P62500 · T22D1_MOUSE
- ProteinTSC22 domain family protein 1
- GeneTsc22d1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1077 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcriptional repressor (By similarity).
Acts on the C-type natriuretic peptide (CNP) promoter (By similarity).
Acts to promote CASP3-mediated apoptosis (By similarity).
Positively regulates TGF-beta signaling by interacting with SMAD7 which inhibits binding of SMAD7 to TGFBR1, preventing recruitment of SMURF ubiquitin ligases to TGFBR1 and inhibiting SMURF-mediated ubiquitination and degradation of TGFBR1 (By similarity).
Contributes to enhancement of TGF-beta signaling by binding to and modulating the transcription activator activity of SMAD4 (By similarity).
Promotes TGF-beta-induced transcription of COL1A2; via its interaction with TFE3 at E-boxes in the gene proximal promoter (PubMed:20713358).
Plays a role in the repression of hematopoietic precursor cell growth (PubMed:19329776).
Promotes IL2 deprivation-induced apoptosis in T-lymphocytes, via repression of TSC22D3/GILZ transcription and activation of the caspase cascade (PubMed:26752201).
Acts on the C-type natriuretic peptide (CNP) promoter (By similarity).
Acts to promote CASP3-mediated apoptosis (By similarity).
Positively regulates TGF-beta signaling by interacting with SMAD7 which inhibits binding of SMAD7 to TGFBR1, preventing recruitment of SMURF ubiquitin ligases to TGFBR1 and inhibiting SMURF-mediated ubiquitination and degradation of TGFBR1 (By similarity).
Contributes to enhancement of TGF-beta signaling by binding to and modulating the transcription activator activity of SMAD4 (By similarity).
Promotes TGF-beta-induced transcription of COL1A2; via its interaction with TFE3 at E-boxes in the gene proximal promoter (PubMed:20713358).
Plays a role in the repression of hematopoietic precursor cell growth (PubMed:19329776).
Promotes IL2 deprivation-induced apoptosis in T-lymphocytes, via repression of TSC22D3/GILZ transcription and activation of the caspase cascade (PubMed:26752201).
Isoform 1
May act to negatively regulate TGFB3 signaling and thereby inhibit cell death in mammary gland cells.
Isoform 2
Positively regulates cell death in response to TGFB3 during mammary gland involution.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Biological Process | negative regulation of apoptotic process | |
Biological Process | negative regulation of hematopoietic stem cell proliferation | |
Biological Process | negative regulation of programmed cell death | |
Biological Process | positive regulation of apoptotic process | |
Biological Process | positive regulation of cell population proliferation | |
Biological Process | positive regulation of programmed cell death | |
Biological Process | positive regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of transforming growth factor beta receptor signaling pathway |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameTSC22 domain family protein 1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP62500
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Increase in DNA synthesis in hematopoietic precursor cells from bone marrow, these cells have a greater ability to proliferate and repopulate an irradiated recipient.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 1024 | Abolishes homodimerization; when associated with A-1030. | ||||
Sequence: L → A | ||||||
Mutagenesis | 1030 | Abolishes homodimerization; when associated with A-1024. | ||||
Sequence: L → A |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000219366 | 1-1077 | TSC22 domain family protein 1 | |||
Sequence: MHQPPESTAAAAAAADISARKMAHPAMFPRRGSGGGSASALNAAGTGVSGAAPSSEDFPPPSLLQPPPPAASSTQGPQPPPPQSLNLLSQAQLQGQPLAPGGTQMKKKSGFQITSVTPAQISASISSNNSIAEDTESYDDLDESHTEDLSSSEILDVSLSRATDLGEPERSSSEETLNNFQEAETPGAVSPNQPHLPQPHLPHLPQQNVVINGNAHPHHLHHHHHPHHGHHLHHGHHHSSHAAVAGPSIPGGPPSSPVSRKLSTTGSSDGGVPVAPPPAVPSSGLPASVMTNIRTPSTTGSLGINSVTGTSATNNVNIAAVGSFSPSVTNSVHGNANINTSNIPNAASISGGPGVTSVVNSSILSGMGNGTVSSSPVANSVLNAAAGITVGVVSSQQQQQQQQQPTVNTSRFRVVKLDSTSEPFKKGRWTCTEFYEKENAVPATEGVAINKVVETVKQTPTEASSSERESTSGSSVSSSVSTLSHYTESVGSGEMMGAPAVVAPQQPPLPPAPPGLQGVALQQLEFSSPAPQSIAAVSMPQSISQSQMSQVQLQPQELSFQQKQTLQPVPLQATMSAATGIQPSPVSVVGVTAAVGQQPSVSSLAQPQLPYSQTAPPVQTPLPGAPPQQLQYGQQQPMVPAQIAPGHGQPVTQNPTSEYVQQQQQPIFQAALSSGQSSSTGTGAGISVIPVAQAQGIQLPGQPTAVQTQPAGAAGQPIGQAQTAVSTVPTGGQIASIGQQANIPTAVQQPSTQVTPSVIQQGAPPSSQVVLPAPTGIIHQGVQTRASSLPQQLVIAPQSTLVTVPPQPQGVETVAQGVVSQQLPTGSPLPSASTISVTNQVSSAAPSGMPSVPTNLVPPQNIAQPPATQNGSLVQSVSQSPLIATNINLPLAQQIPLSSTQFSTQSLAQAIGSQMEDARRPAEPSLGGLPQTMSGDSGGMSAVSDGSSSSLAAPASLFPLKVLPLTTPLVDGEDESSGASVVAIDNKIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTGSPPATTQPQGTTQPPAQPASQGSGSTA | ||||||
Modified residue | 263 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in bone marrow cells (at protein level) (PubMed:19329776).
Expressed in T-cells (PubMed:26752201).
Expressed in the brain (PubMed:19329776).
Expressed in T-cells (PubMed:26752201).
Expressed in the brain (PubMed:19329776).
Isoform 1
Expressed in the myoepithelial cells of the mammary gland ducts and alveoli, expression is consistent throughout pregnancy, lactation and involution (at protein level) (PubMed:19745830).
Expressed in the cortex, medulla and papilla of the kidney (PubMed:17147695).
Expressed in the cortex, medulla and papilla of the kidney (PubMed:17147695).
Isoform 2
Expressed in the myoepithelial cells of the mammary gland, expression significantly increases in the secretory luminal epithelium of the mammary gland at the initiation of involution, with levels decreasing from day 3 of involution onwards (at protein level) (PubMed:19745830).
Expressed in the cortex, medulla and papilla of the kidney (PubMed:17147695).
Expressed in the cortex, medulla and papilla of the kidney (PubMed:17147695).
Induction
Induced by Tgfb1, Pparg and other growth factors (PubMed:12468551, PubMed:1587811).
Induced by Tgfb3 in mammary gland cells (PubMed:19745830).
Induced by TGF-beta via up-regulation of Ybx1 regulator miR-216a which decreases Ybx1 abundance and binding of Ybx1 to Tsc22d1 transcripts, thereby increasing Tsc22d1 translation (PubMed:20713358).
Induced in the glomeruli of a diabetic mouse model (PubMed:20713358).
Induced by Tgfb3 in mammary gland cells (PubMed:19745830).
Induced by TGF-beta via up-regulation of Ybx1 regulator miR-216a which decreases Ybx1 abundance and binding of Ybx1 to Tsc22d1 transcripts, thereby increasing Tsc22d1 translation (PubMed:20713358).
Induced in the glomeruli of a diabetic mouse model (PubMed:20713358).
Gene expression databases
Interaction
Subunit
Forms homodimers (PubMed:12468551).
Forms heterodimers (By similarity).
Component of a complex composed of TSC22D1 (via N-terminus), TGFBR1 and TGFBR2; the interaction between TSC22D1 and TGFBR1 is inhibited by SMAD7 and promoted by TGFB1 (By similarity).
Interacts with SMAD7; the interaction requires TGF-beta and the interaction is inhibited by TGFBR1 (By similarity).
Interacts with TPT1/fortilin; interaction results in the destabilization of TSC22D1 protein and prevents TSC22D1-mediated apoptosis (By similarity).
Interacts with SMAD4 (via N-terminus) (By similarity).
Interacts with ACVRL1/ALK1, ACVR1/ALK2, BMPR1A/ALK3, ACVR1B/ALK4, BMPR1B/ALK6, ACVR2A/ACTRII, and BMPR2 (By similarity).
Interacts with SMAD6 (By similarity).
Interacts with TFE3; the interaction is enhanced in the presence of TGF-beta (PubMed:20713358).
Forms heterodimers (By similarity).
Component of a complex composed of TSC22D1 (via N-terminus), TGFBR1 and TGFBR2; the interaction between TSC22D1 and TGFBR1 is inhibited by SMAD7 and promoted by TGFB1 (By similarity).
Interacts with SMAD7; the interaction requires TGF-beta and the interaction is inhibited by TGFBR1 (By similarity).
Interacts with TPT1/fortilin; interaction results in the destabilization of TSC22D1 protein and prevents TSC22D1-mediated apoptosis (By similarity).
Interacts with SMAD4 (via N-terminus) (By similarity).
Interacts with ACVRL1/ALK1, ACVR1/ALK2, BMPR1A/ALK3, ACVR1B/ALK4, BMPR1B/ALK6, ACVR2A/ACTRII, and BMPR2 (By similarity).
Interacts with SMAD6 (By similarity).
Interacts with TFE3; the interaction is enhanced in the presence of TGF-beta (PubMed:20713358).
Isoform 1
Forms a heterodimer with TSC22D4/THG1.
Isoform 2
Forms a heterodimer with TSC22D4/THG1 (By similarity).
Interacts with histone H1-2 (By similarity).
Interacts with GNL3 (By similarity).
Interacts with histone H1-2 (By similarity).
Interacts with GNL3 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P62500 | Tsc22d4 Q9EQN3 | 2 | EBI-8296837, EBI-7821198 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-98 | Required for interaction with TGFBR1 and promotion of TGF-beta signaling | ||||
Sequence: MHQPPESTAAAAAAADISARKMAHPAMFPRRGSGGGSASALNAAGTGVSGAAPSSEDFPPPSLLQPPPPAASSTQGPQPPPPQSLNLLSQAQLQGQPL | ||||||
Region | 22-112 | Disordered | ||||
Sequence: MAHPAMFPRRGSGGGSASALNAAGTGVSGAAPSSEDFPPPSLLQPPPPAASSTQGPQPPPPQSLNLLSQAQLQGQPLAPGGTQMKKKSGFQ | ||||||
Compositional bias | 59-84 | Pro residues | ||||
Sequence: PPPSLLQPPPPAASSTQGPQPPPPQS | ||||||
Compositional bias | 85-99 | Polar residues | ||||
Sequence: LNLLSQAQLQGQPLA | ||||||
Region | 125-283 | Disordered | ||||
Sequence: ISSNNSIAEDTESYDDLDESHTEDLSSSEILDVSLSRATDLGEPERSSSEETLNNFQEAETPGAVSPNQPHLPQPHLPHLPQQNVVINGNAHPHHLHHHHHPHHGHHLHHGHHHSSHAAVAGPSIPGGPPSSPVSRKLSTTGSSDGGVPVAPPPAVPSS | ||||||
Compositional bias | 172-188 | Polar residues | ||||
Sequence: SSEETLNNFQEAETPGA | ||||||
Compositional bias | 216-240 | Basic residues | ||||
Sequence: HPHHLHHHHHPHHGHHLHHGHHHSS | ||||||
Compositional bias | 458-489 | Polar residues | ||||
Sequence: QTPTEASSSERESTSGSSVSSSVSTLSHYTES | ||||||
Region | 458-492 | Disordered | ||||
Sequence: QTPTEASSSERESTSGSSVSSSVSTLSHYTESVGS | ||||||
Region | 842-874 | Disordered | ||||
Sequence: SSAAPSGMPSVPTNLVPPQNIAQPPATQNGSLV | ||||||
Region | 909-947 | Disordered | ||||
Sequence: QAIGSQMEDARRPAEPSLGGLPQTMSGDSGGMSAVSDGS | ||||||
Compositional bias | 930-947 | Polar residues | ||||
Sequence: PQTMSGDSGGMSAVSDGS | ||||||
Region | 1010-1031 | Leucine-zipper | ||||
Sequence: LKEQIKELIEKNSQLEQENNLL | ||||||
Region | 1042-1077 | Disordered | ||||
Sequence: QFQAQLQTGSPPATTQPQGTTQPPAQPASQGSGSTA |
Sequence similarities
Belongs to the TSC-22/Dip/Bun family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P62500-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsTSC22D1-1
- Length1,077
- Mass (Da)109,811
- Last updated2008-09-02 v2
- Checksum35749C0C1CA1E1B6
P62500-2
- Name2
- SynonymsTSC22D1-2, TSC-22
P62500-3
- Name3
- Differences from canonical
- 303-384: Missing
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_035327 | 1-934 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 59-84 | Pro residues | ||||
Sequence: PPPSLLQPPPPAASSTQGPQPPPPQS | ||||||
Compositional bias | 85-99 | Polar residues | ||||
Sequence: LNLLSQAQLQGQPLA | ||||||
Compositional bias | 172-188 | Polar residues | ||||
Sequence: SSEETLNNFQEAETPGA | ||||||
Compositional bias | 216-240 | Basic residues | ||||
Sequence: HPHHLHHHHHPHHGHHLHHGHHHSS | ||||||
Alternative sequence | VSP_035328 | 303-384 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 395 | in Ref. 4; AAG41218 | ||||
Sequence: S → SQ | ||||||
Sequence conflict | 396-398 | in Ref. 2; BAD32600 | ||||
Sequence: Missing | ||||||
Sequence conflict | 449 | in Ref. 4; AAG41218 and 3; AAH58660 | ||||
Sequence: I → V | ||||||
Compositional bias | 458-489 | Polar residues | ||||
Sequence: QTPTEASSSERESTSGSSVSSSVSTLSHYTES | ||||||
Sequence conflict | 551 | in Ref. 4; AAG41218 | ||||
Sequence: V → L | ||||||
Sequence conflict | 591 | in Ref. 4; AAG41218 and 3; AAH58660 | ||||
Sequence: V → I | ||||||
Sequence conflict | 660 | in Ref. 2; BAD32600 | ||||
Sequence: V → VQQ | ||||||
Sequence conflict | 714 | in Ref. 2; BAD32600 | ||||
Sequence: A → P | ||||||
Sequence conflict | 720 | in Ref. 4; AAG41218 | ||||
Sequence: Q → P | ||||||
Sequence conflict | 737 | in Ref. 4; AAG41218 | ||||
Sequence: I → T | ||||||
Compositional bias | 930-947 | Polar residues | ||||
Sequence: PQTMSGDSGGMSAVSDGS | ||||||
Alternative sequence | VSP_035329 | 935-975 | in isoform 2 | |||
Sequence: GDSGGMSAVSDGSSSSLAAPASLFPLKVLPLTTPLVDGEDE → MKSQWCRPVAMDLGVYQLRHFSISFLSSLLGTENASVRLDN |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X62940 EMBL· GenBank· DDBJ | CAA44712.1 EMBL· GenBank· DDBJ | mRNA | ||
AK173322 EMBL· GenBank· DDBJ | BAD32600.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC058660 EMBL· GenBank· DDBJ | AAH58660.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF201285 EMBL· GenBank· DDBJ | AAG41218.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |