Q99MR6 · SRRT_MOUSE
- ProteinSerrate RNA effector molecule homolog
- GeneSrrt
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids875 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped RNA); however interaction is probably mediated via its interaction with NCBP1/CBP80 component of the CBC complex. Involved in cell cycle progression at S phase. Does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription.
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 | cytoplasm | |
Cellular Component | nuclear body | |
Cellular Component | nucleoplasm | |
Cellular Component | ribonucleoprotein complex | |
Molecular Function | DNA binding | |
Molecular Function | mRNA cap binding complex binding | |
Molecular Function | protein-macromolecule adaptor activity | |
Biological Process | mRNA processing | |
Biological Process | neuronal stem cell population maintenance | |
Biological Process | positive regulation of neurogenesis | |
Biological Process | primary miRNA processing | |
Biological Process | regulation of DNA-templated transcription |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerrate RNA effector molecule homolog
- 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 accessionQ99MR6
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Predominantly nuclear. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent way.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Death around the time of implantation. Deletion in adults leads to proliferative arrest and bone marrow hypoplasia whereas parenchymal organs composed of nonproliferating cells are unaffected.
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-acetylglycine | ||||
Sequence: G | ||||||
Chain | PRO_0000220966 | 2-875 | Serrate RNA effector molecule homolog | |||
Sequence: GDSDDEYDRRRRDKFRRERSDYDRSRERDERRRGDDWNDREWDRGRERRSRGEYRDYDRNRRERFSPPRHELSPPQKRMRRDWDEHSSDPYHSGYDMPYAGGGGGPTYGPPQPWGHPDVHIMQHHVLPIQARLGSIAEIDLGVPPPIMKSFKEFLLSLDDSVDETEAVKRYNDYKLDFRRQQMQDFFLAHKDEEWFRSKYHPDEVGKRRQEARGALQNRLKVFLSLMESGWFDNLLLDIDKADAIVKMLDAAVIKMEGGTENDLRILEQEEEEEQAGKTGEASKKEEARAGPALGEGERKANDKDEKKEDGKQAENDSSNDDKTKKSEGDGDKEEKKEEAEKEAKKSKKRNRKQSGDDSFDEGSVSESESESEGGQAEEEKEEAEEALKEKEKPKEEEKEKPKDAAGLECKPRPLHKTCSLFMRNIAPNISRAEIISLCKRYPGFMRVALSEPQPERRFFRRGWVTFDRSVNIKEICWNLQNIRLRECELSPGVNRDLTRRVRNINGITQHKQIVRNDIKLAAKLIHTLDDRTQLWASEPGTPPVPTSLPSQNPILKNITDYLIEEVSAEEEELLGSSGGPPPEEPPKEGNPAEINVERDEKLIKVLDKLLLYLRIVHSLDYYNTCEYPNEDEMPNRCGIIHVRGPMPPNRISHGEVLEWQKTFEEKLTPLLSVRESLSEEEAQKMGRKDPEQEVEKFVTSNTQELGKDKWLCPLSGKKFKGPEFVRKHIFNKHAEKIEEVKKEVAFFNNFLTDAKRPALPEIKPAQPPGPAQILPPGLTPGLPYPHQTPQGLMPYGQPRPPILGYGAGAVRPAVPTGGPPYPHAPYGAGRGNYDAFRGQGGYPGKPRNRMVRGDPRAIVEYRDLDAPDDVDFF | ||||||
Modified residue | 4 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 8 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 67 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 74 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 136 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 150 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 492 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 539 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 543 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 569 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 670 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 678 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 832 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 839 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 849 | Omega-N-methylarginine | ||||
Sequence: R |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed, with a preference for proliferating cells. Highly expressed in hematopoietic tissues and reduced or absent expression in parenchymal organs like liver and kidney. In the brain, expressed in the subventricular zone by niche astrocytes, ependymal cells and neural stem cells. In this cerebral context, expressed in slowly dividing cells.
Induction
Upon cell proliferation.
Gene expression databases
Interaction
Subunit
Interacts with CASP8AP2 and ERBB4 (By similarity).
Interacts with NCBP1/CBP80 and DROSHA (PubMed:19632182).
Interacts with LUZP4 (By similarity).
Interacts with NCBP2/CBP20 and NCBP3 (By similarity).
Interacts with MTREX (By similarity).
Interacts with NCBP1/CBP80 and DROSHA (PubMed:19632182).
Interacts with LUZP4 (By similarity).
Interacts with NCBP2/CBP20 and NCBP3 (By similarity).
Interacts with MTREX (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-90 | Disordered | ||||
Sequence: MGDSDDEYDRRRRDKFRRERSDYDRSRERDERRRGDDWNDREWDRGRERRSRGEYRDYDRNRRERFSPPRHELSPPQKRMRRDWDEHSSD | ||||||
Compositional bias | 272-361 | Basic and acidic residues | ||||
Sequence: EEEEQAGKTGEASKKEEARAGPALGEGERKANDKDEKKEDGKQAENDSSNDDKTKKSEGDGDKEEKKEEAEKEAKKSKKRNRKQSGDDSF | ||||||
Region | 272-411 | Disordered | ||||
Sequence: EEEEQAGKTGEASKKEEARAGPALGEGERKANDKDEKKEDGKQAENDSSNDDKTKKSEGDGDKEEKKEEAEKEAKKSKKRNRKQSGDDSFDEGSVSESESESEGGQAEEEKEEAEEALKEKEKPKEEEKEKPKDAAGLEC | ||||||
Compositional bias | 363-382 | Acidic residues | ||||
Sequence: EGSVSESESESEGGQAEEEK | ||||||
Compositional bias | 383-411 | Basic and acidic residues | ||||
Sequence: EEAEEALKEKEKPKEEEKEKPKDAAGLEC | ||||||
Region | 571-597 | Disordered | ||||
Sequence: EEEELLGSSGGPPPEEPPKEGNPAEIN | ||||||
Region | 834-853 | Disordered | ||||
Sequence: NYDAFRGQGGYPGKPRNRMV |
Sequence similarities
Belongs to the ARS2 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q99MR6-1
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.
- NameA
- Length875
- Mass (Da)100,452
- Last updated2001-06-01 v1
- Checksum9571445674452886
Q99MR6-2
- NameB
- Differences from canonical
- 775-779: ILPPG → S
Q99MR6-3
- NameC
Q99MR6-4
- NameD
- Differences from canonical
- 809-815: Missing
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1Y7VNN4 | A0A1Y7VNN4_MOUSE | Srrt | 63 | ||
A0A0G2JG75 | A0A0G2JG75_MOUSE | Srrt | 52 | ||
A0A0G2JG65 | A0A0G2JG65_MOUSE | Srrt | 269 | ||
A0A0G2JE73 | A0A0G2JE73_MOUSE | Srrt | 50 | ||
A0A0G2JDF1 | A0A0G2JDF1_MOUSE | Srrt | 239 | ||
A0A0G2JDF8 | A0A0G2JDF8_MOUSE | Srrt | 517 | ||
A0A0G2JDN3 | A0A0G2JDN3_MOUSE | Srrt | 467 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 272-361 | Basic and acidic residues | ||||
Sequence: EEEEQAGKTGEASKKEEARAGPALGEGERKANDKDEKKEDGKQAENDSSNDDKTKKSEGDGDKEEKKEEAEKEAKKSKKRNRKQSGDDSF | ||||||
Compositional bias | 363-382 | Acidic residues | ||||
Sequence: EGSVSESESESEGGQAEEEK | ||||||
Compositional bias | 383-411 | Basic and acidic residues | ||||
Sequence: EEAEEALKEKEKPKEEEKEKPKDAAGLEC | ||||||
Sequence conflict | 567 | in Ref. 3; BAE29458 | ||||
Sequence: E → G | ||||||
Alternative sequence | VSP_000325 | 775-779 | in isoform B and isoform C | |||
Sequence: ILPPG → S | ||||||
Alternative sequence | VSP_000326 | 809-815 | in isoform C and isoform D | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF312033 EMBL· GenBank· DDBJ | AAK28817.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF312033 EMBL· GenBank· DDBJ | AAK28818.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF312033 EMBL· GenBank· DDBJ | AAK28819.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF312033 EMBL· GenBank· DDBJ | AAK28820.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC019117 EMBL· GenBank· DDBJ | AAH19117.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC066831 EMBL· GenBank· DDBJ | AAH66831.1 EMBL· GenBank· DDBJ | mRNA | ||
AK150310 EMBL· GenBank· DDBJ | BAE29458.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |