Q04888 · SOX10_MOUSE
- ProteinTranscription factor SOX-10
- GeneSox10
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids466 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcription factor that plays a central role in developing and mature glia (PubMed:24204311, PubMed:27532821).
Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination (PubMed:24204311, PubMed:27532821).
Once induced, MYRF cooperates with SOX10 to implement the myelination program (PubMed:24204311).
Transcriptional activator of MITF, acting synergistically with PAX3 (By similarity).
Transcriptional activator of MBP, via binding to the gene promoter (By similarity).
Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination (PubMed:24204311, PubMed:27532821).
Once induced, MYRF cooperates with SOX10 to implement the myelination program (PubMed:24204311).
Transcriptional activator of MITF, acting synergistically with PAX3 (By similarity).
Transcriptional activator of MBP, via binding to the gene promoter (By similarity).
Features
Showing features for dna binding.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 104-172 | HMG box | ||||
Sequence: VKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESDKRPFIEEAERLRMQHKKDHPDYK |
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 SOX-10
- 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 accessionQ04888
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion outer membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Defects in Sox10 are the cause of the mouse mutant dominant megacolon (dom). While dom/+ heterozygous mice display regional deficiencies of neural crest-derived enteric ganglia in the distal colon, dom/dom homozygous animals are embryonic lethal.
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 11 | |||||
Sequence: E → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 8 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000048747 | 1-466 | Transcription factor SOX-10 | |||
Sequence: MAEEQDLSEVELSPVGSEEPRCLSPGSAPSLGPDGGGGGSGLRASPGPGELGKVKKEQQDGEADDDKFPVCIREAVSQVLSGYDWTLVPMPVRVNGASKSKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESDKRPFIEEAERLRMQHKKDHPDYKYQPRRRKNGKAAQGEAECPGGEAEQGGAAAIQAHYKSAHLDHRHPEEGSPMSDGNPEHPSGQSHGPPTPPTTPKTELQSGKADPKRDGRSLGEGGKPHIDFGNVDIGEISHEVMSNMETFDVTELDQYLPPNGHPGHVGSYSAAGYGLGSALAVASGHSAWISKPPGVALPTVSPPGVDAKAQVKTETTGPQGPPHYTDQPSTSQIAYTSLSLPHYGSAFPSISRPQFDYSDHQPSGPYYGHAGQASGLYSAFSYMGPSQRPLYTAISDPSPSGPQSHSPTHWEQPVYTTLSRP | ||||||
Modified residue | 24 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in oligodendroglia of the spinal tube (at protein level).
Developmental stage
Expressed in the motor neuron progenitor domain of the spinal tube from 11.5 dpc to postnatal day 6.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-67 | Disordered | ||||
Sequence: MAEEQDLSEVELSPVGSEEPRCLSPGSAPSLGPDGGGGGSGLRASPGPGELGKVKKEQQDGEADDDK | ||||||
Compositional bias | 53-67 | Basic and acidic residues | ||||
Sequence: KVKKEQQDGEADDDK | ||||||
Region | 62-102 | Dimerization (DIM) | ||||
Sequence: EADDDKFPVCIREAVSQVLSGYDWTLVPMPVRVNGASKSKP | ||||||
Compositional bias | 160-184 | Basic and acidic residues | ||||
Sequence: LRMQHKKDHPDYKYQPRRRKNGKAA | ||||||
Region | 160-200 | Disordered | ||||
Sequence: LRMQHKKDHPDYKYQPRRRKNGKAAQGEAECPGGEAEQGGA | ||||||
Region | 213-275 | Disordered | ||||
Sequence: DHRHPEEGSPMSDGNPEHPSGQSHGPPTPPTTPKTELQSGKADPKRDGRSLGEGGKPHIDFGN | ||||||
Region | 228-310 | Transactivation domain (TAM) | ||||
Sequence: PEHPSGQSHGPPTPPTTPKTELQSGKADPKRDGRSLGEGGKPHIDFGNVDIGEISHEVMSNMETFDVTELDQYLPPNGHPGHV | ||||||
Compositional bias | 251-266 | Basic and acidic residues | ||||
Sequence: SGKADPKRDGRSLGEG | ||||||
Region | 344-375 | Disordered | ||||
Sequence: TVSPPGVDAKAQVKTETTGPQGPPHYTDQPST | ||||||
Region | 353-466 | Transactivation domain (TAC) | ||||
Sequence: KAQVKTETTGPQGPPHYTDQPSTSQIAYTSLSLPHYGSAFPSISRPQFDYSDHQPSGPYYGHAGQASGLYSAFSYMGPSQRPLYTAISDPSPSGPQSHSPTHWEQPVYTTLSRP | ||||||
Compositional bias | 357-375 | Polar residues | ||||
Sequence: KTETTGPQGPPHYTDQPST | ||||||
Region | 433-466 | Disordered | ||||
Sequence: RPLYTAISDPSPSGPQSHSPTHWEQPVYTTLSRP | ||||||
Compositional bias | 436-466 | Polar residues | ||||
Sequence: YTAISDPSPSGPQSHSPTHWEQPVYTTLSRP |
Domain
The transactivation domains TAM and TAC (for transactivation domain in the middle and at the C-terminus, respectively) are required to contact transcriptional coactivators and basal transcriptional machinery components and thereby induce gene transactivation.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length466
- Mass (Da)49,949
- Last updated1999-07-15 v2
- Checksum84862547F039E71F
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8VI24 | A0A2R8VI24_MOUSE | Sox10 | 205 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 41 | in Ref. 4; AAB49282 | ||||
Sequence: G → V | ||||||
Compositional bias | 53-67 | Basic and acidic residues | ||||
Sequence: KVKKEQQDGEADDDK | ||||||
Sequence conflict | 119 | in Ref. 6; CAA79484 | ||||
Sequence: R → P | ||||||
Compositional bias | 160-184 | Basic and acidic residues | ||||
Sequence: LRMQHKKDHPDYKYQPRRRKNGKAA | ||||||
Compositional bias | 251-266 | Basic and acidic residues | ||||
Sequence: SGKADPKRDGRSLGEG | ||||||
Sequence conflict | 357 | in Ref. 4; AAB49282 | ||||
Sequence: K → E | ||||||
Compositional bias | 357-375 | Polar residues | ||||
Sequence: KTETTGPQGPPHYTDQPST | ||||||
Compositional bias | 436-466 | Polar residues | ||||
Sequence: YTAISDPSPSGPQSHSPTHWEQPVYTTLSRP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF017182 EMBL· GenBank· DDBJ | AAB99738.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF047043 EMBL· GenBank· DDBJ | AAC24564.1 EMBL· GenBank· DDBJ | mRNA | ||
U66141 EMBL· GenBank· DDBJ | AAB49282.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
BC018551 EMBL· GenBank· DDBJ | AAH18551.1 EMBL· GenBank· DDBJ | mRNA | ||
BC023356 EMBL· GenBank· DDBJ | AAH23356.1 EMBL· GenBank· DDBJ | mRNA | ||
BC025171 EMBL· GenBank· DDBJ | AAH25171.1 EMBL· GenBank· DDBJ | mRNA | ||
Z18959 EMBL· GenBank· DDBJ | CAA79484.1 EMBL· GenBank· DDBJ | mRNA | ||
U70441 EMBL· GenBank· DDBJ | AAC52859.1 EMBL· GenBank· DDBJ | mRNA |