2A5E_MOUSE
ID 2A5E_MOUSE Reviewed; 467 AA.
AC Q61151; Q3V1I5; Q571M6; Q8C2M2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform;
DE AltName: Full=PP2A B subunit isoform B'-epsilon;
DE AltName: Full=PP2A B subunit isoform B56-epsilon;
DE AltName: Full=PP2A B subunit isoform PR61-epsilon;
DE AltName: Full=PP2A B subunit isoform R5-epsilon;
GN Name=Ppp2r5e; Synonyms=Kiaa4006;
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, and NOD; TISSUE=Skin, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-436.
RC TISSUE=Embryonic tail;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 51-437.
RC TISSUE=Embryonic fibroblast;
RX PubMed=8887688; DOI=10.1128/mcb.16.11.6593;
RA Okamoto K., Kamibayashi C., Serrano M., Prives C., Mumby M.C., Beach D.;
RT "p53-dependent association between cyclin G and the B' subunit of protein
RT phosphatase 2A.";
RL Mol. Cell. Biol. 16:6593-6602(1996).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
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. Interacts
CC with cyclin G in vitro.
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. Found in a complex with at least ARL2, PPP2CB;
CC PPP2R1A, PPP2R2A, PPP2R5E and TBCD (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB37234.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD90335.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK088366; BAC40306.1; -; mRNA.
DR EMBL; AK132432; BAE21166.1; -; mRNA.
DR EMBL; BC085149; AAH85149.1; -; mRNA.
DR EMBL; AK220163; BAD90335.1; ALT_INIT; mRNA.
DR EMBL; U49728; AAB37234.1; ALT_FRAME; mRNA.
DR CCDS; CCDS25983.1; -.
DR RefSeq; NP_036154.1; NM_012024.2.
DR RefSeq; XP_006515988.1; XM_006515925.2.
DR AlphaFoldDB; Q61151; -.
DR SMR; Q61151; -.
DR BioGRID; 205071; 8.
DR IntAct; Q61151; 2.
DR MINT; Q61151; -.
DR STRING; 10090.ENSMUSP00000021447; -.
DR iPTMnet; Q61151; -.
DR PhosphoSitePlus; Q61151; -.
DR EPD; Q61151; -.
DR MaxQB; Q61151; -.
DR PaxDb; Q61151; -.
DR PeptideAtlas; Q61151; -.
DR PRIDE; Q61151; -.
DR ProteomicsDB; 285888; -.
DR Antibodypedia; 50; 157 antibodies from 34 providers.
DR DNASU; 26932; -.
DR Ensembl; ENSMUST00000021447; ENSMUSP00000021447; ENSMUSG00000021051.
DR GeneID; 26932; -.
DR KEGG; mmu:26932; -.
DR UCSC; uc007nxe.1; mouse.
DR CTD; 5529; -.
DR MGI; MGI:1349473; Ppp2r5e.
DR VEuPathDB; HostDB:ENSMUSG00000021051; -.
DR eggNOG; KOG2085; Eukaryota.
DR GeneTree; ENSGT01030000234620; -.
DR HOGENOM; CLU_012437_4_0_1; -.
DR InParanoid; Q61151; -.
DR OMA; GADNNCK; -.
DR OrthoDB; 890437at2759; -.
DR PhylomeDB; Q61151; -.
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; 26932; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Ppp2r5e; mouse.
DR PRO; PR:Q61151; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q61151; protein.
DR Bgee; ENSMUSG00000021051; Expressed in rostral migratory stream and 225 other tissues.
DR ExpressionAtlas; Q61151; baseline and differential.
DR Genevisible; Q61151; MM.
DR GO; GO:0005737; C:cytoplasm; TAS:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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; Cytoplasm; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16537"
FT CHAIN 2..467
FT /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT regulatory subunit epsilon isoform"
FT /id="PRO_0000071455"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q16537"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16537"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16537"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16537"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16537"
FT CONFLICT 74
FT /note="F -> C (in Ref. 4; AAB37234)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="L -> W (in Ref. 4; AAB37234)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="F -> S (in Ref. 4; AAB37234)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="N -> T (in Ref. 4; AAB37234)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 54713 MW; 77DA129F9A4EC6AC CRC64;
MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL LKDVPTSEQP
ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI TISRGCLTEQ TYPEVVRMVS
CNIFRTLPPS DSNEFDPEED EPTLEASWPH LQLVYEFFIR FLESQEFQPS IAKKYIDQKF
VLQLLELFDS EDPRERDYLK TVLHRIYGKF LGLRAFIRKQ INNIFLRFVY ETEHFNGVAE
LLEILGSIIN GFALPLKAEH KQFLVKVLIP LHTVRSLSLF HAQLAYCIVQ FLEKDPSLTE
PVIRGLMKFW PKTCSQKEVM FLGELEEILD VIEPSQFVKI QEPLFKQIAK CVSSPHFQVA
ERALYYWNNE YIMSLIEENS NVILPIMFSS LYRISKEHWN PAIVALVYNV LKAFMEMNST
MFDELTATYK SDRQREKKKE KEREELWKKL EDLELKRGLR RDGIIPT
