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Protein

Serine/threonine-protein phosphatase PP2A-3 catalytic subunit

Gene

PP2A3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi61 – 611Manganese 1By similarity
Metal bindingi63 – 631Manganese 1By similarity
Metal bindingi89 – 891Manganese 1By similarity
Metal bindingi89 – 891Manganese 2By similarity
Metal bindingi121 – 1211Manganese 2By similarity
Active sitei122 – 1221Proton donorBy similarity
Metal bindingi171 – 1711Manganese 2By similarity
Metal bindingi245 – 2451Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphoprotein phosphatase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein dephosphorylation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT3G58500-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP2A-3 catalytic subunit (EC:3.1.3.16)
Alternative name(s):
Protein phosphatase 2A isoform 3
Gene namesi
Name:PP2A3
Synonyms:EP7, PP2A4
Ordered Locus Names:At3g58500
ORF Names:F14P22.90
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G58500.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: TAIR
  2. cytosol Source: TAIR
  3. nucleolus Source: TAIR
  4. nucleus Source: TAIR
  5. protein phosphatase type 2A complex Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Serine/threonine-protein phosphatase PP2A-3 catalytic subunitPRO_0000058855Add
BLAST

Proteomic databases

PaxDbiP48578.
PRIDEiP48578.

Expressioni

Gene expression databases

ExpressionAtlasiP48578. baseline.
GenevestigatoriP48578.

Interactioni

Subunit structurei

PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit (subunit A), that associates with a variety of regulatory subunits such as subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families).By similarity

Protein-protein interaction databases

BioGridi10334. 2 interactions.
IntActiP48578. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP48578.
SMRiP48578. Positions 11-313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-2A subfamily.Curated

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172696.
KOiK04382.
OMAiPWEREEC.
PhylomeDBiP48578.

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]

Sequencei

Sequence statusi: Complete.

P48578-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGANSLPTDA TLDLDEQISQ LMQCKPLSEQ QVRALCEKAK EILMDESNVQ
60 70 80 90 100
PVKSPVTICG DIHGQFHDLA ELFRIGGKCP DTNYLFMGDY VDRGYYSVET
110 120 130 140 150
VTLLVGLKVR YPQRITILRG NHESRQITQV YGFYDECLRK YGNANVWKIF
160 170 180 190 200
TDLFDYFPLT ALVESEIFCL HGGLSPSIET LDNIRNFDRV QEVPHEGPMC
210 220 230 240 250
DLLWSDPDDR CGWGISPRGA GYTFGQDISE QFNHTNNLKL IARAHQLVMD
260 270 280 290 300
GFNWAHEQKV VTIFSAPNYC YRCGNMASIL EVDDCRNHTF IQFEPAPRRG
310
EPDVTRRTPD YFL
Length:313
Mass (Da):35,767
Last modified:January 31, 1996 - v1
Checksum:i0636FF10832B1B00
GO

Sequence cautioni

The sequence CAB68188.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08047 mRNA. Translation: AAA64941.1.
U60136 Genomic DNA. Translation: AAD10855.1.
AL137082 Genomic DNA. Translation: CAB68188.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79790.1.
AY057604 mRNA. Translation: AAL14399.1.
AY056222 mRNA. Translation: AAL07071.1.
AY113023 mRNA. Translation: AAM47331.1.
PIRiS52660.
RefSeqiNP_567066.1. NM_115712.3.
UniGeneiAt.25267.

Genome annotation databases

EnsemblPlantsiAT3G58500.1; AT3G58500.1; AT3G58500.
GeneIDi825019.
KEGGiath:AT3G58500.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08047 mRNA. Translation: AAA64941.1.
U60136 Genomic DNA. Translation: AAD10855.1.
AL137082 Genomic DNA. Translation: CAB68188.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE79790.1.
AY057604 mRNA. Translation: AAL14399.1.
AY056222 mRNA. Translation: AAL07071.1.
AY113023 mRNA. Translation: AAM47331.1.
PIRiS52660.
RefSeqiNP_567066.1. NM_115712.3.
UniGeneiAt.25267.

3D structure databases

ProteinModelPortaliP48578.
SMRiP48578. Positions 11-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi10334. 2 interactions.
IntActiP48578. 1 interaction.

Proteomic databases

PaxDbiP48578.
PRIDEiP48578.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G58500.1; AT3G58500.1; AT3G58500.
GeneIDi825019.
KEGGiath:AT3G58500.

Organism-specific databases

TAIRiAT3G58500.

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172696.
KOiK04382.
OMAiPWEREEC.
PhylomeDBiP48578.

Enzyme and pathway databases

BioCyciARA:AT3G58500-MONOMER.

Gene expression databases

ExpressionAtlasiP48578. baseline.
GenevestigatoriP48578.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of a fourth isoform of the catalytic subunit of protein phosphatase 2A from Arabidopsis thaliana."
    Casamayor A., Perez-Callejon E., Pujol G., Arino J., Ferrer A.
    Plant Mol. Biol. 26:523-528(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia GL1.
    Tissue: Leaf.
  2. "Molecular cloning and characterization of two phosphatase 2A catalytic subunit genes from Arabidopsis thaliana."
    Perez-Callejon E., Casamayor A., Pujol G., Camps M., Ferrer A., Arino J.
    Gene 209:105-112(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Arabidopsis PPP family of serine/threonine phosphatases."
    Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.
    Trends Plant Sci. 12:169-176(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiPP2A3_ARATH
AccessioniPrimary (citable) accession number: P48578
Secondary accession number(s): Q9M2G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1996
Last sequence update: January 31, 1996
Last modified: March 31, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.