UniProt ID | 2ABA_ARATH | |
---|---|---|
UniProt AC | Q38821 | |
Protein Name | Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform | |
Gene Name | PP2AB1 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 513 | |
Subcellular Localization | ||
Protein Description | The B regulatory subunit may modulate substrate selectivity and catalytic activity, and also may direct the localization of the catalytic enzyme to a particular subcellular compartment.. | |
Protein Sequence | MNGGDEVVAASADPSLPLEWRFSQVFGERSAGEEVQEVDIISAIEFDNSGNHLATGDRGGRVVLFERTDTNNSSGTRRELEEADYPLRHPEFRYKTEFQSHDPEFDYLKSLEIEEKINKIRWCQTANGALFLLSTNDKTIKFWKVQDKKIKKICDMNSDPSRTVGNGTVASSSNSNITNSCLVNGGVSEVNNSLCNDFSLPAGGISSLRLPVVVTSHESSPVARCRRVYAHAHDYHINSISNNSDGETFISADDLRINLWNLEISNQSFNIVDVKPAKMEDLSEVITSAEFHPTHCNMLAYSSSKGSIRLIDLRQSALCDSHSKLFEEPEQAGPKSFFTEIIASVSDIKFAKEGRYLLSRDYMTLKLWDINMDAGPVATFQVHEYLKPKLCDLYENDSIFDKFECCISGNGLRAATGSYSNLFRVFGVAPGSTETATLEASRNPMRRHVPIPSRPSRALSSITRVVSRGSESPGVDGNTNALDYTTKLLHLAWHPNENSIACAAANSLYMYYA | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MNGGDEVV -------CCCCCEEE | 10.70 | - | |
218 (in isoform 2) | Phosphorylation | - | 53.32 | 23111157 | |
219 | Phosphorylation | VVVTSHESSPVARCR EEEECCCCCHHHHHH | 34.22 | 25561503 | |
219 (in isoform 2) | Phosphorylation | - | 34.22 | 23111157 | |
220 | Phosphorylation | VVTSHESSPVARCRR EEECCCCCHHHHHHH | 22.02 | 23111157 | |
460 | Phosphorylation | SRPSRALSSITRVVS CCHHHHHHHHEEEHH | 20.79 | 30291188 | |
461 | Phosphorylation | RPSRALSSITRVVSR CHHHHHHHHEEEHHC | 28.91 | 23776212 | |
463 | Phosphorylation | SRALSSITRVVSRGS HHHHHHHEEEHHCCC | 21.25 | 23776212 | |
467 | Phosphorylation | SSITRVVSRGSESPG HHHEEEHHCCCCCCC | 28.24 | 30407730 | |
470 | Phosphorylation | TRVVSRGSESPGVDG EEEHHCCCCCCCCCC | 33.52 | 19880383 | |
472 | Phosphorylation | VVSRGSESPGVDGNT EHHCCCCCCCCCCCC | 28.75 | 19880383 | |
479 | Phosphorylation | SPGVDGNTNALDYTT CCCCCCCCCHHHHHH | 27.65 | 23776212 |
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 2ABA_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of 2ABA_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 2ABA_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of 2ABA_ARATH !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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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-460, AND MASSSPECTROMETRY. |