UniProt:P62714 PPP2CB

chain
  • chain:1-309
checksum 51DA9EB0633FC191
comment
  • FUNCTION Catalytic subunit of protein phosphatase 2A (PP2A), a serine/threonine phosphatase involved in the regulation of a wide variety of enzymes, signal transduction pathways, and cellular events (Probable). PP2A can modulate the activity of phosphorylase B kinase, casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (PubMed:18782753).CATALYTIC ACTIVITY O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphateCATALYTIC ACTIVITY O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphateCOFACTOR Binds 2 manganese ions per subunit.SUBUNIT 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 SGO1, most probably through regulatory B56 subunits. Interacts with CTTNBP2NL. Interacts with PTPA (PubMed:12952889). Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD (By similarity). Part of the core of STRIPAK complexes composed of PP2A catalytic and scaffolding subunits, the striatins (PP2A regulatory subunits), the striatin-associated proteins MOB4, STRIP1 and STRIP2, PDCD10 and members of the STE20 kinases, such as STK24 and STK26 (PubMed:18782753).INTERACTION In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles.PTM 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.PTM 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.PTM May be monoubiquitinated by NOSIP.SIMILARITY Belongs to the PPP phosphatase family. PP-1 subfamily.
crossReference
databaseName UniProt
dbId 61104
description
  • recommendedName: fullName evidence="11"Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform shortName: PP2A-beta ecNumber evidence="12"3.1.3.16
displayName UniProt:P62714 PPP2CB
geneName
  • PPP2CB
identifier P62714
isSequenceChanged false
keyword
  • Centromere
  • Chromosome
  • Cytoplasm
  • Cytoskeleton
  • Direct protein sequencing
  • Hydrolase
  • Manganese
  • Metal-binding
  • Methylation
  • Nucleus
  • Phosphoprotein
  • Protein phosphatase
  • Proteomics identification
  • Reference proteome
  • Ubl conjugation
modified [InstanceEdit:9939033] Weiser, Joel, 2025-02-21
moleculeType Protein
name
  • PPP2CB
otherIdentifier
  • 11716041_a_at
  • 11716042_x_at
  • 11726558_a_at
  • 17076083
  • 201374_3p_x_at
  • 201374_PM_x_at
  • 201374_x_at
  • 201375_PM_s_at
  • 201375_s_at
  • 3130214
  • 3130216
  • 3130217
  • 3130218
  • 3130219
  • 3130220
  • 3130222
  • 3130223
  • 3130224
  • 3130225
  • 3130226
  • 3130227
  • 3130228
  • 3130229
  • 3130233
  • 3130234
  • 3130235
  • 3130239
  • 3130240
  • 3130241
  • 3130242
  • 3130243
  • 5516
  • 8150126
  • 924_s_at
  • A_23_P134693
  • GE58000
  • GE79502
  • GO:0000159
  • GO:0000278
  • GO:0000775
  • GO:0000922
  • GO:0003824
  • GO:0004721
  • GO:0004722
  • GO:0005515
  • GO:0005634
  • GO:0005694
  • GO:0005737
  • GO:0005829
  • GO:0005856
  • GO:0006470
  • GO:0007005
  • GO:0008092
  • GO:0008637
  • GO:0010288
  • GO:0010468
  • GO:0010629
  • GO:0010804
  • GO:0016787
  • GO:0030163
  • GO:0031113
  • GO:0034976
  • GO:0042542
  • GO:0043124
  • GO:0043161
  • GO:0044325
  • GO:0046580
  • GO:0046677
  • GO:0046872
  • GO:0048156
  • GO:0090443
  • GO:0140096
  • GO:1902996
  • HMNXSV003036743
  • Hs.80350.0.S1_3p_at
  • Hs.80350.0.S1_3p_x_at
  • ILMN_1675693
  • ILMN_1712659
  • ILMN_1768582
  • J03805_s_at
  • PH_hs_0027708
  • TC08001111.hg
  • g4758951_3p_a_at
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • PP2AB_HUMAN
  • D3DSV4
  • P11082
  • Q6FHK5
sequenceLength 309
species [Species:48887] Homo sapiens
stId uniprot:P62714
url http://purl.uniprot.org/uniprot/P62714
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