2A5A_MOUSE
ID 2A5A_MOUSE Reviewed; 486 AA.
AC Q6PD03; Q8R1U7;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform;
DE AltName: Full=PP2A B subunit isoform B'-alpha;
DE AltName: Full=PP2A B subunit isoform B56-alpha;
DE AltName: Full=PP2A B subunit isoform PR61-alpha;
DE Short=PR61alpha;
DE AltName: Full=PP2A B subunit isoform R5-alpha;
GN Name=Ppp2r5a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain, and Retina;
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 [2]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=15095873; DOI=10.1016/j.jmb.2003.12.047;
RA Martens E., Stevens I., Janssens V., Vermeesch J., Goetz J., Goris J.,
RA Van Hoof C.;
RT "Genomic organisation, chromosomal localisation tissue distribution and
RT developmental regulation of the PR61/B' regulatory subunits of protein
RT phosphatase 2A in mice.";
RL J. Mol. Biol. 336:971-986(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: The B regulatory subunit might modulate substrate selectivity
CC and catalytic activity, and also might direct the localization of the
CC catalytic enzyme to a particular subcellular compartment.
CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant
CC regulatory subunit (PR65 or subunit A), that associates with a variety
CC of regulatory subunits. Proteins that associate with the core dimer
CC include three 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.
CC Interacts with SGO1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Chromosome, centromere {ECO:0000250}. Note=From mitotic prophase to
CC metaphase, localizes at the inner centromere between a pair of sister
CC kinetochores. Decreased expression at the onset of anaphase (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in thymus and
CC ovary. {ECO:0000269|PubMed:15095873}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23062.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC023062; AAH23062.1; ALT_INIT; mRNA.
DR EMBL; BC059026; AAH59026.1; -; mRNA.
DR EMBL; BK000647; DAA01426.1; -; mRNA.
DR CCDS; CCDS15620.1; -.
DR RefSeq; NP_659129.2; NM_144880.4.
DR AlphaFoldDB; Q6PD03; -.
DR SMR; Q6PD03; -.
DR BioGRID; 230562; 12.
DR IntAct; Q6PD03; 1.
DR MINT; Q6PD03; -.
DR STRING; 10090.ENSMUSP00000070726; -.
DR iPTMnet; Q6PD03; -.
DR PhosphoSitePlus; Q6PD03; -.
DR EPD; Q6PD03; -.
DR jPOST; Q6PD03; -.
DR MaxQB; Q6PD03; -.
DR PaxDb; Q6PD03; -.
DR PRIDE; Q6PD03; -.
DR ProteomicsDB; 296442; -.
DR Antibodypedia; 34606; 268 antibodies from 37 providers.
DR DNASU; 226849; -.
DR Ensembl; ENSMUST00000067976; ENSMUSP00000070726; ENSMUSG00000026626.
DR GeneID; 226849; -.
DR KEGG; mmu:226849; -.
DR UCSC; uc007eci.1; mouse.
DR CTD; 5525; -.
DR MGI; MGI:2388479; Ppp2r5a.
DR VEuPathDB; HostDB:ENSMUSG00000026626; -.
DR eggNOG; KOG2085; Eukaryota.
DR GeneTree; ENSGT01030000234620; -.
DR HOGENOM; CLU_012437_4_0_1; -.
DR InParanoid; Q6PD03; -.
DR OMA; NHEDQER; -.
DR OrthoDB; 890437at2759; -.
DR PhylomeDB; Q6PD03; -.
DR TreeFam; TF105556; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
DR Reactome; R-MMU-432142; Platelet sensitization by LDL.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-5673000; RAF activation.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 226849; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ppp2r5a; mouse.
DR PRO; PR:Q6PD03; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q6PD03; protein.
DR Bgee; ENSMUSG00000026626; Expressed in granulocyte and 119 other tissues.
DR ExpressionAtlas; Q6PD03; baseline and differential.
DR Genevisible; Q6PD03; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031430; C:M band; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0090219; P:negative regulation of lipid kinase activity; ISO:MGI.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002554; PP2A_B56.
DR PANTHER; PTHR10257; PTHR10257; 1.
DR Pfam; PF01603; B56; 1.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Centromere; Chromosome; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15172"
FT CHAIN 2..486
FT /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT regulatory subunit alpha isoform"
FT /id="PRO_0000071449"
FT REGION 22..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q15172"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15172"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15172"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15172"
SQ SEQUENCE 486 AA; 56347 MW; BC9B0B80446C1AD2 CRC64;
MSSPSPPAPV ACAAISASEK VDGFTRKSVR KAQRQKRSQG SSQFRSQGSQ AELHPLPQLK
DATSNEQQEL FCQKLQQCCV LFDFMDSVSD LKSKEIKRAT LNELVEYVST NRGVIVESAY
SDIVKMISAN IFRTLPPSDN PDFDPEEDEP TLEASWPHIQ LVYEFFLRFL ESPDFQPSIA
KRYIDQKFVQ QLLELFDSED PRERDFLKTV LHRIYGKFLG LRAFIRKQIN NIFLRFIYET
EHFNGVAELL EILGSIINGF ALPLKAEHKQ FLMKVLIPMH TAKGLALFHA QLAYCVVQFL
EKDTTLTEPV IRGLLKFWPK TCSQKEVMFL GEIEEILDVI EPTQFKKIEE PLFKQISKCV
SSSHFQVAER ALYFWNNEYI LSLIEENIDK ILPIMFASLY KISKEHWNQT IVALVYNVLK
TLMEMNGKLF DDLTSSYKAE RQREKKKELE REELWKKLEE LQLKKALEKQ NNAYNMHSIR
SSTSAK
