2A5E_RABIT
ID 2A5E_RABIT Reviewed; 165 AA.
AC Q28654;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform;
DE AltName: Full=PP2A B subunit isoform B'-delta;
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;
DE Flags: Fragment;
GN Name=PPP2R5E;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand; TISSUE=Brain;
RX PubMed=8576224; DOI=10.1074/jbc.271.5.2578;
RA Csortos C., Zolnierowicz S., Bako E., Durbin S.D., Depaoli-Roach A.A.;
RT "High complexity in the expression of the B' subunit of protein phosphatase
RT 2A0. Evidence for the existence of at least seven novel isoforms.";
RL J. Biol. Chem. 271:2578-2588(1996).
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. 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 -!- TISSUE SPECIFICITY: Highly expressed in testis, lung and brain.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
CC -!- CAUTION: Nomenclature used in PubMed:8576224 refers to PP2A B subunit
CC B' delta isoform, which is cited as PP2A B subunit epsilon-PR61 isoform
CC in later publications. {ECO:0000305}.
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DR EMBL; U38194; AAC48533.1; -; mRNA.
DR AlphaFoldDB; Q28654; -.
DR SMR; Q28654; -.
DR STRING; 9986.ENSOCUP00000003063; -.
DR eggNOG; KOG2085; Eukaryota.
DR InParanoid; Q28654; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:InterPro.
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 SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16537"
FT CHAIN 2..>165
FT /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT regulatory subunit epsilon isoform"
FT /id="PRO_0000071456"
FT REGION 1..41
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 NON_TER 165
SQ SEQUENCE 165 AA; 19048 MW; 6F4A6E32D0D85B7D CRC64;
MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL LKDVPSSEQP
ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI TISRGCLTEQ TYPEVVRMVS
CNIFRTLPPS DSNEFDPEED EPTLEASWPH LQLVYEFFIR FLESQ