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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 SGO1 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
  • G2/M transition of mitotic cell cycle Source: Reactome
  • inactivation of MAPK activity Source: UniProtKB
  • meiotic sister chromatid cohesion, centromeric Source: Ensembl
  • meiotic spindle elongation Source: Ensembl
  • 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
  • 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 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.
ZFISH: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-6804757. Regulation of TP53 Degradation.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
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-8854518. AURKA Activation by TPX2.
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SignaLinkiP30153.
SIGNORiP30153.

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_073718132V → L in MRD36. 1 Publication1
Natural variantiVAR_074488179P → 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 PublicationCorresponds to variant rs786205228dbSNPEnsembl.1
Natural variantiVAR_074489182R → 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 PublicationCorresponds to variant rs786205227dbSNPEnsembl.1
Natural variantiVAR_074490258R → 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 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi5518.
MIMi616362. phenotype.
OpenTargetsiENSG00000105568.
PharmGKBiPA33666.

Polymorphism and mutation databases

BioMutaiPPP2R1A.
DMDMi143811355.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000714002 – 589Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoformAdd BLAST588

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei280N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP30153.
MaxQBiP30153.
PaxDbiP30153.
PeptideAtlasiP30153.
PRIDEiP30153.

2D gel databases

OGPiP30153.
REPRODUCTION-2DPAGEIPI00554737.

PTM databases

iPTMnetiP30153.
PhosphoSitePlusiP30153.
SwissPalmiP30153.

Miscellaneous databases

PMAP-CutDBP30153.

Expressioni

Gene expression databases

BgeeiENSG00000105568.
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 SGO1. 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
CSDC2Q9Y5344EBI-302388,EBI-1763657
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
PPP2R1BP301542EBI-302388,EBI-357094
PPP2R2AP6315111EBI-302388,EBI-1048931
PPP2R2BQ000056EBI-302388,EBI-1052159
PPP2R5AQ151724EBI-302388,EBI-641666
PPP2R5BQ151733EBI-302388,EBI-1369497
PPP2R5CQ133627EBI-302388,EBI-1266156
PPP2R5CQ13362-15EBI-302388,EBI-1266170
PPP2R5CQ13362-22EBI-302388,EBI-1266173
Ppp2r5cQ60996-32EBI-302388,EBI-1369292From a different organism.
PPP2R5DQ147387EBI-302388,EBI-396563
PPP2R5EQ165375EBI-302388,EBI-968374
PPP4CP605103EBI-302388,EBI-1046072
PPP5CP530413EBI-302388,EBI-716663
RELAQ042062EBI-302388,EBI-73886
STRNO438156EBI-302388,EBI-1046642
STRN3Q13033-24EBI-302388,EBI-1053876
TP53P046373EBI-302388,EBI-366083

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi111510. 270 interactors.
DIPiDIP-29394N.
IntActiP30153. 185 interactors.
MINTiMINT-1141071.
STRINGi9606.ENSP00000324804.

Structurei

Secondary structure

1589
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni6 – 8Combined sources3
Helixi11 – 19Combined sources9
Helixi25 – 33Combined sources9
Helixi35 – 41Combined sources7
Helixi44 – 49Combined sources6
Helixi51 – 57Combined sources7
Helixi63 – 73Combined sources11
Helixi78 – 80Combined sources3
Helixi83 – 89Combined sources7
Helixi90 – 96Combined sources7
Beta strandi99 – 101Combined sources3
Helixi102 – 116Combined sources15
Helixi121 – 126Combined sources6
Helixi128 – 136Combined sources9
Beta strandi138 – 140Combined sources3
Helixi141 – 147Combined sources7
Helixi148 – 150Combined sources3
Helixi151 – 154Combined sources4
Turni155 – 157Combined sources3
Helixi160 – 174Combined sources15
Helixi179 – 194Combined sources16
Helixi198 – 203Combined sources6
Helixi205 – 213Combined sources9
Helixi218 – 221Combined sources4
Helixi224 – 234Combined sources11
Helixi237 – 239Combined sources3
Helixi240 – 243Combined sources4
Helixi245 – 252Combined sources8
Helixi257 – 265Combined sources9
Helixi267 – 274Combined sources8
Helixi276 – 281Combined sources6
Helixi283 – 291Combined sources9
Helixi296 – 311Combined sources16
Turni315 – 317Combined sources3
Helixi318 – 324Combined sources7
Helixi326 – 334Combined sources9
Helixi339 – 346Combined sources8
Helixi349 – 352Combined sources4
Helixi353 – 356Combined sources4
Helixi358 – 364Combined sources7
Helixi366 – 373Combined sources8
Helixi378 – 385Combined sources8
Helixi389 – 394Combined sources6
Helixi397 – 412Combined sources16
Helixi417 – 434Combined sources18
Helixi436 – 438Combined sources3
Helixi441 – 449Combined sources9
Helixi450 – 452Combined sources3
Helixi456 – 473Combined sources18
Helixi475 – 481Combined sources7
Helixi483 – 488Combined sources6
Turni489 – 491Combined sources3
Helixi495 – 520Combined sources26
Helixi522 – 527Combined sources6
Helixi528 – 530Combined sources3
Helixi534 – 547Combined sources14
Helixi548 – 550Combined sources3
Helixi553 – 567Combined sources15
Helixi573 – 585Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30153.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati8 – 46HEAT 1Add BLAST39
Repeati47 – 84HEAT 2Add BLAST38
Repeati85 – 123HEAT 3Add BLAST39
Repeati124 – 161HEAT 4Add BLAST38
Repeati162 – 200HEAT 5Add BLAST39
Repeati201 – 239HEAT 6Add BLAST39
Repeati240 – 278HEAT 7Add BLAST39
Repeati279 – 321HEAT 8Add BLAST43
Repeati322 – 360HEAT 9Add BLAST39
Repeati361 – 399HEAT 10Add BLAST39
Repeati400 – 438HEAT 11Add BLAST39
Repeati439 – 477HEAT 12Add BLAST39
Repeati478 – 516HEAT 13Add BLAST39
Repeati517 – 555HEAT 14Add BLAST39
Repeati556 – 589HEAT 15Add BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni8 – 399PP2A subunit B bindingAdd BLAST392
Regioni47 – 321Polyoma small and medium T antigens BindingAdd BLAST275
Regioni85 – 239SV40 small T antigen bindingAdd BLAST155
Regioni400 – 589PP2A subunit C bindingAdd BLAST190

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.
OMAiMSNILPC.
OrthoDBiEOG091G045V.
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)DescriptionActionsGraphical viewLength
Sequence conflicti130P → A in AAA35531 (PubMed:2554323).Curated1
Sequence conflicti258R → A in AAA36399 (PubMed:2159327).Curated1
Sequence conflicti272K → R AA sequence (PubMed:8694763).Curated1
Sequence conflicti551L → P in CAG29336 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073718132V → L in MRD36. 1 Publication1
Natural variantiVAR_074488179P → 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 PublicationCorresponds to variant rs786205228dbSNPEnsembl.1
Natural variantiVAR_074489182R → 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 PublicationCorresponds to variant rs786205227dbSNPEnsembl.1
Natural variantiVAR_074490258R → 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 Publication1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111510. 270 interactors.
DIPiDIP-29394N.
IntActiP30153. 185 interactors.
MINTiMINT-1141071.
STRINGi9606.ENSP00000324804.

PTM databases

iPTMnetiP30153.
PhosphoSitePlusiP30153.
SwissPalmiP30153.

Polymorphism and mutation databases

BioMutaiPPP2R1A.
DMDMi143811355.

2D gel databases

OGPiP30153.
REPRODUCTION-2DPAGEIPI00554737.

Proteomic databases

EPDiP30153.
MaxQBiP30153.
PaxDbiP30153.
PeptideAtlasiP30153.
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.
DisGeNETi5518.
GeneCardsiPPP2R1A.
HGNCiHGNC:9302. PPP2R1A.
HPAiCAB018599.
MIMi605983. gene.
616362. phenotype.
neXtProtiNX_P30153.
OpenTargetsiENSG00000105568.
PharmGKBiPA33666.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0211. Eukaryota.
ENOG410XQVI. LUCA.
GeneTreeiENSGT00730000110944.
HOGENOMiHOG000078539.
HOVERGENiHBG000011.
InParanoidiP30153.
KOiK03456.
OMAiMSNILPC.
OrthoDBiEOG091G045V.
PhylomeDBiP30153.
TreeFamiTF105552.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000105568-MONOMER.
ZFISH: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-6804757. Regulation of TP53 Degradation.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
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-8854518. AURKA Activation by TPX2.
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SignaLinkiP30153.
SIGNORiP30153.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000105568.
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...

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: November 30, 2016
This is version 177 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.