Q9EQN3 · T22D4_MOUSE

  • Protein
    TSC22 domain family protein 4
  • Gene
    Tsc22d4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Binds DNA and acts as a transcriptional repressor (PubMed:27827363).
Involved in the regulation of systematic glucose homeostasis and insulin sensitivity, via transcriptional repression of downstream insulin signaling targets such as OBP2A/LCN13 (PubMed:27827363).
Acts as a negative regulator of lipogenic gene expression in hepatocytes and thereby mediates the control of very low-density lipoprotein release (PubMed:23307490).
May play a role in neurite elongation and survival (PubMed:20878296).

Miscellaneous

Involved in the development of hyperglycaemia and insulin resistance in diabetic mouse models (PubMed:27827363).
May be involved in altered hepatic lipid handling as part of cancer-induced cachexia (PubMed:23307490).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentdendrite
Cellular Componentnucleus
Cellular Componentsynapse
Biological Processglucose homeostasis
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processneuron cellular homeostasis
Biological Processneuron projection extension

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    TSC22 domain family protein 4
  • Alternative names
    • TSC22-related-inducible leucine zipper protein 2

Gene names

    • Name
      Tsc22d4
    • Synonyms
      Thg1-pit

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9EQN3
  • Secondary accessions
    • Q99PD5
    • Q9D2V9

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Cytoplasm
Synapse
Note: Localizes away from the nucleus to neurite processes and synaptic termini as cerebellar granular neurons differentiate (PubMed:20878296).
Accumulates in the cytoplasm of differentiated Purkinje cells (PubMed:20878296).
Localized to both the cytoplasm and nucleus in immature cerebellar granular neurons and atrophic Purkinje cells (PubMed:20878296).

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002193751-387TSC22 domain family protein 4
Modified residue57Phosphothreonine
Modified residue62Phosphoserine
Modified residue165Phosphoserine
Modified residue183Phosphothreonine
Modified residue187Phosphoserine
Modified residue189Phosphoserine
Modified residue219Phosphoserine
Modified residue223Phosphothreonine
Modified residue254Phosphoserine
Modified residue258Phosphoserine
Modified residue271Phosphoserine
Modified residue362Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in the liver (at protein level) (PubMed:23307490, PubMed:27827363).
Expressed in Purkinje cells and proliferating cerebellar granular neurons (at protein level) (PubMed:20878296).
Expressed in the cortex, medulla and papilla of the kidney

Induction

Induced by TGF-beta treatment (PubMed:11707329).
Induced by a wasting-associated liver metabolism as a result of a methionine-choline deficient diet or cancer-induced cachectic phenotype (PubMed:23307490).
Induced by renal hyperosmotic stress (PubMed:17147695).

Developmental stage

Expression starts at 8.5 dpc and undergoes a second peak of activation at 12.5 dpc (PubMed:11707329).
At 12.5 dpc, expression encompasses the entire central nervous system, with highest levels in the dorsal root and trigeminal ganglia (PubMed:11707329).
Expressed in the granule neurons and Purkinje cells in the external and internal granular layers of the cerebellum from postnatal day 6 (PubMed:20878296).

Gene expression databases

Interaction

Subunit

Forms a homodimer or heterodimer (By similarity).
Forms a heterodimer with TSC22D1 isoforms 1 and 2 (By similarity).
Interacts with NRBP1 (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9EQN3Aifm1 Q9Z0X14EBI-7821198, EBI-773597
BINARY Q9EQN3Tsc22d1 P625002EBI-7821198, EBI-8296837

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias1-23Polar residues
Region1-85Disordered
Compositional bias27-48Pro residues
Region135-232Disordered
Compositional bias198-212Polar residues
Region336-357Leucine-zipper
Region368-387Disordered

Sequence similarities

Belongs to the TSC-22/Dip/Bun family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    387
  • Mass (Da)
    39,979
  • Last updated
    2011-07-27 v2
  • Checksum
    D4160FA3AB2DFB90
MSGGKKKSSFQITSVTTDYEGPGSPGASDSPVPPALAGPPPRLPNGDPNPDPGGRGTPRNGSPPPGAPASRFRVVKLPQGLGEPYRRGRWTCVDVYERDLEPPSFGRLLEGIRGASGGTGGRSLDSRLELASLGISTPIPQPGLSQGPTSWLRPPPTSPGPQARSFTGGLGQLAGPGKAKVETPPLSASPPQQRPPGPGTGDSAQTLPSLRVEVESGGSAAATPPLSRRRDGAVRLRMELVAPAETGKVPPTDSRPNSPALYFDASLVHKSPDPFGAAAAQSLSLARSMLAISGHLDSDDDSGSGSLVGIDNKIEQAMDLVKSHLMFAVREEVEVLKEQIRDLAERNAALEQENGLLRALASPEQLAQLPSSGLPRLGPSAPNGPSI

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q3U1U6Q3U1U6_MOUSETsc22d4509
Q9DA18Q9DA18_MOUSETsc22d4149
D3YZZ4D3YZZ4_MOUSETsc22d4168
D3Z6V5D3Z6V5_MOUSETsc22d4210
F6VXN4F6VXN4_MOUSETsc22d496

Sequence caution

The sequence AAK02018.1 differs from that shown. Reason: Frameshift

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias1-23Polar residues
Compositional bias27-48Pro residues
Sequence conflict97in Ref. 1; AAK02018
Compositional bias198-212Polar residues
Sequence conflict339in Ref. 2; AAG41219

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF315352
EMBL· GenBank· DDBJ
AAK02018.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AF201286
EMBL· GenBank· DDBJ
AAG41219.1
EMBL· GenBank· DDBJ
mRNA
BC018544
EMBL· GenBank· DDBJ
AAH18544.1
EMBL· GenBank· DDBJ
mRNA
BC023761
EMBL· GenBank· DDBJ
AAH23761.1
EMBL· GenBank· DDBJ
mRNA
BC145721
EMBL· GenBank· DDBJ
AAI45722.1
EMBL· GenBank· DDBJ
mRNA
BC145723
EMBL· GenBank· DDBJ
AAI45724.1
EMBL· GenBank· DDBJ
mRNA
AK018735
EMBL· GenBank· DDBJ
BAB31377.1
EMBL· GenBank· DDBJ
mRNA
AK143608
EMBL· GenBank· DDBJ
BAE25460.1
EMBL· GenBank· DDBJ
mRNA
CH466529
EMBL· GenBank· DDBJ
EDL19240.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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