2ABB_MACFA
ID 2ABB_MACFA Reviewed; 443 AA.
AC Q4R8L3; Q60HB9; Q95LX5;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform;
DE AltName: Full=PP2A subunit B isoform B55-beta;
DE AltName: Full=PP2A subunit B isoform PR55-beta;
DE AltName: Full=PP2A subunit B isoform R2-beta;
DE AltName: Full=PP2A subunit B isoform beta;
GN Name=PPP2R2B; ORFNames=QtrA-17824, QtsA-12205, QtsA-16107;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Temporal cortex;
RA Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
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). Interacts with TOMM22 (By similarity). Interacts with IER5
CC (via N- and C-terminal regions) (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P36877, ECO:0000250|UniProtKB:Q00005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Membrane {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q4R8L3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4R8L3-2; Sequence=VSP_037980;
CC Name=3;
CC IsoId=Q4R8L3-3; Sequence=VSP_037981;
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC {ECO:0000305}.
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DR EMBL; AB071066; BAB64459.1; -; mRNA.
DR EMBL; AB125208; BAD51996.1; -; mRNA.
DR EMBL; AB168439; BAE00559.1; -; mRNA.
DR RefSeq; XP_005558212.1; XM_005558155.2. [Q4R8L3-1]
DR RefSeq; XP_005558213.1; XM_005558156.2. [Q4R8L3-1]
DR RefSeq; XP_005558214.1; XM_005558157.2. [Q4R8L3-2]
DR RefSeq; XP_005558215.1; XM_005558158.2. [Q4R8L3-2]
DR RefSeq; XP_005558216.1; XM_005558159.1. [Q4R8L3-2]
DR RefSeq; XP_015307573.1; XM_015452087.1. [Q4R8L3-2]
DR RefSeq; XP_015307574.1; XM_015452088.1. [Q4R8L3-2]
DR RefSeq; XP_015307575.1; XM_015452089.1. [Q4R8L3-2]
DR RefSeq; XP_015307576.1; XM_015452090.1. [Q4R8L3-2]
DR RefSeq; XP_015307578.1; XM_015452092.1. [Q4R8L3-2]
DR RefSeq; XP_015307579.1; XM_015452093.1. [Q4R8L3-2]
DR AlphaFoldDB; Q4R8L3; -.
DR SMR; Q4R8L3; -.
DR STRING; 9541.XP_005558205.1; -.
DR Ensembl; ENSMFAT00000024953; ENSMFAP00000006269; ENSMFAG00000002611. [Q4R8L3-1]
DR Ensembl; ENSMFAT00000024959; ENSMFAP00000006275; ENSMFAG00000002611. [Q4R8L3-3]
DR GeneID; 102125257; -.
DR KEGG; mcf:102125257; -.
DR CTD; 5521; -.
DR VEuPathDB; HostDB:ENSMFAG00000002611; -.
DR eggNOG; KOG1354; Eukaryota.
DR GeneTree; ENSGT00950000182864; -.
DR Proteomes; UP000233100; Chromosome 6.
DR Bgee; ENSMFAG00000002611; Expressed in frontal cortex and 10 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; 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 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; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS01024; PR55_1; 1.
DR PROSITE; PS01025; PR55_2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..443
FT /note="Serine/threonine-protein phosphatase 2A 55 kDa
FT regulatory subunit B beta isoform"
FT /id="PRO_0000071422"
FT REPEAT 22..61
FT /note="WD 1"
FT REPEAT 87..128
FT /note="WD 2"
FT REPEAT 171..209
FT /note="WD 3"
FT REPEAT 220..260
FT /note="WD 4"
FT REPEAT 279..317
FT /note="WD 5"
FT REPEAT 334..375
FT /note="WD 6"
FT REPEAT 410..442
FT /note="WD 7"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36877"
FT MOD_RES 295
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P36877"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36877"
FT VAR_SEQ 1..24
FT /note="MEEDIDTRKINNSFLRDHSYATEA -> MNYPDENTYGNKA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12498619"
FT /id="VSP_037980"
FT VAR_SEQ 1
FT /note="M -> MLLSLPALHLQTSEHHPFFQLPHGRLGPWCSPTGSPAPLSCETGCGE
FT GSWILVCRLLVPTQVSLLSM (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_037981"
FT CONFLICT 184
FT /note="D -> N (in Ref. 2; BAD51996)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="L -> F (in Ref. 2; BAD51996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 51710 MW; C383C834B2852B8F CRC64;
MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI FQREQESKNQ
VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV
SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS
VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY
SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD
YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN
FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW
HPSENIIAVA ATNNLYIFQD KVN
