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b4galt4 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 4 [ Fundulus heteroclitus (mummichog) ]

Gene ID: 105919801, updated on 20-Aug-2024

Summary

Gene symbol
b4galt4
Gene description
UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 4
See related
EnsemblRapid:ENSFHEG00000026184
Gene type
protein coding
RefSeq status
MODEL
Organism
Fundulus heteroclitus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; Ovalentaria; Atherinomorphae; Cyprinodontiformes; Fundulidae; Fundulus
Orthologs
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Genomic context

Location:
chromosome: 11
Exon count:
7
Annotation release Status Assembly Chr Location
102 current MU-UCD_Fhet_4.1 (GCF_011125445.2) 11 NC_046371.1 (23238407..23250190, complement)
101 previous assembly Fundulus_heteroclitus-3.0.2 (GCF_000826765.1) Unplaced Scaffold NW_012224870.1 (2607992..2612550, complement)

Chromosome 11 - NC_046371.1Genomic Context describing neighboring genes Neighboring gene GS homeobox 1 Neighboring gene Rho GTPase activating protein 31 Neighboring gene calcium-sensing receptor Neighboring gene cationic amino acid transporter 2 family protein

Genomic regions, transcripts, and products

General protein information

Preferred Names
beta-1,4-galactosyltransferase 4

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Fundulus heteroclitus 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 MU-UCD_Fhet_4.1 Primary Assembly

Genomic

  1. NC_046371.1 Reference MU-UCD_Fhet_4.1 Primary Assembly

    Range
    23238407..23250190 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_036143177.1XP_035999070.1  beta-1,4-galactosyltransferase 4

    Related
    ENSFHEP00000062028.1, ENSFHET00000068664.1
    Conserved Domains (1) summary
    cd00899
    Location:124342
    b4GalT; Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids