P70475 · MYT1L_RAT
- ProteinMyelin transcription factor 1-like protein
- GeneMyt1l
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1187 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcription factor that plays a key role in neuronal differentiation (PubMed:9373037).
Acts by specifically repressing expression of non-neuronal genes during neuron differentiation (By similarity).
In contrast to other transcription repressors that inhibit specific lineages, mediates repression of multiple differentiation programs (By similarity).
Also represses expression of negative regulators of neurogenesis, such as members of the Notch signaling pathway, including HES1 (By similarity).
The combination of three transcription factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to reprogram fibroblasts and other somatic cells into induced neuronal (iN) cells in vitro (By similarity).
Directly binds the 5'-AAGTT-3' core motif present on the promoter of target genes and represses transcription by recruiting a multiprotein complex containing SIN3B (By similarity).
The 5'-AAGTT-3' core motif is absent from the promoter of neural genes (By similarity).
Acts by specifically repressing expression of non-neuronal genes during neuron differentiation (By similarity).
In contrast to other transcription repressors that inhibit specific lineages, mediates repression of multiple differentiation programs (By similarity).
Also represses expression of negative regulators of neurogenesis, such as members of the Notch signaling pathway, including HES1 (By similarity).
The combination of three transcription factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to reprogram fibroblasts and other somatic cells into induced neuronal (iN) cells in vitro (By similarity).
Directly binds the 5'-AAGTT-3' core motif present on the promoter of target genes and represses transcription by recruiting a multiprotein complex containing SIN3B (By similarity).
The 5'-AAGTT-3' core motif is absent from the promoter of neural genes (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 31 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 36 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 49 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 55 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 505 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 510 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 523 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 529 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 549 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 554 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 567 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 573 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 904 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 909 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 922 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 928 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 953 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 958 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 971 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 977 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1006 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1011 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1024 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1030 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C |
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
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMyelin transcription factor 1-like protein
- Short namesMyT1-L; MyT1L
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP70475
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Preferentially binds to DNA binding sites that are in an open chromatin configuration.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000096675 | 1-1187 | Myelin transcription factor 1-like protein | |||
Sequence: MDVDAEEKRHRTRSKGVRVPVEPAIQELFSCPTPGCDGSGHVSGKYARHRSVYGCPLAKKRKTQDKQPQEPAPKRKPFAVKADSSSVDECYESDGTEDMDDKEEDDDEEFSEDNDEQGDDDDEDEVDREDEEEIEEEDDEDDEDDDDGDDVEEEEDDDDEEEEEEEEEEENEDHQMSCTRIMQDPEKDDNNNDEYDNYDELVAKSLLNLGKIAEDAAYRARTESEMNSNTSNSLEDDSDKNENLGRKSELSLDLDSDVVRETVDSLKLLAQGHGVVLSENISDRSYAEGMSQQDSRNMNYVMLGKPMNNGLMEKMVEESDEEVCLSSLECLRNQCFDLARKLSETNPQDRSQPPNMSVRQHVRQEDDFPGRTPDRSYSDMMNLMRLEEQLSPRSRTFSSCAKEDGCHERDDDTTSVNSDRSEEVFDMTKGNLTLLEKAIALETERAKAMREKMAMDAGRRDNLRSYEDQSPRQLAGEDRKSKSSDSHVKKPYYDPSRTEKRESKCPTPGCDGTGHVTGLYPHHRSLSGCPHKDRVPPEILAMHENVLKCPTPGCTGRGHVNSNRNSHRSLSGCPIAAAEKLAKAQEKHQSCDVSKSNQASDRVLRPMCFVKQLEIPQYGYRNNVPTTTPRSNLAKELEKYSKTSFEYNSYDNHTYGKRAIAPKVQTRDISPKGYDDAKRYCKNASPSSSTTSSYAPSSSSNLSCGGGSSASSTCSKSSFDYTHDMEAAHMAATAILNLSTRCREMPQNLSTKPQDLCTARNPDMEVDENGTLDLSMNKQRPRDSCCPVLTPLEPMSPQQQAVMSSRCFQLSEGDCWDLPVDYTKMKPRRVDEEDPKEITPEDLDPFQEALEERRYPGEVTIPSPKPKYPQCKESKKDLITLSGCPLADKSIRSMLATSSQELKCPTPGCDGSGHITGNYASHRSLSGCPRAKKSGIRIAQSKEDKEDQEPIRCPVPGCDGQGHITGKYASHRSASGCPLAAKRQKDGYLNGSQFSWKSVKTEGMSCPTPGCDGSGHVSGSFLTHRSLSGCPRATSAMKKAKLSGEQMLTIKQRASNGIENDEEIKQLDEEIKELNESNSQMEADMIKLRTQVTITTMESNLKTIEEENKVIEQQNESLLHELANLSQSLIHSLANIQLPHMDPINEQNFDAYVTTLTEMYTNQDRYQSPENKALLENIKQAVRGIQV | ||||||
Modified residue | 251 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Brain, testis and pituitary gland. Expression is higher in the brain than in the testis and pituitary gland. Highest level expression seen in the developing CNS.
Developmental stage
Detected at 11.5 dpc and expression is seen throughout the proliferating cortex neuroepithelium, developing medulla, and spinal cord. At 12.5 dpc found in the nasal epithelium and at 13.5 dpc detected in the trigeminal ganglia, dorsal root ganglia and the ganglion cell layer of the retina. At 14 dpc to 15 dpc, expressed at high levels in the brain and spinal cord and then levels subsequently decrease.
Structure
Family & Domains
Features
Showing features for compositional bias, region, zinc finger, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-17 | Basic and acidic residues | ||||
Sequence: MDVDAEEKRHRTRSKGV | ||||||
Region | 1-20 | Disordered | ||||
Sequence: MDVDAEEKRHRTRSKGVRVP | ||||||
Zinc finger | 22-65 | CCHHC-type 1 | ||||
Sequence: EPAIQELFSCPTPGCDGSGHVSGKYARHRSVYGCPLAKKRKTQD | ||||||
Region | 56-178 | Disordered | ||||
Sequence: PLAKKRKTQDKQPQEPAPKRKPFAVKADSSSVDECYESDGTEDMDDKEEDDDEEFSEDNDEQGDDDDEDEVDREDEEEIEEEDDEDDEDDDDGDDVEEEEDDDDEEEEEEEEEEENEDHQMSC | ||||||
Compositional bias | 90-172 | Acidic residues | ||||
Sequence: CYESDGTEDMDDKEEDDDEEFSEDNDEQGDDDDEDEVDREDEEEIEEEDDEDDEDDDDGDDVEEEEDDDDEEEEEEEEEEENE | ||||||
Region | 221-248 | Disordered | ||||
Sequence: RTESEMNSNTSNSLEDDSDKNENLGRKS | ||||||
Compositional bias | 343-359 | Polar residues | ||||
Sequence: SETNPQDRSQPPNMSVR | ||||||
Region | 343-422 | Disordered | ||||
Sequence: SETNPQDRSQPPNMSVRQHVRQEDDFPGRTPDRSYSDMMNLMRLEEQLSPRSRTFSSCAKEDGCHERDDDTTSVNSDRSE | ||||||
Compositional bias | 400-422 | Basic and acidic residues | ||||
Sequence: CAKEDGCHERDDDTTSVNSDRSE | ||||||
Compositional bias | 450-506 | Basic and acidic residues | ||||
Sequence: REKMAMDAGRRDNLRSYEDQSPRQLAGEDRKSKSSDSHVKKPYYDPSRTEKRESKCP | ||||||
Region | 450-509 | Disordered | ||||
Sequence: REKMAMDAGRRDNLRSYEDQSPRQLAGEDRKSKSSDSHVKKPYYDPSRTEKRESKCPTPG | ||||||
Zinc finger | 496-539 | CCHHC-type 2 | ||||
Sequence: SRTEKRESKCPTPGCDGTGHVTGLYPHHRSLSGCPHKDRVPPEI | ||||||
Zinc finger | 540-583 | CCHHC-type 3 | ||||
Sequence: LAMHENVLKCPTPGCTGRGHVNSNRNSHRSLSGCPIAAAEKLAK | ||||||
Region | 684-708 | Disordered | ||||
Sequence: ASPSSSTTSSYAPSSSSNLSCGGGS | ||||||
Zinc finger | 895-938 | CCHHC-type 4 | ||||
Sequence: LATSSQELKCPTPGCDGSGHITGNYASHRSLSGCPRAKKSGIRI | ||||||
Zinc finger | 944-987 | CCHHC-type 5 | ||||
Sequence: DKEDQEPIRCPVPGCDGQGHITGKYASHRSASGCPLAAKRQKDG | ||||||
Zinc finger | 997-1040 | CCHHC-type 6 | ||||
Sequence: KSVKTEGMSCPTPGCDGSGHVSGSFLTHRSLSGCPRATSAMKKA | ||||||
Coiled coil | 1055-1131 | |||||
Sequence: SNGIENDEEIKQLDEEIKELNESNSQMEADMIKLRTQVTITTMESNLKTIEEENKVIEQQNESLLHELANLSQSLIH |
Sequence similarities
Belongs to the MYT1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P70475-1
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
- Length1,187
- Mass (Da)132,926
- Last updated2017-06-07 v3
- Checksum10B2616415195DD1
P70475-2
- Name2
P70475-3
- Name3
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6A7T9 | A0A8I6A7T9_RAT | Myt1l | 328 | ||
A0A5H1ZRT6 | A0A5H1ZRT6_RAT | Myt1l | 1187 | ||
A0A8I6A056 | A0A8I6A056_RAT | Myt1l | 1164 | ||
F1M8L4 | F1M8L4_RAT | Myt1l | 1181 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-17 | Basic and acidic residues | ||||
Sequence: MDVDAEEKRHRTRSKGV | ||||||
Sequence conflict | 39 | in Ref. 1; AAC52728 | ||||
Sequence: S → T | ||||||
Compositional bias | 90-172 | Acidic residues | ||||
Sequence: CYESDGTEDMDDKEEDDDEEFSEDNDEQGDDDDEDEVDREDEEEIEEEDDEDDEDDDDGDDVEEEEDDDDEEEEEEEEEEENE | ||||||
Sequence conflict | 226 | in Ref. 1; AAC52728 | ||||
Sequence: M → V | ||||||
Sequence conflict | 237-239 | in Ref. 1; AAC52728 | ||||
Sequence: DSD → HSS | ||||||
Compositional bias | 343-359 | Polar residues | ||||
Sequence: SETNPQDRSQPPNMSVR | ||||||
Compositional bias | 400-422 | Basic and acidic residues | ||||
Sequence: CAKEDGCHERDDDTTSVNSDRSE | ||||||
Sequence conflict | 415 | in Ref. 1; AAC52728 | ||||
Sequence: S → T | ||||||
Compositional bias | 450-506 | Basic and acidic residues | ||||
Sequence: REKMAMDAGRRDNLRSYEDQSPRQLAGEDRKSKSSDSHVKKPYYDPSRTEKRESKCP | ||||||
Sequence conflict | 517 | in Ref. 1; AAC52728 | ||||
Sequence: T → N | ||||||
Sequence conflict | 561 | in Ref. 3; AAB40718 | ||||
Sequence: N → H | ||||||
Sequence conflict | 804 | in Ref. 3; AAB40718 | ||||
Sequence: S → T | ||||||
Sequence conflict | 918 | in Ref. 3; AAB40718 | ||||
Sequence: N → I | ||||||
Sequence conflict | 1019 | in Ref. 3; AAB40718 | ||||
Sequence: G → A | ||||||
Sequence conflict | 1092-1098 | in Ref. 3; AAB40718 | ||||
Sequence: VTITTME → ITTMD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U48809 EMBL· GenBank· DDBJ | AAC52728.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AABR07063792 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AABR07063793 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AABR07063794 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AABR07063795 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AABR07063796 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AABR07063797 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
U67081 EMBL· GenBank· DDBJ | AAB40718.1 EMBL· GenBank· DDBJ | mRNA |