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P62715

- PP2AB_MOUSE

UniProt

P62715 - PP2AB_MOUSE

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Protein
Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
Gene
Ppp2cb
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase.

Catalytic activityi

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

Cofactori

Binds 2 manganese ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi57 – 571Manganese 1 By similarity
Metal bindingi59 – 591Manganese 1 By similarity
Metal bindingi85 – 851Manganese 1 By similarity
Metal bindingi85 – 851Manganese 2 By similarity
Metal bindingi117 – 1171Manganese 2 By similarity
Active sitei118 – 1181Proton donor By similarity
Metal bindingi167 – 1671Manganese 2 By similarity
Metal bindingi241 – 2411Manganese 2 By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein binding Source: MGI
  3. protein serine/threonine phosphatase activity Source: Ensembl

GO - Biological processi

  1. apoptotic mitochondrial changes Source: MGI
  2. negative regulation of Ras protein signal transduction Source: Ensembl
  3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
  4. protein dephosphorylation Source: Ensembl
  5. regulation of gene expression Source: MGI
  6. response to antibiotic Source: MGI
  7. response to endoplasmic reticulum stress Source: MGI
  8. response to hydrogen peroxide Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196577. MASTL Facilitates Mitotic Progression.
REACT_198526. Spry regulation of FGF signaling.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_203795. DARPP-32 events.
REACT_206803. Cyclin A/B1 associated events during G2/M transition.
REACT_207679. Separation of Sister Chromatids.
REACT_208887. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_210064. ERKs are inactivated.
REACT_215063. ERK/MAPK targets.
REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_217323. Integration of energy metabolism.
REACT_218396. Beta-catenin phosphorylation cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform (EC:3.1.3.16)
Short name:
PP2A-beta
Gene namesi
Name:Ppp2cb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1321161. Ppp2cb.

Subcellular locationi

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

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB-SubCell
  2. cytoplasm Source: MGI
  3. nucleus Source: MGI
  4. protein phosphatase type 2A complex Source: MGI
  5. spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi307 – 3071Y → Q: Loss of trimeric subunit ABC assembly. 1 Publication
Mutagenesisi309 – 3091L → A: Loss of binding to PP2A B-alpha regulatory subunit. 1 Publication
Mutagenesisi309 – 3091L → Q: Loss of trimeric subunit ABC assembly. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
PRO_0000058846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei307 – 3071Phosphotyrosine1 Publication
Modified residuei309 – 3091Leucine methyl ester By similarity

Post-translational modificationi

Reversibly methyl esterified on Leu-309 by leucine carboxyl methyltransferase 1 (Lcmt1) and protein phosphatase methylesterase 1 (Ppme1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization 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.

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP62715.
PaxDbiP62715.
PRIDEiP62715.

PTM databases

PhosphoSiteiP62715.

Expressioni

Gene expression databases

BgeeiP62715.
GenevestigatoriP62715.

Interactioni

Subunit structurei

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. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD By similarity. Interacts with CTTNBP2NL By similarity.

Protein-protein interaction databases

BioGridi202342. 11 interactions.
IntActiP62715. 2 interactions.
STRINGi10090.ENSMUSP00000009774.

Structurei

3D structure databases

ProteinModelPortaliP62715.
SMRiP62715. Positions 6-293.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074618.
HOGENOMiHOG000172696.
HOVERGENiHBG000216.
InParanoidiP62715.
KOiK04382.
OMAiRPPDYFL.
OrthoDBiEOG74N5H2.
PhylomeDBiP62715.
TreeFamiTF105559.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62715-1 [UniParc]FASTAAdd to Basket

« Hide

MDDKAFTKEL DQWVEQLNEC KQLNENQVRT LCEKAKEILT KESNVQEVRC    50
PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL 100
VALKVRYPER ITILRGNHES RQITQVYGFY DECLRKYGNA NVWKYFTDLF 150
DYLPLTALVD GQIFCLHGGL SPSIDTLDHI RALDRLQEVP HEGPMCDLLW 200
SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA HQLVMEGYNW 250
CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV 300
TRRTPDYFL 309
Length:309
Mass (Da):35,575
Last modified:July 19, 2004 - v1
Checksum:i51DA9EB0633FC191
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z67746 mRNA. Translation: CAA91559.1.
BC058582 mRNA. Translation: AAH58582.1.
CCDSiCCDS22233.1.
RefSeqiNP_059070.1. NM_017374.3.
UniGeneiMm.288765.
Mm.29301.

Genome annotation databases

EnsembliENSMUST00000009774; ENSMUSP00000009774; ENSMUSG00000009630.
GeneIDi19053.
KEGGimmu:19053.
UCSCiuc009lkd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z67746 mRNA. Translation: CAA91559.1 .
BC058582 mRNA. Translation: AAH58582.1 .
CCDSi CCDS22233.1.
RefSeqi NP_059070.1. NM_017374.3.
UniGenei Mm.288765.
Mm.29301.

3D structure databases

ProteinModelPortali P62715.
SMRi P62715. Positions 6-293.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202342. 11 interactions.
IntActi P62715. 2 interactions.
STRINGi 10090.ENSMUSP00000009774.

Chemistry

BindingDBi P62715.

PTM databases

PhosphoSitei P62715.

Proteomic databases

MaxQBi P62715.
PaxDbi P62715.
PRIDEi P62715.

Protocols and materials databases

DNASUi 19053.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000009774 ; ENSMUSP00000009774 ; ENSMUSG00000009630 .
GeneIDi 19053.
KEGGi mmu:19053.
UCSCi uc009lkd.1. mouse.

Organism-specific databases

CTDi 5516.
MGIi MGI:1321161. Ppp2cb.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00550000074618.
HOGENOMi HOG000172696.
HOVERGENi HBG000216.
InParanoidi P62715.
KOi K04382.
OMAi RPPDYFL.
OrthoDBi EOG74N5H2.
PhylomeDBi P62715.
TreeFami TF105559.

Enzyme and pathway databases

Reactomei REACT_196577. MASTL Facilitates Mitotic Progression.
REACT_198526. Spry regulation of FGF signaling.
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_203795. DARPP-32 events.
REACT_206803. Cyclin A/B1 associated events during G2/M transition.
REACT_207679. Separation of Sister Chromatids.
REACT_208887. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_210064. ERKs are inactivated.
REACT_215063. ERK/MAPK targets.
REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_217323. Integration of energy metabolism.
REACT_218396. Beta-catenin phosphorylation cascade.

Miscellaneous databases

ChiTaRSi PPP2CB. mouse.
NextBioi 21334.
PROi P62715.
SOURCEi Search...

Gene expression databases

Bgeei P62715.
Genevestigatori P62715.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Goetz J.M., Kues W.
    Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X DBA/2.
    Tissue: Brain.
  2. "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].
    Strain: FVB/N-3.
    Tissue: Mammary gland.
  3. "Molecular cloning of a protein serine/threonine phosphatase containing a putative regulatory tetratricopeptide repeat domain."
    Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.
    J. Biol. Chem. 269:22586-22592(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-83.
  4. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 284-294, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  5. "Tyrosine phosphorylation of protein phosphatase 2A in response to growth stimulation and v-src transformation of fibroblasts."
    Chen J., Parsons S., Brautigan D.L.
    J. Biol. Chem. 269:7957-7962(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-307.
  6. "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the alpha 4 subunit which promotes dephosphorylation of elongation factor-2."
    Chung H., Nairn A.C., Murata K., Brautigan D.L.
    Biochemistry 38:10371-10376(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-307 AND LEU-309.

Entry informationi

Entry nameiPP2AB_MOUSE
AccessioniPrimary (citable) accession number: P62715
Secondary accession number(s): P11082
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: September 3, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi