FUS3 / YBL016W

Protein Help

Protein Overview

Protein abundance data, domains, shared domains with other proteins, protein sequence retrieval for various strains, sequence-based physico-chemical proterties, phosphorylation sites, and external identifiers for the protein.

Aliases
DAC2

Fujimura HA (1992)

Protein Product
mitogen-activated serine/threonine-protein kinase FUS3
Description
Mitogen-activated serine/threonine protein kinase involved in mating; phosphoactivated by Ste7p; substrates include Ste12p, Far1p, Bni1p, Sst2p; inhibits invasive growth during mating by phosphorylating Tec1p, promoting its; inhibits recruitment of Ste5p, Cdc42p-mediated asymmetry and mating morphogenesis

Experimental Data

Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

Gene Experiment Result Reference

Domains and Classification

Collection of computationally identified domains and motifs, as determined by InterProScan analysis; includes protein coordinates for the domain, a domain Description, a Source and corresponding accession ID, and the number of S. cerevisiae genes that share the same domain.

Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

Gene Protein Coordinates Accession ID Description Source No. of Genes
with Domain

Domain Locations

Visual representation of the locations of the domains within the protein, as listed in the Domains and Classification table. Each row displays the domain(s) derived from a different Source, with domains color-coded according to this Source.

Scroll over a domain to view its exact coordinates and its Description.

Shared Domains

This diagram displays domains (colored squares) shared between the given protein (yellow circle) and other proteins (gray circles); the domains are color-coded according to their source, as displayed in the Domain Locations table, above.

Reset

Click on a gene or domain name to go to its specific page within SGD; drag any of the gene or domain objects around within the visualization for easier viewing; click “Reset” to automatically redraw the diagram.

Sequence

Protein sequence for the given gene in S288C and other strains, when available. Amino acids displayed in red represent phosphorylation sites, as curated by PhosphoGRID. More detailed evidence for these phosphorylation sites is presented in the Phosphorylation Sites table, located just below the protein sequence.

Use the pull-down menu under "Strain" to select the sequence for a specific strain. The sequence for that strain will appear and can then be downloaded as a .txt file. Phosphorylated residues, as curated by PhosphoGRID, are shown in red if the residues are present in the selected strain, and are further detailed in the "Phosphorylation Sites" table below the sequence. Note that a residue marked as phosphorylated has not necessarily been shown to be phosphorylated in a specific strain.

* Red amino acids indicate phosphorylation sites. More information below.

Phosphorylation Sites -

Phosphorylation sites for the protein in the selected strain, based on the presence of a residue in the specific strain, as inferred from experimental evidence curated by PhosphoGRID.

Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

Gene Site Site Functions Kinases Source

Sequence-Based Physico-chemical Properties - S288C

Calculated protein properties, including amino acid composition, length, coding region calculations, and atomic composition.

Amino Acid Composition

Sort table using the arrow to the right of a column header to sort by that column; download all properties as a .txt file using the "Download Properties" button.

Amino Acid Frequency Percentage

Physical Details

Length (a.a):
Molecular Weight (Da):
Isoelectric Point (pl):
Formula:
Aliphatic Index:
Instability Index:

Coding Region Translation Calculations

Codon Bias:
Codon Adaptation Index:
Frequence of Optimal Codons:
Hydropathicity of Protein:
Aromaticity Score:

Extinction Coefficients at 280nm

ALL Cys residues appear as half cystines:
NO Cys residues appear as half cystines:

Atomic Composition

Sort table using the arrow to the right of a column header to sort by that column; download all properties as a .txt file using the "Download Properties" button.

Atom Frequency Percentage

External Identifiers

List of external identifiers for the protein from various database sources.

Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.

External ID Source

Resources