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LUZP1 leucine zipper protein 1 [ Chrysochloris asiatica (Cape golden mole) ]

Gene ID: 102812393, updated on 10-Mar-2024

Summary

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Gene symbol
LUZP1
Gene description
leucine zipper protein 1
Gene type
protein coding
RefSeq status
MODEL
Organism
Chrysochloris asiatica
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Afrotheria; Chrysochloridae; Chrysochlorinae; Chrysochloris
Orthologs
human mouse all
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Genomic context

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Location:
chromosome: Un
Exon count:
5
Annotation release Status Assembly Chr Location
100 current ChrAsi1.0 (GCF_000296735.1) Unplaced Scaffold NW_006408565.1 (15515394..15552004)

NW_006408565.1Genomic Context describing neighboring genes Neighboring gene GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase-like Neighboring gene 5-hydroxytryptamine receptor 1D Neighboring gene lysine demethylase 1A Neighboring gene EPH receptor B2

Genomic regions, transcripts, and products

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Genomic Sequence:
NW_006408565 unplaced scaffold reference ChrAsi1.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

General gene information

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Homology

General protein information

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Preferred Names
leucine zipper protein 1

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Chrysochloris asiatica 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 ChrAsi1.0 Primary Assembly

Genomic

  1. NW_006408565.1 Reference ChrAsi1.0 Primary Assembly

    Range
    15515394..15552004
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_006862399.1 → XP_006862461.1  leucine zipper protein 1

    UniProtKB/TrEMBL
    A0A9B0TBI6
    Conserved Domains (2) summary
    pfam15619
    Location:104 → 299
    Lebercilin; Ciliary protein causing Leber congenital amaurosis disease
    cl09111
    Location:259 → 358
    Prefoldin; Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits ...
Nucleotide Protein
Heading Accession and Version

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