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Protein phosphatase PP2A 55 kDa regulatory subunit (PR55) (Protein phosphatase PP2A regulatory subunit B) (Protein twins)

 2ABA_DROME              Reviewed;         499 AA.
P36872; A4V2M9; A4V2N0; Q9VH21; Q9VH22;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
31-JAN-2018, entry version 176.
RecName: Full=Protein phosphatase PP2A 55 kDa regulatory subunit;
Short=PR55;
AltName: Full=Protein phosphatase PP2A regulatory subunit B;
AltName: Full=Protein twins;
Name=tws; Synonyms=aar, Pp2A-85F; ORFNames=CG6235;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B).
PubMed=8382567; DOI=10.1016/0092-8674(93)90080-A;
Mayer-Jaekel R.E., Ohkura H., Gomes R., Sunkel C.E., Baumgartner S.,
Hemmings B.A., Glover D.M.;
"The 55 kd regulatory subunit of Drosophila protein phosphatase 2A is
required for anaphase.";
Cell 72:621-633(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
STRAIN=Oregon-R; TISSUE=Eye imaginal disk;
PubMed=8383623; DOI=10.1101/gad.7.3.429;
Uemura T., Shiomi K., Togashi S., Takeichi M.;
"Mutation of twins encoding a regulator of protein phosphatase 2A
leads to pattern duplication in Drosophila imaginal discs.";
Genes Dev. 7:429-440(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
-!- FUNCTION: Could perform a substrate recognition function or could
be responsible for targeting the enzyme complex to the appropriate
subcellular compartment.
-!- SUBUNIT: PP2A exists in several trimeric forms, all of which
consist of a core composed of a catalytic subunit associated with
a 65 kDa regulatory subunit (PR65) (subunit A). The core complex
associates with a third, variable subunit (subunit B), which
confers distinct properties to the holoenzyme.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A; Synonyms=F;
IsoId=P36872-1; Sequence=Displayed;
Name=B; Synonyms=C, D, E, G, H;
IsoId=P36872-2; Sequence=VSP_005105, VSP_005106;
-!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B
family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1, Met-18, Met-33 or Met-44
is the initiator. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D13004; BAA02367.1; -; mRNA.
EMBL; L07581; AAA99870.1; -; mRNA.
EMBL; L07583; AAA99871.1; -; mRNA.
EMBL; L07585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L07586; AAB00371.1; -; Genomic_DNA.
EMBL; L12544; AAB00371.1; JOINED; Genomic_DNA.
EMBL; L07586; AAB00372.1; -; Genomic_DNA.
EMBL; L12544; AAB00372.1; JOINED; Genomic_DNA.
EMBL; AE014297; AAF54498.1; -; Genomic_DNA.
EMBL; AE014297; AAF54499.3; -; Genomic_DNA.
EMBL; AE014297; AAN13455.1; -; Genomic_DNA.
EMBL; AE014297; AAN13456.1; -; Genomic_DNA.
EMBL; AE014297; AAN13457.1; -; Genomic_DNA.
EMBL; AE014297; AAN13458.1; -; Genomic_DNA.
EMBL; AE014297; AAN13459.1; -; Genomic_DNA.
EMBL; AE014297; AAN13460.1; -; Genomic_DNA.
EMBL; AY061152; AAL28700.1; -; mRNA.
PIR; A45778; A45778.
RefSeq; NP_001287269.1; NM_001300340.1. [P36872-1]
RefSeq; NP_476880.1; NM_057532.4. [P36872-1]
RefSeq; NP_476881.1; NM_057533.3. [P36872-2]
RefSeq; NP_599111.1; NM_134284.3. [P36872-2]
RefSeq; NP_599112.1; NM_134285.2. [P36872-2]
RefSeq; NP_599113.1; NM_134286.3. [P36872-2]
RefSeq; NP_731451.1; NM_169329.2. [P36872-1]
RefSeq; NP_731452.1; NM_169330.2. [P36872-2]
RefSeq; NP_731453.1; NM_169331.2. [P36872-2]
UniGene; Dm.3826; -.
ProteinModelPortal; P36872; -.
SMR; P36872; -.
BioGrid; 71024; 27.
DIP; DIP-19897N; -.
IntAct; P36872; 31.
MINT; MINT-896238; -.
STRING; 7227.FBpp0081665; -.
PaxDb; P36872; -.
PRIDE; P36872; -.
EnsemblMetazoa; FBtr0082186; FBpp0081664; FBgn0004889. [P36872-1]
EnsemblMetazoa; FBtr0082187; FBpp0081665; FBgn0004889. [P36872-1]
EnsemblMetazoa; FBtr0082188; FBpp0081666; FBgn0004889. [P36872-2]
EnsemblMetazoa; FBtr0082189; FBpp0081667; FBgn0004889. [P36872-2]
EnsemblMetazoa; FBtr0082190; FBpp0081668; FBgn0004889. [P36872-2]
EnsemblMetazoa; FBtr0082191; FBpp0081669; FBgn0004889. [P36872-2]
EnsemblMetazoa; FBtr0082192; FBpp0081670; FBgn0004889. [P36872-2]
EnsemblMetazoa; FBtr0082193; FBpp0081671; FBgn0004889. [P36872-2]
EnsemblMetazoa; FBtr0345177; FBpp0311386; FBgn0004889. [P36872-1]
GeneID; 47877; -.
KEGG; dme:Dmel_CG6235; -.
UCSC; CG6235-RC; d. melanogaster.
UCSC; CG6235-RF; d. melanogaster.
CTD; 47877; -.
FlyBase; FBgn0004889; tws.
eggNOG; KOG1354; Eukaryota.
eggNOG; COG5170; LUCA.
GeneTree; ENSGT00390000006311; -.
InParanoid; P36872; -.
KO; K04354; -.
OMA; SPTWKFT; -.
OrthoDB; EOG091G09BB; -.
PhylomeDB; P36872; -.
Reactome; R-DME-209155; Phosphorylation of AXN and APC.
Reactome; R-DME-209190; Phosphorylation of CI.
Reactome; R-DME-209214; Phosphorylation of SMO.
Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
Reactome; R-DME-209396; Phosphorylation of ARM.
Reactome; R-DME-209413; Assembly of the 'destruction complex'.
Reactome; R-DME-209440; Recruitment of the 'destruction complex' to the receptor complex, the degradation of AXN and release of ARM.
Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
Reactome; R-DME-432553; Phosphorylation of PER and TIM.
Reactome; R-DME-432620; Dephosphorylation of PER.
Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SignaLink; P36872; -.
ChiTaRS; tws; fly.
GenomeRNAi; 47877; -.
PRO; PR:P36872; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0004889; -.
ExpressionAtlas; P36872; differential.
Genevisible; P36872; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005829; C:cytosol; HDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB.
GO; GO:0019888; F:protein phosphatase regulator activity; IMP:FlyBase.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:FlyBase.
GO; GO:0007099; P:centriole replication; IMP:FlyBase.
GO; GO:0007098; P:centrosome cycle; IMP:FlyBase.
GO; GO:0007623; P:circadian rhythm; TAS:Reactome.
GO; GO:0001700; P:embryonic development via the syncytial blastoderm; IMP:FlyBase.
GO; GO:0007447; P:imaginal disc pattern formation; IMP:UniProtKB.
GO; GO:0045201; P:maintenance of neuroblast polarity; IMP:FlyBase.
GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IMP:FlyBase.
GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:FlyBase.
GO; GO:0070262; P:peptidyl-serine dephosphorylation; IBA:GO_Central.
GO; GO:0006470; P:protein dephosphorylation; ISS:FlyBase.
GO; GO:0050821; P:protein stabilization; IDA:FlyBase.
GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IMP:UniProtKB.
GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
GO; GO:0016055; P:Wnt signaling pathway; IMP:FlyBase.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR000009; PP2A_PR55.
InterPro; IPR018067; PP2A_PR55_CS.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR11871; PTHR11871; 1.
PIRSF; PIRSF037309; PP2A_PR55; 1.
PRINTS; PR00600; PP2APR55.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 3.
PROSITE; PS01024; PR55_1; 1.
PROSITE; PS01025; PR55_2; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Reference proteome; Repeat;
WD repeat.
CHAIN 1 499 Protein phosphatase PP2A 55 kDa
regulatory subunit.
/FTId=PRO_0000071437.
REPEAT 79 118 WD 1.
REPEAT 144 185 WD 2.
REPEAT 228 266 WD 3.
REPEAT 277 317 WD 4.
REPEAT 336 374 WD 5.
REPEAT 391 432 WD 6.
REPEAT 467 498 WD 7.
VAR_SEQ 1 56 Missing (in isoform B).
{ECO:0000303|PubMed:8382567,
ECO:0000303|PubMed:8383623}.
/FTId=VSP_005105.
VAR_SEQ 57 59 PAS -> MAG (in isoform B).
{ECO:0000303|PubMed:8382567,
ECO:0000303|PubMed:8383623}.
/FTId=VSP_005106.
CONFLICT 211 211 K -> M (in Ref. 1; AAA99871).
{ECO:0000305}.
SEQUENCE 499 AA; 56967 MW; D871A7E3058B7286 CRC64;
MGRWGRQSPV LEPPDPQMQT TPPPPTLPPR TFMRQSSITK IGNMLNTAIN INGAKKPASN
GEASWCFSQI KGALDDDVTD ADIISCVEFN HDGELLATGD KGGRVVIFQR DPASKAANPR
RGEYNVYSTF QSHEPEFDYL KSLEIEEKIN KIRWLQQKNP VHFLLSTNDK TVKLWKVSER
DKSFGGYNTK EENGLIRDPQ NVTALRVPSV KQIPLLVEAS PRRTFANAHT YHINSISVNS
DQETFLSADD LRINLWHLEV VNQSYNIVDI KPTNMEELTE VITAAEFHPT ECNVFVYSSS
KGTIRLCDMR SAALCDRHSK QFEEPENPTN RSFFSEIISS ISDVKLSNSG RYMISRDYLS
IKVWDLHMET KPIETYPVHE YLRAKLCSLY ENDCIFDKFE CCWNGKDSSI MTGSYNNFFR
VFDRNSKKDV TLEASRDIIK PKTVLKPRKV CTGGKRKKDE ISVDCLDFNK KILHTAWHPE
ENIIAVAATN NLFIFQDKF


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