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

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P63331 (PP2AA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Short name=PP2A-alpha
EC=3.1.3.16

Gene names

Name:

Ppp2ca

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGOL2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I. Activates RAF1 by dephosphorylating it at 'Ser-259' By similarity.
Catalytic activity	A phosphoprotein + H₂O = a protein + phosphate.
Cofactor	Binds 1 iron ion per subunit By similarity. Binds 1 manganese ion per subunit By similarity.
Subunit structure	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. Interacts with TP53, SGOL1 and SGOL2. Interacts with AXIN1; the interaction dephosphorylates AXIN1 By similarity. Interacts with PIM3; this interaction promotes dephosphorylation, ubiquitination and proteasomal degradation of PIM3 By similarity. Interacts with RAF1 By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Chromosome › centromere By similarity. Cytoplasm › cytoskeleton › spindle pole By similarity. Note: In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles. Centromeric localization requires the presence of SGOL2 By similarity.
Post-translational modification	Reversibly methyl esterified on Leu-309. Carboxyl methylation may play a role in holoenzyme assembly, enhancing the affinity of the PP2A core enzyme for some, but not all, regulatory subunits. It varies during the cell cycle By similarity. 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 By similarity.
Sequence similarities	Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
Biological process	Meiosis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	meiosis Inferred from electronic annotation. Source: UniProtKB-KW protein dephosphorylation Inferred from direct assay. Source: RGD protein heterotrimerization Inferred from mutant phenotype. Source: MGI regulation of protein autophosphorylation Inferred from mutant phenotype. Source: MGI regulation of protein catabolic process Inferred from mutant phenotype. Source: MGI regulation of receptor activity Inferred from mutant phenotype. Source: MGI
Cellular component	chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein C-terminus binding Inferred from physical interaction. Source: RGD protein heterodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine phosphatase activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 309

309

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

PRO_0000058843

Sites

Active site

118

Proton donor By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Iron By similarity

Metal binding

Manganese By similarity

Metal binding

117

Manganese By similarity

Metal binding

167

Manganese By similarity

Metal binding

241

Manganese By similarity

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

307

Phosphotyrosine By similarity

Modified residue

309

Leucine methyl ester By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P63331 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 8DC11276E6DF9E33
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FASTA

309

35,608

        10         20         30         40         50         60 
MDEKLFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC PVTVCGDVHG 

        70         80         90        100        110        120 
QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYRER ITILRGNHES 

       130        140        150        160        170        180 
RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDTLDHI 

       190        200        210        220        230        240 
RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA 

       250        260        270        280        290        300 
HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV 


TRRTPDYFL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a rat heart cDNA encoding the isotype alpha of the catalytic subunit of protein phosphatase 2A." Posas F., Arino J. Nucleic Acids Res. 17:8369-8369(1989) [PubMed: 2554255] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[2]	"Molecular cloning of cDNA for the catalytic subunit of rat liver type 2A protein phosphatase, and detection of high levels of expression of the gene in normal and cancer cells." Kitagawa Y., Tahira T., Ikeda I., Kikuchi K., Tsuiki S., Sugimura T., Nagao M. Biochim. Biophys. Acta 951:123-129(1988) [PubMed: 2461222] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart and Lung.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X16043 mRNA. Translation: CAA34166.1. X14159 mRNA. Translation: CAB42983.1. M33114 mRNA. Translation: AAA41904.1. BC070914 mRNA. Translation: AAH70914.1. BC072531 mRNA. Translation: AAH72531.1.
IPI	IPI00200391.
PIR	PART2A. S06592.
RefSeq	NP_058735.1. NM_017039.2.
UniGene	Rn.1271.
3D structure databases
ProteinModelPortal	P63331.
SMR	P63331. Positions 6-293.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-199689.
STRING	P63331.
PTM databases
PhosphoSite	P63331.
2D gel databases
World-2DPAGE	0004:P63331.
Proteomic databases
PRIDE	P63331.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000007621; ENSRNOP00000007621; ENSRNOG00000005389.
GeneID	24672.
KEGG	rno:24672.
UCSC	NM_017039. rat.
Organism-specific databases
CTD	5515.
RGD	3380. Ppp2ca.
Phylogenomic databases
eggNOG	maNOG11164.
GeneTree	ENSGT00550000074618.
HOVERGEN	HBG000216.
InParanoid	P63331.
OMA	AIMEIDE.
OrthoDB	EOG4Q58PR.
PhylomeDB	P63331.
Enzyme and pathway databases
Reactome	REACT_113568. Metabolism. REACT_33953. Metabolism of carbohydrates.
Gene expression databases
ArrayExpress	P63331.
Genevestigator	P63331.
GermOnline	ENSRNOG00000005389. Rattus norvegicus.
Family and domain databases
InterPro	IPR004843. Metallo_PEstase_dom. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
KO	K04382.
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	604045.

Entry information

Entry name

PP2AA_RAT

Accession

Primary (citable) accession number: P63331
Secondary accession number(s): O88591, P13353

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents