U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

LOC106582539 beta-1,4-galactosyltransferase 3 [ Salmo salar (Atlantic salmon) ]

Gene ID: 106582539, updated on 30-Nov-2023

Summary

Go to the top of the page Help
Gene symbol
LOC106582539
Gene description
beta-1,4-galactosyltransferase 3
See related
Ensembl:ENSSSAG00000068005
Gene type
protein coding
RefSeq status
MODEL
Organism
Salmo salar
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes; Salmonidae; Salmoninae; Salmo
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
See LOC106582539 in Genome Data Viewer
Location:
chromosome: ssa02
Exon count:
9
Annotation release Status Assembly Chr Location
102 current Ssal_v3.1 (GCF_905237065.1) ssa02 NC_059443.1 (38029257..38058320)
100 previous assembly ICSASG_v2 (GCF_000233375.1) ssa02 NC_027301.1 (26868613..26896957)

Chromosome ssa02 - NC_059443.1Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC106582443 Neighboring gene 26S protease regulatory subunit 6B Neighboring gene spindle assembly checkpoint kinase-like Neighboring gene spindle assembly checkpoint kinase-like

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Manual GO annotation of predictive protein signatures: the InterPro approach to GO curation. Burge S, et al. Database (Oxford), 2012. PMID 22301074, Free PMC Article
  2. TreeGrafter: phylogenetic tree-based annotation of proteins with Gene Ontology terms and other annotations. Tang H, et al. Bioinformatics, 2019 Feb 1. PMID 30032202, Free PMC Article

GeneRIFs: Gene References Into Functions

General gene information

Go to the top of the page Help

Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables glycosyltransferase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in carbohydrate metabolic process IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
beta-1,4-galactosyltransferase 3

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs of Annotated Genomes: Salmo salar Annotation Release 102 details...Open this link in a new tab

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference Ssal_v3.1

Genomic

  1. NC_059443.1 Reference Ssal_v3.1

    Range
    38029257..38058320
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_014165728.2 → XP_014021203.1  beta-1,4-galactosyltransferase 3

    UniProtKB/TrEMBL
    A0A1S3P0T1
    Conserved Domains (1) summary
    cd00899
    Location:133 → 351
    b4GalT; Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids

  2. XM_014165743.2 → XP_014021218.1  beta-1,4-galactosyltransferase 3

    UniProtKB/TrEMBL
    A0A1S3P0T1
    Conserved Domains (1) summary
    cd00899
    Location:133 → 351
    b4GalT; Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids

  3. XM_014165734.2 → XP_014021209.1  beta-1,4-galactosyltransferase 3

    UniProtKB/TrEMBL
    A0A1S3P0T1
    Related
    ENSSSAP00000082809.1, ENSSSAT00000116567.2
    Conserved Domains (1) summary
    cd00899
    Location:133 → 351
    b4GalT; Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids
Nucleotide Protein
Heading Accession and Version

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Molecular Biology Databases