O15119 · TBX3_HUMAN
- ProteinT-box transcription factor TBX3
- GeneTBX3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids743 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcriptional repressor involved in developmental processes (PubMed:10468588).
Binds to the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence, or a half-site, which are present in the regulatory region of several genes (PubMed:12000749).
Probably plays a role in limb pattern formation (PubMed:10468588).
Required for mammary placode induction, and maintenance of the mammary buds during development (By similarity).
Involved in branching morphogenesis in both developing lungs and adult mammary glands, via negative modulation of target genes; acting redundantly with TBX2 (By similarity).
Required, together with TBX2, to maintain cell proliferation in the embryonic lung mesenchyme; perhaps acting downstream of SHH, BMP and TGFbeta signaling (By similarity).
Involved in modulating early inner ear development, acting independently of, and also redundantly with, TBX2 in different subregions of the developing ear (By similarity).
Acts as a negative regulator of PML function in cellular senescence (PubMed:22002537).
Binds to the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence, or a half-site, which are present in the regulatory region of several genes (PubMed:12000749).
Probably plays a role in limb pattern formation (PubMed:10468588).
Required for mammary placode induction, and maintenance of the mammary buds during development (By similarity).
Involved in branching morphogenesis in both developing lungs and adult mammary glands, via negative modulation of target genes; acting redundantly with TBX2 (By similarity).
Required, together with TBX2, to maintain cell proliferation in the embryonic lung mesenchyme; perhaps acting downstream of SHH, BMP and TGFbeta signaling (By similarity).
Involved in modulating early inner ear development, acting independently of, and also redundantly with, TBX2 in different subregions of the developing ear (By similarity).
Acts as a negative regulator of PML function in cellular senescence (PubMed:22002537).
Features
Showing features for dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 107-220 | T-box; first part | ||||
Sequence: LEAKELWDQFHKRGTEMVITKSGRRMFPPFKVRCSGLDKKAKYILLMDIIAADDCRYKFHNSRWMVAGKADPEMPKRMYIHPDSPATGEQWMSKVVTFHKLKLTNNISDKHGFT | ||||||
DNA binding | 241-305 | T-box; second part | ||||
Sequence: ILNSMHKYQPRFHIVRANDILKLPYSTFRTYLFPETEFIAVTAYQNDKITQLKIDNNPFAKGFRD |
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameT-box transcription factor TBX3
- Short namesT-box protein 3
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO15119
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Ulnar-mammary syndrome (UMS)
- Note
- DescriptionCharacterized by ulnar ray defects, obesity, hypogenitalism, delayed puberty, hypoplasia of nipples and apocrine glands.
- See alsoMIM:181450
Natural variants in UMS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_009601 | 143 | L>P | in UMS | |
VAR_009602 | 149 | Y>S | in UMS |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_009601 | 143 | in UMS | |||
Sequence: L → P | ||||||
Mutagenesis | 143 | Reduces binding to T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence. | ||||
Sequence: L → P | ||||||
Natural variant | VAR_009602 | 149 | in UMS | |||
Sequence: Y → S | ||||||
Mutagenesis | 149 | Reduces binding to T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence. | ||||
Sequence: Y → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,446 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000184428 | 1-743 | UniProt | T-box transcription factor TBX3 | |||
Sequence: MSLSMRDPVIPGTSMAYHPFLPHRAPDFAMSAVLGHQPPFFPALTLPPNGAAALSLPGALAKPIMDQLVGAAETGIPFSSLGPQAHLRPLKTMEPEEEVEDDPKVHLEAKELWDQFHKRGTEMVITKSGRRMFPPFKVRCSGLDKKAKYILLMDIIAADDCRYKFHNSRWMVAGKADPEMPKRMYIHPDSPATGEQWMSKVVTFHKLKLTNNISDKHGFTLAFPSDHATWQGNYSFGTQTILNSMHKYQPRFHIVRANDILKLPYSTFRTYLFPETEFIAVTAYQNDKITQLKIDNNPFAKGFRDTGNGRREKRKQLTLQSMRVFDERHKKENGTSDESSSEQAAFNCFAQASSPAASTVGTSNLKDLCPSEGESDAEAESKEEHGPEACDAAKISTTTSEEPCRDKGSPAVKAHLFAAERPRDSGRLDKASPDSRHSPATISSSTRGLGAEERRSPVREGTAPAKVEEARALPGKEAFAPLTVQTDAAAAHLAQGPLPGLGFAPGLAGQQFFNGHPLFLHPSQFAMGGAFSSMAAAGMGPLLATVSGASTGVSGLDSTAMASAAAAQGLSGASAATLPFHLQQHVLASQGLAMSPFGSLFPYPYTYMAAAAAASSAAASSSVHRHPFLNLNTMRPRLRYSPYSIPVPVPDGSSLLTTALPSMAAAAGPLDGKVAALAASPASVAVDSGSELNSRSSTLSSSSMSLSPKLCAEKEAATSELQSIQRLVSGLEAKPDRSRSASP | |||||||
Modified residue (large scale data) | 354 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 371 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 371 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 375 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 409 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 432 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 432 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 435 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 438 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 438 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 441 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 456 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 456 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 680 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 707 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 707 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 738 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 738 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 740 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 742 | UniProt | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with PML (isoform PML-4).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O15119 | CA8 P35219 | 3 | EBI-3452216, EBI-718700 | |
BINARY | O15119 | CSF3 Q8N4W3 | 3 | EBI-3452216, EBI-12843274 | |
BINARY | O15119 | PFDN5 Q99471 | 3 | EBI-3452216, EBI-357275 | |
BINARY | O15119 | PRR20D P86480 | 3 | EBI-3452216, EBI-12754095 | |
BINARY | O15119 | TLE5 Q08117 | 3 | EBI-3452216, EBI-717810 | |
BINARY | O15119 | UFSP1 Q6NVU6 | 3 | EBI-3452216, EBI-12068150 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 301-342 | Disordered | ||||
Sequence: KGFRDTGNGRREKRKQLTLQSMRVFDERHKKENGTSDESSSE | ||||||
Compositional bias | 305-337 | Basic and acidic residues | ||||
Sequence: DTGNGRREKRKQLTLQSMRVFDERHKKENGTSD | ||||||
Region | 357-465 | Disordered | ||||
Sequence: ASTVGTSNLKDLCPSEGESDAEAESKEEHGPEACDAAKISTTTSEEPCRDKGSPAVKAHLFAAERPRDSGRLDKASPDSRHSPATISSSTRGLGAEERRSPVREGTAPA | ||||||
Compositional bias | 371-390 | Basic and acidic residues | ||||
Sequence: SEGESDAEAESKEEHGPEAC | ||||||
Compositional bias | 417-434 | Basic and acidic residues | ||||
Sequence: FAAERPRDSGRLDKASPD | ||||||
Compositional bias | 436-450 | Polar residues | ||||
Sequence: RHSPATISSSTRGLG | ||||||
Region | 544-695 | Transcription repression | ||||
Sequence: ATVSGASTGVSGLDSTAMASAAAAQGLSGASAATLPFHLQQHVLASQGLAMSPFGSLFPYPYTYMAAAAAASSAAASSSVHRHPFLNLNTMRPRLRYSPYSIPVPVPDGSSLLTTALPSMAAAAGPLDGKVAALAASPASVAVDSGSELNSR | ||||||
Region | 688-707 | Disordered | ||||
Sequence: SGSELNSRSSTLSSSSMSLS |
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
O15119-1
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.
- NameII
- NoteContains an interrupted T-box domain.
- Length743
- Mass (Da)79,389
- Last updated2003-02-12 v4
- ChecksumD5572F9CF871E89F
O15119-2
- NameI
- NoteContains an interrupted T-box domain.
- Differences from canonical
- 221-240: Missing
O15119-3
- NameIII
- NoteContains an interrupted T-box domain.
O15119-4
- NameIV
- NoteMay be produced by joining exon 1 to exon 7 thereby eliminating the T-box.
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_006384 | 221-240 | in isoform I | |||
Sequence: Missing | ||||||
Compositional bias | 305-337 | Basic and acidic residues | ||||
Sequence: DTGNGRREKRKQLTLQSMRVFDERHKKENGTSD | ||||||
Sequence conflict | 315 | in Ref. 4; AAF61207 | ||||
Sequence: K → Q | ||||||
Compositional bias | 371-390 | Basic and acidic residues | ||||
Sequence: SEGESDAEAESKEEHGPEAC | ||||||
Compositional bias | 417-434 | Basic and acidic residues | ||||
Sequence: FAAERPRDSGRLDKASPD | ||||||
Compositional bias | 436-450 | Polar residues | ||||
Sequence: RHSPATISSSTRGLG | ||||||
Alternative sequence | VSP_006385 | 490-615 | in isoform III | |||
Sequence: Missing | ||||||
Sequence conflict | 616-628 | in Ref. 1 | ||||
Sequence: SAAASSSVHRHPF → LRQPQLRCTAPL | ||||||
Alternative sequence | VSP_006386 | 661-677 | in isoform III | |||
Sequence: Missing | ||||||
Sequence conflict | 674 | in Ref. 1; AAD50989 | ||||
Sequence: V → A | ||||||
Sequence conflict | 692 | in Ref. 1; AAD50989 | ||||
Sequence: L → P |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF170708 EMBL· GenBank· DDBJ | AAD50989.2 EMBL· GenBank· DDBJ | mRNA | ||
AF002228 EMBL· GenBank· DDBJ | AAC12947.1 EMBL· GenBank· DDBJ | mRNA | ||
AF140240 EMBL· GenBank· DDBJ | AAF61816.1 EMBL· GenBank· DDBJ | mRNA | ||
AF216750 EMBL· GenBank· DDBJ | AAF61207.1 EMBL· GenBank· DDBJ | mRNA | ||
BC025258 EMBL· GenBank· DDBJ | AAH25258.1 EMBL· GenBank· DDBJ | mRNA |