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

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Reviewed, UniProtKB/Swiss-Prot P63331 (PP2AA_RAT)

Last modified November 3, 2009. Version 48. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

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Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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General annotation (Comments)

Function	PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase 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 a 36 kDa catalytic subunit (subunit C) and 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. May indirectly interact with SGOL1, most probably through regulatory B56 subunits By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. 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 By similarity.
Post-translational modification	Reversibly methyl esterified on Leu-309. Carboxyl methylation may play a role in holoenzyme assembly. 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.

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Ontologies

Keywords
Cellular component	Centromere Cytoplasm Cytoskeleton Nucleus
Ligand	Iron Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Methylation Phosphoprotein
Gene Ontology (GO)
Biological process	protein amino acid dephosphorylation Inferred from direct assay. Source: RGD
Cellular component	chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese 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 Ref.2 Inferred from direct assay. Source: RGD
Complete GO annotation...

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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

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Sequences

Sequence

Length

Mass (Da)

Tools

P63331-1 [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

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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.

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Cross-references

Sequence databases
	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.
UniGene	Rn.1271
3D structure databases
HSSP	HSSP built from PDB template 1FJM based on UniProtKB P08129.
SMR	P63331. Positions 2-309.
ModBase	Search...
Protein-protein interaction databases
STRING	P63331.
PTM databases
PhosphoSite	P63331.
Proteomic databases
PRIDE	P63331.
Genome annotation databases
Ensembl	ENSRNOT00000007621; ENSRNOP00000007621; ENSRNOG00000005389; Rattus norvegicus. [Genome view]
GeneID	24672.
KEGG	rno:24672.
UCSC	NM_017039. rat.
Organism-specific databases
CTD	24672.
RGD	3380. Ppp2ca.
Phylogenomic databases
HOVERGEN	P63331.
OMA	AIMEIDE.
Enzyme and pathway databases
BRENDA	3.1.3.16. 248.
Gene expression databases
ArrayExpress	P63331.
Genevestigator	P63331.
GermOnline	ENSRNOG00000005389. Rattus norvegicus.
Family and domain databases
InterPro	IPR004843. M-pesterase. IPR006186. Ser/Thr-sp_prot-phosphatase. [Graphical view]
PANTHER	PTHR11668. T_phtase_apaH. 1 hit.
Pfam	PF00149. Metallophos. 1 hit. [Graphical view]
PRINTS	PR00114. STPHPHTASE.
ProDom	PD000252. T_phtase_apaH. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00156. PP2Ac. 1 hit. [Graphical view]
PROSITE	PS00125. SER_THR_PHOSPHATASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	604045.

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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:	November 3, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

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

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents