Q13283 · G3BP1_HUMAN

  • Protein
    Ras GTPase-activating protein-binding protein 1
  • Gene
    G3BP1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Protein involved in various processes, such as stress granule formation and innate immunity (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:30510222, PubMed:30804210).
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

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Mg2+ is required for helicase activity.

Activity regulation

Under physiological conditions, G3BP1 adopts a compact state that is stabilized by intramolecular interactions between the RG-rich and the acidic regions that inhibit phase separation (PubMed:32302570, PubMed:32302571, PubMed:32302572).
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.

TypeIDPosition(s)Description
Site325-326Cleavage; by human enterovirus 71 protease 3C

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytoplasmic stress granule
Cellular Componentcytosol
Cellular Componentfocal adhesion
Cellular Componentnucleus
Cellular Componentperikaryon
Cellular Componentribonucleoprotein complex
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionDNA binding
Molecular FunctionDNA helicase activity
Molecular FunctionDNA/RNA helicase activity
Molecular Functionendonuclease activity
Molecular Functionmolecular condensate scaffold activity
Molecular FunctionmRNA binding
Molecular Functionribosomal small subunit binding
Molecular FunctionRNA binding
Molecular FunctionRNA helicase activity
Biological Processdefense response to virus
Biological Processinnate immune response
Biological Processnegative regulation of canonical Wnt signaling pathway
Biological Processpositive regulation of stress granule assembly
Biological Processpositive regulation of type I interferon production
Biological ProcessRas protein signal transduction
Biological Processstress granule assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ras GTPase-activating protein-binding protein 1
  • EC number
  • Short names
    G3BP-1
  • Alternative names
    • ATP-dependent DNA helicase VIII (hDH VIII)
    • GAP SH3 domain-binding protein 1

Gene names

    • Name
      G3BP1
    • Synonyms
      G3BP

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q13283
  • Secondary accessions
    • Q5HYE9

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm, cytosol
Perikaryon
Nucleus
Note: Cytoplasmic in proliferating cells (PubMed:11604510).
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

Disease & Variants

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis15Decreased interaction with USP10.
Mutagenesis33Abolished interaction with CAPRIN1 and ability to undergo liquid-liquid phase separation. Abolished interaction with USP10.
Mutagenesis36In 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.
Mutagenesis50In 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.
Mutagenesis59In 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.
Mutagenesis64In 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.
Mutagenesis76In 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.
Natural variantVAR_08894978found in a patient with a neurodevelopmental disorder; uncertain significance; decreased function in stress granule formation shown by rescue assays in transfected G3BP1-deficient cells
Mutagenesis123In 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.
Mutagenesis124Does not affect interaction with USP10.
Natural variantVAR_088950132found in a patient with a neurodevelopmental disorder; uncertain significance; decreased function in stress granule formation shown by rescue assays in transfected G3BP1-deficient cells
Mutagenesis149Slightly increased ability to undergo liquid-liquid phase separation. Increased ability to undergo liquid-liquid phase separation; when associated with A-232. Cytoplasmic.
Mutagenesis149Mimics phosphorylation; decreased ability to undergo liquid-liquid phase separation. Cytoplasmic and nuclear; no assembly of stress granules; no homo-oligomerization.
Natural variantVAR_088951208found in a patient with a neurodevelopmental disorder; uncertain significance; decreased function in stress granule formation shown by rescue assays in transfected G3BP1-deficient cells
Mutagenesis232Slightly increased ability to undergo liquid-liquid phase separation; when associated with A-149. Cytoplasmic. Partially nuclear; when associated with E-149.
Mutagenesis232Cytoplasmic. Partially nuclear; when associated with E-149.
Natural variantVAR_088952320found in a patient with a neurodevelopmental disorder; uncertain significance; decreased function in stress granule formation shown by rescue assays in transfected G3BP1-deficient cells
Mutagenesis325Loss of cleavage by human enterovirus 71 protease 3C.
Mutagenesis353In 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.
Mutagenesis357In 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.
Natural variantVAR_088953366found 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
Mutagenesis376In 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.
Mutagenesis380-382Abolished mRNA-binding and ability to undergo liquid-liquid phase separation.
Mutagenesis393In 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.

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.

Go to variant viewer

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.

TypeIDPosition(s)SourceDescription
Initiator methionine1UniProtRemoved
ChainPRO_00001947982-466UniProtRas GTPase-activating protein-binding protein 1
Modified residue (large scale data)7PRIDEPhosphoserine
Cross-link36UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue (large scale data)47PRIDEPhosphoserine
Cross-link50UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue (large scale data)56PRIDEPhosphotyrosine
Cross-link59UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link64UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link76UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue (large scale data)119PRIDEPhosphoserine
Cross-link123UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue (large scale data)125PRIDEPhosphotyrosine
Modified residue143UniProtPhosphothreonine
Modified residue (large scale data)143PRIDEPhosphothreonine
Modified residue149UniProtPhosphoserine
Modified residue (large scale data)149PRIDEPhosphoserine
Modified residue (large scale data)162PRIDEPhosphothreonine
Modified residue (large scale data)230PRIDEPhosphoserine
Modified residue231UniProtPhosphoserine
Modified residue (large scale data)231PRIDEPhosphoserine
Modified residue232UniProtPhosphoserine
Modified residue (large scale data)232PRIDEPhosphoserine
Modified residue (large scale data)241PRIDEPhosphothreonine
Modified residue250UniProtPhosphoserine
Modified residue (large scale data)250PRIDEPhosphoserine
Modified residue253UniProtPhosphoserine
Modified residue (large scale data)253PRIDEPhosphoserine
Modified residue (large scale data)256PRIDEPhosphoserine
Cross-link353UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link357UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residue373UniProtPhosphoserine
Modified residue (large scale data)373PRIDEPhosphoserine
Modified residue376UniProtN6-acetyllysine; alternate
Cross-link376UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Cross-link376UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link393UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residue429UniProtAsymmetric dimethylarginine
Modified residue435UniProtAsymmetric dimethylarginine; alternate
Modified residue435UniProtDimethylated arginine; alternate
Modified residue435UniProtOmega-N-methylarginine; alternate
Modified residue447UniProtOmega-N-methylarginine
Modified residue460UniProtDimethylated arginine; alternate
Modified residue460UniProtOmega-N-methylarginine; alternate
Modified residue465UniProtOmega-N-methylarginine

Post-translational modification

Phosphorylation of the acidic disordered region regulates stress granule assembly (PubMed:32302571, PubMed:32302572).
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).
Ubiquitinated by TRIM21 via 'Lys-63'-linked polyubiquitination in the NTF2 domain in response to heat shock, leading to stress granule disassembly: ubiquitination promotes interaction with the FAF2 adapter, followed by interaction with VCP, which extracts G3BP1 from stress granules, leading to stress granule disassembly (PubMed:34739333, PubMed:36692217).
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).
(Microbial infection) Cleaved by human enterovirus 71; this cleavage induces the disassembly of cytoplasmic stress granules (PubMed:30006004).
Cleaved by Foot-and-mouth disease virus; this cleavage suppresses the formation of cytoplasmic stress granules (PubMed:30404792).
Arg-435 is dimethylated, probably to asymmetric dimethylarginine.
(Microbial infection) Cleaved by Encephalomyocarditis virus protease 3C; this cleavage suppresses the formation of cytoplasmic stress granules.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Homodimer and oligomer (PubMed:12642610, PubMed:24324649).
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).
(Microbial infection) Interacts with Semliki forest virus non-structural protein 3 (via C-terminus); this interaction inhibits the formation of stress granules on viral mRNAs and the nsp3-G3BP1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes.
(Microbial infection) Interacts with Chikungunya virus non-structural protein 3 (via C-terminus); this interaction inhibits the formation of stress granules on viral mRNAs and the nsp3-G3BP1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes.
(Microbial infection) Interacts with Sindbis virus non-structural protein 3 (via C-terminus); this interaction inhibits the formation of stress granules on viral mRNAs and the nsp3-G3BP1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes.
(Microbial infection) Interacts with Zika virus capsid protein C; this interaction is probably linked to the inhibition of stress granules formation by the virus.
(Microbial infection) Interacts with reovirus type 2 protein sigma-NS; this interaction induces the relocalization of G3BP1 to the outer periphery of sigma-NS/mu-Ns viral factories and is probably involved in the suppression of the integrated stress response by the virus.

Binary interactions

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain11-133NTF2
Region142-225Acidic disordered region
Region144-172Disordered
Region184-243Disordered
Compositional bias188-206Acidic residues
Compositional bias207-223Basic and acidic residues
Compositional bias225-243Polar residues
Region255-329Disordered
Domain340-415RRM
Region410-466RG-rich region
Compositional bias413-430Basic and acidic residues
Region413-466Disordered

Domain

Can mediate both protein-protein and protein-RNA interactions via the NTF2 domain and RNA-binding domain RRM; protein-protein and protein-RNA interactions are essential for undergoing liquid-liquid phase separation (LLPS).
The acidic disordered region acts as a negative regulator of phase separation.
The NTF2 domain mediates interaction with CAPRIN1 and USP10 regulators, thereby regulating assembly of stress granules.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    466
  • Mass (Da)
    52,164
  • Last updated
    1996-11-01 v1
  • Checksum
    0F9429D78E0C7F59
MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQEDLRTFSWASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ

Q13283-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 34 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A7P0P2U7A0A7P0P2U7_HUMANG3BP1367
A0A7I2YQC2A0A7I2YQC2_HUMANG3BP117
A0A7I2YQF2A0A7I2YQF2_HUMANG3BP185
A0A7I2YQB1A0A7I2YQB1_HUMANG3BP161
A0A7I2YQM1A0A7I2YQM1_HUMANG3BP1102
A0A7I2YQN9A0A7I2YQN9_HUMANG3BP1426
A0A7I2YQH0A0A7I2YQH0_HUMANG3BP1134
A0A7I2YQU8A0A7I2YQU8_HUMANG3BP1334
A0A7I2YQP3A0A7I2YQP3_HUMANG3BP136
A0A7I2YQQ8A0A7I2YQQ8_HUMANG3BP163
A0A7I2YQR4A0A7I2YQR4_HUMANG3BP168
A0A7I2V274A0A7I2V274_HUMANG3BP140
E5RIF8E5RIF8_HUMANG3BP1106
E5RJU8E5RJU8_HUMANG3BP1153
E5RH42E5RH42_HUMANG3BP1117
E5RH00E5RH00_HUMANG3BP137
E5RI46E5RI46_HUMANG3BP131
A0A7I2V326A0A7I2V326_HUMANG3BP1110
A0A7I2V2X7A0A7I2V2X7_HUMANG3BP149
A0A7I2V2S5A0A7I2V2S5_HUMANG3BP1170
A0A7I2V2V1A0A7I2V2V1_HUMANG3BP1151
A0A7I2V3C4A0A7I2V3C4_HUMANG3BP166
A0A7I2V3Y4A0A7I2V3Y4_HUMANG3BP159
A0A7I2V3V2A0A7I2V3V2_HUMANG3BP139
A0A7I2V494A0A7I2V494_HUMANG3BP154
A0A7I2V496A0A7I2V496_HUMANG3BP161
A0A7I2V4D8A0A7I2V4D8_HUMANG3BP149
A0A7I2V548A0A7I2V548_HUMANG3BP1158
A0A7I2V565A0A7I2V565_HUMANG3BP174
A0A7I2V533A0A7I2V533_HUMANG3BP137
A0A7I2V4Y8A0A7I2V4Y8_HUMANG3BP156
A0A7I2V5H1A0A7I2V5H1_HUMANG3BP1114
A0A7I2V5M7A0A7I2V5M7_HUMANG3BP1476
A0A7I2V651A0A7I2V651_HUMANG3BP1304

Features

Showing features for alternative sequence, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_056280118-122in isoform 2
Alternative sequenceVSP_056281123-466in isoform 2
Compositional bias188-206Acidic residues
Compositional bias207-223Basic and acidic residues
Compositional bias225-243Polar residues
Compositional bias413-430Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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