Q13283 · G3BP1_HUMAN
- ProteinRas GTPase-activating protein-binding protein 1
- GeneG3BP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids466 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays an essential role in stress granule formation (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:34739333, PubMed:35977029, PubMed:36183834, PubMed:36279435, PubMed:36692217, PubMed:37379838).
Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:27022092, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:36279435, PubMed:37379838).
Promotes formation of stress granules phase-separated membraneless compartment by undergoing liquid-liquid phase separation (LLPS) upon unfolded RNA-binding: functions as a molecular switch that triggers RNA-dependent LLPS in response to a rise in intracellular free RNA concentrations (PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:34739333, PubMed:36279435, PubMed:36692217).
Also acts as an ATP- and magnesium-dependent helicase: unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency (PubMed:9889278).
Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA (PubMed:9889278).
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 (PubMed:9889278).
Plays an essential role in innate immunity by promoting CGAS and RIGI activity (PubMed:30510222, PubMed:30804210).
Participates in the DNA-triggered cGAS/STING pathway by promoting the DNA binding and activation of CGAS (PubMed:30510222).
Triggers the condensation of cGAS, a process probably linked to the formation of membrane-less organelles (PubMed:34779554).
Enhances also RIGI-induced type I interferon production probably by helping RIGI at sensing pathogenic RNA (PubMed:30804210).
May also act as a phosphorylation-dependent sequence-specific endoribonuclease in vitro: Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR (PubMed:11604510).
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
- ATP + H2O = ADP + H+ + phosphate
Cofactor
Activity regulation
Upon stress, polysomes disassemble and mRNAs are released in an unfolded protein-free state (PubMed:32302570, PubMed:32302571, PubMed:32302572).
Binding of unfolded mRNA to G3BP1 outcompetes the intramolecular interactions and RNA-bound G3BP1 adopts an expanded conformation in which the RG-rich region becomes exposed to engage in protein-protein and protein-RNA interactions, allowing physical cross-linking of RNA molecules to form protein-RNA condensates, leading to liquid-liquid phase separation (LLPS) (PubMed:32302570, PubMed:32302571, PubMed:32302572).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 325-326 | Cleavage; by human enterovirus 71 protease 3C | ||||
Sequence: QG |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRas GTPase-activating protein-binding protein 1
- EC number
- Short namesG3BP-1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13283
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Cytosolic and partially nuclear in resting cells (PubMed:11604510).
Recruited to stress granules in response to arsenite treatment (PubMed:12642610, PubMed:20180778).
The unphosphorylated form is recruited to stress granules (PubMed:12642610).
HRAS signaling contributes to this process by regulating G3BP dephosphorylation (PubMed:12642610).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 15 | Decreased interaction with USP10. | ||||
Sequence: F → W | ||||||
Mutagenesis | 33 | Abolished interaction with CAPRIN1 and ability to undergo liquid-liquid phase separation. Abolished interaction with USP10. | ||||
Sequence: F → W | ||||||
Mutagenesis | 36 | In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-50, R-59, R-64, R-76, R-123, R-353, R-357, R-376 and R-393. In 6KR; strongly decreased ubiquitination in response to heat shock, leading to decreased stress granule disassembly; when associated with R-50, R-59, R-64, R-76 and R-123. In 4KR; decreased ubiquitination in response to heat shock, leading to slightly decreased stress granule disassembly; when associated with R-50, R-59 and R-64. | ||||
Sequence: K → R | ||||||
Mutagenesis | 50 | In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-59, R-64, R-76, R-123, R-353, R-357, R-376 and R-393. In 6KR; strongly decreased ubiquitination in response to heat shock, leading to decreased stress granule disassembly; when associated with R-36, R-59, R-64, R-76 and R-123. In 4KR; decreased ubiquitination in response to heat shock, leading to slightly decreased stress granule disassembly; when associated with R-36, R-59 and R-64. | ||||
Sequence: K → R | ||||||
Mutagenesis | 59 | In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-64, R-76, R-123, R-353, R-357, R-376 and R-393. In 6KR; strongly decreased ubiquitination in response to heat shock, leading to decreased stress granule disassembly; when associated with R-36, R-50, R-64, R-76 and R-123. In 4KR; decreased ubiquitination in response to heat shock, leading to slightly decreased stress granule disassembly; when associated with R-36, R-50 and R-64. | ||||
Sequence: K → R | ||||||
Mutagenesis | 64 | In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-76, R-123, R-353, R-357, R-376 and R-393. In 6KR; strongly decreased ubiquitination in response to heat shock, leading to decreased stress granule disassembly; when associated with R-36, R-50, R-59, R-76 and R-123. In 4KR; decreased ubiquitination in response to heat shock, leading to slightly decreased stress granule disassembly; when associated with R-36, R-50 and R-59. | ||||
Sequence: K → R | ||||||
Mutagenesis | 76 | In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-64, R-123, R-353, R-357, R-376 and R-393. In 6KR; strongly decreased ubiquitination in response to heat shock, leading to decreased stress granule disassembly; when associated with R-36, R-50, R-59, R-64 and R-123. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_088949 | 78 | found in a patient with a neurodevelopmental disorder; uncertain significance; decreased function in stress granule formation shown by rescue assays in transfected G3BP1-deficient cells | |||
Sequence: R → C | ||||||
Mutagenesis | 123 | In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-64, R-76, R-353, R-357, R-376 and R-393. In 6KR; strongly decreased ubiquitination in response to heat shock, leading to decreased stress granule disassembly; when associated with R-36, R-50, R-59, R-64 and R-76. | ||||
Sequence: K → R | ||||||
Mutagenesis | 124 | Does not affect interaction with USP10. | ||||
Sequence: F → W | ||||||
Natural variant | VAR_088950 | 132 | found in a patient with a neurodevelopmental disorder; uncertain significance; decreased function in stress granule formation shown by rescue assays in transfected G3BP1-deficient cells | |||
Sequence: R → I | ||||||
Mutagenesis | 149 | Slightly increased ability to undergo liquid-liquid phase separation. Increased ability to undergo liquid-liquid phase separation; when associated with A-232. Cytoplasmic. | ||||
Sequence: S → A | ||||||
Mutagenesis | 149 | Mimics phosphorylation; decreased ability to undergo liquid-liquid phase separation. Cytoplasmic and nuclear; no assembly of stress granules; no homo-oligomerization. | ||||
Sequence: S → E | ||||||
Natural variant | VAR_088951 | 208 | found in a patient with a neurodevelopmental disorder; uncertain significance; decreased function in stress granule formation shown by rescue assays in transfected G3BP1-deficient cells | |||
Sequence: S → C | ||||||
Mutagenesis | 232 | Slightly increased ability to undergo liquid-liquid phase separation; when associated with A-149. Cytoplasmic. Partially nuclear; when associated with E-149. | ||||
Sequence: S → A | ||||||
Mutagenesis | 232 | Cytoplasmic. Partially nuclear; when associated with E-149. | ||||
Sequence: S → E | ||||||
Natural variant | VAR_088952 | 320 | found in a patient with a neurodevelopmental disorder; uncertain significance; decreased function in stress granule formation shown by rescue assays in transfected G3BP1-deficient cells | |||
Sequence: R → C | ||||||
Mutagenesis | 325 | Loss of cleavage by human enterovirus 71 protease 3C. | ||||
Sequence: Q → G | ||||||
Mutagenesis | 353 | In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-64, R-76, R-123,R-357, R-376 and R-393. | ||||
Sequence: K → R | ||||||
Mutagenesis | 357 | In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-64, R-76, R-123, R-353, R-376 and R-393. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_088953 | 366 | found in a patient with a neurodevelopmental disorder; uncertain significance; no effect on function in stress granule formation shown by rescue assays in transfected G3BP1-deficient cells | |||
Sequence: V → M | ||||||
Mutagenesis | 376 | In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-64, R-76, R-123, R-353, R-357 and R-393. | ||||
Sequence: K → R | ||||||
Mutagenesis | 380-382 | Abolished mRNA-binding and ability to undergo liquid-liquid phase separation. | ||||
Sequence: FGF → GDG | ||||||
Mutagenesis | 393 | In 10KR; abolished ubiquitination in response to heat shock, leading to decreased stress granule disassembly when associated with R-36, R-50, R-59, R-64, R-76, R-123, R-353, R-357 and R-376. | ||||
Sequence: K → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 554 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue (large scale data), cross-link, modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Chain | PRO_0000194798 | 2-466 | UniProt | Ras GTPase-activating protein-binding protein 1 | |||
Sequence: VMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQEDLRTFSWASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 36 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 50 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 56 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Cross-link | 59 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 64 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 76 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 119 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 123 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 125 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 143 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 143 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 149 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 149 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 230 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 231 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 232 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 232 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 241 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 250 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 250 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 253 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 253 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 256 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 353 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 357 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 373 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 373 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 376 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 376 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Cross-link | 376 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 393 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | |||||||
Modified residue | 429 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 435 | UniProt | Asymmetric dimethylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 435 | UniProt | Dimethylated arginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 435 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 447 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 460 | UniProt | Dimethylated arginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 460 | UniProt | Omega-N-methylarginine; alternate | ||||
Sequence: R | |||||||
Modified residue | 465 | UniProt | Omega-N-methylarginine | ||||
Sequence: R |
Post-translational modification
RASA1-dependent phosphorylation of Ser-149 induces a conformational change that prevents self-association (PubMed:11604510, PubMed:12642610).
Dephosphorylation after HRAS activation is required for stress granule assembly (PubMed:11604510, PubMed:12642610).
Ser-149 phosphorylation induces partial nuclear localization (PubMed:11604510).
In case of prolonged stress, ubiquitination by TRIM21 leads to autophagy-dependent degradation of G3BP1 via recruitment of ubiquitinated G3BP1 by SQSTM1 and/or CALCOCO2 to autophagosomes (PubMed:34739333, PubMed:36692217).
Cleaved by Foot-and-mouth disease virus; this cleavage suppresses the formation of cytoplasmic stress granules (PubMed:30404792).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP1 (By similarity).
Binds to the SH3 domain of Ras GTPase-activating protein (RASA1) in proliferating cells (By similarity).
No interaction in quiescent cells (By similarity).
Interacts (via NTF2 domain) with USP10; inhibiting stress granule formation by lowering G3BP1 valence (PubMed:11439350, PubMed:23279204, PubMed:27022092, PubMed:31981475, PubMed:32302570, PubMed:36183834, PubMed:36279435).
Interacts (via NTF2 domain) with CAPRIN1; promoting stress granule formation by lowering the saturation-concentration of G3BP1 (PubMed:17210633, PubMed:27022092, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:36183834, PubMed:36279435).
Interacts (via NTF2 domain) with UBAP2L; promoting stress granule formation (PubMed:32302570).
Associates (via RG-rich region) with 40S ribosome subunits (PubMed:27022092).
Interacts with RPTOR and SPAG5; this complex is increased by oxidative stress (PubMed:23953116).
Interacts with ATXN2L (PubMed:23209657).
Interacts with STYXL1 (PubMed:20180778).
Interacts with CGAS (via N-terminus); this interaction promotes the DNA-binding and activation of CGAS (PubMed:30510222, PubMed:34779554).
Interacts (via C-terminus) with RIGI (PubMed:30804210).
Interacts with PABPC1 (PubMed:23279204).
Interacts with QKI (isoforms QKI6 and QKI7); directing N7-methylguanine-containing mRNAs to stress granules (PubMed:37379838).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-133 | NTF2 | ||||
Sequence: VGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRY | ||||||
Region | 142-225 | Acidic disordered region | ||||
Sequence: VTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPE | ||||||
Region | 144-172 | Disordered | ||||
Sequence: EPQEESEEEVEEPEERQQTPEVVPDDSGT | ||||||
Region | 184-243 | Disordered | ||||
Sequence: EEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQ | ||||||
Compositional bias | 188-206 | Acidic residues | ||||
Sequence: EEPVAEPEPDPEPEPEQEP | ||||||
Compositional bias | 207-223 | Basic and acidic residues | ||||
Sequence: VSEIQEEKPEPVLEETA | ||||||
Compositional bias | 225-243 | Polar residues | ||||
Sequence: EDAQKSSSPAPADIAQTVQ | ||||||
Region | 255-329 | Disordered | ||||
Sequence: TSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEQGDIE | ||||||
Domain | 340-415 | RRM | ||||
Sequence: HQLFIGNLPHEVDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKT | ||||||
Region | 410-466 | RG-rich region | ||||
Sequence: VEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ | ||||||
Compositional bias | 413-430 | Basic and acidic residues | ||||
Sequence: KKTRAAREGDRRDNRLRG | ||||||
Region | 413-466 | Disordered | ||||
Sequence: KKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ |
Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q13283-1
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.
- Name1
- Length466
- Mass (Da)52,164
- Last updated1996-11-01 v1
- Checksum0F9429D78E0C7F59
Q13283-2
- Name2
Computationally mapped potential isoform sequences
There are 34 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A7P0P2U7 | A0A7P0P2U7_HUMAN | G3BP1 | 367 | ||
A0A7I2YQC2 | A0A7I2YQC2_HUMAN | G3BP1 | 17 | ||
A0A7I2YQF2 | A0A7I2YQF2_HUMAN | G3BP1 | 85 | ||
A0A7I2YQB1 | A0A7I2YQB1_HUMAN | G3BP1 | 61 | ||
A0A7I2YQM1 | A0A7I2YQM1_HUMAN | G3BP1 | 102 | ||
A0A7I2YQN9 | A0A7I2YQN9_HUMAN | G3BP1 | 426 | ||
A0A7I2YQH0 | A0A7I2YQH0_HUMAN | G3BP1 | 134 | ||
A0A7I2YQU8 | A0A7I2YQU8_HUMAN | G3BP1 | 334 | ||
A0A7I2YQP3 | A0A7I2YQP3_HUMAN | G3BP1 | 36 | ||
A0A7I2YQQ8 | A0A7I2YQQ8_HUMAN | G3BP1 | 63 | ||
A0A7I2YQR4 | A0A7I2YQR4_HUMAN | G3BP1 | 68 | ||
A0A7I2V274 | A0A7I2V274_HUMAN | G3BP1 | 40 | ||
E5RIF8 | E5RIF8_HUMAN | G3BP1 | 106 | ||
E5RJU8 | E5RJU8_HUMAN | G3BP1 | 153 | ||
E5RH42 | E5RH42_HUMAN | G3BP1 | 117 | ||
E5RH00 | E5RH00_HUMAN | G3BP1 | 37 | ||
E5RI46 | E5RI46_HUMAN | G3BP1 | 31 | ||
A0A7I2V326 | A0A7I2V326_HUMAN | G3BP1 | 110 | ||
A0A7I2V2X7 | A0A7I2V2X7_HUMAN | G3BP1 | 49 | ||
A0A7I2V2S5 | A0A7I2V2S5_HUMAN | G3BP1 | 170 | ||
A0A7I2V2V1 | A0A7I2V2V1_HUMAN | G3BP1 | 151 | ||
A0A7I2V3C4 | A0A7I2V3C4_HUMAN | G3BP1 | 66 | ||
A0A7I2V3Y4 | A0A7I2V3Y4_HUMAN | G3BP1 | 59 | ||
A0A7I2V3V2 | A0A7I2V3V2_HUMAN | G3BP1 | 39 | ||
A0A7I2V494 | A0A7I2V494_HUMAN | G3BP1 | 54 | ||
A0A7I2V496 | A0A7I2V496_HUMAN | G3BP1 | 61 | ||
A0A7I2V4D8 | A0A7I2V4D8_HUMAN | G3BP1 | 49 | ||
A0A7I2V548 | A0A7I2V548_HUMAN | G3BP1 | 158 | ||
A0A7I2V565 | A0A7I2V565_HUMAN | G3BP1 | 74 | ||
A0A7I2V533 | A0A7I2V533_HUMAN | G3BP1 | 37 | ||
A0A7I2V4Y8 | A0A7I2V4Y8_HUMAN | G3BP1 | 56 | ||
A0A7I2V5H1 | A0A7I2V5H1_HUMAN | G3BP1 | 114 | ||
A0A7I2V5M7 | A0A7I2V5M7_HUMAN | G3BP1 | 476 | ||
A0A7I2V651 | A0A7I2V651_HUMAN | G3BP1 | 304 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_056280 | 118-122 | in isoform 2 | |||
Sequence: GSVAN → SLKKK | ||||||
Alternative sequence | VSP_056281 | 123-466 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 188-206 | Acidic residues | ||||
Sequence: EEPVAEPEPDPEPEPEQEP | ||||||
Compositional bias | 207-223 | Basic and acidic residues | ||||
Sequence: VSEIQEEKPEPVLEETA | ||||||
Compositional bias | 225-243 | Polar residues | ||||
Sequence: EDAQKSSSPAPADIAQTVQ | ||||||
Compositional bias | 413-430 | Basic and acidic residues | ||||
Sequence: KKTRAAREGDRRDNRLRG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U32519 EMBL· GenBank· DDBJ | AAB07787.1 EMBL· GenBank· DDBJ | mRNA | ||
AK300098 EMBL· GenBank· DDBJ | BAG61899.1 EMBL· GenBank· DDBJ | mRNA | ||
BX647869 EMBL· GenBank· DDBJ | CAI46065.1 EMBL· GenBank· DDBJ | mRNA | ||
AC091982 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC006997 EMBL· GenBank· DDBJ | AAH06997.1 EMBL· GenBank· DDBJ | mRNA |