ID 2A5E_HUMAN Reviewed; 467 AA.
AC Q16537; A4FU37; B7ZKK8; Q52LW4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 01-MAY-2013, entry version 108.
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 449-455.
RC TISSUE=Fetal retina;
RX PubMed=8694763;
RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I.,
RA Merlevede W., Goris J., Hemmings B.A.;
RT "The variable subunit associated with protein phosphatase 2A0 defines
RT a novel multimember family of regulatory subunits.";
RL Biochem. J. 317:187-194(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RX PubMed=8703017; DOI=10.1074/jbc.271.36.22081;
RA McCright B., Rivers A.M., Audlin S., Virshup D.M.;
RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
RT encodes differentiation-induced phosphoproteins that target PP2A to
RT both nucleus and cytoplasm.";
RL J. Biol. Chem. 271:22081-22089(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH SGOL1.
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
RT cohesin.";
RL Nature 441:46-52(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32 AND SER-34,
RP AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: The B regulatory subunit might modulate substrate
CC selectivity and catalytic activity, and also might direct the
CC localization of the catalytic enzyme to a particular subcellular
CC compartment.
CC -!- SUBUNIT: Found in a complex with at least ARL2, PPP2CB; PPP2R1A,
CC PPP2R2A, PPP2R5E and TBCD (By similarity). PP2A consists of a
CC common heterodimeric core enzyme, composed of a 36 kDa catalytic
CC subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65
CC or subunit A), that associates with a variety of regulatory
CC subunits. Proteins that associate with the core dimer include
CC 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
CC variable regulatory subunit, viral proteins, and cell signaling
CC molecules. Interacts with SGOL1.
CC -!- INTERACTION:
CC O96017:CHEK2; NbExp=3; IntAct=EBI-968374, EBI-1180783;
CC P30153:PPP2R1A; NbExp=3; IntAct=EBI-968374, EBI-302388;
CC P30154:PPP2R1B; NbExp=3; IntAct=EBI-968374, EBI-357094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated on serine residues.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family.
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DR EMBL; Z69029; CAA93153.1; -; mRNA.
DR EMBL; L76703; AAB69752.1; -; mRNA.
DR EMBL; BC093766; AAH93766.1; -; mRNA.
DR EMBL; BC101479; AAI01480.1; -; mRNA.
DR EMBL; BC143231; AAI43232.1; -; mRNA.
DR IPI; IPI00002853; -.
DR RefSeq; NP_006237.1; NM_006246.2.
DR UniGene; Hs.334868; -.
DR ProteinModelPortal; Q16537; -.
DR IntAct; Q16537; 25.
DR MINT; MINT-1198703; -.
DR STRING; 9606.ENSP00000337641; -.
DR PhosphoSite; Q16537; -.
DR DMDM; 7387498; -.
DR PaxDb; Q16537; -.
DR PRIDE; Q16537; -.
DR DNASU; 5529; -.
DR Ensembl; ENST00000337537; ENSP00000337641; ENSG00000154001.
DR GeneID; 5529; -.
DR KEGG; hsa:5529; -.
DR UCSC; uc001xgd.1; human.
DR CTD; 5529; -.
DR GeneCards; GC14M063838; -.
DR HGNC; HGNC:9313; PPP2R5E.
DR HPA; HPA006034; -.
DR MIM; 601647; gene.
DR neXtProt; NX_Q16537; -.
DR PharmGKB; PA33677; -.
DR eggNOG; NOG264925; -.
DR HOGENOM; HOG000067326; -.
DR HOVERGEN; HBG000009; -.
DR InParanoid; Q16537; -.
DR KO; K11584; -.
DR OMA; VSRGYLT; -.
DR OrthoDB; EOG483D4M; -.
DR PhylomeDB; Q16537; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; PPP2R5E; human.
DR GenomeRNAi; 5529; -.
DR NextBio; 21418; -.
DR ArrayExpress; Q16537; -.
DR Bgee; Q16537; -.
DR CleanEx; HS_PPP2R5E; -.
DR Genevestigator; Q16537; -.
DR GermOnline; ENSG00000154001; Homo sapiens.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; ARM-type_fold; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 467 Serine/threonine-protein phosphatase 2A
FT 56 kDa regulatory subunit epsilon
FT isoform.
FT /FTId=PRO_0000071454.
FT MOD_RES 30 30 Phosphoserine.
FT MOD_RES 32 32 Phosphoserine.
FT MOD_RES 34 34 Phosphoserine.
SQ SEQUENCE 467 AA; 54699 MW; DD9CE11433F499CF CRC64;
MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL LKDVPSSEQP
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
//
