Full text data of PPP2R5B
PPP2R5B
[Confidence: low (only semi-automatic identification from reviews)]
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15173
ID 2A5B_HUMAN Reviewed; 497 AA.
AC Q15173; Q13853;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform;
DE AltName: Full=PP2A B subunit isoform B'-beta;
DE AltName: Full=PP2A B subunit isoform B56-beta;
DE AltName: Full=PP2A B subunit isoform PR61-beta;
DE AltName: Full=PP2A B subunit isoform R5-beta;
GN Name=PPP2R5B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1).
RC TISSUE=Fetal brain;
RX PubMed=7592815; DOI=10.1074/jbc.270.44.26123;
RA McCright B., Virshup D.M.;
RT "Identification of a new family of protein phosphatase 2A regulatory
RT subunits.";
RL J. Biol. Chem. 270:26123-26128(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2), AND PARTIAL PROTEIN
RP SEQUENCE.
RC TISSUE=Brain;
RX PubMed=8694763;
RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I.,
RA Merlevede W., Goris J., Hemmings B.A.;
RT "The variable subunit associated with protein phosphatase 2A0 defines
RT a novel multimember family of regulatory subunits.";
RL Biochem. J. 317:187-194(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=8703017; DOI=10.1074/jbc.271.36.22081;
RA McCright B., Rivers A.M., Audlin S., Virshup D.M.;
RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
RT encodes differentiation-induced phosphoproteins that target PP2A to
RT both nucleus and cytoplasm.";
RL J. Biol. Chem. 271:22081-22089(1996).
RN [5]
RP INTERACTION WITH SGOL1.
RX PubMed=16541025; DOI=10.1038/nature04663;
RA Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
RA Kawashima S.A., Watanabe Y.;
RT "Shugoshin collaborates with protein phosphatase 2A to protect
RT cohesin.";
RL Nature 441:46-52(2006).
RN [6]
RP FUNCTION, PHOSPHORYLATION AT SER-32; SER-35; SER-44; SER-46; SER-47
RP AND SER-48, AND INTERACTION WITH AKT1.
RX PubMed=21329884; DOI=10.1016/j.molcel.2011.02.007;
RA Rodgers J.T., Vogel R.O., Puigserver P.;
RT "Clk2 and B56-beta mediate insulin-regulated assembly of the PP2A
RT phosphatase holoenzyme complex on Akt.";
RL Mol. Cell 41:471-479(2011).
CC -!- FUNCTION: The B regulatory subunit might modulate substrate
CC selectivity and catalytic activity, and also might direct the
CC localization of the catalytic enzyme to a particular subcellular
CC compartment. The phosphorylated form mediates the interaction
CC between AKT1 and PP2A phosphatase leading to dephosphorylation of
CC AKT1 on the 'Thr-308' and 'Ser-373' residues.
CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme,
CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
CC constant regulatory subunit (PR65 or subunit A), that associates
CC with a variety of regulatory subunits. Proteins that associate
CC with the core dimer include three families of regulatory subunits
CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56
CC families), the 48 kDa variable regulatory subunit, viral proteins,
CC and cell signaling molecules. Interacts with SGOL1. Interacts with
CC AKT1.
CC -!- INTERACTION:
CC O96017:CHEK2; NbExp=2; IntAct=EBI-1369497, EBI-1180783;
CC P46695:IER3; NbExp=4; IntAct=EBI-1369497, EBI-1748945;
CC P67775:PPP2CA; NbExp=4; IntAct=EBI-1369497, EBI-712311;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Beta-1;
CC IsoId=Q15173-1; Sequence=Displayed;
CC Name=Beta-2;
CC IsoId=Q15173-2; Sequence=VSP_005109;
CC -!- TISSUE SPECIFICITY: Highest expression in brain.
CC -!- INDUCTION: By retinoic acid; in neuroblastoma cell lines.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L42374; AAC37602.1; -; mRNA.
DR EMBL; Z69028; CAA93152.1; -; mRNA.
DR EMBL; BC045619; AAH45619.1; -; mRNA.
DR PIR; I70147; I70147.
DR RefSeq; NP_006235.1; NM_006244.3.
DR UniGene; Hs.75199; -.
DR ProteinModelPortal; Q15173; -.
DR SMR; Q15173; 75-443.
DR IntAct; Q15173; 7.
DR MINT; MINT-2835290; -.
DR STRING; 9606.ENSP00000164133; -.
DR PhosphoSite; Q15173; -.
DR DMDM; 7387497; -.
DR PaxDb; Q15173; -.
DR PRIDE; Q15173; -.
DR DNASU; 5526; -.
DR Ensembl; ENST00000164133; ENSP00000164133; ENSG00000068971.
DR GeneID; 5526; -.
DR KEGG; hsa:5526; -.
DR UCSC; uc001oby.3; human.
DR CTD; 5526; -.
DR GeneCards; GC11P064692; -.
DR HGNC; HGNC:9310; PPP2R5B.
DR HPA; HPA036607; -.
DR MIM; 601644; gene.
DR neXtProt; NX_Q15173; -.
DR PharmGKB; PA33673; -.
DR eggNOG; NOG264925; -.
DR HOGENOM; HOG000067326; -.
DR HOVERGEN; HBG000009; -.
DR InParanoid; Q15173; -.
DR KO; K11584; -.
DR OMA; FIYEFEH; -.
DR PhylomeDB; Q15173; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q15173; -.
DR GeneWiki; PPP2R5B; -.
DR GenomeRNAi; 5526; -.
DR NextBio; 21396; -.
DR PRO; PR:Q15173; -.
DR ArrayExpress; Q15173; -.
DR Bgee; Q15173; -.
DR CleanEx; HS_PPP2R5B; -.
DR Genevestigator; Q15173; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:ProtInc.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002554; PP2A_B56.
DR PANTHER; PTHR10257; PTHR10257; 1.
DR Pfam; PF01603; B56; 1.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1 497 Serine/threonine-protein phosphatase 2A
FT 56 kDa regulatory subunit beta isoform.
FT /FTId=PRO_0000071450.
FT MOD_RES 32 32 Phosphoserine; by CLK2 (Probable).
FT MOD_RES 35 35 Phosphoserine; by CLK2 (Probable).
FT MOD_RES 44 44 Phosphoserine; by CLK2 (Probable).
FT MOD_RES 46 46 Phosphoserine; by CLK2 (Probable).
FT MOD_RES 47 47 Phosphoserine; by CLK2 (Probable).
FT MOD_RES 48 48 Phosphoserine; by CLK2 (Probable).
FT VAR_SEQ 1 19 METKLPPASTPTSPSSPGL -> MITVNPPLPQDTVNLF
FT (in isoform Beta-2).
FT /FTId=VSP_005109.
FT CONFLICT 57 58 QE -> IF (in Ref. 2; AA sequence).
FT CONFLICT 177 178 ES -> GA (in Ref. 2; AA sequence).
FT CONFLICT 181 181 F -> M (in Ref. 2; AA sequence).
FT CONFLICT 184 184 S -> M (in Ref. 2; AA sequence).
FT CONFLICT 461 461 W -> E (in Ref. 2; AA sequence).
SQ 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
//
ID 2A5B_HUMAN Reviewed; 497 AA.
AC Q15173; Q13853;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform;
DE AltName: Full=PP2A B subunit isoform B'-beta;
DE AltName: Full=PP2A B subunit isoform B56-beta;
DE AltName: Full=PP2A B subunit isoform PR61-beta;
DE AltName: Full=PP2A B subunit isoform R5-beta;
GN Name=PPP2R5B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-1).
RC TISSUE=Fetal brain;
RX PubMed=7592815; DOI=10.1074/jbc.270.44.26123;
RA McCright B., Virshup D.M.;
RT "Identification of a new family of protein phosphatase 2A regulatory
RT subunits.";
RL J. Biol. Chem. 270:26123-26128(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2), AND PARTIAL PROTEIN
RP SEQUENCE.
RC TISSUE=Brain;
RX PubMed=8694763;
RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I.,
RA Merlevede W., Goris J., Hemmings B.A.;
RT "The variable subunit associated with protein phosphatase 2A0 defines
RT a novel multimember family of regulatory subunits.";
RL Biochem. J. 317:187-194(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=8703017; DOI=10.1074/jbc.271.36.22081;
RA McCright B., Rivers A.M., Audlin S., Virshup D.M.;
RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
RT encodes differentiation-induced phosphoproteins that target PP2A to
RT both nucleus and cytoplasm.";
RL J. Biol. Chem. 271:22081-22089(1996).
RN [5]
RP INTERACTION WITH SGOL1.
RX PubMed=16541025; DOI=10.1038/nature04663;
RA Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
RA Kawashima S.A., Watanabe Y.;
RT "Shugoshin collaborates with protein phosphatase 2A to protect
RT cohesin.";
RL Nature 441:46-52(2006).
RN [6]
RP FUNCTION, PHOSPHORYLATION AT SER-32; SER-35; SER-44; SER-46; SER-47
RP AND SER-48, AND INTERACTION WITH AKT1.
RX PubMed=21329884; DOI=10.1016/j.molcel.2011.02.007;
RA Rodgers J.T., Vogel R.O., Puigserver P.;
RT "Clk2 and B56-beta mediate insulin-regulated assembly of the PP2A
RT phosphatase holoenzyme complex on Akt.";
RL Mol. Cell 41:471-479(2011).
CC -!- FUNCTION: The B regulatory subunit might modulate substrate
CC selectivity and catalytic activity, and also might direct the
CC localization of the catalytic enzyme to a particular subcellular
CC compartment. The phosphorylated form mediates the interaction
CC between AKT1 and PP2A phosphatase leading to dephosphorylation of
CC AKT1 on the 'Thr-308' and 'Ser-373' residues.
CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme,
CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
CC constant regulatory subunit (PR65 or subunit A), that associates
CC with a variety of regulatory subunits. Proteins that associate
CC with the core dimer include three families of regulatory subunits
CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56
CC families), the 48 kDa variable regulatory subunit, viral proteins,
CC and cell signaling molecules. Interacts with SGOL1. Interacts with
CC AKT1.
CC -!- INTERACTION:
CC O96017:CHEK2; NbExp=2; IntAct=EBI-1369497, EBI-1180783;
CC P46695:IER3; NbExp=4; IntAct=EBI-1369497, EBI-1748945;
CC P67775:PPP2CA; NbExp=4; IntAct=EBI-1369497, EBI-712311;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Beta-1;
CC IsoId=Q15173-1; Sequence=Displayed;
CC Name=Beta-2;
CC IsoId=Q15173-2; Sequence=VSP_005109;
CC -!- TISSUE SPECIFICITY: Highest expression in brain.
CC -!- INDUCTION: By retinoic acid; in neuroblastoma cell lines.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L42374; AAC37602.1; -; mRNA.
DR EMBL; Z69028; CAA93152.1; -; mRNA.
DR EMBL; BC045619; AAH45619.1; -; mRNA.
DR PIR; I70147; I70147.
DR RefSeq; NP_006235.1; NM_006244.3.
DR UniGene; Hs.75199; -.
DR ProteinModelPortal; Q15173; -.
DR SMR; Q15173; 75-443.
DR IntAct; Q15173; 7.
DR MINT; MINT-2835290; -.
DR STRING; 9606.ENSP00000164133; -.
DR PhosphoSite; Q15173; -.
DR DMDM; 7387497; -.
DR PaxDb; Q15173; -.
DR PRIDE; Q15173; -.
DR DNASU; 5526; -.
DR Ensembl; ENST00000164133; ENSP00000164133; ENSG00000068971.
DR GeneID; 5526; -.
DR KEGG; hsa:5526; -.
DR UCSC; uc001oby.3; human.
DR CTD; 5526; -.
DR GeneCards; GC11P064692; -.
DR HGNC; HGNC:9310; PPP2R5B.
DR HPA; HPA036607; -.
DR MIM; 601644; gene.
DR neXtProt; NX_Q15173; -.
DR PharmGKB; PA33673; -.
DR eggNOG; NOG264925; -.
DR HOGENOM; HOG000067326; -.
DR HOVERGEN; HBG000009; -.
DR InParanoid; Q15173; -.
DR KO; K11584; -.
DR OMA; FIYEFEH; -.
DR PhylomeDB; Q15173; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q15173; -.
DR GeneWiki; PPP2R5B; -.
DR GenomeRNAi; 5526; -.
DR NextBio; 21396; -.
DR PRO; PR:Q15173; -.
DR ArrayExpress; Q15173; -.
DR Bgee; Q15173; -.
DR CleanEx; HS_PPP2R5B; -.
DR Genevestigator; Q15173; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:ProtInc.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002554; PP2A_B56.
DR PANTHER; PTHR10257; PTHR10257; 1.
DR Pfam; PF01603; B56; 1.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1 497 Serine/threonine-protein phosphatase 2A
FT 56 kDa regulatory subunit beta isoform.
FT /FTId=PRO_0000071450.
FT MOD_RES 32 32 Phosphoserine; by CLK2 (Probable).
FT MOD_RES 35 35 Phosphoserine; by CLK2 (Probable).
FT MOD_RES 44 44 Phosphoserine; by CLK2 (Probable).
FT MOD_RES 46 46 Phosphoserine; by CLK2 (Probable).
FT MOD_RES 47 47 Phosphoserine; by CLK2 (Probable).
FT MOD_RES 48 48 Phosphoserine; by CLK2 (Probable).
FT VAR_SEQ 1 19 METKLPPASTPTSPSSPGL -> MITVNPPLPQDTVNLF
FT (in isoform Beta-2).
FT /FTId=VSP_005109.
FT CONFLICT 57 58 QE -> IF (in Ref. 2; AA sequence).
FT CONFLICT 177 178 ES -> GA (in Ref. 2; AA sequence).
FT CONFLICT 181 181 F -> M (in Ref. 2; AA sequence).
FT CONFLICT 184 184 S -> M (in Ref. 2; AA sequence).
FT CONFLICT 461 461 W -> E (in Ref. 2; AA sequence).
SQ 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
//
MIM
601644
*RECORD*
*FIELD* NO
601644
*FIELD* TI
*601644 PROTEIN PHOSPHATASE 2, REGULATORY SUBUNIT B (B56), BETA; PPP2R5B
*FIELD* TX
read moreFor background information on protein phosphatase 2A (PP2A) and its
subunits, see PPP2R5A (601643).
GENE FUNCTION
McCright and Virshup (1995) noted that the beta (PPP2R5B), delta
(PPP2R5D; 601646), and epsilon (PPP2R5E; 601647) subunits of PP2A are
expressed at highest levels in the brain and the expression of the beta
and delta subunits increases when neuroblastoma cells are induced to
differentiate with retinoic acid.
MAPPING
McCright et al. (1996) mapped the gene for the beta subunit, designated
PPP2R5B, to 11q12 by fluorescence in situ hybridization. The European
Consortium on MEN1 (1997) localized the PPP2R5B gene to 11q13 in the
course of constructing a contig of the region containing the MEN1 gene
(613733).
*FIELD* RF
1. European Consortium on MEN1: Mapping of the gene encoding the
B56-beta subunit of protein phosphatase 2A (PPP2R5B) to a 0.5-Mb region
of chromosome 11q13 and its exclusion as a candidate gene for multiple
endocrine neoplasia type 1 (MEN1). Hum. Genet. 100: 481-485, 1997.
2. McCright, B.; Brothman, A. R.; Virshup, D. M.: Assignment of human
protein phosphatase 2A regulatory subunit genes B56-alpha, B56-beta,
B56-gamma, B56-delta, and B56-epsilon (PPP2R5A--PPP2R5E), highly expressed
in muscle and brain, to chromosome regions 1q41, 11q12, 3p21, 6p21.1,
and 7p11.2-to-p12. Genomics 36: 168-170, 1996.
3. McCright, B.; Virshup, D. M.: Identification of a new family of
protein phosphatase 2A regulatory subunits. J. Biol. Chem. 270:
26123-26128, 1995.
*FIELD* CN
Victor A. McKusick - updated: 9/12/1997
*FIELD* CD
Alan F. Scott: 1/23/1997
*FIELD* ED
carol: 02/09/2011
alopez: 4/27/2010
terry: 9/12/1997
mark: 2/10/1997
jenny: 1/28/1997
mark: 1/23/1997
*RECORD*
*FIELD* NO
601644
*FIELD* TI
*601644 PROTEIN PHOSPHATASE 2, REGULATORY SUBUNIT B (B56), BETA; PPP2R5B
*FIELD* TX
read moreFor background information on protein phosphatase 2A (PP2A) and its
subunits, see PPP2R5A (601643).
GENE FUNCTION
McCright and Virshup (1995) noted that the beta (PPP2R5B), delta
(PPP2R5D; 601646), and epsilon (PPP2R5E; 601647) subunits of PP2A are
expressed at highest levels in the brain and the expression of the beta
and delta subunits increases when neuroblastoma cells are induced to
differentiate with retinoic acid.
MAPPING
McCright et al. (1996) mapped the gene for the beta subunit, designated
PPP2R5B, to 11q12 by fluorescence in situ hybridization. The European
Consortium on MEN1 (1997) localized the PPP2R5B gene to 11q13 in the
course of constructing a contig of the region containing the MEN1 gene
(613733).
*FIELD* RF
1. European Consortium on MEN1: Mapping of the gene encoding the
B56-beta subunit of protein phosphatase 2A (PPP2R5B) to a 0.5-Mb region
of chromosome 11q13 and its exclusion as a candidate gene for multiple
endocrine neoplasia type 1 (MEN1). Hum. Genet. 100: 481-485, 1997.
2. McCright, B.; Brothman, A. R.; Virshup, D. M.: Assignment of human
protein phosphatase 2A regulatory subunit genes B56-alpha, B56-beta,
B56-gamma, B56-delta, and B56-epsilon (PPP2R5A--PPP2R5E), highly expressed
in muscle and brain, to chromosome regions 1q41, 11q12, 3p21, 6p21.1,
and 7p11.2-to-p12. Genomics 36: 168-170, 1996.
3. McCright, B.; Virshup, D. M.: Identification of a new family of
protein phosphatase 2A regulatory subunits. J. Biol. Chem. 270:
26123-26128, 1995.
*FIELD* CN
Victor A. McKusick - updated: 9/12/1997
*FIELD* CD
Alan F. Scott: 1/23/1997
*FIELD* ED
carol: 02/09/2011
alopez: 4/27/2010
terry: 9/12/1997
mark: 2/10/1997
jenny: 1/28/1997
mark: 1/23/1997