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P11493 (PP2AB_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
Short name=PP2A-beta
EC=3.1.3.16
Gene names
Name:PPP2CB
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length293 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript 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.

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. Binds PPME1 By similarity. May indirectly interact with SGOL1, most probably through regulatory B56 subunits. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD By similarity. Interacts with CTTNBP2NL By similarity.

Subcellular location

Cytoplasm. 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 By similarity.

Post-translational modification

Reversibly methyl esterified on Leu-293. Carboxyl methylation may play a role in holoenzyme assembly. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 293›293Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
PRO_0000058847

Sites

Active site1021Proton donor By similarity
Metal binding411Iron By similarity
Metal binding431Iron By similarity
Metal binding691Iron By similarity
Metal binding691Manganese By similarity
Metal binding1011Manganese By similarity
Metal binding1511Manganese By similarity
Metal binding2251Manganese By similarity

Amino acid modifications

Modified residue2911Phosphotyrosine By similarity
Modified residue2931Leucine methyl ester By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P11493 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: EEFE8E6F0FEF8710

FASTA29333,610
        10         20         30         40         50         60 
LNECKQLNEN QVRTLCEKAK EILTKESNVQ EVRCPVTVCG DVHGQFHDLM ELFRIGGKSP 

        70         80         90        100        110        120 
DTNYLFMGDY VDRGYYSVET VTLLVALKVR YPERITILRG NHESRQITQV YGFYDECLRK 

       130        140        150        160        170        180 
YGNANVWKYF TDLFDYLPLT ALVDGQIFCL HGGLSPSIDT LDHIRALDRL QEVPHEGPMC 

       190        200        210        220        230        240 
DLLWSDPDDR GGWGISPRGA GYTFGQDISE TFNHANGLTL VSRAHQLVME GYNWCHDRNV 

       250        260        270        280        290 
VTIFSAPNYC YRCGNQAAIM ELDDTLKYSF LQFDPAPRRG EPHVTRRTPD YFL

« Hide

References

[1]"Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A."
Stone S.R., Hofsteenge J., Hemmings B.A.
Biochemistry 26:7215-7220(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M20193 mRNA. Translation: AAA30982.1.
PIRB27430.
UniGeneSsc.236.

3D structure databases

ProteinModelPortalP11493.
SMRP11493. Positions 1-293.
ModBaseSearch...

Proteomic databases

PaxDbP11493.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0639.
HOVERGENHBG000216.

Family and domain databases

InterProIPR004843. Metallo_PEstase_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP11493.

Entry information

Entry namePP2AB_PIG
AccessionPrimary (citable) accession number: P11493
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 1, 1996
Last modified: May 1, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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