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PP2A-B', isoform B

 Q8IN89_DROME            Unreviewed;       984 AA.
Q8IN89;
01-MAR-2003, integrated into UniProtKB/TrEMBL.
01-MAR-2003, sequence version 1.
03-JUL-2019, entry version 128.
SubName: Full=Well-rounded, isoform B {ECO:0000313|EMBL:AAN13758.1};
Name=wrd {ECO:0000313|EMBL:AAN13758.1,
ECO:0000313|FlyBase:FBgn0042693};
Synonyms=anon-WO0118547.420 {ECO:0000313|EMBL:AAN13758.1},
B' {ECO:0000313|EMBL:AAN13758.1}, B56-1 {ECO:0000313|EMBL:AAN13758.1},
BcDNA:GM05554 {ECO:0000313|EMBL:AAN13758.1},
CG 7913 {ECO:0000313|EMBL:AAN13758.1},
CG7901 {ECO:0000313|EMBL:AAN13758.1},
CG7913 {ECO:0000313|EMBL:AAN13758.1},
dB56-1 {ECO:0000313|EMBL:AAN13758.1},
Dmel\CG7913 {ECO:0000313|EMBL:AAN13758.1},
dPP2A {ECO:0000313|EMBL:AAN13758.1},
dPP2A-B56-1 {ECO:0000313|EMBL:AAN13758.1},
i234 {ECO:0000313|EMBL:AAN13758.1},
PP2A {ECO:0000313|EMBL:AAN13758.1},
PP2A B' {ECO:0000313|EMBL:AAN13758.1},
PP2A-B {ECO:0000313|EMBL:AAN13758.1},
PP2A-B' {ECO:0000313|EMBL:AAN13758.1},
pp2A-B' {ECO:0000313|EMBL:AAN13758.1},
PP2A[B'-1] {ECO:0000313|EMBL:AAN13758.1},
PR61 {ECO:0000313|EMBL:AAN13758.1}, Wrd {ECO:0000313|EMBL:AAN13758.1};
ORFNames=CG7913 {ECO:0000313|FlyBase:FBgn0042693},
Dmel_CG7913 {ECO:0000313|EMBL:AAN13758.1};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000313|EMBL:AAN13758.1, ECO:0000313|Proteomes:UP000000803};
[1] {ECO:0000313|EMBL:AAN13758.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L.,
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., 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., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J., 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., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
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., WoodageT, 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., 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).
[2] {ECO:0000313|EMBL:AAN13758.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537568;
Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
"Finishing a whole-genome shotgun: release 3 of the Drosophila
melanogaster euchromatic genome sequence.";
Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
[3] {ECO:0000313|EMBL:AAN13758.1, ECO:0000313|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D., 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).
[4] {ECO:0000313|EMBL:AAN13758.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537573;
Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M.,
Ashburner M., Celniker S.E.;
"The transposable elements of the Drosophila melanogaster euchromatin:
a genomics perspective.";
Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002).
[5] {ECO:0000313|EMBL:AAN13758.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537574;
Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
Karpen G.H.;
"Heterochromatic sequences in a Drosophila whole-genome shotgun
assembly.";
Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
[6] {ECO:0000313|EMBL:AAN13758.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
Ashburner M., Anxolabehere D.;
"Combined evidence annotation of transposable elements in genome
sequences.";
PLoS Comput. Biol. 1:166-175(2005).
[7] {ECO:0000313|EMBL:AAN13758.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569856; DOI=10.1126/science.1139815;
Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
"The Release 5.1 annotation of Drosophila melanogaster
heterochromatin.";
Science 316:1586-1591(2007).
[8] {ECO:0000313|EMBL:AAN13758.1, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569867; DOI=10.1126/science.1139816;
Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
Dimitri P., Karpen G.H., Celniker S.E.;
"Sequence finishing and mapping of Drosophila melanogaster
heterochromatin.";
Science 316:1625-1628(2007).
-----------------------------------------------------------------------
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EMBL; AE014297; AAN13758.1; -; Genomic_DNA.
RefSeq; NP_732295.1; NM_169789.2.
SMR; Q8IN89; -.
DIP; DIP-22751N; -.
IntAct; Q8IN89; 1.
STRING; 7227.FBpp0082978; -.
PaxDb; Q8IN89; -.
PRIDE; Q8IN89; -.
EnsemblMetazoa; FBtr0083556; FBpp0082978; FBgn0042693.
GeneID; 42169; -.
UCSC; CG7913-RB; d. melanogaster.
CTD; 42169; -.
FlyBase; FBgn0042693; wrd.
eggNOG; KOG2085; Eukaryota.
eggNOG; ENOG410XQJW; LUCA.
GeneTree; ENSGT00950000182781; -.
InParanoid; Q8IN89; -.
PhylomeDB; Q8IN89; -.
Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-DME-196299; Beta-catenin phosphorylation cascade.
Reactome; R-DME-198753; ERK/MAPK targets.
Reactome; R-DME-202670; ERKs are inactivated.
GenomeRNAi; 42169; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0042693; Expressed in 31 organ(s), highest expression level in head.
ExpressionAtlas; Q8IN89; baseline and differential.
Genevisible; Q8IN89; DM.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
GO; GO:0019888; F:protein phosphatase regulator activity; NAS:FlyBase.
GO; GO:0006914; P:autophagy; IMP:FlyBase.
GO; GO:0043066; P:negative regulation of apoptotic process; NAS:FlyBase.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:FlyBase.
GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:FlyBase.
GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
GO; GO:0006470; P:protein dephosphorylation; IDA:FlyBase.
GO; GO:0031952; P:regulation of protein autophosphorylation; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
GO; GO:0097479; P:synaptic vesicle localization; IMP:FlyBase.
GO; GO:0070328; P:triglyceride homeostasis; IMP:FlyBase.
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.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
Complete proteome {ECO:0000313|Proteomes:UP000000803};
Proteomics identification {ECO:0000213|PeptideAtlas:Q8IN89};
Reference proteome {ECO:0000313|Proteomes:UP000000803}.
REGION 1 58 Disordered. {ECO:0000256|MobiDB-
lite:Q8IN89}.
REGION 71 160 Disordered. {ECO:0000256|MobiDB-
lite:Q8IN89}.
REGION 204 245 Disordered. {ECO:0000256|MobiDB-
lite:Q8IN89}.
REGION 905 984 Disordered. {ECO:0000256|MobiDB-
lite:Q8IN89}.
COMPBIAS 13 57 Polar. {ECO:0000256|MobiDB-lite:Q8IN89}.
COMPBIAS 94 108 Polar. {ECO:0000256|MobiDB-lite:Q8IN89}.
COMPBIAS 138 160 Polar. {ECO:0000256|MobiDB-lite:Q8IN89}.
COMPBIAS 932 975 Polyampholyte. {ECO:0000256|MobiDB-
lite:Q8IN89}.
SEQUENCE 984 AA; 105970 MW; 911B50BDDDD1C5DD CRC64;
MVFGAMLLTG NGLKGPKQQQ QQHQQEPQQQ QQQSQQQQQE QKKPAPIKSS SKEQETQPIA
AGYYALGIRI PKSPSFHSGL DQLADDELDD QVQDQQQEQQ QTGSRFRFSS VEELKAKFEG
RKTPLSPPEA AAGGAAGSGA PTTSSSPSSS STSSNSSASA LSSLSQAASS SLASAAANSS
ASSSAATYGG GANSAAAALI ASSPFGSQSS TSSLSLSSNA GMSKNAAGAG SGSGSGTTST
GAASGSNSLV STLAQHFSAA TSAAASAAAA AASSASAASS SSASSSSTAT NNAASSSIAA
SKSPVSAAAA IKNILNATKS VGTSAAAAAA AAATSSSSSP SSAAAVPSSA ATAVAAVPTT
SDVPAEEMRP TVAQNLVGGI SISLGIGQRN GGAAPASSAV MVTPNATMVV TTSSLSIRQN
GDILPGHPAG LQPSPQTLQQ LTGSPGRARD RNLFYTPPTA SVAMALPALR ETAASEREEL
FIQKIQQCCT LFDFSEPLSD LKFKEVKRAA LHEMVDFLTN QNGVITEVIY PEAINMFAVN
LFRTLPPSSN PNGAEFDPEE DEPTLESSWP HLQLVYELFL RFLESPDFQP SMAKRFIDHQ
FVLQLLDLFD SEDPRERDFL KTVLHRIYGK FLGLRAFIRK QINNVFYRFI YETEHHNGIA
ELLEILGSII NGFALPLKEE HKQFLLKVLL PLHKAKSLSV YHPQLTYCVV QFLEKDPSLS
EAVIKSLLKF WPKTHSPKEV MFLNELEELL DVIEPAEFQK VMVPLFRQIA KCVSSPHFQV
AERALYYWNN EYIMSLITDN SAVILPIMFP ALNRNSKTHW NKTIHGLIYN ALKLFMEIDQ
RLFDECSKNY KQEKQMEREK LSQREELWQQ VESLAKTNPE WTKARRFNDC LPVSDSRALC
DQYSENSDSA YDQSEQRARQ PPPPLPPQKQ AHQEPREIRG ERNKDKPLLR RKSDLPSDSG
TVKALNEHKR TDEYLTTPPP DGNY


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[PPP2R2B] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta)
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[PPP2R5E] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform (PP2A B subunit isoform B'-epsilon) (PP2A B subunit isoform B56-epsilon) (PP2A B subunit isoform PR61-epsilon) (PP2A B subunit isoform R5-epsilon)
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[PTPA PPP2R4] Serine/threonine-protein phosphatase 2A activator (EC 5.2.1.8) (PP2A, subunit B', PR53 isoform) (Phosphotyrosyl phosphatase activator) (PTPA) (Serine/threonine-protein phosphatase 2A regulatory subunit 4) (Serine/threonine-protein phosphatase 2A regulatory subunit B')
[RTS1 SCS1 YOR014W OR26.04] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (PP2A, B subunit, B' delta isoform) (Protein RTS1) (Protein SCS1)
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[B'THETA At1g13460 T6J4.19] Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' theta isoform (AtB' theta) (PP2A, B' subunit, theta isoform)
[tws aar Pp2A-85F CG6235] Protein phosphatase PP2A 55 kDa regulatory subunit (PR55) (Protein phosphatase PP2A regulatory subunit B) (Protein twins)
[PPP2R1A] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (Medium tumor antigen-associated 61 kDa protein) (PP2A subunit A isoform PR65-alpha) (PP2A subunit A isoform R1-alpha)
[Ppp2r1a] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (PP2A subunit A isoform PR65-alpha) (PP2A subunit A isoform R1-alpha)
[Ppp2r2a] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PP2A subunit B isoform B55-alpha) (PP2A subunit B isoform BRA) (PP2A subunit B isoform PR55-alpha) (PP2A subunit B isoform R2-alpha) (PP2A subunit B isoform alpha)
[B'ZETA At3g21650 MIL23.22] Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' zeta isoform (AtB' zeta) (PP2A, B' subunit, zeta isoform)
[wrd anon-WO0118547.420 B' B56-1 BcDNA:GM05554 CG 7913 CG7901 CG7913 dB56-1 Dmel\CG7913 dPP2A dPP2A-B56-1 i234 PP2A PP2A B' PP2A-B PP2A-B' pp2A-B' PP2A[B'-1] PR61 Wrd CG7913 Dmel_CG7913] Well-rounded, isoform B
[Ptpa Ppp2r4] Serine/threonine-protein phosphatase 2A activator (EC 5.2.1.8) (PP2A, subunit B', PR53 isoform) (Phosphotyrosyl phosphatase activator) (PTPA) (Serine/threonine-protein phosphatase 2A regulatory subunit 4) (Serine/threonine-protein phosphatase 2A regulatory subunit B')
[PP2A3 PP2A4 At2g42500 MHK10.22] Serine/threonine-protein phosphatase PP2A-3 catalytic subunit (EC 3.1.3.16) (Protein phosphatase 2A isoform 3)
[PP2A4 EP7 PP2A3 At3g58500 F14P22.90] Serine/threonine-protein phosphatase PP2A-4 catalytic subunit (EC 3.1.3.16) (Protein phosphatase 2A isoform 4)
[Ppp2r5c] Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (PP2A B subunit isoform B'-alpha-3) (PP2A B subunit isoform B'-gamma) (PP2A B subunit isoform B56-gamma) (PP2A B subunit isoform PR61-gamma) (PP2A B subunit isoform R5-gamma)
[PP2AA1 EER1 RCN1 REGA At1g25490 F2J7.19] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (AtA alpha) (PP2A, subunit A, alpha isoform) (PR-65 A) (Protein ROOTS CURL IN NAPHTHYLPHTHALAMIC ACID 1) (Protein enhancer of ethylene-response 1)
[Ppp2r2a] Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PP2A subunit B isoform B55-alpha) (PP2A subunit B isoform PR55-alpha) (PP2A subunit B isoform R2-alpha) (PP2A subunit B isoform alpha)

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[31322823] 2-Phenyloxazole-4-carboxamide as new scaffold for selective inhibition of human monoamine oxidase B.
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[31307247] Non-covalent immunoproteasome inhibitors induce cell cycle arrest in multiple myeloma MM.1R cells.
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[31285503] Phosphorylation of p23-1 cochaperone by protein kinase CK2 affects root development in Arabidopsis.
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[31281948] Blood amyloid-β protein isoforms are affected by HIV-1 in a subtype-dependent pattern.