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

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Reviewed, UniProtKB/Swiss-Prot P62716 (PP2AB_RAT)

Last modified November 3, 2009. Version 49. 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 beta isoform
      Short name=PP2A-beta
    EC=3.1.3.16

Gene names

Name:

Ppp2cb

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.
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) (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. Binds PPME1 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. Demethylated by PME1 (in vitro) 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	Methylation Phosphoprotein
Gene Ontology (GO)
Biological process	negative regulation of Ras protein signal transduction Inferred from direct assay. Source: RGD 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 domain specific 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...

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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 beta isoform

PRO_0000058849

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

307

Phosphotyrosine By similarity

Modified residue

309

Leucine methyl ester By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

P62716-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 51DA9EB0633FC191
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FASTA

309

35,575

        10         20         30         40         50         60 
MDDKAFTKEL DQWVEQLNEC KQLNENQVRT LCEKAKEILT KESNVQEVRC PVTVCGDVHG 

        70         80         90        100        110        120 
QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYPER 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 beta of the catalytic subunit of protein phosphatase 2A." Posas F., Arino J. Nucleic Acids Res. 17:8370-8370(1989) [PubMed: 2554256] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[2]	"Molecular cloning of rat phosphoprotein phosphatase 2A beta cDNA and increased expressions of phosphatase 2A alpha and 2A beta in rat liver tumors." Kitagawa Y., Sakai R., Tahira T., Tsuda H., Ito N., Sugimura T., Nagao M. Biochem. Biophys. Res. Commun. 157:821-827(1988) [PubMed: 2849437] [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: Kidney.
[4]	"Multiplicity of protein serine-threonine phosphatases in PC12 pheochromocytoma and FTO-2B hepatoma cells." Wadzinski B.E., Heasley L.E., Johnson G.L. J. Biol. Chem. 265:21504-21508(1990) [PubMed: 2174876] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 204-260. Tissue: Hepatoma and Pheochromocytoma.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M23591 mRNA. Translation: AAA41912.1. X16044 mRNA. Translation: CAA34167.1. X14087 mRNA. Translation: CAA32249.1. M58438 mRNA. Translation: AAA41911.1. BC085926 mRNA. Translation: AAH85926.1. M58439 mRNA. Translation: AAA41913.1.
IPI	IPI00190462.
PIR	PART2B. S08486.
RefSeq	NP_058736.1.
UniGene	Rn.977
3D structure databases
HSSP	HSSP built from PDB template 1FJM based on UniProtKB P08129.
SMR	P62716. Positions 2-309.
ModBase	Search...
Protein-protein interaction databases
STRING	P62716.
PTM databases
PhosphoSite	P62716.
Proteomic databases
PRIDE	P62716.
Genome annotation databases
Ensembl	ENSRNOT00000020663; ENSRNOP00000020663; ENSRNOG00000015182; Rattus norvegicus. [Genome view]
GeneID	24673.
KEGG	rno:24673.
UCSC	NM_017040. rat.
Organism-specific databases
CTD	24673.
RGD	3381. Ppp2cb.
Phylogenomic databases
HOVERGEN	P62716.
OMA	ERLMQCK.
Enzyme and pathway databases
BRENDA	3.1.3.16. 248.
Gene expression databases
ArrayExpress	P62716.
Genevestigator	P62716.
GermOnline	ENSRNOG00000015182. 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	604049.

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Entry information

Entry name

PP2AB_RAT

Accession

Primary (citable) accession number: P62716
Secondary accession number(s): P11082, Q6LDK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	November 3, 2009
This is version 49 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