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RENBP renin binding protein [ Equus asinus (ass) ]

Gene ID: 106825628, updated on 13-Mar-2024

Summary

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Gene symbol
RENBP
Gene description
renin binding protein
See related
Ensembl:ENSEASG00005019286
Gene type
protein coding
RefSeq status
MODEL
Organism
Equus asinus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus
Orthologs
human mouse all
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Genomic context

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See RENBP in Genome Data Viewer
Location:
chromosome: X
Exon count:
11
Annotation release Status Assembly Chr Location
101 current ASM1607732v2 (GCF_016077325.2) X NC_052207.1 (88910425..88917400, complement)
100 previous assembly ASM130575v1 (GCF_001305755.1) Unplaced Scaffold NW_014638653.1 (293119..300492)

Chromosome X - NC_052207.1Genomic Context describing neighboring genes Neighboring gene arginine vasopressin receptor 2 Neighboring gene Rho GTPase activating protein 4 Neighboring gene N-alpha-acetyltransferase 10, NatA catalytic subunit Neighboring gene host cell factor C1 Neighboring gene transmembrane protein 187

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Bibliography

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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

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Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables N-acylglucosamine 2-epimerase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables peptidase inhibitor activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in N-acetylglucosamine metabolic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in N-acetylmannosamine metabolic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in carbohydrate metabolic process IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

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Preferred Names
N-acylglucosamine 2-epimerase

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Equus asinus Annotation Release 101 details...Open this link in a new tab

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

Reference ASM1607732v2

Genomic

  1. NC_052207.1 Reference ASM1607732v2

    Range
    88910425..88917400 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_044763745.1 → XP_044619680.1  N-acylglucosamine 2-epimerase isoform X1

    UniProtKB/TrEMBL
    A0A8C4MNV6
    Related
    ENSEASP00005028373.1, ENSEAST00005030813.2
    Conserved Domains (1) summary
    cd00249
    Location:14 → 407
    AGE; AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is ...

  2. XM_044763746.1 → XP_044619681.1  N-acylglucosamine 2-epimerase isoform X2

    Conserved Domains (1) summary
    cd00249
    Location:9 → 345
    AGE; AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is ...

  3. XM_044763747.1 → XP_044619682.1  N-acylglucosamine 2-epimerase isoform X3

    Conserved Domains (1) summary
    cd00249
    Location:1 → 334
    AGE; AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is ...
Nucleotide Protein
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