P15806 · TFE2_MOUSE
- ProteinTranscription factor E2-alpha
- GeneTcf3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids651 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcriptional regulator involved in the initiation of neuronal differentiation and mesenchymal to epithelial transition (PubMed:15226298, PubMed:18214987).
Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation (PubMed:18214987).
Together with TCF15, required for the mesenchymal to epithelial transition (PubMed:11309385, PubMed:15226298).
Dimers bind DNA on E-box motifs: 5'-CANNTG-3' (PubMed:15226298, PubMed:18214987, PubMed:30426815).
Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer (By similarity).
Binds to IEB1 and IEB2, which are short DNA sequences in the insulin gene transcription control region (PubMed:2181401).
Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like muscle or early B-cell differentiation (PubMed:18214987).
Together with TCF15, required for the mesenchymal to epithelial transition (PubMed:11309385, PubMed:15226298).
Dimers bind DNA on E-box motifs: 5'-CANNTG-3' (PubMed:15226298, PubMed:18214987, PubMed:30426815).
Binds to the kappa-E2 site in the kappa immunoglobulin gene enhancer (By similarity).
Binds to IEB1 and IEB2, which are short DNA sequences in the insulin gene transcription control region (PubMed:2181401).
Isoform E47
Facilitates ATOH7 binding to DNA at the consensus sequence 5'-CAGGTG-3', and positively regulates transcriptional activity.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranscription factor E2-alpha
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP15806
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Mice are smaller than their wild-type littermates and fail to thrive 14 days after birth.
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 387 | |||||
Sequence: L → LQ |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 29 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000127468 | 1-651 | Transcription factor E2-alpha | |||
Sequence: MMNQSQRMAPVGSDKELSDLLDFSMMFPLPVANGKSRPASLGGTQFAGSGLEDRPSSGSWGSSDQNSSSFDPSRTYSEGAHFSDSHSSLPPSTFLGAGLGGKGSERNAYATFGRDTSVGTLSQAGFLPGELSLSSPGPLSPSGIKSSSQYYPSFPSNPRRRAADGGLDTQPKKVRKVPPGLPSSVYPPSSGDSYSRDAAAYPSAKTPSSAYPSPFYVADGSLHPSAELWSTPSQVGFGPMLGDGSSPLPLAPGSSSVGSGTFGGLQQQDRMGYQLHGSEVNGSLPAVSSFSAAPGTYSGTSGHTPPVSGAAAESLLGTRGTTASSSGDALGKALASIYSPDHSSNNFSPSPSTPVGSPQGLPGTSQWPRAGAPSALSPNYDAGLHGLSKMEDRLDEAIHVLRSHAVGTASDLHGLLPGHGALTTSFTGPMSLGGRHAGLVGGSHPEEGLTSGASLLHNHASLPSQPSSLPDLSQRPPDSYSGLGRAGTTAGASEIKREEKEDEEIASVADAEEDKKDLKVPRTRTSPDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFKELGRMCQLHLSSEKPQTKLLILHQAVAVILSLEQQVRERNLNPKAACLKRREEEKVSGVVGDPQLALSAAHPGLGEAHNPAGHL | ||||||
Modified residue | 135 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 140 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 353 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 357 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 369 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 377 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 496 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 526 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 528 | In isoform P15806-2; Phosphothreonine | ||||
Sequence: D | ||||||
Modified residue | 533 | In isoform P15806-2; Phosphoserine | ||||
Sequence: D | ||||||
Cross-link | 622 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Post-translational modification
Phosphorylated following NGF stimulation.
Undergoes Notch-induced ubiquitination and subsequent proteasomal degradation which is mediated by ASB1 or ASB2, the substrate-recognition components of probable ECS E3 ubiquitin-protein ligase complexes.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Expressed during the development of the nervous system.
Gene expression databases
Interaction
Subunit
Homodimer (PubMed:12196028).
Heterodimer; efficient DNA binding requires dimerization with another bHLH protein (PubMed:15226298).
Forms a heterodimer with TWIST1 and TWIST2 (PubMed:23395635, PubMed:7589808).
Forms a heterodimer with NEUROD1; the heterodimer is inhibited in presence of ID2, but not NR0B2, to E-box element (PubMed:18069799, PubMed:23395635).
Forms a heterodimer with TCF15; the heterodimer binds E-box element (PubMed:15226298, PubMed:23395635).
Forms a heterodimer with MYOG; heterodimerization enhances MYOG DNA-binding and transcriptional activities (PubMed:12196028).
Forms a heterodimer with ATOH8; repress transcription of TCF3 and TCF3-NEUROG3 dimer-induced transactivation of E box-dependent promoters (PubMed:23938248).
Component of a nuclear TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3 (PubMed:16407974).
Interacts with NEUROD2 (PubMed:18214987).
Interacts with EP300 (By similarity).
Interacts with PTF1A, TGFB1I1 and UBE2I (PubMed:11318877, PubMed:16291758, PubMed:9409784).
Interacts with BHLHA9 (By similarity).
Interacts with ASB2; the interaction is mediated by SKP2 and targets TCF3 for Notch-induced proteasomal degradation (By similarity).
Interacts with transcription factor ASCL5/AmeloD
Heterodimer; efficient DNA binding requires dimerization with another bHLH protein (PubMed:15226298).
Forms a heterodimer with TWIST1 and TWIST2 (PubMed:23395635, PubMed:7589808).
Forms a heterodimer with NEUROD1; the heterodimer is inhibited in presence of ID2, but not NR0B2, to E-box element (PubMed:18069799, PubMed:23395635).
Forms a heterodimer with TCF15; the heterodimer binds E-box element (PubMed:15226298, PubMed:23395635).
Forms a heterodimer with MYOG; heterodimerization enhances MYOG DNA-binding and transcriptional activities (PubMed:12196028).
Forms a heterodimer with ATOH8; repress transcription of TCF3 and TCF3-NEUROG3 dimer-induced transactivation of E box-dependent promoters (PubMed:23938248).
Component of a nuclear TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3 (PubMed:16407974).
Interacts with NEUROD2 (PubMed:18214987).
Interacts with EP300 (By similarity).
Interacts with PTF1A, TGFB1I1 and UBE2I (PubMed:11318877, PubMed:16291758, PubMed:9409784).
Interacts with BHLHA9 (By similarity).
Interacts with ASB2; the interaction is mediated by SKP2 and targets TCF3 for Notch-induced proteasomal degradation (By similarity).
Interacts with transcription factor ASCL5/AmeloD
Isoform E47
Forms a heterodimer with ATOH7; required for ATOH7 DNA-binding.
Isoform E12
Interacts with RALGAPA1 (PubMed:12200424).
Interacts with FIGLA (By similarity).
Interacts with FIGLA (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P15806 | Hand1 Q64279 | 2 | EBI-81370, EBI-81361 | |
BINARY | P15806 | Hand2 Q61039 | 2 | EBI-81370, EBI-81388 | |
BINARY | P15806 | Id2 P41136 | 2 | EBI-81370, EBI-309167 | |
BINARY | P15806 | Tal1 P22091 | 4 | EBI-81370, EBI-8006437 | |
BINARY | P15806-2 | Id2 P41136 | 6 | EBI-413585, EBI-309167 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 32-107 | Disordered | ||||
Sequence: ANGKSRPASLGGTQFAGSGLEDRPSSGSWGSSDQNSSSFDPSRTYSEGAHFSDSHSSLPPSTFLGAGLGGKGSERN | ||||||
Compositional bias | 50-92 | Polar residues | ||||
Sequence: GLEDRPSSGSWGSSDQNSSSFDPSRTYSEGAHFSDSHSSLPPS | ||||||
Compositional bias | 131-155 | Polar residues | ||||
Sequence: LSLSSPGPLSPSGIKSSSQYYPSFP | ||||||
Region | 131-208 | Disordered | ||||
Sequence: LSLSSPGPLSPSGIKSSSQYYPSFPSNPRRRAADGGLDTQPKKVRKVPPGLPSSVYPPSSGDSYSRDAAAYPSAKTPS | ||||||
Compositional bias | 341-364 | Polar residues | ||||
Sequence: DHSSNNFSPSPSTPVGSPQGLPGT | ||||||
Region | 341-378 | Disordered | ||||
Sequence: DHSSNNFSPSPSTPVGSPQGLPGTSQWPRAGAPSALSP | ||||||
Region | 387-422 | Leucine-zipper | ||||
Sequence: LSKMEDRLDEAIHVLRSHAVGTASDLHGLLPGHGAL | ||||||
Compositional bias | 457-475 | Polar residues | ||||
Sequence: HNHASLPSQPSSLPDLSQR | ||||||
Region | 457-549 | Disordered | ||||
Sequence: HNHASLPSQPSSLPDLSQRPPDSYSGLGRAGTTAGASEIKREEKEDEEIASVADAEEDKKDLKVPRTRTSPDEDEDDLLPPEQKAEREKERRV | ||||||
Compositional bias | 492-549 | Basic and acidic residues | ||||
Sequence: ASEIKREEKEDEEIASVADAEEDKKDLKVPRTRTSPDEDEDDLLPPEQKAEREKERRV | ||||||
Domain | 546-599 | bHLH | ||||
Sequence: ERRVANNARERLRVRDINEAFKELGRMCQLHLSSEKPQTKLLILHQAVAVILSL |
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P15806-1
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.
- NameE12
- Length651
- Mass (Da)67,701
- Last updated2004-08-16 v2
- Checksum7904ABB37B8D39CB
P15806-2
- NameE47
- Differences from canonical
- 527-598: PDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFKELGRMCQLHLSSEKPQTKLLILHQAVAVILS → STDEVLSLEEKDLRDRERRMANNARERVRVRDINEAFRELGRMCQLHLKSDKAQTKLLILQQAVQVILG
Computationally mapped potential isoform sequences
There are 10 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PVV1 | E9PVV1_MOUSE | Tcf3 | 650 | ||
E9PVV2 | E9PVV2_MOUSE | Tcf3 | 649 | ||
E9PWE3 | E9PWE3_MOUSE | Tcf3 | 645 | ||
E9PWE4 | E9PWE4_MOUSE | Tcf3 | 648 | ||
E9PWE5 | E9PWE5_MOUSE | Tcf3 | 648 | ||
E9PWE2 | E9PWE2_MOUSE | Tcf3 | 653 | ||
A0A0R4J011 | A0A0R4J011_MOUSE | Tcf3 | 649 | ||
A0A0R4J014 | A0A0R4J014_MOUSE | Tcf3 | 652 | ||
F6T941 | F6T941_MOUSE | Tcf3 | 638 | ||
D3Z037 | D3Z037_MOUSE | Tcf3 | 66 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 50-92 | Polar residues | ||||
Sequence: GLEDRPSSGSWGSSDQNSSSFDPSRTYSEGAHFSDSHSSLPPS | ||||||
Compositional bias | 131-155 | Polar residues | ||||
Sequence: LSLSSPGPLSPSGIKSSSQYYPSFP | ||||||
Sequence conflict | 156 | in Ref. 1; AAK18618 | ||||
Sequence: S → N | ||||||
Sequence conflict | 164 | in Ref. 1; AAK18618 | ||||
Sequence: D → N | ||||||
Sequence conflict | 167 | in Ref. 3; AAH18260 | ||||
Sequence: L → LA | ||||||
Sequence conflict | 294 | in Ref. 2; BAB30842 | ||||
Sequence: P → T | ||||||
Compositional bias | 341-364 | Polar residues | ||||
Sequence: DHSSNNFSPSPSTPVGSPQGLPGT | ||||||
Compositional bias | 457-475 | Polar residues | ||||
Sequence: HNHASLPSQPSSLPDLSQR | ||||||
Compositional bias | 492-549 | Basic and acidic residues | ||||
Sequence: ASEIKREEKEDEEIASVADAEEDKKDLKVPRTRTSPDEDEDDLLPPEQKAEREKERRV | ||||||
Alternative sequence | VSP_011354 | 527-598 | in isoform E47 | |||
Sequence: PDEDEDDLLPPEQKAEREKERRVANNARERLRVRDINEAFKELGRMCQLHLSSEKPQTKLLILHQAVAVILS → STDEVLSLEEKDLRDRERRMANNARERVRVRDINEAFRELGRMCQLHLKSDKAQTKLLILQQAVQVILG | ||||||
Sequence conflict | 633 | in Ref. 3; AAH06860 | ||||
Sequence: A → P |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF352579 EMBL· GenBank· DDBJ | AAK18618.1 EMBL· GenBank· DDBJ | mRNA | ||
AK017617 EMBL· GenBank· DDBJ | BAB30842.1 EMBL· GenBank· DDBJ | mRNA | ||
AK038738 EMBL· GenBank· DDBJ | BAC30118.1 EMBL· GenBank· DDBJ | mRNA | ||
AK156265 EMBL· GenBank· DDBJ | BAE33647.1 EMBL· GenBank· DDBJ | mRNA | ||
BC006860 EMBL· GenBank· DDBJ | AAH06860.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018260 EMBL· GenBank· DDBJ | AAH18260.1 EMBL· GenBank· DDBJ | mRNA | ||
X17500 EMBL· GenBank· DDBJ | CAA35541.1 EMBL· GenBank· DDBJ | mRNA | ||
D16631 EMBL· GenBank· DDBJ | BAA04057.1 EMBL· GenBank· DDBJ | mRNA | ||
D16632 EMBL· GenBank· DDBJ | BAA04058.1 EMBL· GenBank· DDBJ | mRNA | ||
D16633 EMBL· GenBank· DDBJ | BAA04059.1 EMBL· GenBank· DDBJ | mRNA | ||
D16634 EMBL· GenBank· DDBJ | BAA04060.1 EMBL· GenBank· DDBJ | mRNA | ||
D16635 EMBL· GenBank· DDBJ | BAA04061.1 EMBL· GenBank· DDBJ | mRNA | ||
D16636 EMBL· GenBank· DDBJ | BAA04062.1 EMBL· GenBank· DDBJ | mRNA | ||
D16637 EMBL· GenBank· DDBJ | BAA04063.1 EMBL· GenBank· DDBJ | mRNA | ||
D16638 EMBL· GenBank· DDBJ | BAA04064.1 EMBL· GenBank· DDBJ | mRNA | ||
D29919 EMBL· GenBank· DDBJ | BAA06218.1 EMBL· GenBank· DDBJ | mRNA |