Full text data of PPP2R2A
PPP2R2A
[Confidence: low (only semi-automatic identification from reviews)]
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
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)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P63151
ID 2ABA_HUMAN Reviewed; 447 AA.
AC P63151; B2RBU8; B4E1T7; P50409; Q00007;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 27-SEP-2004, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform;
DE AltName: Full=PP2A subunit B isoform B55-alpha;
DE AltName: Full=PP2A subunit B isoform PR55-alpha;
DE AltName: Full=PP2A subunit B isoform R2-alpha;
DE AltName: Full=PP2A subunit B isoform alpha;
GN Name=PPP2R2A;
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 1), AND TISSUE SPECIFICITY.
RC TISSUE=Lung fibroblast;
RX PubMed=1849734; DOI=10.1021/bi00229a001;
RA Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J.,
RA Merlevede W., Hofsteenge J., Hemmings B.A.;
RT "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A:
RT evidence for a neuronal-specific isoform.";
RL Biochemistry 30:3589-3597(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Blood;
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 [6]
RP INTERACTION WITH TP53.
RX PubMed=17245430; DOI=10.1038/sj.emboj.7601519;
RA Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.;
RT "A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-
RT induced dephosphorylation of p53 at Thr55.";
RL EMBO J. 26:402-411(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(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.
CC -!- SUBUNIT: Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
CC PPP2R2A, PPP2R5E and TBCD (By similarity). PP2A consists of a
CC common heterodimeric core enzyme, composed of a 36 kDa catalytic
CC subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65
CC or subunit A), that associates with a variety of regulatory
CC subunits. Proteins that associate with the core dimer include
CC 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
CC variable regulatory subunit, viral proteins, and cell signaling
CC molecules. Interacts with TP53.
CC -!- INTERACTION:
CC P30153:PPP2R1A; NbExp=8; IntAct=EBI-1048931, EBI-302388;
CC P30154:PPP2R1B; NbExp=2; IntAct=EBI-1048931, EBI-357094;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P63151-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P63151-2; Sequence=VSP_043100;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B
CC family.
CC -!- SIMILARITY: Contains 7 WD repeats.
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DR EMBL; M64929; AAA36490.1; -; mRNA.
DR EMBL; AK303981; BAG64899.1; -; mRNA.
DR EMBL; AK314823; BAG37345.1; -; mRNA.
DR EMBL; AC022911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63578.1; -; Genomic_DNA.
DR EMBL; BC041071; AAH41071.1; -; mRNA.
DR PIR; A38351; A38351.
DR RefSeq; NP_001171062.1; NM_001177591.1.
DR RefSeq; NP_002708.1; NM_002717.3.
DR UniGene; Hs.146339; -.
DR PDB; 3DW8; X-ray; 2.85 A; B/E=1-447.
DR PDBsum; 3DW8; -.
DR ProteinModelPortal; P63151; -.
DR SMR; P63151; 8-446.
DR DIP; DIP-29398N; -.
DR IntAct; P63151; 16.
DR MINT; MINT-2835351; -.
DR STRING; 9606.ENSP00000370113; -.
DR BindingDB; P63151; -.
DR ChEMBL; CHEMBL4284; -.
DR PhosphoSite; P63151; -.
DR DMDM; 52783535; -.
DR PaxDb; P63151; -.
DR PeptideAtlas; P63151; -.
DR PRIDE; P63151; -.
DR DNASU; 5520; -.
DR Ensembl; ENST00000315985; ENSP00000325074; ENSG00000221914.
DR Ensembl; ENST00000380737; ENSP00000370113; ENSG00000221914.
DR GeneID; 5520; -.
DR KEGG; hsa:5520; -.
DR UCSC; uc003xeu.3; human.
DR CTD; 5520; -.
DR GeneCards; GC08P026204; -.
DR HGNC; HGNC:9304; PPP2R2A.
DR MIM; 604941; gene.
DR neXtProt; NX_P63151; -.
DR PharmGKB; PA33668; -.
DR eggNOG; COG5170; -.
DR HOGENOM; HOG000089745; -.
DR HOVERGEN; HBG000012; -.
DR InParanoid; P63151; -.
DR KO; K04354; -.
DR OMA; GTQQGHH; -.
DR OrthoDB; EOG7Q5HCZ; -.
DR PhylomeDB; P63151; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_71; Gene Expression.
DR SignaLink; P63151; -.
DR ChiTaRS; PPP2R2A; human.
DR EvolutionaryTrace; P63151; -.
DR GeneWiki; PPP2R2A; -.
DR GenomeRNAi; 5520; -.
DR NextBio; 21352; -.
DR PRO; PR:P63151; -.
DR ArrayExpress; P63151; -.
DR Bgee; P63151; -.
DR CleanEx; HS_PPP2R2A; -.
DR Genevestigator; P63151; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0007084; P:mitotic nuclear envelope reassembly; TAS:Reactome.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR000009; PP2A_PR55.
DR InterPro; IPR018067; PP2A_PR55_CS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR PANTHER; PTHR11871; PTHR11871; 1.
DR PIRSF; PIRSF037309; PP2A_PR55; 1.
DR PRINTS; PR00600; PP2APR55.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 3.
DR PROSITE; PS01024; PR55_1; 1.
DR PROSITE; PS01025; PR55_2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Reference proteome; Repeat; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 447 Serine/threonine-protein phosphatase 2A
FT 55 kDa regulatory subunit B alpha
FT isoform.
FT /FTId=PRO_0000071415.
FT REPEAT 26 65 WD 1.
FT REPEAT 91 132 WD 2.
FT REPEAT 175 213 WD 3.
FT REPEAT 224 264 WD 4.
FT REPEAT 283 321 WD 5.
FT REPEAT 338 379 WD 6.
FT REPEAT 414 446 WD 7.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 2 MA -> MFPKFSLRSMFH (in isoform 2).
FT /FTId=VSP_043100.
FT STRAND 13 16
FT STRAND 21 23
FT HELIX 27 29
FT STRAND 30 36
FT STRAND 38 47
FT STRAND 50 57
FT STRAND 71 78
FT STRAND 83 85
FT HELIX 86 88
FT STRAND 90 92
FT STRAND 98 101
FT STRAND 106 114
FT STRAND 119 132
FT STRAND 156 172
FT STRAND 182 185
FT STRAND 189 195
FT STRAND 197 204
FT STRAND 207 216
FT HELIX 222 224
FT STRAND 229 234
FT STRAND 241 246
FT STRAND 251 255
FT TURN 256 258
FT STRAND 260 262
FT STRAND 267 269
FT HELIX 280 284
FT STRAND 288 293
FT STRAND 297 312
FT STRAND 323 325
FT HELIX 327 329
FT TURN 330 332
FT HELIX 333 338
FT HELIX 341 343
FT STRAND 348 350
FT STRAND 354 360
FT STRAND 365 370
FT TURN 371 373
FT STRAND 376 380
FT HELIX 410 412
FT STRAND 421 424
FT STRAND 426 434
FT STRAND 439 443
SQ SEQUENCE 447 AA; 51692 MW; F4D407FF7ADA4ED6 CRC64;
MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE
NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK
LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI
NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN
TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM
MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG
SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL
HTAWHPKENI IAVATTNNLY IFQDKVN
//
ID 2ABA_HUMAN Reviewed; 447 AA.
AC P63151; B2RBU8; B4E1T7; P50409; Q00007;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 27-SEP-2004, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform;
DE AltName: Full=PP2A subunit B isoform B55-alpha;
DE AltName: Full=PP2A subunit B isoform PR55-alpha;
DE AltName: Full=PP2A subunit B isoform R2-alpha;
DE AltName: Full=PP2A subunit B isoform alpha;
GN Name=PPP2R2A;
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 1), AND TISSUE SPECIFICITY.
RC TISSUE=Lung fibroblast;
RX PubMed=1849734; DOI=10.1021/bi00229a001;
RA Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J.,
RA Merlevede W., Hofsteenge J., Hemmings B.A.;
RT "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A:
RT evidence for a neuronal-specific isoform.";
RL Biochemistry 30:3589-3597(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Blood;
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 [6]
RP INTERACTION WITH TP53.
RX PubMed=17245430; DOI=10.1038/sj.emboj.7601519;
RA Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.;
RT "A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-
RT induced dephosphorylation of p53 at Thr55.";
RL EMBO J. 26:402-411(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(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.
CC -!- SUBUNIT: Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
CC PPP2R2A, PPP2R5E and TBCD (By similarity). PP2A consists of a
CC common heterodimeric core enzyme, composed of a 36 kDa catalytic
CC subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65
CC or subunit A), that associates with a variety of regulatory
CC subunits. Proteins that associate with the core dimer include
CC 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
CC variable regulatory subunit, viral proteins, and cell signaling
CC molecules. Interacts with TP53.
CC -!- INTERACTION:
CC P30153:PPP2R1A; NbExp=8; IntAct=EBI-1048931, EBI-302388;
CC P30154:PPP2R1B; NbExp=2; IntAct=EBI-1048931, EBI-357094;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P63151-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P63151-2; Sequence=VSP_043100;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B
CC family.
CC -!- SIMILARITY: Contains 7 WD repeats.
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DR EMBL; M64929; AAA36490.1; -; mRNA.
DR EMBL; AK303981; BAG64899.1; -; mRNA.
DR EMBL; AK314823; BAG37345.1; -; mRNA.
DR EMBL; AC022911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63578.1; -; Genomic_DNA.
DR EMBL; BC041071; AAH41071.1; -; mRNA.
DR PIR; A38351; A38351.
DR RefSeq; NP_001171062.1; NM_001177591.1.
DR RefSeq; NP_002708.1; NM_002717.3.
DR UniGene; Hs.146339; -.
DR PDB; 3DW8; X-ray; 2.85 A; B/E=1-447.
DR PDBsum; 3DW8; -.
DR ProteinModelPortal; P63151; -.
DR SMR; P63151; 8-446.
DR DIP; DIP-29398N; -.
DR IntAct; P63151; 16.
DR MINT; MINT-2835351; -.
DR STRING; 9606.ENSP00000370113; -.
DR BindingDB; P63151; -.
DR ChEMBL; CHEMBL4284; -.
DR PhosphoSite; P63151; -.
DR DMDM; 52783535; -.
DR PaxDb; P63151; -.
DR PeptideAtlas; P63151; -.
DR PRIDE; P63151; -.
DR DNASU; 5520; -.
DR Ensembl; ENST00000315985; ENSP00000325074; ENSG00000221914.
DR Ensembl; ENST00000380737; ENSP00000370113; ENSG00000221914.
DR GeneID; 5520; -.
DR KEGG; hsa:5520; -.
DR UCSC; uc003xeu.3; human.
DR CTD; 5520; -.
DR GeneCards; GC08P026204; -.
DR HGNC; HGNC:9304; PPP2R2A.
DR MIM; 604941; gene.
DR neXtProt; NX_P63151; -.
DR PharmGKB; PA33668; -.
DR eggNOG; COG5170; -.
DR HOGENOM; HOG000089745; -.
DR HOVERGEN; HBG000012; -.
DR InParanoid; P63151; -.
DR KO; K04354; -.
DR OMA; GTQQGHH; -.
DR OrthoDB; EOG7Q5HCZ; -.
DR PhylomeDB; P63151; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_71; Gene Expression.
DR SignaLink; P63151; -.
DR ChiTaRS; PPP2R2A; human.
DR EvolutionaryTrace; P63151; -.
DR GeneWiki; PPP2R2A; -.
DR GenomeRNAi; 5520; -.
DR NextBio; 21352; -.
DR PRO; PR:P63151; -.
DR ArrayExpress; P63151; -.
DR Bgee; P63151; -.
DR CleanEx; HS_PPP2R2A; -.
DR Genevestigator; P63151; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0010467; P:gene expression; TAS:Reactome.
DR GO; GO:0007084; P:mitotic nuclear envelope reassembly; TAS:Reactome.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR000009; PP2A_PR55.
DR InterPro; IPR018067; PP2A_PR55_CS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR PANTHER; PTHR11871; PTHR11871; 1.
DR PIRSF; PIRSF037309; PP2A_PR55; 1.
DR PRINTS; PR00600; PP2APR55.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 3.
DR PROSITE; PS01024; PR55_1; 1.
DR PROSITE; PS01025; PR55_2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Reference proteome; Repeat; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 447 Serine/threonine-protein phosphatase 2A
FT 55 kDa regulatory subunit B alpha
FT isoform.
FT /FTId=PRO_0000071415.
FT REPEAT 26 65 WD 1.
FT REPEAT 91 132 WD 2.
FT REPEAT 175 213 WD 3.
FT REPEAT 224 264 WD 4.
FT REPEAT 283 321 WD 5.
FT REPEAT 338 379 WD 6.
FT REPEAT 414 446 WD 7.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 2 MA -> MFPKFSLRSMFH (in isoform 2).
FT /FTId=VSP_043100.
FT STRAND 13 16
FT STRAND 21 23
FT HELIX 27 29
FT STRAND 30 36
FT STRAND 38 47
FT STRAND 50 57
FT STRAND 71 78
FT STRAND 83 85
FT HELIX 86 88
FT STRAND 90 92
FT STRAND 98 101
FT STRAND 106 114
FT STRAND 119 132
FT STRAND 156 172
FT STRAND 182 185
FT STRAND 189 195
FT STRAND 197 204
FT STRAND 207 216
FT HELIX 222 224
FT STRAND 229 234
FT STRAND 241 246
FT STRAND 251 255
FT TURN 256 258
FT STRAND 260 262
FT STRAND 267 269
FT HELIX 280 284
FT STRAND 288 293
FT STRAND 297 312
FT STRAND 323 325
FT HELIX 327 329
FT TURN 330 332
FT HELIX 333 338
FT HELIX 341 343
FT STRAND 348 350
FT STRAND 354 360
FT STRAND 365 370
FT TURN 371 373
FT STRAND 376 380
FT HELIX 410 412
FT STRAND 421 424
FT STRAND 426 434
FT STRAND 439 443
SQ SEQUENCE 447 AA; 51692 MW; F4D407FF7ADA4ED6 CRC64;
MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE
NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK
LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI
NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN
TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM
MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG
SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL
HTAWHPKENI IAVATTNNLY IFQDKVN
//
MIM
604941
*RECORD*
*FIELD* NO
604941
*FIELD* TI
*604941 PROTEIN PHOSPHATASE 2, REGULATORY SUBUNIT B, ALPHA; PPP2R2A
;;PR55-ALPHA;;
read moreB55-ALPHA
*FIELD* TX
CLONING
Protein phosphorylation on serine and threonine residues by protein
kinases is responsible for the communication of many intracellular
signals. Equally important is the dephosphorylation of proteins by
serine/threonine phosphatases. Protein phosphatase-2A (PP2A; see
176915), a heterotrimeric serine/threonine phosphatase, has a
particularly complex set of regulatory subunits controlling its function
and localization. By screening lung fibroblast and fetal brain cDNA
libraries using 2 overlapping oligonucleotides corresponding to a
tryptic peptide derived from the 55-kD subunit of rabbit PP2A (PR55),
Mayer et al. (1991) isolated human cDNAs encoding PPP2R2A and PPP2R2B
(604325), which they termed PR55-alpha and PR55-beta, respectively. The
deduced 447-amino acid PPP2R2A protein has a calculated molecular mass
of approximately 52 kD. SDS-PAGE analysis, however, showed that PPP2R2A
was expressed as a 55-kD protein. The nucleotide sequence of PPP2R2A is
75% identical to PPP2R2B in the coding region. Northern blot analysis
detected PPP2R2A transcripts of 2.3 and 2.5 kb, as well as a less
abundant one of 4.4 kb, in all cell lines examined.
GENE FUNCTION
Hyperphosphorylation of Tau (MAPT; 157140) contributes to Alzheimer
disease (104300), and PP2A dephosphorylates Tau, reducing its
deleterious effect. Using an in vitro assay with recombinant human
proteins, Xu et al. (2008) showed that the B-alpha subunit specifically
and markedly facilitated dephosphorylation of phosphorylated Tau by
heterotrimeric PP2A.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PPP2R2A
gene to chromosome 8 (TMAP WI-18898).
*FIELD* RF
1. Mayer, R. E.; Hendrix, P.; Cron, P.; Matthies, R.; Stone, S. R.;
Goris, J.; Merlevede, W.; Hofsteenge, J.; Hemmings, B. A.: Structure
of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence
for a neuronal-specific isoform. Biochemistry 30: 3589-3597, 1991.
2. Xu, Y.; Chen, Y.; Zhang, P.; Jeffrey, P. D.; Shi, Y.: Structure
of a protein phosphatase 2A holoenzyme: insights into B55-mediated
Tau dephosphorylation. Molec. Cell 31: 873-885, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 5/29/2009
*FIELD* CD
Paul J. Converse: 5/9/2000
*FIELD* ED
mgross: 06/02/2009
terry: 5/29/2009
mgross: 12/1/2006
mgross: 5/10/2000
mgross: 5/9/2000
*RECORD*
*FIELD* NO
604941
*FIELD* TI
*604941 PROTEIN PHOSPHATASE 2, REGULATORY SUBUNIT B, ALPHA; PPP2R2A
;;PR55-ALPHA;;
read moreB55-ALPHA
*FIELD* TX
CLONING
Protein phosphorylation on serine and threonine residues by protein
kinases is responsible for the communication of many intracellular
signals. Equally important is the dephosphorylation of proteins by
serine/threonine phosphatases. Protein phosphatase-2A (PP2A; see
176915), a heterotrimeric serine/threonine phosphatase, has a
particularly complex set of regulatory subunits controlling its function
and localization. By screening lung fibroblast and fetal brain cDNA
libraries using 2 overlapping oligonucleotides corresponding to a
tryptic peptide derived from the 55-kD subunit of rabbit PP2A (PR55),
Mayer et al. (1991) isolated human cDNAs encoding PPP2R2A and PPP2R2B
(604325), which they termed PR55-alpha and PR55-beta, respectively. The
deduced 447-amino acid PPP2R2A protein has a calculated molecular mass
of approximately 52 kD. SDS-PAGE analysis, however, showed that PPP2R2A
was expressed as a 55-kD protein. The nucleotide sequence of PPP2R2A is
75% identical to PPP2R2B in the coding region. Northern blot analysis
detected PPP2R2A transcripts of 2.3 and 2.5 kb, as well as a less
abundant one of 4.4 kb, in all cell lines examined.
GENE FUNCTION
Hyperphosphorylation of Tau (MAPT; 157140) contributes to Alzheimer
disease (104300), and PP2A dephosphorylates Tau, reducing its
deleterious effect. Using an in vitro assay with recombinant human
proteins, Xu et al. (2008) showed that the B-alpha subunit specifically
and markedly facilitated dephosphorylation of phosphorylated Tau by
heterotrimeric PP2A.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PPP2R2A
gene to chromosome 8 (TMAP WI-18898).
*FIELD* RF
1. Mayer, R. E.; Hendrix, P.; Cron, P.; Matthies, R.; Stone, S. R.;
Goris, J.; Merlevede, W.; Hofsteenge, J.; Hemmings, B. A.: Structure
of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence
for a neuronal-specific isoform. Biochemistry 30: 3589-3597, 1991.
2. Xu, Y.; Chen, Y.; Zhang, P.; Jeffrey, P. D.; Shi, Y.: Structure
of a protein phosphatase 2A holoenzyme: insights into B55-mediated
Tau dephosphorylation. Molec. Cell 31: 873-885, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 5/29/2009
*FIELD* CD
Paul J. Converse: 5/9/2000
*FIELD* ED
mgross: 06/02/2009
terry: 5/29/2009
mgross: 12/1/2006
mgross: 5/10/2000
mgross: 5/9/2000