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B4GALT7 beta-1,4-galactosyltransferase 7 [ Bison bison bison ]

Gene ID: 104993320, updated on 12-Mar-2024

Summary

Gene symbol
B4GALT7
Gene description
beta-1,4-galactosyltransferase 7
See related
Ensembl:ENSBBBG00000010990
Gene type
protein coding
RefSeq status
MODEL
Organism
Bison bison bison (sub-species: bison)
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bison
Orthologs
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Genomic context

See B4GALT7 in Genome Data Viewer
Location:
chromosome: Un
Exon count:
6
Annotation release Status Assembly Chr Location
100 current Bison_UMD1.0 (GCF_000754665.1) Unplaced Scaffold NW_011494810.1 (2264071..2272855, complement)

NW_011494810.1Genomic Context describing neighboring genes Neighboring gene required for meiotic nuclear division 5 homolog B Neighboring gene nuclear nucleic acid-binding protein C1D pseudogene Neighboring gene NEDD4 binding protein 3 Neighboring gene elongation factor 1-alpha 1-like Neighboring gene transmembrane p24 trafficking protein 9

Genomic regions, transcripts, and products

Genomic Sequence:
NW_011494810.1 Unplaced Scaffold Reference Bison_UMD1.0 Primary Assembly

General protein information

Preferred Names
beta-1,4-galactosyltransferase 7

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Bison bison bison Annotation Release 100 details...Open this link in a new tab

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

Reference Bison_UMD1.0 Primary Assembly

Genomic

  1. NW_011494810.1 Reference Bison_UMD1.0 Primary Assembly

    Range
    2264071..2272855 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_010846524.1XP_010844826.1  beta-1,4-galactosyltransferase 7

    UniProtKB/TrEMBL
    A0A6P3HQM9
    Related
    ENSBBBP00000018211.1, ENSBBBT00000012922.1
    Conserved Domains (1) summary
    cd00899
    Location:92315
    b4GalT; Beta-4-Galactosyltransferase is involved in the formation of the poly-N-acetyllactosamine core structures present in glycoproteins and glycosphingolipids