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P62714

- PP2AB_HUMAN

UniProt

P62714 - PP2AB_HUMAN

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Protein

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

Gene

PPP2CB

Organism
Homo sapiens (Human)
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.1 Publication

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 1By similarity
Metal bindingi59 – 591Manganese 1By similarity
Metal bindingi85 – 851Manganese 1By similarity
Metal bindingi85 – 851Manganese 2By similarity
Metal bindingi117 – 1171Manganese 2By similarity
Active sitei118 – 1181Proton donorBy similarity
Metal bindingi167 – 1671Manganese 2By similarity
Metal bindingi241 – 2411Manganese 2By similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_111080. Spry regulation of FGF signaling.
REACT_12436. ERKs are inactivated.
REACT_12599. ERK/MAPK targets.
REACT_1383. Glycolysis.
REACT_150182. MASTL Facilitates Mitotic Progression.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_1505. Integration of energy metabolism.
REACT_15334. DARPP-32 events.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_19405. CTLA4 inhibitory signaling.
REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_23879. Platelet sensitization by LDL.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_682. Mitotic Prometaphase.
REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_821. Cyclin D associated events in G1.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:9300. PPP2CB.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication. Chromosomecentromere 1 Publication. Cytoplasmcytoskeletonspindle pole 1 Publication
Note: In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles.

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-KW
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. nucleus Source: UniProtKB-KW
  6. protein phosphatase type 2A complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33664.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Serine/threonine-protein phosphatase 2A catalytic subunit beta isoformPRO_0000058845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei307 – 3071PhosphotyrosineBy similarity
Modified residuei309 – 3091Leucine methyl ester1 Publication

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.1 Publication
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.

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP62714.
PaxDbiP62714.
PRIDEiP62714.

2D gel databases

OGPiP62714.
REPRODUCTION-2DPAGEIPI00429689.

PTM databases

PhosphoSiteiP62714.

Expressioni

Gene expression databases

BgeeiP62714.
CleanExiHS_PPP2CB.
ExpressionAtlasiP62714. baseline and differential.
GenevestigatoriP62714.

Organism-specific databases

HPAiCAB018600.
HPA043236.

Interactioni

Subunit structurei

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.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q13642-23EBI-1044367,EBI-8477209
AXIN2Q9Y2T14EBI-1044367,EBI-4400025
IGBP1P783183EBI-1044367,EBI-1055954

Protein-protein interaction databases

BioGridi111508. 110 interactions.
IntActiP62714. 80 interactions.
MINTiMINT-1348293.
STRINGi9606.ENSP00000221138.

Structurei

3D structure databases

ProteinModelPortaliP62714.
SMRiP62714. Positions 6-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074618.
HOGENOMiHOG000172696.
HOVERGENiHBG000216.
InParanoidiP62714.
KOiK04382.
OMAiRPPDYFL.
PhylomeDBiP62714.
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.

P62714-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDDKAFTKEL DQWVEQLNEC KQLNENQVRT LCEKAKEILT KESNVQEVRC
60 70 80 90 100
PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL
110 120 130 140 150
VALKVRYPER ITILRGNHES RQITQVYGFY DECLRKYGNA NVWKYFTDLF
160 170 180 190 200
DYLPLTALVD GQIFCLHGGL SPSIDTLDHI RALDRLQEVP HEGPMCDLLW
210 220 230 240 250
SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA HQLVMEGYNW
260 270 280 290 300
CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV

TRRTPDYFL
Length:309
Mass (Da):35,575
Last modified:July 19, 2004 - v1
Checksum:i51DA9EB0633FC191
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191E → D in AAB38020. (PubMed:2837763)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS6079.1.
PIRiB37135. PAHU2B.
RefSeqiNP_001009552.1. NM_001009552.1.
UniGeneiHs.491440.

Genome annotation databases

EnsembliENST00000221138; ENSP00000221138; ENSG00000104695.
GeneIDi5516.
KEGGihsa:5516.
UCSCiuc003xik.3. human.

Polymorphism databases

DMDMi50402236.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS6079.1.
PIRi B37135. PAHU2B.
RefSeqi NP_001009552.1. NM_001009552.1.
UniGenei Hs.491440.

3D structure databases

ProteinModelPortali P62714.
SMRi P62714. Positions 6-293.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111508. 110 interactions.
IntActi P62714. 80 interactions.
MINTi MINT-1348293.
STRINGi 9606.ENSP00000221138.

Chemistry

BindingDBi P62714.
DrugBanki DB00163. Vitamin E.

PTM databases

PhosphoSitei P62714.

Polymorphism databases

DMDMi 50402236.

2D gel databases

OGPi P62714.
REPRODUCTION-2DPAGE IPI00429689.

Proteomic databases

MaxQBi P62714.
PaxDbi P62714.
PRIDEi P62714.

Protocols and materials databases

DNASUi 5516.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000221138 ; ENSP00000221138 ; ENSG00000104695 .
GeneIDi 5516.
KEGGi hsa:5516.
UCSCi uc003xik.3. human.

Organism-specific databases

CTDi 5516.
GeneCardsi GC08M030631.
HGNCi HGNC:9300. PPP2CB.
HPAi CAB018600.
HPA043236.
MIMi 176916. gene.
neXtProti NX_P62714.
PharmGKBi PA33664.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00550000074618.
HOGENOMi HOG000172696.
HOVERGENi HBG000216.
InParanoidi P62714.
KOi K04382.
OMAi RPPDYFL.
PhylomeDBi P62714.
TreeFami TF105559.

Enzyme and pathway databases

Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_111080. Spry regulation of FGF signaling.
REACT_12436. ERKs are inactivated.
REACT_12599. ERK/MAPK targets.
REACT_1383. Glycolysis.
REACT_150182. MASTL Facilitates Mitotic Progression.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_1505. Integration of energy metabolism.
REACT_15334. DARPP-32 events.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_19405. CTLA4 inhibitory signaling.
REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_23879. Platelet sensitization by LDL.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_682. Mitotic Prometaphase.
REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_821. Cyclin D associated events in G1.

Miscellaneous databases

ChiTaRSi PPP2CB. human.
GeneWikii PPP2CB.
GenomeRNAii 5516.
NextBioi 21334.
PROi P62714.
SOURCEi Search...

Gene expression databases

Bgeei P62714.
CleanExi HS_PPP2CB.
ExpressionAtlasi P62714. baseline and differential.
Genevestigatori P62714.

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. "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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPP2AB_HUMAN
AccessioniPrimary (citable) accession number: P62714
Secondary accession number(s): D3DSV4, P11082, Q6FHK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: October 29, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3