2ABA_PIG
ID 2ABA_PIG Reviewed; 426 AA.
AC Q29090;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform;
DE AltName: Full=PP2A subunit B isoform B55-alpha;
DE AltName: Full=PP2A subunit B isoform PR55-alpha;
DE AltName: Full=PP2A subunit B isoform R2-alpha;
DE AltName: Full=PP2A subunit B isoform alpha;
DE Flags: Fragment;
GN Name=PPP2R2A;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mayer-Jaekel R.E.;
RL Thesis (1992), Friedrich Miescher Institut / Basel, Switzerland.
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. Essential for
CC serine/threonine-protein phosphatase 2A-mediated dephosphorylation of
CC WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1
CC protein levels, and promoting the G2/M checkpoint.
CC {ECO:0000250|UniProtKB:P63151}.
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 (By
CC similarity). Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
CC PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with TP53 (By
CC similarity). Interacts with IER5 (By similarity). Interacts with
CC MFHAS1; the interaction is direct (By similarity). Interacts with
CC PABIR1/FAM122A (By similarity). Interacts with CRTC3 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P63151,
CC ECO:0000250|UniProtKB:Q6P1F6}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC {ECO:0000305}.
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DR EMBL; Z34932; CAA84404.1; -; mRNA.
DR AlphaFoldDB; Q29090; -.
DR SMR; Q29090; -.
DR STRING; 9823.ENSSSCP00000010312; -.
DR PaxDb; Q29090; -.
DR PeptideAtlas; Q29090; -.
DR PRIDE; Q29090; -.
DR eggNOG; KOG1354; Eukaryota.
DR HOGENOM; CLU_021713_3_3_1; -.
DR InParanoid; Q29090; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q29090; SS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR000009; PP2A_PR55.
DR InterPro; IPR018067; PP2A_PR55_CS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11871; PTHR11871; 1.
DR PIRSF; PIRSF037309; PP2A_PR55; 1.
DR PRINTS; PR00600; PP2APR55.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS01024; PR55_1; 1.
DR PROSITE; PS01025; PR55_2; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN <1..426
FT /note="Serine/threonine-protein phosphatase 2A 55 kDa
FT regulatory subunit B alpha isoform"
FT /id="PRO_0000071418"
FT REPEAT 5..44
FT /note="WD 1"
FT REPEAT 70..111
FT /note="WD 2"
FT REPEAT 154..192
FT /note="WD 3"
FT REPEAT 203..243
FT /note="WD 4"
FT REPEAT 262..300
FT /note="WD 5"
FT REPEAT 317..358
FT /note="WD 6"
FT REPEAT 393..425
FT /note="WD 7"
FT NON_TER 1
SQ SEQUENCE 426 AA; 49614 MW; 3AAD7EB338B03534 CRC64;
DDDVAEADII STVEFNHSGE LLATGDKGGR VVIFQQEQEN KIQSHSRGEY NVYSTFQSHE
PEFDYLKSLE IEEKINKIRW LPQKNAAQFL LSTNDKTIKL WKISERDKRP EGYNLKEEDG
RYRDPTTVTT LRVPVFRPMD LMVEASPRRI FANAHTYHIN SISINSDYET YLSADDLRIN
LWHLEITDRS FNIVDIKPAN MEELTEVITA AEFHPNSCNT FVYSSSKGTI RLCDMRASAL
CDRHSKLFEE PEDPSNRSFF SEIISSISDV KFSHSGRYMM TRDYLSVKIW DLNMENRPVE
TYQVHEYLRS KLCSLYENDC IFDKFECCWN GSDSVVMTGS YNNFFRMFDR NTKRDITLEA
SRENNKPRTV LKPRKVCASG KRKKDEISVD SLDFNKKILH TAWHPKENII AVATTNNLYI
FQDKVN