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P62714 (PP2AB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.7

Catalytic activity

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

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Subunit structure

Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD By similarity. 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. May indirectly interact with SGOL1, most probably through regulatory B56 subunits. Interacts with CTTNBP2NL. Ref.8 Ref.10 Ref.11 Ref.12

Subcellular location

Cytoplasm. Nucleus. Chromosomecentromere. Cytoplasmcytoskeletonspindle pole. Note: In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles. Ref.11

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). Ref.9 Ref.10

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.

Sequence similarities

Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Nucleus
   LigandIron
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMMethylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic mitochondrial changes

Inferred from electronic annotation. Source: Ensembl

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of Ras protein signal transduction

Inferred from electronic annotation. Source: Ensembl

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

protein dephosphorylation

Traceable author statement Ref.1. Source: UniProtKB

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

response to antibiotic

Inferred from electronic annotation. Source: Ensembl

response to endoplasmic reticulum stress

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein phosphatase type 2A complex

Traceable author statement Ref.9. Source: UniProtKB

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine phosphatase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
PRO_0000058845

Sites

Active site1181Proton donor By similarity
Metal binding571Iron By similarity
Metal binding591Iron By similarity
Metal binding851Iron By similarity
Metal binding851Manganese By similarity
Metal binding1171Manganese By similarity
Metal binding1671Manganese By similarity
Metal binding2411Manganese By similarity

Amino acid modifications

Modified residue3071Phosphotyrosine By similarity
Modified residue3091Leucine methyl ester Ref.9

Experimental info

Sequence conflict191E → D in AAB38020. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P62714 [UniParc].

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

FASTA30935,575
        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 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of the cDNA encoding the human lung protein phosphatase 2A beta catalytic subunit."
Hemmings B.A., Wernet W., Mayer R., Maurer F., Hofsteenge J., Stone S.R.
Nucleic Acids Res. 16:11366-11366(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic subunit isotypes."
Arino J., Woon C.W., Brautigan D.L., Miller T.B. Jr., Johnson G.L.
Proc. Natl. Acad. Sci. U.S.A. 85:4252-4256(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-309.
Tissue: Liver.
[5]"Structure and transcriptional regulation of protein phosphatase 2A catalytic subunit genes."
Khew-Goodall Y., Mayer R.E., Maurer F., Stone S.R., Hemmings B.A.
Biochemistry 30:89-97(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[7]"Activation of SV40 DNA replication in vitro by cellular protein phosphatase 2A."
Virshup D.M., Kauffman M.G., Kelly T.J.
EMBO J. 8:3891-3898(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 91-97; 111-114; 122-127; 137-144 AND 207-238, FUNCTION.
[8]"Polyoma small and middle T antigens and SV40 small t antigen form stable complexes with protein phosphatase 2A."
Pallas D.C., Shahrik L.K., Martin B.L., Jaspers S., Miller T.B. Jr., Brautigan D.L., Roberts T.M.
Cell 60:167-176(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 75-89; 215-234; 270-294 AND 303-309, INTERACTION WITH VIRAL PROTEINS.
[9]"The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo."
Favre B., Zolnierowicz S., Turowski P., Hemmings B.A.
J. Biol. Chem. 269:16311-16317(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LEU-309.
[10]"A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A."
Ogris E., Du X., Nelson K.C., Mak E.K., Yu X.X., Lane W.S., Pallas D.C.
J. Biol. Chem. 274:14382-14391(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PME1, DEMETHYLATION.
[11]"Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SGOL1.
[12]"A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein."
Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., Aebersold R., Raught B., Gingras A.C.
Mol. Cell. Proteomics 8:157-171(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTTNBP2NL.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12656 mRNA. Translation: CAA31183.1.
CR541747 mRNA. Translation: CAG46547.1.
J03805 mRNA. Translation: AAB38020.1.
CH471080 Genomic DNA. Translation: EAW63434.1.
CH471080 Genomic DNA. Translation: EAW63435.1.
CH471080 Genomic DNA. Translation: EAW63436.1.
BC012022 mRNA. Translation: AAH12022.1.
M60484 Genomic DNA. Translation: AAA36467.1.
PIRPAHU2B. B37135.
RefSeqNP_001009552.1. NM_001009552.1.
UniGeneHs.491440.

3D structure databases

ProteinModelPortalP62714.
SMRP62714. Positions 6-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111508. 91 interactions.
IntActP62714. 78 interactions.
MINTMINT-1348293.
STRING9606.ENSP00000221138.

Chemistry

BindingDBP62714.
DrugBankDB00163. Vitamin E.

PTM databases

PhosphoSiteP62714.

Polymorphism databases

DMDM50402236.

2D gel databases

OGPP62714.
REPRODUCTION-2DPAGEIPI00429689.

Proteomic databases

PaxDbP62714.
PRIDEP62714.

Protocols and materials databases

DNASU5516.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221138; ENSP00000221138; ENSG00000104695.
GeneID5516.
KEGGhsa:5516.
UCSCuc003xik.3. human.

Organism-specific databases

CTD5516.
GeneCardsGC08M030631.
HGNCHGNC:9300. PPP2CB.
HPACAB018600.
HPA043236.
MIM176916. gene.
neXtProtNX_P62714.
PharmGKBPA33664.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172696.
HOVERGENHBG000216.
InParanoidP62714.
KOK04382.
OMAVENDIFC.
PhylomeDBP62714.
TreeFamTF105559.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP62714.
BgeeP62714.
CleanExHS_PPP2CB.
GenevestigatorP62714.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
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

ChiTaRSPPP2CB. human.
GeneWikiPPP2CB.
GenomeRNAi5516.
NextBio21334.
PROP62714.
SOURCESearch...

Entry information

Entry namePP2AB_HUMAN
AccessionPrimary (citable) accession number: P62714
Secondary accession number(s): D3DSV4, P11082, Q6FHK5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM