Basic Information
Gene ID
Position
GWHBAVD00000011:65588939-65592166 (-)
3227bp
Gene Type
gene
Gene Description (Protein Product)
serine arginine-rich splicing factor
Organism
Also AS AT4G35785evm.TU.chr9.352

Gene Structure

upstream:

Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
Ginchr9.848 serine arginine-rich splicing factor
Ginchr9.929 Ubiquitin-like domain
Ginchr9.758 Zinc knuckle

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Annotation

Orthologous Group
Orthologous ID Species Number All hits in PereRegDB Hits of this species Orthologous Detail

Expression Profile
DataSet Number of Samples expressed(TPM>1) Mean Min Max Standard deviation(SD) Coeffcient variation(CV)


Pathway
GO Term Description GO Category
GO:0003674 molecular_function MF
GO:0003676 nucleic acid binding MF
GO:0003723 RNA binding MF
GO:0005488 binding MF
GO:0006139 nucleobase-containing compound metabolic process BP
GO:0006325 chromatin organization BP
GO:0006396 RNA processing BP
GO:0006464 protein modification process BP
GO:0006473 protein acetylation BP
GO:0006475 internal protein amino acid acetylation BP
GO:0006725 cellular aromatic compound metabolic process BP
GO:0006807 nitrogen compound metabolic process BP
GO:0006996 organelle organization BP
GO:0008150 biological_process BP
GO:0008152 metabolic process BP
GO:0008380 RNA splicing BP
GO:0009314 response to radiation BP
GO:0009416 response to light stimulus BP
GO:0009628 response to abiotic stimulus BP
GO:0009642 response to light intensity BP
GO:0009644 response to high light intensity BP
GO:0009987 cellular process BP
GO:0010467 gene expression BP
GO:0010468 regulation of gene expression BP
GO:0016043 cellular component organization BP
GO:0016070 RNA metabolic process BP
GO:0016569 obsolete covalent chromatin modification BP
GO:0016570 histone modification BP
GO:0016573 histone acetylation BP
GO:0018193 peptidyl-amino acid modification BP
GO:0018205 peptidyl-lysine modification BP
GO:0018393 internal peptidyl-lysine acetylation BP
GO:0018394 peptidyl-lysine acetylation BP
GO:0019219 regulation of nucleobase-containing compound metabolic process BP
GO:0019222 regulation of metabolic process BP
GO:0019538 protein metabolic process BP
GO:0031323 regulation of cellular metabolic process BP
GO:0034641 cellular nitrogen compound metabolic process BP
GO:0036211 protein modification process BP
GO:0043170 macromolecule metabolic process BP
GO:0043412 macromolecule modification BP
GO:0043484 regulation of RNA splicing BP
GO:0043543 protein acylation BP
GO:0044237 cellular metabolic process BP
GO:0044238 primary metabolic process BP
GO:0044260 cellular macromolecule metabolic process BP
GO:0044267 protein metabolic process BP
GO:0046483 heterocycle metabolic process BP
GO:0050789 regulation of biological process BP
GO:0050794 regulation of cellular process BP
GO:0050896 response to stimulus BP
GO:0051171 regulation of nitrogen compound metabolic process BP
GO:0051252 regulation of RNA metabolic process BP
GO:0051276 chromosome organization BP
GO:0060255 regulation of macromolecule metabolic process BP
GO:0065007 biological regulation BP
GO:0071704 organic substance metabolic process BP
GO:0071840 cellular component organization or biogenesis BP
GO:0080090 regulation of primary metabolic process BP
GO:0090304 nucleic acid metabolic process BP
GO:0097159 organic cyclic compound binding MF
GO:1901360 organic cyclic compound metabolic process BP
GO:1901363 heterocyclic compound binding MF
GO:1901564 organonitrogen compound metabolic process BP
KEGG Term Name Description
map03040 Spliceosome After transcription, eukaryotic mRNA precursors contain protein-coding exons and noncoding introns. In the following splicing, introns are excised and exons are joined by a macromolecular complex, the spliceosome. The standard spliceosome is made up of five small nuclear ribonucleoproteins (snRNPs), U1, U2, U4, U5, and U6 snRNPs, and several spliceosome-associated proteins (SAPs). Spliceosomes are not a simple stable complex, but a dynamic family of particles that assemble on the mRNA precursor and help fold it into a conformation that allows transesterification to proceed. Various spliceosome forms (e.g. A-, B- and C-complexes) have been identified.