| UniProt ID | 2AAA_HUMAN | |
|---|---|---|
| UniProt AC | P30153 | |
| Protein Name | Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform | |
| Gene Name | PPP2R1A | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 589 | |
| Subcellular Localization | Cytoplasm . Chromosome, centromere . Lateral cell membrane . Cell projection, dendrite . Centromeric localization requires the presence of BUB1. | |
| Protein Description | The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT. [PubMed: 15525651 Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis] | |
| Protein Sequence | MAAADGDDSLYPIAVLIDELRNEDVQLRLNSIKKLSTIALALGVERTRSELLPFLTDTIYDEDEVLLALAEQLGTFTTLVGGPEYVHCLLPPLESLATVEETVVRDKAVESLRAISHEHSPSDLEAHFVPLVKRLAGGDWFTSRTSACGLFSVCYPRVSSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKVLELDNVKSEIIPMFSNLASDEQDSVRLLAVEACVNIAQLLPQEDLEALVMPTLRQAAEDKSWRVRYMVADKFTELQKAVGPEITKTDLVPAFQNLMKDCEAEVRAAASHKVKEFCENLSADCRENVIMSQILPCIKELVSDANQHVKSALASVIMGLSPILGKDNTIEHLLPLFLAQLKDECPEVRLNIISNLDCVNEVIGIRQLSQSLLPAIVELAEDAKWRVRLAIIEYMPLLAGQLGVEFFDEKLNSLCMAWLVDHVYAIREAATSNLKKLVEKFGKEWAHATIIPKVLAMSGDPNYLHRMTTLFCINVLSEVCGQDITTKHMLPTVLRMAGDPVANVRFNVAKSLQKIGPILDNSTLQSEVKPILEKLTQDQDVDVKYFAQEALTVLSLA | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAAADGDDS ------CCCCCCCCC | 16.03 | 19413330 | |
| 9 | Phosphorylation | AAADGDDSLYPIAVL CCCCCCCCHHHHHHH | 34.25 | 26552605 | |
| 11 | Phosphorylation | ADGDDSLYPIAVLID CCCCCCHHHHHHHHH | 9.13 | 26552605 | |
| 34 | Ubiquitination | LRLNSIKKLSTIALA HHHHHHHHHHHHHHH | 46.10 | 21890473 | |
| 36 | Phosphorylation | LNSIKKLSTIALALG HHHHHHHHHHHHHHC | 27.01 | 27251275 | |
| 37 | Phosphorylation | NSIKKLSTIALALGV HHHHHHHHHHHHHCC | 22.24 | 27251275 | |
| 47 | Phosphorylation | LALGVERTRSELLPF HHHCCCCHHHHHHHH | 25.66 | 18452278 | |
| 107 | Ubiquitination | EETVVRDKAVESLRA HHHHHHHHHHHHHHH | 43.71 | 21890473 | |
| 107 | Acetylation | EETVVRDKAVESLRA HHHHHHHHHHHHHHH | 43.71 | 25953088 | |
| 107 | 2-Hydroxyisobutyrylation | EETVVRDKAVESLRA HHHHHHHHHHHHHHH | 43.71 | - | |
| 116 | Phosphorylation | VESLRAISHEHSPSD HHHHHHHCCCCCHHH | 23.10 | 23312004 | |
| 120 | Phosphorylation | RAISHEHSPSDLEAH HHHCCCCCHHHHHHH | 24.10 | 28348404 | |
| 122 | Phosphorylation | ISHEHSPSDLEAHFV HCCCCCHHHHHHHHH | 58.82 | 28348404 | |
| 133 | Ubiquitination | AHFVPLVKRLAGGDW HHHHHHHHHHHCCCC | 49.75 | 21890473 | |
| 133 | 2-Hydroxyisobutyrylation | AHFVPLVKRLAGGDW HHHHHHHHHHHCCCC | 49.75 | - | |
| 133 | Acetylation | AHFVPLVKRLAGGDW HHHHHHHHHHHCCCC | 49.75 | 25953088 | |
| 134 | Methylation | HFVPLVKRLAGGDWF HHHHHHHHHHCCCCC | 23.45 | 115488561 | |
| 152 | Phosphorylation | TSACGLFSVCYPRVS CCCCCCHHHHHHHHH | 19.13 | 28152594 | |
| 155 | Phosphorylation | CGLFSVCYPRVSSAV CCCHHHHHHHHHHHH | 7.60 | 28152594 | |
| 159 | Phosphorylation | SVCYPRVSSAVKAEL HHHHHHHHHHHHHHH | 17.54 | 24719451 | |
| 160 | Phosphorylation | VCYPRVSSAVKAELR HHHHHHHHHHHHHHH | 33.94 | 23312004 | |
| 163 | Acetylation | PRVSSAVKAELRQYF HHHHHHHHHHHHHHH | 35.54 | 26822725 | |
| 163 | Ubiquitination | PRVSSAVKAELRQYF HHHHHHHHHHHHHHH | 35.54 | 21890473 | |
| 167 | Methylation | SAVKAELRQYFRNLC HHHHHHHHHHHHHHC | 22.21 | 115488545 | |
| 174 | Glutathionylation | RQYFRNLCSDDTPMV HHHHHHHCCCCCHHH | 4.84 | 22555962 | |
| 180 | Sulfoxidation | LCSDDTPMVRRAAAS HCCCCCHHHHHHHHH | 3.88 | 21406390 | |
| 188 | Ubiquitination | VRRAAASKLGEFAKV HHHHHHHHHHHHHHH | 56.64 | 21890473 | |
| 188 | Acetylation | VRRAAASKLGEFAKV HHHHHHHHHHHHHHH | 56.64 | 23749302 | |
| 188 | 2-Hydroxyisobutyrylation | VRRAAASKLGEFAKV HHHHHHHHHHHHHHH | 56.64 | - | |
| 194 | Ubiquitination | SKLGEFAKVLELDNV HHHHHHHHHHCCCCC | 53.31 | 21890473 | |
| 194 | Acetylation | SKLGEFAKVLELDNV HHHHHHHHHHCCCCC | 53.31 | 27452117 | |
| 194 | 2-Hydroxyisobutyrylation | SKLGEFAKVLELDNV HHHHHHHHHHCCCCC | 53.31 | - | |
| 202 | Ubiquitination | VLELDNVKSEIIPMF HHCCCCCCHHCHHHH | 48.93 | 21890473 | |
| 208 | Sulfoxidation | VKSEIIPMFSNLASD CCHHCHHHHCCCCCC | 3.97 | 28183972 | |
| 255 | Acetylation | LRQAAEDKSWRVRYM HHHHHHCCCHHHHHH | 43.34 | 25953088 | |
| 255 | Ubiquitination | LRQAAEDKSWRVRYM HHHHHHCCCHHHHHH | 43.34 | 21890473 | |
| 255 | 2-Hydroxyisobutyrylation | LRQAAEDKSWRVRYM HHHHHHCCCHHHHHH | 43.34 | - | |
| 256 | Phosphorylation | RQAAEDKSWRVRYMV HHHHHCCCHHHHHHH | 32.22 | 23882029 | |
| 262 | Sulfoxidation | KSWRVRYMVADKFTE CCHHHHHHHHHHHHH | 1.08 | 21406390 | |
| 266 | Ubiquitination | VRYMVADKFTELQKA HHHHHHHHHHHHHHH | 44.44 | 21890473 | |
| 266 | 2-Hydroxyisobutyrylation | VRYMVADKFTELQKA HHHHHHHHHHHHHHH | 44.44 | - | |
| 266 | Acetylation | VRYMVADKFTELQKA HHHHHHHHHHHHHHH | 44.44 | 26822725 | |
| 272 | Ubiquitination | DKFTELQKAVGPEIT HHHHHHHHHHCCCCC | 58.63 | 21890473 | |
| 272 | 2-Hydroxyisobutyrylation | DKFTELQKAVGPEIT HHHHHHHHHHCCCCC | 58.63 | - | |
| 272 | Acetylation | DKFTELQKAVGPEIT HHHHHHHHHHCCCCC | 58.63 | 23236377 | |
| 280 | Ubiquitination | AVGPEITKTDLVPAF HHCCCCCHHHHHHHH | 45.78 | 21906983 | |
| 280 | Acetylation | AVGPEITKTDLVPAF HHCCCCCHHHHHHHH | 45.78 | 19608861 | |
| 292 | Ubiquitination | PAFQNLMKDCEAEVR HHHHHHHHHCHHHHH | 63.49 | - | |
| 292 | Acetylation | PAFQNLMKDCEAEVR HHHHHHHHHCHHHHH | 63.49 | 25953088 | |
| 305 | Ubiquitination | VRAAASHKVKEFCEN HHHHHHHHHHHHHHC | 53.13 | 21890473 | |
| 307 | Ubiquitination | AAASHKVKEFCENLS HHHHHHHHHHHHCCC | 50.29 | 21890473 | |
| 307 | Acetylation | AAASHKVKEFCENLS HHHHHHHHHHHHCCC | 50.29 | 26051181 | |
| 335 | Phosphorylation | PCIKELVSDANQHVK HHHHHHHHCHHHHHH | 43.56 | 20068231 | |
| 342 | Ubiquitination | SDANQHVKSALASVI HCHHHHHHHHHHHHH | 28.08 | - | |
| 343 | Phosphorylation | DANQHVKSALASVIM CHHHHHHHHHHHHHH | 27.68 | 21712546 | |
| 347 | Phosphorylation | HVKSALASVIMGLSP HHHHHHHHHHHHCHH | 17.02 | 28348404 | |
| 350 | Sulfoxidation | SALASVIMGLSPILG HHHHHHHHHCHHHCC | 4.07 | 28183972 | |
| 353 | Phosphorylation | ASVIMGLSPILGKDN HHHHHHCHHHCCCCC | 12.26 | - | |
| 374 | Acetylation | PLFLAQLKDECPEVR HHHHHHHCCCCCHHH | 39.13 | 25038526 | |
| 374 | Ubiquitination | PLFLAQLKDECPEVR HHHHHHHCCCCCHHH | 39.13 | 20639865 | |
| 390 | S-nitrosocysteine | NIISNLDCVNEVIGI HHHHCCHHHHHHHHH | 3.89 | - | |
| 390 | Glutathionylation | NIISNLDCVNEVIGI HHHHCCHHHHHHHHH | 3.89 | 22555962 | |
| 390 | S-nitrosylation | NIISNLDCVNEVIGI HHHHCCHHHHHHHHH | 3.89 | 19483679 | |
| 390 | S-palmitoylation | NIISNLDCVNEVIGI HHHHCCHHHHHHHHH | 3.89 | 29575903 | |
| 401 | Phosphorylation | VIGIRQLSQSLLPAI HHHHHHHHHHHHHHH | 14.91 | 21406692 | |
| 403 | Phosphorylation | GIRQLSQSLLPAIVE HHHHHHHHHHHHHHH | 28.62 | 21406692 | |
| 416 | Ubiquitination | VELAEDAKWRVRLAI HHHHHHCCHHHHHHH | 48.10 | 21890473 | |
| 442 | Sumoylation | GVEFFDEKLNSLCMA CCHHCHHHHHHHHHH | 55.61 | - | |
| 464 | Phosphorylation | AIREAATSNLKKLVE HHHHHHHHHHHHHHH | 35.12 | 24114839 | |
| 467 | Ubiquitination | EAATSNLKKLVEKFG HHHHHHHHHHHHHHC | 48.59 | 21906983 | |
| 467 | 2-Hydroxyisobutyrylation | EAATSNLKKLVEKFG HHHHHHHHHHHHHHC | 48.59 | - | |
| 467 | Acetylation | EAATSNLKKLVEKFG HHHHHHHHHHHHHHC | 48.59 | 25953088 | |
| 472 | 2-Hydroxyisobutyrylation | NLKKLVEKFGKEWAH HHHHHHHHHCHHHHH | 52.52 | - | |
| 472 | Ubiquitination | NLKKLVEKFGKEWAH HHHHHHHHHCHHHHH | 52.52 | 21890473 | |
| 472 | Acetylation | NLKKLVEKFGKEWAH HHHHHHHHHCHHHHH | 52.52 | 25953088 | |
| 475 | Acetylation | KLVEKFGKEWAHATI HHHHHHCHHHHHHHH | 53.89 | 26051181 | |
| 475 | Ubiquitination | KLVEKFGKEWAHATI HHHHHHCHHHHHHHH | 53.89 | 21890473 | |
| 485 | Ubiquitination | AHATIIPKVLAMSGD HHHHHHHHHHHHCCC | 39.20 | 21890473 | |
| 489 | Sulfoxidation | IIPKVLAMSGDPNYL HHHHHHHHCCCCCHH | 3.93 | 28465586 | |
| 495 | Phosphorylation | AMSGDPNYLHRMTTL HHCCCCCHHHHHHHH | 14.85 | - | |
| 519 | Ubiquitination | CGQDITTKHMLPTVL HCCCCCHHHHHHHHH | 20.54 | - | |
| 521 | Sulfoxidation | QDITTKHMLPTVLRM CCCCHHHHHHHHHHH | 5.23 | 30846556 | |
| 527 | Methylation | HMLPTVLRMAGDPVA HHHHHHHHHCCCCCH | 14.47 | 115488553 | |
| 528 | Sulfoxidation | MLPTVLRMAGDPVAN HHHHHHHHCCCCCHH | 4.23 | 21406390 | |
| 542 | Acetylation | NVRFNVAKSLQKIGP HCHHHHHHHHHHHCC | 47.63 | 25953088 | |
| 542 | Ubiquitination | NVRFNVAKSLQKIGP HCHHHHHHHHHHHCC | 47.63 | 21890473 | |
| 542 | Succinylation | NVRFNVAKSLQKIGP HCHHHHHHHHHHHCC | 47.63 | 23954790 | |
| 546 | Ubiquitination | NVAKSLQKIGPILDN HHHHHHHHHCCCCCC | 55.73 | 21890473 | |
| 554 | Phosphorylation | IGPILDNSTLQSEVK HCCCCCCCCCHHHHH | 30.11 | 27050516 | |
| 555 | Phosphorylation | GPILDNSTLQSEVKP CCCCCCCCCHHHHHH | 34.76 | 27050516 | |
| 555 | O-linked_Glycosylation | GPILDNSTLQSEVKP CCCCCCCCCHHHHHH | 34.76 | 23301498 | |
| 558 | Phosphorylation | LDNSTLQSEVKPILE CCCCCCHHHHHHHHH | 47.68 | 23312004 | |
| 561 | Sumoylation | STLQSEVKPILEKLT CCCHHHHHHHHHHHH | 23.45 | - | |
| 561 | Acetylation | STLQSEVKPILEKLT CCCHHHHHHHHHHHH | 23.45 | 20167786 | |
| 561 | Ubiquitination | STLQSEVKPILEKLT CCCHHHHHHHHHHHH | 23.45 | 21890473 | |
| 566 | Ubiquitination | EVKPILEKLTQDQDV HHHHHHHHHHCCCCC | 54.08 | - | |
| 584 | Phosphorylation | YFAQEALTVLSLA-- HHHHHHHHHHHCC-- | 26.84 | - | |
| 587 | Phosphorylation | QEALTVLSLA----- HHHHHHHHCC----- | 20.22 | 28348404 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of 2AAA_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 2AAA_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 616362 | Mental retardation, autosomal dominant 36 (MRD36) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
| "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 LYS-280, AND MASS SPECTROMETRY. | |
