Tdpoz9 TD and POZ domain containing 9 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Tdpoz9provided by MGI
Official Full Name: TD and POZ domain containing 9provided by MGI
Primary source: MGI:MGI:3702970
See related: Ensembl:ENSMUSG00000094328 AllianceGenome:MGI:3702970
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Gm9125; EG668359
Summary: Predicted to enable ubiquitin protein ligase binding activity. Predicted to be involved in proteasome-mediated ubiquitin-dependent protein catabolic process; protein polyubiquitination; and regulation of proteolysis. Predicted to be part of Cul3-RING ubiquitin ligase complex. Predicted to be active in cytoplasm and nucleus. Orthologous to human SPOP (speckle type BTB/POZ protein). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Low expression observed in reference dataset See more
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Genomic context

Location:: 3 F2.1; 3 40.51 cM

Exon count:: 2

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	3	NC_000069.7 (93955288..93962192, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	3	NC_000069.6 (94047981..94054885, complement)

Chromosome 3 - NC_000069.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Submit: New GeneRIF Correction

General gene information

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Markers

Spopl1 (e-PCR), detects polymorphism
- UniSTS:265749

NoName (e-PCR)
- UniSTS:495671

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables ubiquitin protein ligase binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in proteasome-mediated ubiquitin-dependent protein catabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of proteolysis	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: TD and POZ domain-containing protein 1-like

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001163730.2 → NP_001157202.1 TD and POZ domain-containing protein 1-like

See identical proteins and their annotated locations for NP_001157202.1

Status: VALIDATED

Source sequence(s)

AC156570, AK033449

Consensus CDS

CCDS57232.1

UniProtKB/Swiss-Prot

P0DMR6

UniProtKB/TrEMBL

Q05AE5

Related

ENSMUSP00000138015.2, ENSMUST00000180746.2

Conserved Domains (4) summary

smart00225
Location:189 → 287

BTB; Broad-Complex, Tramtrack and Bric a brac

cd14734
Location:287 → 349

SPOP_C; BACK-like Domain C-terminal to BTB in speckle-type POZ protein (SPOP) and similar proteins

pfam00651
Location:178 → 284

BTB; BTB/POZ domain

cl02446
Location:16 → 154

MATH; MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane ...