

38391.

SOURCE

Search...

Entry information

Entry name

G3BP1_HUMAN

Accession

Primary (citable) accession number: Q13283

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2001
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.