UniProt ID | NCBP2_ARATH | |
---|---|---|
UniProt AC | Q9XFD1 | |
Protein Name | Nuclear cap-binding protein subunit 2 | |
Gene Name | CBP20 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 257 | |
Subcellular Localization | Nucleus . Cytoplasm . Predominantly nuclear. | |
Protein Description | Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5' cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing and RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs). The CBC complex is involved in miRNA-mediated RNA interference and is required for primary miRNA processing. In the CBC complex, CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires ABH1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. CBP20 also plays a role in stabilization of ABH1/CBP80 and ABH1/CBP80 localization to the nucleus. Involved in flowering regulation via its interaction with FRIGIDA.. | |
Protein Sequence | MASLFKEQAKLSAYRDRRFSGTQEEFDEALRASTTVYIGNVSFYTTEEQLYELFSRAGEIKKIIMGLDKNTKTPCGFCFVLFYSREDTEDAVKYISGTILDDRPIRVDFDWGFQEGRQWGRGRSGGQVRDEYRTDYDPARGGYGKLVQKELEAQRQLVDYGTGSLGAYPQAAPTNYGNGRRGGGNYGQGGQNRHGRGDYHRKRQRDDDRYGRDNSRRNTDHESRRDTDSDMRPEKNPRFRESGDSDDDGEDDRKRRS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
20 | Phosphorylation | AYRDRRFSGTQEEFD HHHHCCCCCCHHHHH | 38.84 | 30291188 | |
242 | Phosphorylation | KNPRFRESGDSDDDG CCCCHHHCCCCCCCC | 43.58 | 23776212 | |
245 | Phosphorylation | RFRESGDSDDDGEDD CHHHCCCCCCCCCCH | 46.60 | 19880383 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of NCBP2_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NCBP2_ARATH !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of NCBP2_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
VIP2_ARATH | VIP2 | physical | 23424246 | |
SRRT_ARATH | SE | physical | 24137006 | |
FRIG0_ARATH | FRI | physical | 19429606 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Phosphorylation | |
Reference | PubMed |
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASSSPECTROMETRY. |