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P67775

- PP2AA_HUMAN

UniProt

P67775 - PP2AA_HUMAN

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Protein

Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform

Gene
PPP2CA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 SGOL2 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'.3 Publications

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Binds 2 manganese ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi57 – 571Manganese 1
Metal bindingi59 – 591Manganese 1
Metal bindingi85 – 851Manganese 1
Metal bindingi85 – 851Manganese 2
Metal bindingi117 – 1171Manganese 2
Active sitei118 – 1181Proton donor By similarity
Metal bindingi167 – 1671Manganese 2
Metal bindingi241 – 2411Manganese 2

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. protein serine/threonine phosphatase activity Source: Ensembl

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. ceramide metabolic process Source: UniProtKB
  3. fibroblast growth factor receptor signaling pathway Source: Reactome
  4. gene expression Source: Reactome
  5. inactivation of MAPK activity Source: UniProtKB
  6. meiotic nuclear division Source: UniProtKB-KW
  7. mesoderm development Source: Ensembl
  8. mitotic cell cycle Source: Reactome
  9. mitotic nuclear envelope reassembly Source: Reactome
  10. mRNA metabolic process Source: Reactome
  11. negative regulation of cell growth Source: UniProtKB
  12. negative regulation of epithelial to mesenchymal transition Source: BHF-UCL
  13. negative regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
  14. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  15. positive regulation of protein serine/threonine kinase activity Source: BHF-UCL
  16. protein dephosphorylation Source: UniProtKB
  17. protein heterotrimerization Source: Ensembl
  18. regulation of cell adhesion Source: UniProtKB
  19. regulation of cell differentiation Source: UniProtKB
  20. regulation of DNA replication Source: UniProtKB
  21. regulation of growth Source: UniProtKB
  22. regulation of protein autophosphorylation Source: Ensembl
  23. regulation of protein catabolic process Source: Ensembl
  24. regulation of receptor activity Source: Ensembl
  25. regulation of transcription, DNA-templated Source: UniProtKB
  26. regulation of Wnt signaling pathway Source: UniProtKB
  27. response to organic substance Source: UniProtKB
  28. RNA metabolic process Source: Reactome
  29. RNA splicing Source: UniProtKB
  30. second-messenger-mediated signaling Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Meiosis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS03696-MONOMER.
ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_111080. Spry regulation of FGF signaling.
REACT_12436. ERKs are inactivated.
REACT_12599. ERK/MAPK targets.
REACT_1383. Glycolysis.
REACT_150182. MASTL Facilitates Mitotic Progression.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_1505. Integration of energy metabolism.
REACT_15334. DARPP-32 events.
REACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_19405. CTLA4 inhibitory signaling.
REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_23879. Platelet sensitization by LDL.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_682. Mitotic Prometaphase.
REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_821. Cyclin D associated events in G1.
SignaLinkiP67775.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (EC:3.1.3.16)
Short name:
PP2A-alpha
Alternative name(s):
Replication protein C
Short name:
RP-C
Gene namesi
Name:PPP2CA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:9299. PPP2CA.

Subcellular locationi

Cytoplasm. Nucleus. Chromosomecentromere. Cytoplasmcytoskeletonspindle pole
Note: In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles. Centromeric localization requires the presence of SGOL2 By similarity.1 Publication

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB-SubCell
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. membrane Source: UniProtKB
  5. microtubule cytoskeleton Source: UniProtKB
  6. mitochondrion Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. plasma membrane Source: Ensembl
  9. protein phosphatase type 2A complex Source: UniProtKB
  10. spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi309 – 3091L → A: Loss of binding to PP2A B-alpha regulatory subunit. 1 Publication

Organism-specific databases

PharmGKBiPA33663.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoformPRO_0000058839Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei307 – 3071Phosphotyrosine
Modified residuei309 – 3091Leucine methyl ester1 Publication

Post-translational modificationi

Reversibly methyl esterified on Leu-309 by leucine carboxyl methyltransferase 1 (LCMT1) and protein phosphatase methylesterase 1 (PPME1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization.
Phosphorylation of either threonine (by autophosphorylation-activated protein kinase) or tyrosine results in inactivation of the phosphatase. Auto-dephosphorylation has been suggested as a mechanism for reactivation.

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP67775.
PaxDbiP67775.
PRIDEiP67775.

PTM databases

PhosphoSiteiP67775.

Expressioni

Gene expression databases

ArrayExpressiP67775.
BgeeiP67775.
CleanExiHS_PPP2CA.
GenevestigatoriP67775.

Organism-specific databases

HPAiCAB003848.

Interactioni

Subunit structurei

PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with NXN; the interaction is direct By similarity. Interacts with TP53, SGOL1 and SGOL2. Interacts with AXIN1; the interaction dephosphorylates AXIN1. Interacts with PIM3; this interaction promotes dephosphorylation, ubiquitination and proteasomal degradation of PIM3. Interacts with RAF1. Interaction with IGBP1 protects unassembled PPP2CA from degradative ubiquitination. Interacts with GSK3B (via C2 domain).11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317495EBI-712311,EBI-296087
ANP32AP396872EBI-712311,EBI-359234
E7P031293EBI-712311,EBI-866453From a different organism.
E7P040202EBI-712311,EBI-7005254From a different organism.
H2AFXP161042EBI-712311,EBI-494830
IER3P466952EBI-712311,EBI-1748945
IGBP1P7831810EBI-712311,EBI-1055954
Igbp1Q612493EBI-712311,EBI-7002233From a different organism.
IKBKBO149203EBI-712311,EBI-81266
IKBKGQ9Y6K94EBI-712311,EBI-81279
KISS1RQ969F83EBI-712311,EBI-8481408
NxnP973462EBI-712311,EBI-309684From a different organism.
PPP2R1AP3015314EBI-712311,EBI-302388
PPP2R1BP301547EBI-712311,EBI-357094
PPP2R2CQ9Y2T43EBI-712311,EBI-1774058
PPP2R5AQ151723EBI-712311,EBI-641666
PPP2R5BQ151734EBI-712311,EBI-1369497
PPP2R5CQ133627EBI-712311,EBI-1266156
RBL1P287492EBI-712311,EBI-971402
RBL2Q089992EBI-712311,EBI-971439
RELAQ042064EBI-712311,EBI-73886
STRNO438153EBI-712311,EBI-1046642
TIPRLO756633EBI-712311,EBI-1054735
TRIP13Q156453EBI-712311,EBI-358993

Protein-protein interaction databases

BioGridi111507. 159 interactions.
DIPiDIP-29395N.
IntActiP67775. 115 interactions.
MINTiMINT-215645.
STRINGi9606.ENSP00000418447.

Structurei

Secondary structure

1
309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1816
Helixi25 – 3915
Beta strandi44 – 485
Beta strandi50 – 556
Helixi62 – 7211
Turni75 – 773
Beta strandi80 – 823
Beta strandi87 – 915
Helixi93 – 10614
Turni108 – 1103
Beta strandi111 – 1133
Helixi121 – 1277
Helixi129 – 1379
Beta strandi138 – 1403
Helixi141 – 15010
Beta strandi155 – 1595
Turni160 – 1623
Beta strandi163 – 1686
Helixi177 – 1826
Beta strandi186 – 1883
Beta strandi191 – 1933
Helixi194 – 2007
Beta strandi205 – 2117
Beta strandi215 – 2206
Helixi222 – 23211
Beta strandi235 – 2395
Beta strandi247 – 2515
Turni252 – 2554
Beta strandi256 – 2594
Helixi265 – 2673
Beta strandi273 – 2786
Beta strandi284 – 2896

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IAEX-ray3.50C/F1-309[»]
2IE3X-ray2.80C1-309[»]
2IE4X-ray2.60C1-309[»]
2NPPX-ray3.30C/F1-309[»]
2NYLX-ray3.80C/F2-294[»]
2NYMX-ray3.60C/F2-294[»]
3C5WX-ray2.80C1-309[»]
3DW8X-ray2.85C/F1-309[»]
3FGAX-ray2.70C1-309[»]
3K7VX-ray2.85C1-309[»]
3K7WX-ray2.96C1-309[»]
3P71X-ray2.70C1-309[»]
4I5LX-ray2.43C/F1-309[»]
4I5NX-ray2.80C/F1-309[»]
4IYPX-ray2.80C6-153[»]
4LACX-ray2.82C1-309[»]
ProteinModelPortaliP67775.
SMRiP67775. Positions 2-296.

Miscellaneous databases

EvolutionaryTraceiP67775.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172696.
HOVERGENiHBG000216.
InParanoidiP67775.
KOiK04382.
OMAiQVKTLCD.
OrthoDBiEOG74N5H2.
PhylomeDBiP67775.
TreeFamiTF105559.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P67775-1) [UniParc]FASTAAdd to Basket

Also known as: PP2Acalpha1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MDEKVFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC    50
PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL 100
VALKVRYRER ITILRGNHES RQITQVYGFY DECLRKYGNA NVWKYFTDLF 150
DYLPLTALVD GQIFCLHGGL SPSIDTLDHI RALDRLQEVP HEGPMCDLLW 200
SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA HQLVMEGYNW 250
CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV 300
TRRTPDYFL 309
Length:309
Mass (Da):35,594
Last modified:October 11, 2004 - v1
Checksum:iC602291F78F34555
GO
Isoform 2 (identifier: P67775-2) [UniParc]FASTAAdd to Basket

Also known as: PP2Acalpha2

The sequence of this isoform differs from the canonical sequence as follows:
     193-246: Missing.

Note: Catalytically inactive, shows enhanced binding to IGBP1, and does not interact with the scaffolding subunit PPP2R1A.

Show »
Length:255
Mass (Da):29,735
Checksum:iB50450F64CB286AB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521V → A.
Corresponds to variant rs11552681 [ dbSNP | Ensembl ].
VAR_051735

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei193 – 24654Missing in isoform 2. VSP_044320Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12646 mRNA. Translation: CAA31176.1.
J03804 mRNA. Translation: AAB38019.1.
M60483 Genomic DNA. Translation: AAA36466.1.
BC000400 mRNA. Translation: AAH00400.1.
BC002657 mRNA. Translation: AAH02657.1.
BC019275 mRNA. Translation: AAH19275.1.
BC031696 mRNA. Translation: AAH31696.1.
CCDSiCCDS4173.1. [P67775-1]
PIRiS01986. PAHU2A.
RefSeqiNP_002706.1. NM_002715.2. [P67775-1]
UniGeneiHs.105818.

Genome annotation databases

EnsembliENST00000481195; ENSP00000418447; ENSG00000113575. [P67775-1]
GeneIDi5515.
KEGGihsa:5515.
UCSCiuc003kze.3. human. [P67775-1]

Polymorphism databases

DMDMi54038809.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12646 mRNA. Translation: CAA31176.1 .
J03804 mRNA. Translation: AAB38019.1 .
M60483 Genomic DNA. Translation: AAA36466.1 .
BC000400 mRNA. Translation: AAH00400.1 .
BC002657 mRNA. Translation: AAH02657.1 .
BC019275 mRNA. Translation: AAH19275.1 .
BC031696 mRNA. Translation: AAH31696.1 .
CCDSi CCDS4173.1. [P67775-1 ]
PIRi S01986. PAHU2A.
RefSeqi NP_002706.1. NM_002715.2. [P67775-1 ]
UniGenei Hs.105818.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IAE X-ray 3.50 C/F 1-309 [» ]
2IE3 X-ray 2.80 C 1-309 [» ]
2IE4 X-ray 2.60 C 1-309 [» ]
2NPP X-ray 3.30 C/F 1-309 [» ]
2NYL X-ray 3.80 C/F 2-294 [» ]
2NYM X-ray 3.60 C/F 2-294 [» ]
3C5W X-ray 2.80 C 1-309 [» ]
3DW8 X-ray 2.85 C/F 1-309 [» ]
3FGA X-ray 2.70 C 1-309 [» ]
3K7V X-ray 2.85 C 1-309 [» ]
3K7W X-ray 2.96 C 1-309 [» ]
3P71 X-ray 2.70 C 1-309 [» ]
4I5L X-ray 2.43 C/F 1-309 [» ]
4I5N X-ray 2.80 C/F 1-309 [» ]
4IYP X-ray 2.80 C 6-153 [» ]
4LAC X-ray 2.82 C 1-309 [» ]
ProteinModelPortali P67775.
SMRi P67775. Positions 2-296.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111507. 159 interactions.
DIPi DIP-29395N.
IntActi P67775. 115 interactions.
MINTi MINT-215645.
STRINGi 9606.ENSP00000418447.

Chemistry

BindingDBi P67775.
ChEMBLi CHEMBL4703.
DrugBanki DB00163. Vitamin E.

PTM databases

PhosphoSitei P67775.

Polymorphism databases

DMDMi 54038809.

Proteomic databases

MaxQBi P67775.
PaxDbi P67775.
PRIDEi P67775.

Protocols and materials databases

DNASUi 5515.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000481195 ; ENSP00000418447 ; ENSG00000113575 . [P67775-1 ]
GeneIDi 5515.
KEGGi hsa:5515.
UCSCi uc003kze.3. human. [P67775-1 ]

Organism-specific databases

CTDi 5515.
GeneCardsi GC05M133530.
HGNCi HGNC:9299. PPP2CA.
HPAi CAB003848.
MIMi 176915. gene.
neXtProti NX_P67775.
PharmGKBi PA33663.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0639.
HOGENOMi HOG000172696.
HOVERGENi HBG000216.
InParanoidi P67775.
KOi K04382.
OMAi QVKTLCD.
OrthoDBi EOG74N5H2.
PhylomeDBi P67775.
TreeFami TF105559.

Enzyme and pathway databases

BioCyci MetaCyc:HS03696-MONOMER.
Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_111080. Spry regulation of FGF signaling.
REACT_12436. ERKs are inactivated.
REACT_12599. ERK/MAPK targets.
REACT_1383. Glycolysis.
REACT_150182. MASTL Facilitates Mitotic Progression.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_1505. Integration of energy metabolism.
REACT_15334. DARPP-32 events.
REACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_19405. CTLA4 inhibitory signaling.
REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_23879. Platelet sensitization by LDL.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_682. Mitotic Prometaphase.
REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_821. Cyclin D associated events in G1.
SignaLinki P67775.

Miscellaneous databases

EvolutionaryTracei P67775.
GeneWikii PPP2CA.
GenomeRNAii 5515.
NextBioi 21330.
PROi P67775.
SOURCEi Search...

Gene expression databases

ArrayExpressi P67775.
Bgeei P67775.
CleanExi HS_PPP2CA.
Genevestigatori P67775.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of the cDNA encoding the human lung protein phosphatase 2A alpha catalytic subunit."
    Stone S.R., Mayer R., Wernet W., Maurer F., Hofsteenge J., Hemmings B.A.
    Nucleic Acids Res. 16:11365-11365(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fibroblast.
  2. "Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic subunit isotypes."
    Arino J., Woon C.W., Brautigan D.L., Miller T.B. Jr., Johnson G.L.
    Proc. Natl. Acad. Sci. U.S.A. 85:4252-4256(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "Structure and transcriptional regulation of protein phosphatase 2A catalytic subunit genes."
    Khew-Goodall Y., Mayer R.E., Maurer F., Stone S.R., Hemmings B.A.
    Biochemistry 30:89-97(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung, Placenta and Uterus.
  5. "Dephosphorylation of simian virus 40 large-T antigen and p53 protein by protein phosphatase 2A: inhibition by small-t antigen."
    Scheidtmann K.H., Mumby M.C., Rundell K., Walter G.
    Mol. Cell. Biol. 11:1996-2003(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEPHOSPHORYLATION OF SV40 LARGE-T ANTIGEN AND P53 PROTEIN.
  6. "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) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LEU-309.
  7. "Alpha 4 associates with protein phosphatases 2A, 4, and 6."
    Chen J., Peterson R.T., Schreiber S.L.
    Biochem. Biophys. Res. Commun. 247:827-832(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGBP1.
  8. "Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Balpha subunit."
    Bryant J.C., Westphal R.S., Wadzinski B.E.
    Biochem. J. 339:241-246(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LEU-309.
  9. "Activation of SV40 DNA replication in vitro by cellular protein phosphatase 2A."
    Virshup D.M., Kauffman M.G., Kelly T.J.
    EMBO J. 8:3891-3898(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, ACTIVATION OF SV40 REPLICATION.
  10. "Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain."
    Hsu W., Zeng L., Costantini F.
    J. Biol. Chem. 274:3439-3445(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AXIN1, FUNCTION.
  11. "Raf-1-associated protein phosphatase 2A as a positive regulator of kinase activation."
    Abraham D., Podar K., Pacher M., Kubicek M., Welzel N., Hemmings B.A., Dilworth S.M., Mischak H., Kolch W., Baccarini M.
    J. Biol. Chem. 275:22300-22304(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAF1.
  12. "PP2A is required for centromeric localization of Sgo1 and proper chromosome segregation."
    Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.
    Dev. Cell 10:575-585(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SGOL1.
  13. "Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
    Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
    Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SGOL1.
  14. "Protein phosphatase 2A regulates the stability of Pim protein kinases."
    Losman J.A., Chen X.P., Vuong B.Q., Fay S., Rothman P.B.
    J. Biol. Chem. 278:4800-4805(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIM3.
  15. "A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced dephosphorylation of p53 at Thr55."
    Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.
    EMBO J. 26:402-411(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TP53.
  16. "Tripin/hSgo2 recruits MCAK to the inner centromere to correct defective kinetochore attachments."
    Huang H., Feng J., Famulski J., Rattner J.B., Liu S.T., Kao G.D., Muschel R., Chan G.K., Yen T.J.
    J. Cell Biol. 177:413-424(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGOL2.
  17. "Alpha4 is an essential regulator of PP2A phosphatase activity."
    Kong M., Ditsworth D., Lindsten T., Thompson C.B.
    Mol. Cell 36:51-60(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGBP1.
  18. "Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination."
    McConnell J.L., Watkins G.R., Soss S.E., Franz H.S., McCorvey L.R., Spiller B.W., Chazin W.J., Wadzinski B.E.
    Biochemistry 49:1713-1718(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGBP1.
  19. "Role of DAB2IP in modulating epithelial-to-mesenchymal transition and prostate cancer metastasis."
    Xie D., Gore C., Liu J., Pong R.C., Mason R., Hao G., Long M., Kabbani W., Yu L., Zhang H., Chen H., Sun X., Boothman D.A., Min W., Hsieh J.T.
    Proc. Natl. Acad. Sci. U.S.A. 107:2485-2490(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GSK3B.
  20. "Identification and characterization of an alternatively spliced isoform of the human protein phosphatase 2Aalpha catalytic subunit."
    Migueleti D.L., Smetana J.H., Nunes H.F., Kobarg J., Zanchin N.I.
    J. Biol. Chem. 287:4853-4862(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 2).
  21. "Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit alpha4, altering PP2A stability and microtubule-associated protein phosphorylation."
    Watkins G.R., Wang N., Mazalouskas M.D., Gomez R.J., Guthrie C.R., Kraemer B.C., Schweiger S., Spiller B.W., Wadzinski B.E.
    J. Biol. Chem. 287:24207-24215(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins."
    Xing Y., Xu Y., Chen Y., Jeffrey P.D., Chao Y., Lin Z., Li Z., Strack S., Stock J.B., Shi Y.
    Cell 127:341-353(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS, COFACTOR.
  23. "Structural mechanism of demethylation and inactivation of protein phosphatase 2A."
    Xing Y., Li Z., Chen Y., Stock J.B., Jeffrey P.D., Shi Y.
    Cell 133:154-163(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PPP2R1A AND PPME1.

Entry informationi

Entry nameiPP2AA_HUMAN
AccessioniPrimary (citable) accession number: P67775
Secondary accession number(s): P05323, P13197
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: September 3, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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