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A0CNL9

- PP2A2_PARTE

UniProt

A0CNL9 - PP2A2_PARTE

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Protein
Serine/threonine-protein phosphatase PP2A catalytic subunit 2
Gene
Ppn2, GSPATT00008828001
Organism
Paramecium tetraurelia
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Binds 2 manganese ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi62 – 621Manganese 1 By similarity
Metal bindingi64 – 641Manganese 1 By similarity
Metal bindingi90 – 901Manganese 1 By similarity
Metal bindingi90 – 901Manganese 2 By similarity
Metal bindingi122 – 1221Manganese 2 By similarity
Active sitei123 – 1231Proton donor By similarity
Metal bindingi172 – 1721Manganese 2 By similarity
Metal bindingi247 – 2471Manganese 2 By similarity

GO - Molecular functioni

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

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP2A catalytic subunit 2 (EC:3.1.3.16)
Short name:
PPN 2
Gene namesi
Name:Ppn2
ORF Names:GSPATT00008828001
OrganismiParamecium tetraurelia
Taxonomic identifieri5888 [NCBI]
Taxonomic lineageiEukaryotaAlveolataCiliophoraIntramacronucleataOligohymenophoreaPeniculidaParameciidaeParamecium
ProteomesiUP000000600: Partially assembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315Serine/threonine-protein phosphatase PP2A catalytic subunit 2
PRO_0000307835Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei315 – 3151Leucine methyl ester By similarity

Post-translational modificationi

Reversibly methyl esterified on Leu-315 by leucine carboxyl methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1 (PPE1). 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.

Keywords - PTMi

Methylation

Structurei

3D structure databases

ProteinModelPortaliA0CNL9.
SMRiA0CNL9. Positions 15-315.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK04382.

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.

A0CNL9-1 [UniParc]FASTAAdd to Basket

« Hide

MASLNKLSSN EIGNIDRQIA KLRQGQILTE QEVKSLCIKA KEILQDEPNI    50
IQVRAPLTIC GDIHGQFHDL IELFQIGGNL PDTNYLFLGD YVDRGSQSVE 100
TFSLMLSLKV RYKDRIVLLR GNHENREINK IYGFYDECFR KYGNEIVWKQ 150
FTEVFGYLPL SAIVEQQIFC AHGGLSPAME SVDQIKQLNR VQDIPHEGLM 200
CDLLWSDPEE TKNGWGISPR GAGWTWGCDI TEKFLHSNKL KQIARAHQLV 250
MEGIQKVHNQ KTITIFSAPN YCYRCGNQAC IVEVDEQLKM NQTQFEPAPR 300
ENEPHTTRRV PDYFL 315
Length:315
Mass (Da):36,176
Last modified:November 28, 2006 - v1
Checksum:i5D2073F13028956E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CT868119 Genomic DNA. Translation: CAK72386.1.
RefSeqiXP_001439783.1. XM_001439746.1.
UniGeneiPte.28154.

Genome annotation databases

EnsemblProtistsiCAK72386; CAK72386; GSPATT00008828001.
GeneIDi5025568.
KEGGiptm:GSPATT00008828001.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CT868119 Genomic DNA. Translation: CAK72386.1 .
RefSeqi XP_001439783.1. XM_001439746.1.
UniGenei Pte.28154.

3D structure databases

ProteinModelPortali A0CNL9.
SMRi A0CNL9. Positions 15-315.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblProtistsi CAK72386 ; CAK72386 ; GSPATT00008828001 .
GeneIDi 5025568.
KEGGi ptm:GSPATT00008828001.

Phylogenomic databases

KOi K04382.

Family and domain databases

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

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Stock d4-2.

Entry informationi

Entry nameiPP2A2_PARTE
AccessioniPrimary (citable) accession number: A0CNL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: November 28, 2006
Last modified: July 9, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi