| UniProt ID | PP2AA_HUMAN | |
|---|---|---|
| UniProt AC | P67775 | |
| Protein Name | Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform | |
| Gene Name | PPP2CA | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 309 | |
| Subcellular Localization | Cytoplasm . Nucleus . Chromosome, centromere . Cytoplasm, cytoskeleton, spindle pole . In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles. Centromeric localization requires the pres | |
| Protein Description | PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGO2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at 'Ser-259'.. | |
| Protein Sequence | MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHVTRRTPDYFL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MDEKVFTK -------CCHHHHHH | 15.76 | - | |
| 4 | Acetylation | ----MDEKVFTKELD ----CCHHHHHHHHH | 38.08 | 23749302 | |
| 4 | Sumoylation | ----MDEKVFTKELD ----CCHHHHHHHHH | 38.08 | - | |
| 4 | Ubiquitination | ----MDEKVFTKELD ----CCHHHHHHHHH | 38.08 | 19608861 | |
| 4 | Sumoylation | ----MDEKVFTKELD ----CCHHHHHHHHH | 38.08 | 19608861 | |
| 8 | Ubiquitination | MDEKVFTKELDQWIE CCHHHHHHHHHHHHH | 44.83 | 21906983 | |
| 8 | Sumoylation | MDEKVFTKELDQWIE CCHHHHHHHHHHHHH | 44.83 | - | |
| 20 | Glutathionylation | WIEQLNECKQLSESQ HHHHHHHHHHCCHHH | 3.11 | 22555962 | |
| 21 | Ubiquitination | IEQLNECKQLSESQV HHHHHHHHHCCHHHH | 48.36 | 21906983 | |
| 24 | Phosphorylation | LNECKQLSESQVKSL HHHHHHCCHHHHHHH | 32.48 | 23312004 | |
| 26 | Phosphorylation | ECKQLSESQVKSLCE HHHHCCHHHHHHHHH | 36.58 | 28348404 | |
| 29 | Ubiquitination | QLSESQVKSLCEKAK HCCHHHHHHHHHHHH | 30.03 | 21906983 | |
| 29 | Acetylation | QLSESQVKSLCEKAK HCCHHHHHHHHHHHH | 30.03 | 25953088 | |
| 34 | Ubiquitination | QVKSLCEKAKEILTK HHHHHHHHHHHHHHC | 64.86 | 21906983 | |
| 36 | Ubiquitination | KSLCEKAKEILTKES HHHHHHHHHHHHCCC | 57.25 | 21890473 | |
| 36 | Acetylation | KSLCEKAKEILTKES HHHHHHHHHHHHCCC | 57.25 | 26051181 | |
| 41 | Acetylation | KAKEILTKESNVQEV HHHHHHHCCCCCCEE | 56.55 | 66701717 | |
| 41 | Ubiquitination | KAKEILTKESNVQEV HHHHHHHCCCCCCEE | 56.55 | 21906983 | |
| 43 | Phosphorylation | KEILTKESNVQEVRC HHHHHCCCCCCEEEC | 43.80 | 26437602 | |
| 74 | Ubiquitination | ELFRIGGKSPDTNYL HHHHCCCCCCCCCEE | 54.31 | 21906983 | |
| 75 | Phosphorylation | LFRIGGKSPDTNYLF HHHCCCCCCCCCEEE | 31.14 | 21712546 | |
| 78 | Phosphorylation | IGGKSPDTNYLFMGD CCCCCCCCCEEECCC | 29.19 | - | |
| 86 | Phosphorylation | NYLFMGDYVDRGYYS CEEECCCCCCCCCEE | 9.87 | - | |
| 124 | Phosphorylation | NHESRQITQVYGFYD CCCHHHHHEEEEHHH | 12.02 | 24043423 | |
| 127 | Phosphorylation | SRQITQVYGFYDECL HHHHHEEEEHHHHHH | 7.53 | 28152594 | |
| 130 | Phosphorylation | ITQVYGFYDECLRKY HHEEEEHHHHHHHHH | 13.38 | 28152594 | |
| 136 | Ubiquitination | FYDECLRKYGNANVW HHHHHHHHHCCCCHH | 44.56 | 21906983 | |
| 196 | Glutathionylation | VPHEGPMCDLLWSDP CCCCCCCCCEECCCC | 3.62 | 22555962 | |
| 212 | Phosphorylation | DRGGWGISPRGAGYT CCCCCCCCCCCCCCC | 12.47 | 26074081 | |
| 218 | Phosphorylation | ISPRGAGYTFGQDIS CCCCCCCCCCCCCHH | 9.81 | 26074081 | |
| 219 | Phosphorylation | SPRGAGYTFGQDISE CCCCCCCCCCCCHHH | 22.00 | 26074081 | |
| 225 | Phosphorylation | YTFGQDISETFNHAN CCCCCCHHHHHHHCC | 38.58 | 26074081 | |
| 248 | Phosphorylation | HQLVMEGYNWCHDRN HHHHHCCCCCCCCCC | 7.68 | 24927040 | |
| 265 | Phosphorylation | TIFSAPNYCYRCGNQ EEEECCCCHHHCCCE | 6.98 | 20090780 | |
| 266 | S-nitrosylation | IFSAPNYCYRCGNQA EEECCCCHHHCCCEE | 1.88 | 19483679 | |
| 266 | S-nitrosocysteine | IFSAPNYCYRCGNQA EEECCCCHHHCCCEE | 1.88 | - | |
| 267 | Phosphorylation | FSAPNYCYRCGNQAA EECCCCHHHCCCEEE | 9.89 | 28152594 | |
| 283 | Ubiquitination | MELDDTLKYSFLQFD EECCCCCEEEEEECC | 40.72 | 21906983 | |
| 284 | Nitration | ELDDTLKYSFLQFDP ECCCCCEEEEEECCC | 14.04 | - | |
| 284 | Phosphorylation | ELDDTLKYSFLQFDP ECCCCCEEEEEECCC | 14.04 | 28796482 | |
| 285 | Phosphorylation | LDDTLKYSFLQFDPA CCCCCEEEEEECCCC | 20.21 | 28796482 | |
| 295 | Methylation | QFDPAPRRGEPHVTR ECCCCCCCCCCCCCC | 53.41 | - | |
| 301 | Phosphorylation | RRGEPHVTRRTPDYF CCCCCCCCCCCCCCC | 16.05 | 29214152 | |
| 304 | Phosphorylation | EPHVTRRTPDYFL-- CCCCCCCCCCCCC-- | 19.74 | 30266825 | |
| 307 | Phosphorylation | VTRRTPDYFL----- CCCCCCCCCC----- | 14.16 | 20558158 | |
| 309 | Methylation | RRTPDYFL------- CCCCCCCC------- | 5.81 | 8206937 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 307 | Y | Phosphorylation | Kinase | EGFR | P00533 | PSP |
| 307 | Y | Phosphorylation | Kinase | INSR | P06213 | PSP |
| 307 | Y | Phosphorylation | Kinase | LCK | P06239 | PSP |
| 307 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
| - | K | Ubiquitination | E3 ubiquitin ligase | NOSIP | Q9Y314 | PMID:25546391 |
| - | K | Ubiquitination | E3 ubiquitin ligase | MPG | P29372 | PMID:22199232 |
| - | K | Ubiquitination | E3 ubiquitin ligase | MID1 | O15344 | PMID:11685209 |
| - | K | Ubiquitination | E3 ubiquitin ligase | UBR5 | O95071 | PMID:31392083 |
| - | K | Ubiquitination | E3 ubiquitin ligase | MPG | P29372 | PMID:25207814 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PP2AA_HUMAN !! | ||||||
* 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 PP2AA_HUMAN !! | ||||||
| Kegg Disease | |
|---|---|
| There are no disease associations of PTM sites. | |
| OMIM Disease | |
| There are no disease associations of PTM sites. | |
| Kegg Drug | |
| There are no disease associations of PTM sites. | |
| DrugBank | |
| DB00163 | Vitamin E |
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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-4, AND MASSSPECTROMETRY. | |
| Methylation | |
| Reference | PubMed |
| "The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo."; Favre B., Zolnierowicz S., Turowski P., Hemmings B.A.; J. Biol. Chem. 269:16311-16317(1994). Cited for: METHYLATION AT LEU-309. | |
| Phosphorylation | |
| Reference | PubMed |
| "Protein phosphatase 2A dephosphorylates simian virus 40 large Tantigen specifically at residues involved in regulation of DNA-bindingactivity."; Scheidtmann K.H., Virshup D.M., Kelly T.J.; J. Virol. 65:2098-2101(1991). Cited for: SITES OF DEPHOSPHORYLATION AT SV40 LARGE-T ANTIGEN. | |
