PP2AB_HUMAN
ID PP2AB_HUMAN Reviewed; 309 AA.
AC P62714; D3DSV4; P11082; Q6FHK5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform {ECO:0000305};
DE Short=PP2A-beta;
DE EC=3.1.3.16 {ECO:0000305|PubMed:10318862};
GN Name=PPP2CB {ECO:0000312|HGNC:HGNC:9300};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=2849765; DOI=10.1093/nar/16.23.11366;
RA Hemmings B.A., Wernet W., Mayer R., Maurer F., Hofsteenge J., Stone S.R.;
RT "The nucleotide sequence of the cDNA encoding the human lung protein
RT phosphatase 2A beta catalytic subunit.";
RL Nucleic Acids Res. 16:11366-11366(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-309.
RC TISSUE=Liver;
RX PubMed=2837763; DOI=10.1073/pnas.85.12.4252;
RA Arino J., Woon C.W., Brautigan D.L., Miller T.B. Jr., Johnson G.L.;
RT "Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic
RT subunit isotypes.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4252-4256(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1846293; DOI=10.1021/bi00215a014;
RA Khew-Goodall Y., Mayer R.E., Maurer F., Stone S.R., Hemmings B.A.;
RT "Structure and transcriptional regulation of protein phosphatase 2A
RT catalytic subunit genes.";
RL Biochemistry 30:89-97(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 91-97; 111-114; 122-127; 137-144 AND 207-238, AND
RP FUNCTION.
RX PubMed=2555176; DOI=10.1002/j.1460-2075.1989.tb08568.x;
RA Virshup D.M., Kauffman M.G., Kelly T.J.;
RT "Activation of SV40 DNA replication in vitro by cellular protein
RT phosphatase 2A.";
RL EMBO J. 8:3891-3898(1989).
RN [8]
RP PROTEIN SEQUENCE OF 75-89; 215-234; 270-294 AND 303-309, AND INTERACTION
RP WITH VIRAL PROTEINS.
RX PubMed=2153055; DOI=10.1016/0092-8674(90)90726-u;
RA Pallas D.C., Shahrik L.K., Martin B.L., Jaspers S., Miller T.B. Jr.,
RA Brautigan D.L., Roberts T.M.;
RT "Polyoma small and middle T antigens and SV40 small t antigen form stable
RT complexes with protein phosphatase 2A.";
RL Cell 60:167-176(1990).
RN [9]
RP METHYLATION AT LEU-309.
RX PubMed=8206937; DOI=10.1016/s0021-9258(17)34009-7;
RA Favre B., Zolnierowicz S., Turowski P., Hemmings B.A.;
RT "The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in
RT vivo.";
RL J. Biol. Chem. 269:16311-16317(1994).
RN [10]
RP INTERACTION WITH PME1, DEMETHYLATION, AND MUTAGENESIS OF HIS-59 AND
RP HIS-118.
RX PubMed=10318862; DOI=10.1074/jbc.274.20.14382;
RA Ogris E., Du X., Nelson K.C., Mak E.K., Yu X.X., Lane W.S., Pallas D.C.;
RT "A protein phosphatase methylesterase (PME-1) is one of several novel
RT proteins stably associating with two inactive mutants of protein
RT phosphatase 2A.";
RL J. Biol. Chem. 274:14382-14391(1999).
RN [11]
RP INTERACTION WITH PTPA.
RX PubMed=12952889; DOI=10.1101/gad.259903;
RA Fellner T., Lackner D.H., Hombauer H., Piribauer P., Mudrak I.,
RA Zaragoza K., Juno C., Ogris E.;
RT "A novel and essential mechanism determining specificity and activity of
RT protein phosphatase 2A (PP2A) in vivo.";
RL Genes Dev. 17:2138-2150(2003).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SGO1.
RX PubMed=16541025; DOI=10.1038/nature04663;
RA Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
RA Kawashima S.A., Watanabe Y.;
RT "Shugoshin collaborates with protein phosphatase 2A to protect cohesin.";
RL Nature 441:46-52(2006).
RN [13]
RP INTERACTION WITH CTTNBP2NL.
RX PubMed=18782753; DOI=10.1074/mcp.m800266-mcp200;
RA Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G.,
RA Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I.,
RA Aebersold R., Raught B., Gingras A.C.;
RT "A PP2A phosphatase high density interaction network identifies a novel
RT striatin-interacting phosphatase and kinase complex linked to the cerebral
RT cavernous malformation 3 (CCM3) protein.";
RL Mol. Cell. Proteomics 8:157-171(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalytic subunit of protein phosphatase 2A (PP2A), a
CC serine/threonine phosphatase involved in the regulation of a wide
CC variety of enzymes, signal transduction pathways, and cellular events
CC (Probable). PP2A can modulate the activity of phosphorylase B kinase,
CC casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase.
CC {ECO:0000269|PubMed:2555176, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000305|PubMed:10318862};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000305|PubMed:10318862};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000305|PubMed:10318862};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005;
CC Evidence={ECO:0000305|PubMed:10318862};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
CC PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD (By similarity). PP2A
CC consists of a common heterodimeric core enzyme (composed of a 36 kDa
CC catalytic subunit (subunit C) and a 65 kDa constant regulatory subunit
CC (PR65) (subunit A)) that associates with a variety of regulatory
CC subunits. Proteins that associate with the core dimer include three
CC families of regulatory subunits B (the R2/B/PR55/B55,
CC R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable
CC regulatory subunit, viral proteins, and cell signaling molecules. Binds
CC PPME1. May indirectly interact with SGO1, most probably through
CC regulatory B56 subunits. Interacts with CTTNBP2NL. Interacts with PTPA
CC (PubMed:12952889). {ECO:0000250|UniProtKB:Q0P594,
CC ECO:0000269|PubMed:10318862, ECO:0000269|PubMed:12952889,
CC ECO:0000269|PubMed:16541025, ECO:0000269|PubMed:18782753,
CC ECO:0000269|PubMed:2153055}.
CC -!- INTERACTION:
CC P62714; Q9Y2T1: AXIN2; NbExp=4; IntAct=EBI-1044367, EBI-4400025;
CC P62714; Q06787-7: FMR1; NbExp=3; IntAct=EBI-1044367, EBI-25856644;
CC P62714; P78318: IGBP1; NbExp=6; IntAct=EBI-1044367, EBI-1055954;
CC P62714; Q5VSL9: STRIP1; NbExp=5; IntAct=EBI-1044367, EBI-1773588;
CC P62714; O75663: TIPRL; NbExp=2; IntAct=EBI-1044367, EBI-1054735;
CC P62714; Q13642-2; NbExp=3; IntAct=EBI-1044367, EBI-8477209;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16541025}. Nucleus
CC {ECO:0000269|PubMed:16541025}. Chromosome, centromere
CC {ECO:0000269|PubMed:16541025}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:16541025}. Note=In prometaphase cells, but not in
CC anaphase cells, localizes at centromeres. During mitosis, also found at
CC spindle poles.
CC -!- PTM: Reversibly methyl esterified on Leu-309 by leucine carboxyl
CC methyltransferase 1 (LCMT1) and protein phosphatase methylesterase 1
CC (PPME1). Carboxyl methylation influences the affinity of the catalytic
CC subunit for the different regulatory subunits, thereby modulating the
CC PP2A holoenzyme's substrate specificity, enzyme activity and cellular
CC localization. {ECO:0000269|PubMed:8206937}.
CC -!- PTM: Phosphorylation of either threonine (by autophosphorylation-
CC activated protein kinase) or tyrosine results in inactivation of the
CC phosphatase. Auto-dephosphorylation has been suggested as a mechanism
CC for reactivation.
CC -!- PTM: May be monoubiquitinated by NOSIP. {ECO:0000250|UniProtKB:P62715}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; X12656; CAA31183.1; -; mRNA.
DR EMBL; CR541747; CAG46547.1; -; mRNA.
DR EMBL; J03805; AAB38020.1; -; mRNA.
DR EMBL; CH471080; EAW63434.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63435.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63436.1; -; Genomic_DNA.
DR EMBL; BC012022; AAH12022.1; -; mRNA.
DR EMBL; M60484; AAA36467.1; -; Genomic_DNA.
DR CCDS; CCDS6079.1; -.
DR PIR; B37135; PAHU2B.
DR RefSeq; NP_001009552.1; NM_001009552.1.
DR AlphaFoldDB; P62714; -.
DR SMR; P62714; -.
DR BioGRID; 111508; 206.
DR CORUM; P62714; -.
DR DIP; DIP-42325N; -.
DR IntAct; P62714; 161.
DR MINT; P62714; -.
DR STRING; 9606.ENSP00000221138; -.
DR ChEMBL; CHEMBL2435; -.
DR DrugBank; DB00163; Vitamin E.
DR DEPOD; PPP2CB; -.
DR iPTMnet; P62714; -.
DR MetOSite; P62714; -.
DR PhosphoSitePlus; P62714; -.
DR SwissPalm; P62714; -.
DR BioMuta; PPP2CB; -.
DR DMDM; 50402236; -.
DR OGP; P62714; -.
DR REPRODUCTION-2DPAGE; IPI00429689; -.
DR EPD; P62714; -.
DR jPOST; P62714; -.
DR MassIVE; P62714; -.
DR MaxQB; P62714; -.
DR PaxDb; P62714; -.
DR PeptideAtlas; P62714; -.
DR PRIDE; P62714; -.
DR ProteomicsDB; 57418; -.
DR Antibodypedia; 4349; 424 antibodies from 33 providers.
DR DNASU; 5516; -.
DR Ensembl; ENST00000221138.9; ENSP00000221138.4; ENSG00000104695.13.
DR GeneID; 5516; -.
DR KEGG; hsa:5516; -.
DR MANE-Select; ENST00000221138.9; ENSP00000221138.4; NM_001009552.2; NP_001009552.1.
DR UCSC; uc003xik.4; human.
DR CTD; 5516; -.
DR DisGeNET; 5516; -.
DR GeneCards; PPP2CB; -.
DR HGNC; HGNC:9300; PPP2CB.
DR HPA; ENSG00000104695; Low tissue specificity.
DR MIM; 176916; gene.
DR neXtProt; NX_P62714; -.
DR OpenTargets; ENSG00000104695; -.
DR PharmGKB; PA33664; -.
DR VEuPathDB; HostDB:ENSG00000104695; -.
DR eggNOG; KOG0371; Eukaryota.
DR GeneTree; ENSGT00550000074618; -.
DR HOGENOM; CLU_004962_0_5_1; -.
DR InParanoid; P62714; -.
DR OMA; DHINYAF; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; P62714; -.
DR TreeFam; TF105559; -.
DR PathwayCommons; P62714; -.
DR Reactome; R-HSA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-163685; Integration of energy metabolism.
DR Reactome; R-HSA-163767; PP2A-mediated dephosphorylation of key metabolic factors.
DR Reactome; R-HSA-180024; DARPP-32 events.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-HSA-198753; ERK/MAPK targets.
DR Reactome; R-HSA-202670; ERKs are inactivated.
DR Reactome; R-HSA-2465910; MASTL Facilitates Mitotic Progression.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
DR Reactome; R-HSA-432142; Platelet sensitization by LDL.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-HSA-5339716; Signaling by GSK3beta mutants.
DR Reactome; R-HSA-5358747; CTNNB1 S33 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358749; CTNNB1 S37 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358751; CTNNB1 S45 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358752; CTNNB1 T41 mutants aren't phosphorylated.
DR Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
DR Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
DR Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-5673000; RAF activation.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-HSA-9634600; Regulation of glycolysis by fructose 2,6-bisphosphate metabolism.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; P62714; -.
DR SIGNOR; P62714; -.
DR BioGRID-ORCS; 5516; 12 hits in 1085 CRISPR screens.
DR ChiTaRS; PPP2CB; human.
DR GeneWiki; PPP2CB; -.
DR GenomeRNAi; 5516; -.
DR Pharos; P62714; Tbio.
DR PRO; PR:P62714; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P62714; protein.
DR Bgee; ENSG00000104695; Expressed in pons and 208 other tissues.
DR ExpressionAtlas; P62714; baseline and differential.
DR Genevisible; P62714; HS.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; TAS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:ARUK-UCL.
DR GO; GO:0048156; F:tau protein binding; NAS:ARUK-UCL.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IGI:ARUK-UCL.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IGI:ARUK-UCL.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; TAS:ARUK-UCL.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; TAS:ARUK-UCL.
DR GO; GO:1904528; P:positive regulation of microtubule binding; ISS:ARUK-UCL.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0006470; P:protein dephosphorylation; TAS:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0010288; P:response to lead ion; ISS:ARUK-UCL.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Centromere; Chromosome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Hydrolase; Manganese; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Ubl conjugation.
FT CHAIN 1..309
FT /note="Serine/threonine-protein phosphatase 2A catalytic
FT subunit beta isoform"
FT /id="PRO_0000058845"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 307
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62715"
FT MOD_RES 309
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000269|PubMed:8206937"
FT MUTAGEN 59
FT /note="H->Q: Catalytically inactive. No effect on
FT interaction with PPME1."
FT /evidence="ECO:0000269|PubMed:10318862"
FT MUTAGEN 118
FT /note="H->Q: Catalytically inactive. No effect on
FT interaction with PPME1."
FT /evidence="ECO:0000269|PubMed:10318862"
FT CONFLICT 19
FT /note="E -> D (in Ref. 4; AAB38020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 35575 MW; 51DA9EB0633FC191 CRC64;
MDDKAFTKEL DQWVEQLNEC KQLNENQVRT LCEKAKEILT KESNVQEVRC PVTVCGDVHG
QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYPER ITILRGNHES
RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDTLDHI
RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA
HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV
TRRTPDYFL
