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

 2A5B_HUMAN              Reviewed;         497 AA.
Q15173; Q13853;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 168.
RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform;
AltName: Full=PP2A B subunit isoform B'-beta;
AltName: Full=PP2A B subunit isoform B56-beta;
AltName: Full=PP2A B subunit isoform PR61-beta;
AltName: Full=PP2A B subunit isoform R5-beta;
Name=PPP2R5B;
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 BETA-1).
TISSUE=Fetal brain;
PubMed=7592815; DOI=10.1074/jbc.270.44.26123;
McCright B., Virshup D.M.;
"Identification of a new family of protein phosphatase 2A regulatory
subunits.";
J. Biol. Chem. 270:26123-26128(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2), AND PARTIAL PROTEIN
SEQUENCE.
TISSUE=Brain;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1).
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).
[4]
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
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).
[5]
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).
[6]
FUNCTION, PHOSPHORYLATION AT SER-32; SER-35; SER-44; SER-46; SER-47
AND SER-48, AND INTERACTION WITH AKT1.
PubMed=21329884; DOI=10.1016/j.molcel.2011.02.007;
Rodgers J.T., Vogel R.O., Puigserver P.;
"Clk2 and B56-beta mediate insulin-regulated assembly of the PP2A
phosphatase holoenzyme complex on Akt.";
Mol. Cell 41:471-479(2011).
[7]
INTERACTION WITH CUL3 AND KLHL15, IDENTIFICATION IN PP2A COMPLEX,
UBIQUITINATION, AND MUTAGENESIS OF TYR-52; 103-LYS-ARG-104 AND
232-ARG-LYS-233.
PubMed=23135275; DOI=10.1074/jbc.M112.420281;
Oberg E.A., Nifoussi S.K., Gingras A.C., Strack S.;
"Selective proteasomal degradation of the B'beta subunit of protein
phosphatase 2A by the E3 ubiquitin ligase adaptor Kelch-like 15.";
J. Biol. Chem. 287:43378-43389(2012).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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: As the regulatory component of the serine/threonine-
protein phosphatase 2A (PP2A) holoenzyme, modulates substrate
specificity, subcellular localization, and responsiveness to
phosphorylation. The phosphorylated form mediates the interaction
between PP2A and AKT1, leading to AKT1 dephosphorylation.
{ECO:0000269|PubMed:21329884}.
-!- SUBUNIT: Component of the serine/threonine-protein phosphatase 2A
complex (PP2A). This complex consists of a common heterodimeric
core enzyme, composed of a 36 kDa catalytic subunit (subunit C)
and a 65 kDa constant scaffold 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 (PubMed:23135275).
Interacts with SGO1 (PubMed:16541025). Interacts with AKT1
(PubMed:21329884). Interacts with CUL3 and KLHL15; this
interaction leads to proteasomal degradation (PubMed:23135275).
{ECO:0000269|PubMed:16541025, ECO:0000269|PubMed:21329884,
ECO:0000269|PubMed:23135275}.
-!- INTERACTION:
O96017:CHEK2; NbExp=2; IntAct=EBI-1369497, EBI-1180783;
P46695:IER3; NbExp=4; IntAct=EBI-1369497, EBI-1748945;
P67775:PPP2CA; NbExp=5; IntAct=EBI-1369497, EBI-712311;
P30153:PPP2R1A; NbExp=3; IntAct=EBI-1369497, EBI-302388;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8703017}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Beta-1;
IsoId=Q15173-1; Sequence=Displayed;
Name=Beta-2;
IsoId=Q15173-2; Sequence=VSP_005109;
-!- TISSUE SPECIFICITY: Highest expression in brain.
-!- INDUCTION: By retinoic acid; in neuroblastoma cell lines.
-!- PTM: Ubiquitinated by E3 CUL3-KLHL15 complex; this modification
leads to proteasomal degradation. {ECO:0000269|PubMed:23135275}.
-!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L42374; AAC37602.1; -; mRNA.
EMBL; Z69028; CAA93152.1; -; mRNA.
EMBL; BC045619; AAH45619.1; -; mRNA.
CCDS; CCDS8085.1; -. [Q15173-1]
PIR; I70147; I70147.
RefSeq; NP_006235.1; NM_006244.3. [Q15173-1]
UniGene; Hs.75199; -.
ProteinModelPortal; Q15173; -.
SMR; Q15173; -.
BioGrid; 111518; 14.
ELM; Q15173; -.
IntAct; Q15173; 9.
MINT; Q15173; -.
STRING; 9606.ENSP00000164133; -.
iPTMnet; Q15173; -.
PhosphoSitePlus; Q15173; -.
BioMuta; PPP2R5B; -.
DMDM; 7387497; -.
EPD; Q15173; -.
MaxQB; Q15173; -.
PaxDb; Q15173; -.
PeptideAtlas; Q15173; -.
PRIDE; Q15173; -.
TopDownProteomics; Q15173-1; -. [Q15173-1]
DNASU; 5526; -.
Ensembl; ENST00000164133; ENSP00000164133; ENSG00000068971. [Q15173-1]
GeneID; 5526; -.
KEGG; hsa:5526; -.
UCSC; uc001oby.4; human. [Q15173-1]
CTD; 5526; -.
DisGeNET; 5526; -.
EuPathDB; HostDB:ENSG00000068971.13; -.
GeneCards; PPP2R5B; -.
HGNC; HGNC:9310; PPP2R5B.
HPA; HPA036607; -.
MIM; 601644; gene.
neXtProt; NX_Q15173; -.
OpenTargets; ENSG00000068971; -.
PharmGKB; PA33673; -.
eggNOG; KOG2085; Eukaryota.
eggNOG; ENOG410XQJW; LUCA.
GeneTree; ENSGT00550000074525; -.
HOGENOM; HOG000067326; -.
HOVERGEN; HBG000009; -.
InParanoid; Q15173; -.
KO; K11584; -.
OMA; FIYEFEH; -.
OrthoDB; EOG091G06HU; -.
PhylomeDB; Q15173; -.
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-381038; XBP1(S) activates chaperone genes.
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; Q15173; -.
SIGNOR; Q15173; -.
ChiTaRS; PPP2R5B; human.
GeneWiki; PPP2R5B; -.
GenomeRNAi; 5526; -.
PRO; PR:Q15173; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000068971; -.
CleanEx; HS_PPP2R5B; -.
ExpressionAtlas; Q15173; baseline and differential.
Genevisible; Q15173; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
GO; GO:0019888; F:protein phosphatase regulator activity; TAS:ProtInc.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; IEA:Ensembl.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
GO; GO:0031334; P:positive regulation of protein complex assembly; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0031952; P:regulation of protein autophosphorylation; IEA:Ensembl.
GO; GO:0010469; P:regulation of signaling receptor activity; IEA:Ensembl.
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;
Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Phosphoprotein; Reference proteome;
Ubl conjugation.
CHAIN 1 497 Serine/threonine-protein phosphatase 2A
56 kDa regulatory subunit beta isoform.
/FTId=PRO_0000071450.
MOD_RES 32 32 Phosphoserine; by CLK2.
{ECO:0000305|PubMed:21329884}.
MOD_RES 35 35 Phosphoserine; by CLK2.
{ECO:0000305|PubMed:21329884}.
MOD_RES 44 44 Phosphoserine; by CLK2.
{ECO:0000305|PubMed:21329884}.
MOD_RES 46 46 Phosphoserine; by CLK2.
{ECO:0000305|PubMed:21329884}.
MOD_RES 47 47 Phosphoserine; by CLK2.
{ECO:0000305|PubMed:21329884}.
MOD_RES 48 48 Phosphoserine; by CLK2.
{ECO:0000305|PubMed:21329884}.
VAR_SEQ 1 19 METKLPPASTPTSPSSPGL -> MITVNPPLPQDTVNLF
(in isoform Beta-2).
{ECO:0000303|PubMed:8694763}.
/FTId=VSP_005109.
MUTAGEN 52 52 Y->S: Loss of KLHL15-binding and enhanced
stability. {ECO:0000269|PubMed:23135275}.
MUTAGEN 103 104 KR->DE: Impaired trimer formation with
PP2A subunits A/C, no effect on KLHL15-
binding. {ECO:0000269|PubMed:23135275}.
MUTAGEN 232 233 RK->ED: Impaired trimer formation with
PP2A subunits A/C, no effect on KLHL15-
binding. {ECO:0000269|PubMed:23135275}.
CONFLICT 57 58 QE -> IF (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 177 178 ES -> GA (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 181 181 F -> M (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 184 184 S -> M (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 461 461 W -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 497 AA; 57393 MW; 8BEF84F20A77982D CRC64;
METKLPPAST PTSPSSPGLS PVPPPDKVDG FSRRSLRRAR PRRSHSSSQF RYQSNQQELT
PLPLLKDVPA SELHELLSRK LAQCGVMFDF LDCVADLKGK EVKRAALNEL VECVGSTRGV
LIEPVYPDII RMISVNIFRT LPPSENPEFD PEEDEPNLEP SWPHLQLVYE FFLRFLESPD
FQPSVAKRYV DQKFVLMLLE LFDSEDPRER EYLKTILHRV YGKFLGLRAY IRKQCNHIFL
RFIYEFEHFN GVAELLEILG SIINGFALPL KTEHKQFLVR VLIPLHSVKS LSVFHAQLAY
CVVQFLEKDA TLTEHVIRGL LKYWPKTCTQ KEVMFLGEME EILDVIEPSQ FVKIQEPLFK
QVARCVSSPH FQVAERALYF WNNEYILSLI EDNCHTVLPA VFGTLYQVSK EHWNQTIVSL
IYNVLKTFME MNGKLFDELT ASYKLEKQQE QQKAQERQEL WQGLEELRLR RLQGTQGAKE
APLQRLTPQV AASGGQS


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