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MBTPS2 membrane bound transcription factor peptidase, site 2 [ Oryctolagus cuniculus (rabbit) ]

Gene ID: 100344858, updated on 8-Mar-2024

Summary

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Gene symbol
MBTPS2
Gene description
membrane bound transcription factor peptidase, site 2
See related
Ensembl:ENSOCUG00000016386
Gene type
protein coding
RefSeq status
MODEL
Organism
Oryctolagus cuniculus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus
Orthologs
human mouse all
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Genomic context

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See MBTPS2 in Genome Data Viewer
Location:
chromosome: X
Exon count:
11
Annotation release Status Assembly Chr Location
RS_2023_02 current UM_NZW_1.0 (GCF_009806435.1) X NC_067395.1 (7592230..7636510)

Chromosome X - NC_067395.1Genomic Context describing neighboring genes Neighboring gene small muscle protein X-linked Neighboring gene heterogeneous nuclear ribonucleoprotein A1-like Neighboring gene axin interactor, dorsalization-associated protein-like Neighboring gene YY2 transcription factor Neighboring gene spermine synthase Neighboring gene phosphate regulating endopeptidase X-linked

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_067395.1 Chromosome X Reference UM_NZW_1.0 Primary Assembly

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 metalloendopeptidase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables protein binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in membrane protein intracellular domain proteolysis IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in positive regulation of DNA-binding transcription factor activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in regulation of response to endoplasmic reticulum stress IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
 PubMed 
located_in membrane IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

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Preferred Names
membrane-bound transcription factor site-2 protease

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: GCF_009806435.1-RS_2023_02

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

Reference UM_NZW_1.0 Primary Assembly

Genomic

  1. NC_067395.1 Reference UM_NZW_1.0 Primary Assembly

    Range
    7592230..7636510
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_002719970.4 → XP_002720016.1  membrane-bound transcription factor site-2 protease

    UniProtKB/TrEMBL
    A0A5F9CCP1, G1TBI7
    Related
    ENSOCUP00000014085.3
    Conserved Domains (3) summary
    cd05709
    Location:422 → 511
    S2P-M50; Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of this family use proteolytic ...
    cd06162
    Location:14 → 232
    S2P-M50_PDZ_SREBP; Sterol regulatory element-binding protein (SREBP) Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50A), regulates intramembrane proteolysis (RIP) of SREBP and is part of a signal transduction mechanism involved in sterol and lipid ...
    cl00117
    Location:258 → 302
    PDZ; PDZ domain, also called DHR (Dlg homologous region) or GLGF (after a conserved sequence motif). Many PDZ domains bind C-terminal polypeptides, though binding to internal (non-C-terminal) polypeptides and even to lipids has been demonstrated. ...
Nucleotide Protein
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