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Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform (PP2A B subunit isoform B'-epsilon) (PP2A B subunit isoform B56-epsilon) (PP2A B subunit isoform PR61-epsilon) (PP2A B subunit isoform R5-epsilon)

 2A5E_HUMAN              Reviewed;         467 AA.
Q16537; A4FU37; B7ZAW5; B7ZKK8; B7ZKK9; J3KQN6; Q52LW4;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
20-JUN-2018, entry version 154.
RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform;
AltName: Full=PP2A B subunit isoform B'-epsilon;
AltName: Full=PP2A B subunit isoform B56-epsilon;
AltName: Full=PP2A B subunit isoform PR61-epsilon;
AltName: Full=PP2A B subunit isoform R5-epsilon;
Name=PPP2R5E;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF
449-455.
TISSUE=Fetal retina;
PubMed=8694763; DOI=10.1042/bj3170187;
Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I.,
Merlevede W., Goris J., Hemmings B.A.;
"The variable subunit associated with protein phosphatase 2A0 defines
a novel multimember family of regulatory subunits.";
Biochem. J. 317:187-194(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=8703017; DOI=10.1074/jbc.271.36.22081;
McCright B., Rivers A.M., Audlin S., Virshup D.M.;
"The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
encodes differentiation-induced phosphoproteins that target PP2A to
both nucleus and cytoplasm.";
J. Biol. Chem. 271:22081-22089(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH SGO1.
PubMed=16541025; DOI=10.1038/nature04663;
Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
Kawashima S.A., Watanabe Y.;
"Shugoshin collaborates with protein phosphatase 2A to protect
cohesin.";
Nature 441:46-52(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-32 AND SER-34,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: The B regulatory subunit might modulate substrate
selectivity and catalytic activity, and also might direct the
localization of the catalytic enzyme to a particular subcellular
compartment.
-!- SUBUNIT: Found in a complex with at least ARL2, PPP2CB; PPP2R1A,
PPP2R2A, PPP2R5E and 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
or 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. Interacts with SGO1. {ECO:0000250,
ECO:0000269|PubMed:16541025}.
-!- INTERACTION:
O96017:CHEK2; NbExp=3; IntAct=EBI-968374, EBI-1180783;
Q86YF9:DZIP1; NbExp=3; IntAct=EBI-968374, EBI-998108;
Q9HC29:NOD2; NbExp=2; IntAct=EBI-968374, EBI-7445625;
P30153:PPP2R1A; NbExp=7; IntAct=EBI-968374, EBI-302388;
P30154:PPP2R1B; NbExp=3; IntAct=EBI-968374, EBI-357094;
Q9H0H5:RACGAP1; NbExp=5; IntAct=EBI-968374, EBI-717233;
Q8IUH5:ZDHHC17; NbExp=2; IntAct=EBI-968374, EBI-524753;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q16537-1; Sequence=Displayed;
Name=2;
IsoId=Q16537-2; Sequence=VSP_054588;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q16537-3; Sequence=VSP_055163;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylated on serine residues.
-!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z69029; CAA93153.1; -; mRNA.
EMBL; L76703; AAB69752.1; -; mRNA.
EMBL; AK316430; BAH14801.1; -; mRNA.
EMBL; AL118555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL132992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL136038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC093766; AAH93766.1; -; mRNA.
EMBL; BC101479; AAI01480.1; -; mRNA.
EMBL; BC143231; AAI43232.1; -; mRNA.
EMBL; BC143234; AAI43235.1; -; mRNA.
CCDS; CCDS61467.1; -. [Q16537-3]
CCDS; CCDS61468.1; -. [Q16537-2]
CCDS; CCDS9758.1; -. [Q16537-1]
RefSeq; NP_001269108.1; NM_001282179.1. [Q16537-1]
RefSeq; NP_001269109.1; NM_001282180.1. [Q16537-2]
RefSeq; NP_001269110.1; NM_001282181.1. [Q16537-3]
RefSeq; NP_001269111.1; NM_001282182.1. [Q16537-3]
RefSeq; NP_006237.1; NM_006246.3. [Q16537-1]
UniGene; Hs.334868; -.
UniGene; Hs.594347; -.
ProteinModelPortal; Q16537; -.
BioGrid; 111521; 72.
ELM; Q16537; -.
IntAct; Q16537; 37.
MINT; Q16537; -.
STRING; 9606.ENSP00000337641; -.
iPTMnet; Q16537; -.
PhosphoSitePlus; Q16537; -.
DMDM; 7387498; -.
EPD; Q16537; -.
MaxQB; Q16537; -.
PaxDb; Q16537; -.
PeptideAtlas; Q16537; -.
PRIDE; Q16537; -.
DNASU; 5529; -.
Ensembl; ENST00000337537; ENSP00000337641; ENSG00000154001. [Q16537-1]
Ensembl; ENST00000422769; ENSP00000404632; ENSG00000154001. [Q16537-3]
Ensembl; ENST00000555899; ENSP00000452396; ENSG00000154001. [Q16537-2]
GeneID; 5529; -.
KEGG; hsa:5529; -.
UCSC; uc001xgd.3; human. [Q16537-1]
CTD; 5529; -.
DisGeNET; 5529; -.
EuPathDB; HostDB:ENSG00000154001.13; -.
GeneCards; PPP2R5E; -.
HGNC; HGNC:9313; PPP2R5E.
HPA; CAB072342; -.
HPA; HPA006034; -.
MIM; 601647; gene.
neXtProt; NX_Q16537; -.
OpenTargets; ENSG00000154001; -.
PharmGKB; PA33677; -.
eggNOG; KOG2085; Eukaryota.
eggNOG; ENOG410XQJW; LUCA.
GeneTree; ENSGT00550000074525; -.
HOGENOM; HOG000067326; -.
HOVERGEN; HBG000009; -.
InParanoid; Q16537; -.
KO; K11584; -.
OMA; CCTVFDF; -.
OrthoDB; EOG091G06HU; -.
PhylomeDB; Q16537; -.
TreeFam; TF105556; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
Reactome; R-HSA-432142; Platelet sensitization by LDL.
Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-HSA-5339716; Misspliced GSK3beta mutants stabilize beta-catenin.
Reactome; R-HSA-5358747; S33 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358749; S37 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358751; S45 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358752; T41 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-5673000; RAF activation.
Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SignaLink; Q16537; -.
ChiTaRS; PPP2R5E; human.
GeneWiki; PPP2R5E; -.
GenomeRNAi; 5529; -.
PRO; PR:Q16537; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000154001; -.
CleanEx; HS_PPP2R5E; -.
Genevisible; Q16537; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
GO; GO:0019888; F:protein phosphatase regulator activity; TAS:ProtInc.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002554; PP2A_B56.
PANTHER; PTHR10257; PTHR10257; 1.
Pfam; PF01603; B56; 1.
PIRSF; PIRSF028043; PP2A_B56; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 467 Serine/threonine-protein phosphatase 2A
56 kDa regulatory subunit epsilon
isoform.
/FTId=PRO_0000071454.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 7 7 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 32 32 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
VAR_SEQ 1 76 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055163.
VAR_SEQ 430 435 KSDRQR -> N (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054588.
CONFLICT 194 194 R -> W (in Ref. 3; BAH14801).
{ECO:0000305}.
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


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