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Protein

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

Gene

PPP2CA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 SGO2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at 'Ser-259'.By similarity3 Publications

Catalytic activityi

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

Cofactori

Mn2+1 PublicationNote: Binds 2 manganese ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi57Manganese 11 Publication1
Metal bindingi59Manganese 11 Publication1
Metal bindingi85Manganese 11 Publication1
Metal bindingi85Manganese 21 Publication1
Metal bindingi117Manganese 21 Publication1
Active sitei118Proton donorBy similarity1
Metal bindingi167Manganese 21 Publication1
Metal bindingi241Manganese 21 Publication1

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • ceramide metabolic process Source: UniProtKB
  • inactivation of MAPK activity Source: UniProtKB
  • meiotic cell cycle Source: UniProtKB-KW
  • mesoderm development Source: Ensembl
  • mitotic nuclear envelope reassembly Source: Reactome
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of epithelial to mesenchymal transition Source: BHF-UCL
  • negative regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • positive regulation of protein serine/threonine kinase activity Source: BHF-UCL
  • 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 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 - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Meiosis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS03696-MONOMER.
ZFISH:HS03696-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-2995383. Initiation of Nuclear Envelope Reformation.
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-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-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SignaLinkiP67775.
SIGNORiP67775.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:9299. PPP2CA.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi309L → A: Loss of binding to PP2A B-alpha regulatory subunit. 1 Publication1

Organism-specific databases

DisGeNETi5515.
OpenTargetsiENSG00000113575.
PharmGKBiPA33663.

Chemistry databases

ChEMBLiCHEMBL4703.
DrugBankiDB00163. Vitamin E.

Polymorphism and mutation databases

BioMutaiPPP2CA.
DMDMi54038809.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000588391 – 309Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoformAdd BLAST309

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei307PhosphotyrosineBy similarity1
Modified residuei309Leucine methyl ester1 Publication1

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.1 Publication
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.
May be monoubiquitinated by NOSIP.By similarity

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP67775.
MaxQBiP67775.
PaxDbiP67775.
PeptideAtlasiP67775.
PRIDEiP67775.

PTM databases

DEPODiP67775.
iPTMnetiP67775.
PhosphoSitePlusiP67775.

Expressioni

Gene expression databases

BgeeiENSG00000113575.
CleanExiHS_PPP2CA.
ExpressionAtlasiP67775. baseline and differential.
GenevisibleiP67775. HS.

Organism-specific databases

HPAiCAB003848.
HPA043236.

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 KCTD20 (By similarity). Interacts with BTBD10 (By similarity). Interacts with TP53, SGO1 and SGO2. 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).By similarity13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317494EBI-712311,EBI-296087
ANP32AP396872EBI-712311,EBI-359234
E7P031293EBI-712311,EBI-866453From a different organism.
E7P040202EBI-712311,EBI-7005254From a different organism.
IER3P466952EBI-712311,EBI-1748945
IGBP1P7831812EBI-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.
PPP2R1AP3015316EBI-712311,EBI-302388
PPP2R1BP301547EBI-712311,EBI-357094
PPP2R2CQ9Y2T43EBI-712311,EBI-1774058
PPP2R5AQ151724EBI-712311,EBI-641666
PPP2R5BQ151734EBI-712311,EBI-1369497
PPP2R5CQ133627EBI-712311,EBI-1266156
RBL1P287492EBI-712311,EBI-971402
RBL2Q089992EBI-712311,EBI-971439
RELAQ042066EBI-712311,EBI-73886
STRNO438154EBI-712311,EBI-1046642
TIPRLO756633EBI-712311,EBI-1054735
TRIP13Q156455EBI-712311,EBI-358993

Protein-protein interaction databases

BioGridi111507. 240 interactors.
DIPiDIP-29395N.
IntActiP67775. 150 interactors.
MINTiMINT-215645.
STRINGi9606.ENSP00000418447.

Chemistry databases

BindingDBiP67775.

Structurei

Secondary structure

1309
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 18Combined sources16
Helixi25 – 39Combined sources15
Beta strandi44 – 48Combined sources5
Beta strandi50 – 55Combined sources6
Helixi62 – 72Combined sources11
Turni75 – 77Combined sources3
Beta strandi80 – 82Combined sources3
Beta strandi87 – 91Combined sources5
Helixi93 – 106Combined sources14
Turni108 – 110Combined sources3
Beta strandi111 – 113Combined sources3
Helixi121 – 127Combined sources7
Helixi129 – 137Combined sources9
Beta strandi138 – 140Combined sources3
Helixi141 – 150Combined sources10
Beta strandi155 – 159Combined sources5
Turni160 – 162Combined sources3
Beta strandi163 – 168Combined sources6
Helixi177 – 182Combined sources6
Beta strandi186 – 188Combined sources3
Beta strandi191 – 193Combined sources3
Helixi194 – 200Combined sources7
Beta strandi205 – 211Combined sources7
Beta strandi215 – 220Combined sources6
Helixi222 – 232Combined sources11
Beta strandi235 – 239Combined sources5
Beta strandi247 – 251Combined sources5
Turni252 – 255Combined sources4
Beta strandi256 – 259Combined sources4
Helixi265 – 267Combined sources3
Beta strandi273 – 278Combined sources6
Beta strandi284 – 289Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP67775.

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

Phylogenomic databases

eggNOGiKOG0371. Eukaryota.
COG0639. LUCA.
GeneTreeiENSGT00550000074618.
HOGENOMiHOG000172696.
HOVERGENiHBG000216.
InParanoidiP67775.
KOiK04382.
OMAiWIENLMA.
OrthoDBiEOG091G0B6S.
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. AlignAdd to basket

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

        10         20         30         40         50
MDEKVFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC
60 70 80 90 100
PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL
110 120 130 140 150
VALKVRYRER ITILRGNHES RQITQVYGFY DECLRKYGNA NVWKYFTDLF
160 170 180 190 200
DYLPLTALVD GQIFCLHGGL SPSIDTLDHI RALDRLQEVP HEGPMCDLLW
210 220 230 240 250
SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA HQLVMEGYNW
260 270 280 290 300
CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV

TRRTPDYFL
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_05173552V → A.Corresponds to variant rs11552681dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_044320193 – 246Missing in isoform 2. CuratedAdd BLAST54

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human. [P67775-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi111507. 240 interactors.
DIPiDIP-29395N.
IntActiP67775. 150 interactors.
MINTiMINT-215645.
STRINGi9606.ENSP00000418447.

Chemistry databases

BindingDBiP67775.
ChEMBLiCHEMBL4703.
DrugBankiDB00163. Vitamin E.

PTM databases

DEPODiP67775.
iPTMnetiP67775.
PhosphoSitePlusiP67775.

Polymorphism and mutation databases

BioMutaiPPP2CA.
DMDMi54038809.

Proteomic databases

EPDiP67775.
MaxQBiP67775.
PaxDbiP67775.
PeptideAtlasiP67775.
PRIDEiP67775.

Protocols and materials databases

DNASUi5515.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000481195; ENSP00000418447; ENSG00000113575. [P67775-1]
GeneIDi5515.
KEGGihsa:5515.
UCSCiuc003kze.4. human. [P67775-1]

Organism-specific databases

CTDi5515.
DisGeNETi5515.
GeneCardsiPPP2CA.
HGNCiHGNC:9299. PPP2CA.
HPAiCAB003848.
HPA043236.
MIMi176915. gene.
neXtProtiNX_P67775.
OpenTargetsiENSG00000113575.
PharmGKBiPA33663.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0371. Eukaryota.
COG0639. LUCA.
GeneTreeiENSGT00550000074618.
HOGENOMiHOG000172696.
HOVERGENiHBG000216.
InParanoidiP67775.
KOiK04382.
OMAiWIENLMA.
OrthoDBiEOG091G0B6S.
PhylomeDBiP67775.
TreeFamiTF105559.

Enzyme and pathway databases

BioCyciMetaCyc:HS03696-MONOMER.
ZFISH:HS03696-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-2995383. Initiation of Nuclear Envelope Reformation.
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-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-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SignaLinkiP67775.
SIGNORiP67775.

Miscellaneous databases

ChiTaRSiPPP2CA. human.
EvolutionaryTraceiP67775.
GeneWikiiPPP2CA.
GenomeRNAii5515.
PROiP67775.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113575.
CleanExiHS_PPP2CA.
ExpressionAtlasiP67775. baseline and differential.
GenevisibleiP67775. HS.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 136 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

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.