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Protein

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Gene

PPP2R1A

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

Functioni

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. Required for proper chromosome segregation and for centromeric localization of SGOL1 in mitosis.1 Publication

GO - Molecular functioni

  • antigen binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein phosphatase type 2A regulator activity Source: UniProtKB
  • protein serine/threonine phosphatase activity Source: Ensembl

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • ceramide metabolic process Source: UniProtKB
  • chromosome segregation Source: UniProtKB
  • female meiotic division Source: Ensembl
  • fibroblast growth factor receptor signaling pathway Source: Reactome
  • G2/M transition of mitotic cell cycle Source: Reactome
  • gene expression Source: Reactome
  • inactivation of MAPK activity Source: UniProtKB
  • meiotic sister chromatid cohesion, centromeric Source: Ensembl
  • meiotic spindle elongation Source: Ensembl
  • mitotic cell cycle Source: Reactome
  • mitotic nuclear envelope reassembly Source: Reactome
  • mitotic sister chromatid separation Source: Ensembl
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • organelle organization Source: Reactome
  • peptidyl-serine dephosphorylation Source: Ensembl
  • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  • protein complex assembly Source: UniProtKB
  • protein dephosphorylation Source: UniProtKB
  • regulation of cell adhesion Source: UniProtKB
  • regulation of cell differentiation Source: UniProtKB
  • regulation of DNA replication Source: UniProtKB
  • regulation of growth Source: UniProtKB
  • regulation of meiotic cell cycle process involved in oocyte maturation Source: Ensembl
  • regulation of protein phosphatase type 2A activity Source: GOC
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of Wnt signaling pathway Source: UniProtKB
  • response to organic substance Source: UniProtKB
  • RNA splicing Source: UniProtKB
  • second-messenger-mediated signaling Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Chromosome partition

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000105568-MONOMER.
ReactomeiR-HSA-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-HSA-1295596. Spry regulation of FGF signaling.
R-HSA-163685. Integration of energy metabolism.
R-HSA-163767. PP2A-mediated dephosphorylation of key metabolic factors.
R-HSA-180024. DARPP-32 events.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-196299. Beta-catenin phosphorylation cascade.
R-HSA-198753. ERK/MAPK targets.
R-HSA-202670. ERKs are inactivated.
R-HSA-2465910. MASTL Facilitates Mitotic Progression.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2995383. Initiation of Nuclear Envelope Reformation.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-389513. CTLA4 inhibitory signaling.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5339716. Misspliced GSK3beta mutants stabilize beta-catenin.
R-HSA-5358747. S33 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358749. S37 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358751. S45 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358752. T41 mutants of beta-catenin aren't phosphorylated.
R-HSA-5467337. APC truncation mutants have impaired AXIN binding.
R-HSA-5467340. AXIN missense mutants destabilize the destruction complex.
R-HSA-5467348. Truncations of AMER1 destabilize the destruction complex.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5673000. RAF activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-69231. Cyclin D associated events in G1.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-70171. Glycolysis.
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SignaLinkiP30153.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Alternative name(s):
Medium tumor antigen-associated 61 kDa protein
PP2A subunit A isoform PR65-alpha
PP2A subunit A isoform R1-alpha
Gene namesi
Name:PPP2R1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9302. PPP2R1A.

Subcellular locationi

  • Cytoplasm By similarity
  • Chromosomecentromere 1 Publication

  • Note: Centromeric localization requires the presence of BUB1.

GO - Cellular componenti

  • chromosome, centromeric region Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • microtubule cytoskeleton Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleus Source: UniProtKB
  • protein phosphatase type 2A complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Mental retardation, autosomal dominant 36 (MRD36)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.
See also OMIM:616362
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321V → L in MRD36. 1 Publication
VAR_073718
Natural varianti179 – 1791P → L in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; does not affect PPP2R3A binding; decreases phosphatase activity of PPP2CA. 1 Publication
VAR_074488
Natural varianti182 – 1821R → W in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; reduces PPP2R3A binding; decreases phosphatase activity of PPP2CA. 1 Publication
VAR_074489
Natural varianti258 – 2581R → H in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; reduces PPP2R3A binding; does not affect phosphatase activity of PPP2CA. 1 Publication
VAR_074490

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi616362. phenotype.
PharmGKBiPA33666.

Polymorphism and mutation databases

BioMutaiPPP2R1A.
DMDMi143811355.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 589588Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoformPRO_0000071400Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei280 – 2801N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP30153.
MaxQBiP30153.
PaxDbiP30153.
PRIDEiP30153.

2D gel databases

OGPiP30153.
REPRODUCTION-2DPAGEIPI00554737.

PTM databases

iPTMnetiP30153.
PhosphoSiteiP30153.
SwissPalmiP30153.

Miscellaneous databases

PMAP-CutDBP30153.

Expressioni

Gene expression databases

BgeeiP30153.
CleanExiHS_PPP2R1A.
ExpressionAtlasiP30153. baseline and differential.
GenevisibleiP30153. HS.

Organism-specific databases

HPAiCAB018599.

Interactioni

Subunit structurei

Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphoylation sites (By similarity). 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 IPO9. Interacts with TP53 and SGOL1. Interacts with PLA2G16; this interaction might decrease PP2A activity. Interacts with CTTNBP2NL.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P030813EBI-302388,EBI-1266256From a different organism.
AKT1P317492EBI-302388,EBI-296087
CFTRP135696EBI-302388,EBI-349854
E7P031293EBI-302388,EBI-866453From a different organism.
E7P040202EBI-302388,EBI-7005254From a different organism.
KIAA1524Q8TCG14EBI-302388,EBI-1379376
NxnP973462EBI-302388,EBI-309684From a different organism.
PLA2G16P538167EBI-302388,EBI-746318
PPP2CAP6777516EBI-302388,EBI-712311
PPP2CBP627145EBI-302388,EBI-1044367
PPP2R1BP301542EBI-302388,EBI-357094
PPP2R2AP6315110EBI-302388,EBI-1048931
PPP2R2BQ000056EBI-302388,EBI-1052159
PPP2R5AQ151724EBI-302388,EBI-641666
PPP2R5CQ133626EBI-302388,EBI-1266156
PPP2R5CQ13362-15EBI-302388,EBI-1266170
PPP2R5CQ13362-22EBI-302388,EBI-1266173
Ppp2r5cQ60996-32EBI-302388,EBI-1369292From a different organism.
PPP2R5DQ147386EBI-302388,EBI-396563
PPP2R5EQ165374EBI-302388,EBI-968374
PPP4CP605104EBI-302388,EBI-1046072
PPP5CP530413EBI-302388,EBI-716663
RELAQ042062EBI-302388,EBI-73886
STK24Q9Y6E03EBI-302388,EBI-740175
STRNO438156EBI-302388,EBI-1046642
TP53P046373EBI-302388,EBI-366083

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi111510. 255 interactions.
DIPiDIP-29394N.
IntActiP30153. 183 interactions.
MINTiMINT-1141071.
STRINGi9606.ENSP00000324804.

Structurei

Secondary structure

1
589
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni6 – 83Combined sources
Helixi11 – 199Combined sources
Helixi25 – 339Combined sources
Helixi35 – 417Combined sources
Helixi44 – 496Combined sources
Helixi51 – 577Combined sources
Helixi63 – 7311Combined sources
Helixi78 – 803Combined sources
Helixi83 – 897Combined sources
Helixi90 – 967Combined sources
Beta strandi99 – 1013Combined sources
Helixi102 – 11615Combined sources
Helixi121 – 1266Combined sources
Helixi128 – 1369Combined sources
Beta strandi138 – 1403Combined sources
Helixi141 – 1477Combined sources
Helixi148 – 1503Combined sources
Helixi151 – 1544Combined sources
Turni155 – 1573Combined sources
Helixi160 – 17415Combined sources
Helixi179 – 19416Combined sources
Helixi198 – 2036Combined sources
Helixi205 – 2139Combined sources
Helixi218 – 2214Combined sources
Helixi224 – 23411Combined sources
Helixi237 – 2393Combined sources
Helixi240 – 2434Combined sources
Helixi245 – 2528Combined sources
Helixi257 – 2659Combined sources
Helixi267 – 2748Combined sources
Helixi276 – 2816Combined sources
Helixi283 – 2919Combined sources
Helixi296 – 31116Combined sources
Turni315 – 3173Combined sources
Helixi318 – 3247Combined sources
Helixi326 – 3349Combined sources
Helixi339 – 3468Combined sources
Helixi349 – 3524Combined sources
Helixi353 – 3564Combined sources
Helixi358 – 3647Combined sources
Helixi366 – 3738Combined sources
Helixi378 – 3858Combined sources
Helixi389 – 3946Combined sources
Helixi397 – 41216Combined sources
Helixi417 – 43418Combined sources
Helixi436 – 4383Combined sources
Helixi441 – 4499Combined sources
Helixi450 – 4523Combined sources
Helixi456 – 47318Combined sources
Helixi475 – 4817Combined sources
Helixi483 – 4886Combined sources
Turni489 – 4913Combined sources
Helixi495 – 52026Combined sources
Helixi522 – 5276Combined sources
Helixi528 – 5303Combined sources
Helixi534 – 54714Combined sources
Helixi548 – 5503Combined sources
Helixi553 – 56715Combined sources
Helixi573 – 58513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B3UX-ray2.30A/B2-589[»]
2IE3X-ray2.80A1-589[»]
2IE4X-ray2.60A1-589[»]
2NPPX-ray3.30A/D1-589[»]
2NYLX-ray3.80A/D8-589[»]
2NYMX-ray3.60A/D8-589[»]
2PKGX-ray3.30A/B10-589[»]
3C5WX-ray2.80A9-589[»]
3DW8X-ray2.85A/D9-589[»]
3K7VX-ray2.85A1-589[»]
3K7WX-ray2.96A1-589[»]
4I5LX-ray2.43A/D6-589[»]
4I5NX-ray2.80A/D6-589[»]
4LACX-ray2.82A404-589[»]
ProteinModelPortaliP30153.
SMRiP30153. Positions 2-589.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30153.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati8 – 4639HEAT 1Add
BLAST
Repeati47 – 8438HEAT 2Add
BLAST
Repeati85 – 12339HEAT 3Add
BLAST
Repeati124 – 16138HEAT 4Add
BLAST
Repeati162 – 20039HEAT 5Add
BLAST
Repeati201 – 23939HEAT 6Add
BLAST
Repeati240 – 27839HEAT 7Add
BLAST
Repeati279 – 32143HEAT 8Add
BLAST
Repeati322 – 36039HEAT 9Add
BLAST
Repeati361 – 39939HEAT 10Add
BLAST
Repeati400 – 43839HEAT 11Add
BLAST
Repeati439 – 47739HEAT 12Add
BLAST
Repeati478 – 51639HEAT 13Add
BLAST
Repeati517 – 55539HEAT 14Add
BLAST
Repeati556 – 58934HEAT 15Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 399392PP2A subunit B bindingAdd
BLAST
Regioni47 – 321275Polyoma small and medium T antigens BindingAdd
BLAST
Regioni85 – 239155SV40 small T antigen bindingAdd
BLAST
Regioni400 – 589190PP2A subunit C bindingAdd
BLAST

Domaini

Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure.

Sequence similaritiesi

Contains 15 HEAT repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0211. Eukaryota.
ENOG410XQVI. LUCA.
GeneTreeiENSGT00730000110944.
HOGENOMiHOG000078539.
HOVERGENiHBG000011.
InParanoidiP30153.
KOiK03456.
OMAiMALGPQR.
OrthoDBiEOG764722.
PhylomeDBiP30153.
TreeFamiTF105552.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
IPR031090. PP2A_A_meta.
[Graphical view]
PANTHERiPTHR10648:SF9. PTHR10648:SF9. 1 hit.
PfamiPF02985. HEAT. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 11 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30153-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE
60 70 80 90 100
LLPFLTDTIY DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE
110 120 130 140 150
ETVVRDKAVE SLRAISHEHS PSDLEAHFVP LVKRLAGGDW FTSRTSACGL
160 170 180 190 200
FSVCYPRVSS AVKAELRQYF RNLCSDDTPM VRRAAASKLG EFAKVLELDN
210 220 230 240 250
VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL EALVMPTLRQ
260 270 280 290 300
AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA
310 320 330 340 350
AASHKVKEFC ENLSADCREN VIMSQILPCI KELVSDANQH VKSALASVIM
360 370 380 390 400
GLSPILGKDN TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL
410 420 430 440 450
SQSLLPAIVE LAEDAKWRVR LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW
460 470 480 490 500
LVDHVYAIRE AATSNLKKLV EKFGKEWAHA TIIPKVLAMS GDPNYLHRMT
510 520 530 540 550
TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV AKSLQKIGPI
560 570 580
LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA
Length:589
Mass (Da):65,309
Last modified:April 3, 2007 - v4
Checksum:i5174EBE94D537836
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301P → A in AAA35531 (PubMed:2554323).Curated
Sequence conflicti258 – 2581R → A in AAA36399 (PubMed:2159327).Curated
Sequence conflicti272 – 2721K → R AA sequence (PubMed:8694763).Curated
Sequence conflicti551 – 5511L → P in CAG29336 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321V → L in MRD36. 1 Publication
VAR_073718
Natural varianti179 – 1791P → L in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; does not affect PPP2R3A binding; decreases phosphatase activity of PPP2CA. 1 Publication
VAR_074488
Natural varianti182 – 1821R → W in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; reduces PPP2R3A binding; decreases phosphatase activity of PPP2CA. 1 Publication
VAR_074489
Natural varianti258 – 2581R → H in MRD36; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; reduces PPP2R3A binding; does not affect phosphatase activity of PPP2CA. 1 Publication
VAR_074490

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31786 mRNA. Translation: AAA35531.1.
J02902 mRNA. Translation: AAA36399.1.
CR450340 mRNA. Translation: CAG29336.1.
BC001537 mRNA. Translation: AAH01537.1.
CCDSiCCDS12849.1.
PIRiA34541.
RefSeqiNP_055040.2. NM_014225.5.
UniGeneiHs.467192.

Genome annotation databases

EnsembliENST00000322088; ENSP00000324804; ENSG00000105568.
GeneIDi5518.
KEGGihsa:5518.
UCSCiuc002pyp.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31786 mRNA. Translation: AAA35531.1.
J02902 mRNA. Translation: AAA36399.1.
CR450340 mRNA. Translation: CAG29336.1.
BC001537 mRNA. Translation: AAH01537.1.
CCDSiCCDS12849.1.
PIRiA34541.
RefSeqiNP_055040.2. NM_014225.5.
UniGeneiHs.467192.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B3UX-ray2.30A/B2-589[»]
2IE3X-ray2.80A1-589[»]
2IE4X-ray2.60A1-589[»]
2NPPX-ray3.30A/D1-589[»]
2NYLX-ray3.80A/D8-589[»]
2NYMX-ray3.60A/D8-589[»]
2PKGX-ray3.30A/B10-589[»]
3C5WX-ray2.80A9-589[»]
3DW8X-ray2.85A/D9-589[»]
3K7VX-ray2.85A1-589[»]
3K7WX-ray2.96A1-589[»]
4I5LX-ray2.43A/D6-589[»]
4I5NX-ray2.80A/D6-589[»]
4LACX-ray2.82A404-589[»]
ProteinModelPortaliP30153.
SMRiP30153. Positions 2-589.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111510. 255 interactions.
DIPiDIP-29394N.
IntActiP30153. 183 interactions.
MINTiMINT-1141071.
STRINGi9606.ENSP00000324804.

PTM databases

iPTMnetiP30153.
PhosphoSiteiP30153.
SwissPalmiP30153.

Polymorphism and mutation databases

BioMutaiPPP2R1A.
DMDMi143811355.

2D gel databases

OGPiP30153.
REPRODUCTION-2DPAGEIPI00554737.

Proteomic databases

EPDiP30153.
MaxQBiP30153.
PaxDbiP30153.
PRIDEiP30153.

Protocols and materials databases

DNASUi5518.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322088; ENSP00000324804; ENSG00000105568.
GeneIDi5518.
KEGGihsa:5518.
UCSCiuc002pyp.4. human.

Organism-specific databases

CTDi5518.
GeneCardsiPPP2R1A.
HGNCiHGNC:9302. PPP2R1A.
HPAiCAB018599.
MIMi605983. gene.
616362. phenotype.
neXtProtiNX_P30153.
PharmGKBiPA33666.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0211. Eukaryota.
ENOG410XQVI. LUCA.
GeneTreeiENSGT00730000110944.
HOGENOMiHOG000078539.
HOVERGENiHBG000011.
InParanoidiP30153.
KOiK03456.
OMAiMALGPQR.
OrthoDBiEOG764722.
PhylomeDBiP30153.
TreeFamiTF105552.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000105568-MONOMER.
ReactomeiR-HSA-113501. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
R-HSA-1295596. Spry regulation of FGF signaling.
R-HSA-163685. Integration of energy metabolism.
R-HSA-163767. PP2A-mediated dephosphorylation of key metabolic factors.
R-HSA-180024. DARPP-32 events.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-196299. Beta-catenin phosphorylation cascade.
R-HSA-198753. ERK/MAPK targets.
R-HSA-202670. ERKs are inactivated.
R-HSA-2465910. MASTL Facilitates Mitotic Progression.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2995383. Initiation of Nuclear Envelope Reformation.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-389513. CTLA4 inhibitory signaling.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5339716. Misspliced GSK3beta mutants stabilize beta-catenin.
R-HSA-5358747. S33 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358749. S37 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358751. S45 mutants of beta-catenin aren't phosphorylated.
R-HSA-5358752. T41 mutants of beta-catenin aren't phosphorylated.
R-HSA-5467337. APC truncation mutants have impaired AXIN binding.
R-HSA-5467340. AXIN missense mutants destabilize the destruction complex.
R-HSA-5467348. Truncations of AMER1 destabilize the destruction complex.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5673000. RAF activation.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-69231. Cyclin D associated events in G1.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-70171. Glycolysis.
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SignaLinkiP30153.

Miscellaneous databases

ChiTaRSiPPP2R1A. human.
EvolutionaryTraceiP30153.
GeneWikiiPPP2R1A.
GenomeRNAii5518.
NextBioi21342.
PMAP-CutDBP30153.
PROiP30153.
SOURCEiSearch...

Gene expression databases

BgeeiP30153.
CleanExiHS_PPP2R1A.
ExpressionAtlasiP30153. baseline and differential.
GenevisibleiP30153. HS.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
IPR031090. PP2A_A_meta.
[Graphical view]
PANTHERiPTHR10648:SF9. PTHR10648:SF9. 1 hit.
PfamiPF02985. HEAT. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 11 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence of cDNA encoding polyoma medium tumor antigen-associated 61-kDa protein."
    Walter G., Ferre F., Espiritu O., Carbone-Wiley A.
    Proc. Natl. Acad. Sci. U.S.A. 86:8669-8672(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 242-255.
    Tissue: Placenta.
  2. "Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure."
    Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J., Merlevede W., Hofsteenge J., Stone S.R.
    Biochemistry 29:3166-3173(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
    Tissue: Colon.
  5. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 34-46, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  6. "The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits."
    Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., Merlevede W., Goris J., Hemmings B.A.
    Biochem. J. 317:187-194(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 204-214; 261-272 AND 521-527.
  7. "Molecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigens."
    Ruediger R., Hentz M., Fait J., Mumby M., Walter G.
    J. Virol. 68:123-129(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: BINDING DOMAINS.
  8. "Interaction between protein phosphatase 2A and members of the importin beta superfamily."
    Lubert E.J., Sarge K.D.
    Biochem. Biophys. Res. Commun. 303:908-913(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IPO9.
  9. "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, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SGOL1.
  10. "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.
  11. "Mechanisms of the HRSL3 tumor suppressor function in ovarian carcinoma cells."
    Nazarenko I., Schafer R., Sers C.
    J. Cell Sci. 120:1393-1404(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLA2G16.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein."
    Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., Aebersold R., Raught B., Gingras A.C.
    Mol. Cell. Proteomics 8:157-171(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTTNBP2NL.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "Large-scale discovery of novel genetic causes of developmental disorders."
    Deciphering Developmental Disorders Study
    Nature 519:223-228(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MRD36, VARIANT MRD36 LEU-132.
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs."
    Groves M.R., Hanlon N., Turowski P., Hemmings B.A., Barford D.
    Cell 96:99-110(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  22. "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) OF 9-589 IN COMPLEX WITH WITH PPP2CA AND PPME1.
  23. Cited for: VARIANTS MRD36 LEU-179; TRP-182 AND HIS-258, CHARACTERIZATION MRD36 OF VARIANTS LEU-179; TRP-182 AND HIS-258.

Entry informationi

Entry namei2AAA_HUMAN
AccessioniPrimary (citable) accession number: P30153
Secondary accession number(s): Q13773, Q6ICQ3, Q96DH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 3, 2007
Last modified: April 13, 2016
This is version 170 of the entry and version 4 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 19
    Human chromosome 19: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.