O43439 · MTG8R_HUMAN
- ProteinProtein CBFA2T2
- GeneCBFA2T2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids604 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Via association with PRDM14 is involved in regulation of embryonic stem cell (ESC) pluripotency (PubMed:27281218).
Involved in primordial germ cell (PCG) formation. Stabilizes PRDM14 and OCT4 on chromatin in a homooligomerization-dependent manner (By similarity).
Can repress the expression of MMP7 in a ZBTB33-dependent manner (PubMed:23251453).
May function as a complex with the chimeric protein RUNX1/AML1-CBFA2T1/MTG8 (AML1-MTG8/ETO fusion protein) which is produced in acute myeloid leukemia with the chromosomal translocation t(8;21). May thus be involved in the repression of AML1-dependent transcription and the induction of G-CSF/CSF3-dependent cell growth. May be a tumor suppressor gene candidate involved in myeloid tumors with the deletion of the 20q11 region. Through heteromerization with CBFA2T3/MTG16 may be involved in regulation of the proliferation and the differentiation of erythroid progenitors by repressing the expression of TAL1 target genes (By similarity).
Required for the maintenance of the secretory cell lineage in the small intestine. Can inhibit Notch signaling probably by association with RBPJ and may be involved in GFI1-mediated Paneth cell differentiation (By similarity).
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 20-21 | Breakpoint for translocation to form RUNX1-CBFA2T2 in acute myeloid leukemia | ||||
Sequence: KV | ||||||
Binding site | 507 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 510 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 518 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 521 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 527 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 531 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 539 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 543 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | transcription corepressor activity | |
Biological Process | DNA-templated transcription | |
Biological Process | intestinal epithelial cell differentiation | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | negative regulation of neuron projection development | |
Biological Process | negative regulation of Notch signaling pathway | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | positive regulation of neuron projection development |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
The subsequence GLNGGYQDELVDHRLTEREWADEWKHLDHALNCIMEMVEKTRRSMAVLRRCQESDREELNYWKRRYNENTELRKTGTELV, which contains the NHR2 domain, shows transcriptional repressor activity in a high-throughput recruitment assay.
Names & Taxonomy
Protein names
- Recommended nameProtein CBFA2T2
- Alternative names
Gene names
- Community suggested namesCBFA2T2
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO43439
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 629 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000218301 | 1-604 | UniProt | Protein CBFA2T2 | |||
Sequence: MAKESGISLKEIQVLARQWKVGPEKRVPAMPGSPVEVKIQSRSSPPTMPPLPPINPGGPRPVSFTPTALSNGINHSPPTLNGAPSPPQRFSNGPASSTSSALTNQQLPATCGARQLSKLKRFLTTLQQFGNDISPEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARAAKQTPSQYLAQHEHLLLNTSIASPADSSELLMEVHGNGKRPSPERREENSFDRDTIAPEPPAKRVCTISPAPRHSPALTVPLMNPGGQFHPTPPPLQHYTLEDIATSHLYREPNKMLEHREVRDRHHSLGLNGGYQDELVDHRLTEREWADEWKHLDHALNCIMEMVEKTRRSMAVLRRCQESDREELNYWKRRYNENTELRKTGTELVSRQHSPGSADSLSNDSQREFNSRPGTGYVPVEFWKKTEEAVNKVKIQAMSEVQKAVAEAEQKAFEVIATERARMEQTIADVKRQAAEDAFLVINEQEESTENCWNCGRKASETCSGCNIARYCGSFCQHKDWERHHRLCGQNLHGQSPHGQGRPLLPVGRGSSARSADCSVPSPALDKTSATTSRSSTPASVTAIDTNGL | |||||||
Modified residue | 33 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 33 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 38 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 44 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 262 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 264 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 264 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 323 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 409 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 409 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 412 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 449 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 551 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 577 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 577 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 591 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 592 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 595 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Can interact with RUNX1T1/CBFA2T1 and CBFA2T3/MTG16; heterotetramerization between members of the CBFA2T family is proposed (PubMed:12242670, PubMed:14703694, PubMed:16616331).
Forms a heterooligomer with the AML1-MTG8/ETO fusion protein (PubMed:9447981).
Interacts with PRDM14 (PubMed:27281218).
Interacts with RBPJ, GFI1, TCF4. Interacts with TAL1 and CBFA2T3/MTG16; the heteromer with CBFA2T3/MTG16 may function in repression of TAL1 (By similarity).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, coiled coil, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 25-105 | Disordered | ||||
Sequence: KRVPAMPGSPVEVKIQSRSSPPTMPPLPPINPGGPRPVSFTPTALSNGINHSPPTLNGAPSPPQRFSNGPASSTSSALTNQ | ||||||
Compositional bias | 45-60 | Pro residues | ||||
Sequence: PPTMPPLPPINPGGPR | ||||||
Compositional bias | 64-105 | Polar residues | ||||
Sequence: FTPTALSNGINHSPPTLNGAPSPPQRFSNGPASSTSSALTNQ | ||||||
Region | 107-215 | Interaction with PRDM14 | ||||
Sequence: LPATCGARQLSKLKRFLTTLQQFGNDISPEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARAAKQTPSQYLAQHEHLLLNTS | ||||||
Domain | 113-208 | TAFH | ||||
Sequence: ARQLSKLKRFLTTLQQFGNDISPEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARAAKQTPSQYLAQHE | ||||||
Region | 229-265 | Disordered | ||||
Sequence: VHGNGKRPSPERREENSFDRDTIAPEPPAKRVCTISP | ||||||
Compositional bias | 233-254 | Basic and acidic residues | ||||
Sequence: GKRPSPERREENSFDRDTIAPE | ||||||
Region | 331-377 | Nervy homology region 2 (NHR2) | ||||
Sequence: QDELVDHRLTEREWADEWKHLDHALNCIMEMVEKTRRSMAVLRRCQE | ||||||
Region | 397-427 | Disordered | ||||
Sequence: RKTGTELVSRQHSPGSADSLSNDSQREFNSR | ||||||
Compositional bias | 403-427 | Polar residues | ||||
Sequence: LVSRQHSPGSADSLSNDSQREFNSR | ||||||
Region | 435-484 | Nervy homology region 3 (NHR3) | ||||
Sequence: VEFWKKTEEAVNKVKIQAMSEVQKAVAEAEQKAFEVIATERARMEQTIAD | ||||||
Coiled coil | 451-491 | |||||
Sequence: QAMSEVQKAVAEAEQKAFEVIATERARMEQTIADVKRQAAE | ||||||
Zinc finger | 507-543 | MYND-type | ||||
Sequence: CWNCGRKASETCSGCNIARYCGSFCQHKDWERHHRLC | ||||||
Region | 547-604 | Disordered | ||||
Sequence: LHGQSPHGQGRPLLPVGRGSSARSADCSVPSPALDKTSATTSRSSTPASVTAIDTNGL | ||||||
Compositional bias | 570-604 | Polar residues | ||||
Sequence: SADCSVPSPALDKTSATTSRSSTPASVTAIDTNGL |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
O43439-1
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
- SynonymsMTGR1b
- Length604
- Mass (Da)67,133
- Last updated1998-06-01 v1
- Checksum1E55618844908169
O43439-2
- Name2
- SynonymsMTGR1a, EHT
- Differences from canonical
- 1-29: Missing
O43439-3
- Name3
O43439-4
- Name4
- Differences from canonical
- 1-20: MAKESGISLKEIQVLARQWK → MGFHHVGQARLELLTSGDLPALASQRAGIT
O43439-5
- Name5
- Differences from canonical
- 1-21: MAKESGISLKEIQVLARQWKV → MVGVPGAAAFQL
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q68DC6 | Q68DC6_HUMAN | CBFA2T2 | 152 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_008122 | 1-20 | in isoform 4 | |||
Sequence: MAKESGISLKEIQVLARQWK → MGFHHVGQARLELLTSGDLPALASQRAGIT | ||||||
Alternative sequence | VSP_047410 | 1-21 | in isoform 5 | |||
Sequence: MAKESGISLKEIQVLARQWKV → MVGVPGAAAFQL | ||||||
Alternative sequence | VSP_008121 | 1-29 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 31 | in Ref. 7; AAH15066 | ||||
Sequence: P → H | ||||||
Compositional bias | 45-60 | Pro residues | ||||
Sequence: PPTMPPLPPINPGGPR | ||||||
Compositional bias | 64-105 | Polar residues | ||||
Sequence: FTPTALSNGINHSPPTLNGAPSPPQRFSNGPASSTSSALTNQ | ||||||
Compositional bias | 233-254 | Basic and acidic residues | ||||
Sequence: GKRPSPERREENSFDRDTIAPE | ||||||
Alternative sequence | VSP_008123 | 240-292 | in isoform 3 | |||
Sequence: RREENSFDRDTIAPEPPAKRVCTISPAPRHSPALTVPLMNPGGQFHPTPPPLQ → SCIIHLKSMGVASRHEYFSGTLQMPAHPVRNSTLENLWVDCSRSLRSTVLPFP | ||||||
Sequence conflict | 266 | in Ref. 4; AK307887 | ||||
Sequence: A → V | ||||||
Alternative sequence | VSP_008124 | 293-604 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 403-427 | Polar residues | ||||
Sequence: LVSRQHSPGSADSLSNDSQREFNSR | ||||||
Compositional bias | 570-604 | Polar residues | ||||
Sequence: SADCSVPSPALDKTSATTSRSSTPASVTAIDTNGL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF039200 EMBL· GenBank· DDBJ | AAC17499.1 EMBL· GenBank· DDBJ | mRNA | ||
AF068266 EMBL· GenBank· DDBJ | AAC19378.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF013970 EMBL· GenBank· DDBJ | AAC39841.1 EMBL· GenBank· DDBJ | mRNA | ||
AF069747 EMBL· GenBank· DDBJ | AAD02825.1 EMBL· GenBank· DDBJ | mRNA | ||
AF076461 EMBL· GenBank· DDBJ | AAD41221.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF076452 EMBL· GenBank· DDBJ | AAD41221.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF076453 EMBL· GenBank· DDBJ | AAD41221.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF076454 EMBL· GenBank· DDBJ | AAD41221.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF076455 EMBL· GenBank· DDBJ | AAD41221.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF076456 EMBL· GenBank· DDBJ | AAD41221.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF076457 EMBL· GenBank· DDBJ | AAD41221.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF076458 EMBL· GenBank· DDBJ | AAD41221.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF076459 EMBL· GenBank· DDBJ | AAD41221.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF076460 EMBL· GenBank· DDBJ | AAD41221.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK307887 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AK314159 EMBL· GenBank· DDBJ | BAG36843.1 EMBL· GenBank· DDBJ | mRNA | ||
AL034421 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL121906 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL162505 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471077 EMBL· GenBank· DDBJ | EAW76311.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC015066 EMBL· GenBank· DDBJ | AAH15066.1 EMBL· GenBank· DDBJ | mRNA | ||
BC016298 EMBL· GenBank· DDBJ | AAH16298.2 EMBL· GenBank· DDBJ | mRNA | ||
BC040344 EMBL· GenBank· DDBJ | AAH40344.1 EMBL· GenBank· DDBJ | mRNA | ||
AF052210 EMBL· GenBank· DDBJ | AAC64699.1 EMBL· GenBank· DDBJ | mRNA |