Q6PFR5 · TRA2A_MOUSE
- ProteinTransformer-2 protein homolog alpha
- GeneTra2a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids281 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing.
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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Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Cellular Component | spliceosomal complex | |
Molecular Function | identical protein binding | |
Molecular Function | RNA binding | |
Biological Process | mRNA processing | |
Biological Process | positive regulation of mRNA splicing, via spliceosome | |
Biological Process | RNA splicing |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameTransformer-2 protein homolog alpha
- Short namesTRA-2 alpha; TRA2-alpha
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ6PFR5
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Modified residue | 2 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000081982 | 2-281 | Transformer-2 protein homolog alpha | |||
Sequence: SDVEENNFEGRESRSQSKSPTGTPARVKSESRSGSRSPSRVSKHSESHSRSRSKSRSRSRRHSHRRYTRSRSHSHRRRSRSRSYTPEYRRRRSRSHSPMSNRRRHTGSRANPDPNTCLGVFGLSLYTTERDLREVFSRYGPLSGVNVVYDQRTGRSRGFAFVYFERIDDSKEAMERANGMELDGRRIRVDYSITKRAHTPTPGIYMGRPTHSGGGGGGGGGGGGGGGGGGGRRRDSYYDRGYDRGYDRYEDYDYRRRSPSPYYSRYRSRSRSRSYSPRRY | ||||||
Modified residue | 14 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 24 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 80 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 82 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 84 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 86 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 94 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 96 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 196 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 200 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 202 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 233 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 237 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated in the RS domains.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in inner ear.
Interaction
Subunit
Binds to A3 enhancer proteins SRp75, SRp55, SRp40 and SRp30 (Probable). Interacts with ILDR1 (via C-terminus) and ILDR2 (PubMed:28785060).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6PFR5 | Nol3 Q9D1X0 | 4 | EBI-913075, EBI-913097 | |
BINARY | Q6PFR5 | Srsf7 Q8BL97 | 4 | EBI-913075, EBI-913123 | |
BINARY | Q6PFR5 | Tra2a Q6PFR5 | 2 | EBI-913075, EBI-913075 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-116 | Disordered | ||||
Sequence: MSDVEENNFEGRESRSQSKSPTGTPARVKSESRSGSRSPSRVSKHSESHSRSRSKSRSRSRRHSHRRYTRSRSHSHRRRSRSRSYTPEYRRRRSRSHSPMSNRRRHTGSRANPDPN | ||||||
Compositional bias | 14-37 | Polar residues | ||||
Sequence: SRSQSKSPTGTPARVKSESRSGSR | ||||||
Compositional bias | 50-86 | Basic residues | ||||
Sequence: SRSRSKSRSRSRRHSHRRYTRSRSHSHRRRSRSRSYT | ||||||
Domain | 117-195 | RRM | ||||
Sequence: TCLGVFGLSLYTTERDLREVFSRYGPLSGVNVVYDQRTGRSRGFAFVYFERIDDSKEAMERANGMELDGRRIRVDYSIT | ||||||
Region | 196-223 | Linker | ||||
Sequence: KRAHTPTPGIYMGRPTHSGGGGGGGGGG | ||||||
Region | 199-281 | Disordered | ||||
Sequence: HTPTPGIYMGRPTHSGGGGGGGGGGGGGGGGGGGRRRDSYYDRGYDRGYDRYEDYDYRRRSPSPYYSRYRSRSRSRSYSPRRY | ||||||
Compositional bias | 234-261 | Basic and acidic residues | ||||
Sequence: RRDSYYDRGYDRGYDRYEDYDYRRRSPS |
Sequence similarities
Belongs to the splicing factor SR family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length281
- Mass (Da)32,316
- Last updated2004-07-05 v1
- Checksum8074C89D4494D7F0
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0N4SVC2 | A0A0N4SVC2_MOUSE | Tra2a | 280 | ||
A0A0N4SV13 | A0A0N4SV13_MOUSE | Tra2a | 59 | ||
E9QP00 | E9QP00_MOUSE | Tra2a | 282 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 14-37 | Polar residues | ||||
Sequence: SRSQSKSPTGTPARVKSESRSGSR | ||||||
Compositional bias | 50-86 | Basic residues | ||||
Sequence: SRSRSKSRSRSRRHSHRRYTRSRSHSHRRRSRSRSYT | ||||||
Compositional bias | 234-261 | Basic and acidic residues | ||||
Sequence: RRDSYYDRGYDRGYDRYEDYDYRRRSPS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC057448 EMBL· GenBank· DDBJ | AAH57448.1 EMBL· GenBank· DDBJ | mRNA |