Q8VYA5 · RSZ33_ARATH
- ProteinSerine/arginine-rich splicing factor RS2Z33
- GeneRS2Z33
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids290 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Splicing factor involved in constitutive and/or alternative splicing. Regulates the splicing of its own pre-mRNA and the alternative splicing of RS30, RS31 and RS34. Associates the cyclin-dependent kinase G1 (CDKG1) with the spliceosome and recruits it to U1 snRNP to facilitate splicing.
Miscellaneous
The splicing pattern of the pre-mRNA is regulated in a tissue-specific manner and by development, and changes in response to various types of abiotic stresses (PubMed:17319848), but is not affected by the light/dark regimes (PubMed:24763593).
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nuclear speck | |
Cellular Component | spliceosomal complex | |
Molecular Function | mRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | mRNA splicing, via spliceosome | |
Biological Process | RNA splicing | |
Biological Process | spliceosomal complex assembly |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameSerine/arginine-rich splicing factor RS2Z33
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8VYA5
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000416998 | 1-290 | Serine/arginine-rich splicing factor RS2Z33 | |||
Sequence: MPRYDDRYGNTRLYVGRLSSRTRTRDLERLFSRYGRVRDVDMKRDYAFVEFGDPRDADDARHYLDGRDFDGSRITVEFSRGAPRGSRDFDSRGPPPGAGRCFNCGVDGHWARDCTAGDWKNKCYRCGERGHIERNCKNSPKKLRRSGSYSRSPVRSRSPRRRRSPSRSLSRSRSYSRSRSPVRRRERSVEERSRSPKRMDDSLSPRARDRSPVLDDEGSPKIIDGSPPPSPKLQKEVGSDRDGGSPQDNGRNSVVSPVVGAGGDSSKEDRSPVDDDYEPNRTSPRGSESP | ||||||
Modified residue | 164 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 166 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 180 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 202 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 204 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 211 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 219 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 226 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 230 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 239 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 245 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 256 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 271 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 283 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 287 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Extensively phosphorylated on serine residues in the RS domain.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in roots, flowers, anthers, pollen, ovules, style and developing seeds. Not detected in stems or leaves.
Gene expression databases
Interaction
Subunit
Component of the spliceosome. Interacts with SNRNP35, CDKG1, cyp59, SR33, SR34, RSZ21, RSZ22, SCL28, SCL30, SCL30A, SCL33 and SC35 (PubMed:10593939, PubMed:12176998, PubMed:15987817, PubMed:16497658, PubMed:23404887).
Interacts with MOS14 (PubMed:21738492).
Interacts with MOS14 (PubMed:21738492).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, zinc finger, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-81 | RRM | ||||
Sequence: TRLYVGRLSSRTRTRDLERLFSRYGRVRDVDMKRDYAFVEFGDPRDADDARHYLDGRDFDGSRITVEFSRG | ||||||
Zinc finger | 99-116 | CCHC-type 1 | ||||
Sequence: GRCFNCGVDGHWARDCTA | ||||||
Zinc finger | 121-138 | CCHC-type 2 | ||||
Sequence: NKCYRCGERGHIERNCKN | ||||||
Region | 135-290 | Disordered | ||||
Sequence: NCKNSPKKLRRSGSYSRSPVRSRSPRRRRSPSRSLSRSRSYSRSRSPVRRRERSVEERSRSPKRMDDSLSPRARDRSPVLDDEGSPKIIDGSPPPSPKLQKEVGSDRDGGSPQDNGRNSVVSPVVGAGGDSSKEDRSPVDDDYEPNRTSPRGSESP | ||||||
Compositional bias | 179-217 | Basic and acidic residues | ||||
Sequence: RSPVRRRERSVEERSRSPKRMDDSLSPRARDRSPVLDDE | ||||||
Compositional bias | 267-282 | Basic and acidic residues | ||||
Sequence: KEDRSPVDDDYEPNRT |
Sequence similarities
Belongs to the splicing factor SR family. RS2Z subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q8VYA5-1
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
- Length290
- Mass (Da)32,893
- Last updated2002-03-01 v1
- Checksum4B0407A7E106EFA2
Q8VYA5-2
- Name2
- Differences from canonical
- 1-49: MPRYDDRYGNTRLYVGRLSSRTRTRDLERLFSRYGRVRDVDMKRDYAFV → MWENTPCMWSLLSSHFRNQ
Q8VYA5-3
- Name3
- Differences from canonical
- 1-41: Missing
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_043113 | 1-41 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_043112 | 1-49 | in isoform 2 | |||
Sequence: MPRYDDRYGNTRLYVGRLSSRTRTRDLERLFSRYGRVRDVDMKRDYAFV → MWENTPCMWSLLSSHFRNQ | ||||||
Sequence conflict | 50 | in Ref. 6; BAD44429 | ||||
Sequence: E → V | ||||||
Sequence conflict | 139 | in Ref. 1; CAC03605 | ||||
Sequence: S → Q | ||||||
Sequence conflict | 173 | in Ref. 1; CAC03605 | ||||
Sequence: R → G | ||||||
Compositional bias | 179-217 | Basic and acidic residues | ||||
Sequence: RSPVRRRERSVEERSRSPKRMDDSLSPRARDRSPVLDDE | ||||||
Compositional bias | 267-282 | Basic and acidic residues | ||||
Sequence: KEDRSPVDDDYEPNRT |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ293801 EMBL· GenBank· DDBJ | CAC03605.1 EMBL· GenBank· DDBJ | mRNA | ||
AC005896 EMBL· GenBank· DDBJ | AAC98054.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC09385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC09386.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC09387.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | ANM63217.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | ANM63218.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | ANM63219.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY072315 EMBL· GenBank· DDBJ | AAL61922.1 EMBL· GenBank· DDBJ | mRNA | ||
AY114563 EMBL· GenBank· DDBJ | AAM47882.1 EMBL· GenBank· DDBJ | mRNA | ||
AK176551 EMBL· GenBank· DDBJ | BAD44314.1 EMBL· GenBank· DDBJ | mRNA | ||
BX842463 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BX842467 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AK176666 EMBL· GenBank· DDBJ | BAD44429.1 EMBL· GenBank· DDBJ | mRNA |