Full text data of PPP2R5A
PPP2R5A
[Confidence: low (only semi-automatic identification from reviews)]
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform (PP2A B subunit isoform B'-alpha; PP2A B subunit isoform B56-alpha; PP2A B subunit isoform PR61-alpha; PR61alpha; PP2A B subunit isoform R5-alpha)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform (PP2A B subunit isoform B'-alpha; PP2A B subunit isoform B56-alpha; PP2A B subunit isoform PR61-alpha; PR61alpha; PP2A B subunit isoform R5-alpha)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15172
ID 2A5A_HUMAN Reviewed; 486 AA.
AC Q15172; B2R6D2; B7Z7L2; D3DT99; Q2NL72; Q5VVB2; Q8TBI9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform;
DE AltName: Full=PP2A B subunit isoform B'-alpha;
DE AltName: Full=PP2A B subunit isoform B56-alpha;
DE AltName: Full=PP2A B subunit isoform PR61-alpha;
DE Short=PR61alpha;
DE AltName: Full=PP2A B subunit isoform R5-alpha;
GN Name=PPP2R5A;
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).
RC TISSUE=Mammary cancer;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Tongue;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(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=Hippocampus, and Testis;
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 PROTEIN SEQUENCE OF 47-56; 129-132; 347-354; 448-462 AND 471-480.
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 [7]
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 [8]
RP SUBCELLULAR LOCATION, AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(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: 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.
CC -!- INTERACTION:
CC O96017:CHEK2; NbExp=2; IntAct=EBI-641666, EBI-1180783;
CC Q9BVP2:GNL3; NbExp=3; IntAct=EBI-641666, EBI-641642;
CC P67775:PPP2CA; NbExp=3; IntAct=EBI-641666, EBI-712311;
CC P30153:PPP2R1A; NbExp=3; IntAct=EBI-641666, EBI-302388;
CC P30154:PPP2R1B; NbExp=2; IntAct=EBI-641666, EBI-357094;
CC Q5FBB7:SGOL1; NbExp=3; IntAct=EBI-641666, EBI-989069;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere.
CC Note=From mitotic prophase to metaphase, localizes at the inner
CC centromere between a pair of sister kinetochores. Decreased
CC expression at the onset of anaphase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15172-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15172-2; Sequence=VSP_042889;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed with the highest expression
CC in heart and skeletal muscle.
CC -!- PTM: Phosphorylated on serine residues.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family.
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DR EMBL; L42373; AAC37601.1; -; mRNA.
DR EMBL; AK302202; BAH13648.1; -; mRNA.
DR EMBL; AK312530; BAG35429.1; -; mRNA.
DR EMBL; AL451060; CAH71821.1; -; Genomic_DNA.
DR EMBL; AL360091; CAH71821.1; JOINED; Genomic_DNA.
DR EMBL; AL360091; CAH73229.1; -; Genomic_DNA.
DR EMBL; AL451060; CAH73229.1; JOINED; Genomic_DNA.
DR EMBL; CH471100; EAW93392.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93393.1; -; Genomic_DNA.
DR EMBL; BC022474; AAH22474.1; -; mRNA.
DR EMBL; BC110883; AAI10884.1; -; mRNA.
DR PIR; I55449; I55449.
DR RefSeq; NP_001186685.1; NM_001199756.1.
DR RefSeq; NP_006234.1; NM_006243.3.
DR UniGene; Hs.744012; -.
DR ProteinModelPortal; Q15172; -.
DR SMR; Q15172; 66-461.
DR DIP; DIP-459N; -.
DR IntAct; Q15172; 19.
DR MINT; MINT-88251; -.
DR STRING; 9606.ENSP00000261461; -.
DR BindingDB; Q15172; -.
DR ChEMBL; CHEMBL4763; -.
DR PhosphoSite; Q15172; -.
DR DMDM; 7387496; -.
DR OGP; Q15172; -.
DR PaxDb; Q15172; -.
DR PeptideAtlas; Q15172; -.
DR PRIDE; Q15172; -.
DR DNASU; 5525; -.
DR Ensembl; ENST00000261461; ENSP00000261461; ENSG00000066027.
DR Ensembl; ENST00000537030; ENSP00000442866; ENSG00000066027.
DR GeneID; 5525; -.
DR KEGG; hsa:5525; -.
DR UCSC; uc001hjb.3; human.
DR CTD; 5525; -.
DR GeneCards; GC01P212458; -.
DR HGNC; HGNC:9309; PPP2R5A.
DR MIM; 601643; gene.
DR neXtProt; NX_Q15172; -.
DR PharmGKB; PA33672; -.
DR eggNOG; NOG264925; -.
DR HOGENOM; HOG000067326; -.
DR HOVERGEN; HBG000009; -.
DR InParanoid; Q15172; -.
DR KO; K11584; -.
DR OMA; YITHGRG; -.
DR OrthoDB; EOG7C2R2S; -.
DR PhylomeDB; Q15172; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q15172; -.
DR ChiTaRS; PPP2R5A; human.
DR GeneWiki; PPP2R5A; -.
DR GenomeRNAi; 5525; -.
DR NextBio; 21392; -.
DR PRO; PR:Q15172; -.
DR Bgee; Q15172; -.
DR CleanEx; HS_PPP2R5A; -.
DR Genevestigator; Q15172; -.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0031430; C:M band; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:ProtInc.
DR GO; GO:0090005; P:negative regulation of establishment of protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0090219; P:negative regulation of lipid kinase activity; IMP:BHF-UCL.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; Centromere; Chromosome; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 486 Serine/threonine-protein phosphatase 2A
FT 56 kDa regulatory subunit alpha isoform.
FT /FTId=PRO_0000071448.
FT COMPBIAS 2 5 Poly-Ser.
FT MOD_RES 41 41 Phosphoserine.
FT MOD_RES 42 42 Phosphoserine.
FT VAR_SEQ 1 61 MSSSSPPAGAASAAISASEKVDGFTRKSVRKAQRQKRSQGS
FT SQFRSQGSQAELHPLPQLKD -> MIMN (in isoform
FT 2).
FT /FTId=VSP_042889.
FT CONFLICT 52 52 E -> F (in Ref. 6; AA sequence).
FT CONFLICT 54 54 H -> S (in Ref. 6; AA sequence).
FT CONFLICT 176 176 Q -> R (in Ref. 5; AAH22474).
FT CONFLICT 389 389 D -> N (in Ref. 5; AAH22474).
FT CONFLICT 451 451 R -> E (in Ref. 6; AA sequence).
SQ SEQUENCE 486 AA; 56194 MW; D31407F7032A6D44 CRC64;
MSSSSPPAGA ASAAISASEK VDGFTRKSVR KAQRQKRSQG SSQFRSQGSQ AELHPLPQLK
DATSNEQQEL FCQKLQQCCI LFDFMDSVSD LKSKEIKRAT LNELVEYVST NRGVIVESAY
SDIVKMISAN IFRTLPPSDN PDFDPEEDEP TLEASWPHIQ LVYEFFLRFL ESPDFQPSIA
KRYIDQKFVQ QLLELFDSED PRERDFLKTV LHRIYGKFLG LRAFIRKQIN NIFLRFIYET
EHFNGVAELL EILGSIINGF ALPLKAEHKQ FLMKVLIPMH TAKGLALFHA QLAYCVVQFL
EKDTTLTEPV IRGLLKFWPK TCSQKEVMFL GEIEEILDVI EPTQFKKIEE PLFKQISKCV
SSSHFQVAER ALYFWNNEYI LSLIEENIDK ILPIMFASLY KISKEHWNPT IVALVYNVLK
TLMEMNGKLF DDLTSSYKAE RQREKKKELE REELWKKLEE LKLKKALEKQ NSAYNMHSIL
SNTSAE
//
ID 2A5A_HUMAN Reviewed; 486 AA.
AC Q15172; B2R6D2; B7Z7L2; D3DT99; Q2NL72; Q5VVB2; Q8TBI9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform;
DE AltName: Full=PP2A B subunit isoform B'-alpha;
DE AltName: Full=PP2A B subunit isoform B56-alpha;
DE AltName: Full=PP2A B subunit isoform PR61-alpha;
DE Short=PR61alpha;
DE AltName: Full=PP2A B subunit isoform R5-alpha;
GN Name=PPP2R5A;
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).
RC TISSUE=Mammary cancer;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Tongue;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(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=Hippocampus, and Testis;
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 PROTEIN SEQUENCE OF 47-56; 129-132; 347-354; 448-462 AND 471-480.
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 [7]
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 [8]
RP SUBCELLULAR LOCATION, AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(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: 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.
CC -!- INTERACTION:
CC O96017:CHEK2; NbExp=2; IntAct=EBI-641666, EBI-1180783;
CC Q9BVP2:GNL3; NbExp=3; IntAct=EBI-641666, EBI-641642;
CC P67775:PPP2CA; NbExp=3; IntAct=EBI-641666, EBI-712311;
CC P30153:PPP2R1A; NbExp=3; IntAct=EBI-641666, EBI-302388;
CC P30154:PPP2R1B; NbExp=2; IntAct=EBI-641666, EBI-357094;
CC Q5FBB7:SGOL1; NbExp=3; IntAct=EBI-641666, EBI-989069;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere.
CC Note=From mitotic prophase to metaphase, localizes at the inner
CC centromere between a pair of sister kinetochores. Decreased
CC expression at the onset of anaphase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15172-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15172-2; Sequence=VSP_042889;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed with the highest expression
CC in heart and skeletal muscle.
CC -!- PTM: Phosphorylated on serine residues.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family.
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DR EMBL; L42373; AAC37601.1; -; mRNA.
DR EMBL; AK302202; BAH13648.1; -; mRNA.
DR EMBL; AK312530; BAG35429.1; -; mRNA.
DR EMBL; AL451060; CAH71821.1; -; Genomic_DNA.
DR EMBL; AL360091; CAH71821.1; JOINED; Genomic_DNA.
DR EMBL; AL360091; CAH73229.1; -; Genomic_DNA.
DR EMBL; AL451060; CAH73229.1; JOINED; Genomic_DNA.
DR EMBL; CH471100; EAW93392.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93393.1; -; Genomic_DNA.
DR EMBL; BC022474; AAH22474.1; -; mRNA.
DR EMBL; BC110883; AAI10884.1; -; mRNA.
DR PIR; I55449; I55449.
DR RefSeq; NP_001186685.1; NM_001199756.1.
DR RefSeq; NP_006234.1; NM_006243.3.
DR UniGene; Hs.744012; -.
DR ProteinModelPortal; Q15172; -.
DR SMR; Q15172; 66-461.
DR DIP; DIP-459N; -.
DR IntAct; Q15172; 19.
DR MINT; MINT-88251; -.
DR STRING; 9606.ENSP00000261461; -.
DR BindingDB; Q15172; -.
DR ChEMBL; CHEMBL4763; -.
DR PhosphoSite; Q15172; -.
DR DMDM; 7387496; -.
DR OGP; Q15172; -.
DR PaxDb; Q15172; -.
DR PeptideAtlas; Q15172; -.
DR PRIDE; Q15172; -.
DR DNASU; 5525; -.
DR Ensembl; ENST00000261461; ENSP00000261461; ENSG00000066027.
DR Ensembl; ENST00000537030; ENSP00000442866; ENSG00000066027.
DR GeneID; 5525; -.
DR KEGG; hsa:5525; -.
DR UCSC; uc001hjb.3; human.
DR CTD; 5525; -.
DR GeneCards; GC01P212458; -.
DR HGNC; HGNC:9309; PPP2R5A.
DR MIM; 601643; gene.
DR neXtProt; NX_Q15172; -.
DR PharmGKB; PA33672; -.
DR eggNOG; NOG264925; -.
DR HOGENOM; HOG000067326; -.
DR HOVERGEN; HBG000009; -.
DR InParanoid; Q15172; -.
DR KO; K11584; -.
DR OMA; YITHGRG; -.
DR OrthoDB; EOG7C2R2S; -.
DR PhylomeDB; Q15172; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q15172; -.
DR ChiTaRS; PPP2R5A; human.
DR GeneWiki; PPP2R5A; -.
DR GenomeRNAi; 5525; -.
DR NextBio; 21392; -.
DR PRO; PR:Q15172; -.
DR Bgee; Q15172; -.
DR CleanEx; HS_PPP2R5A; -.
DR Genevestigator; Q15172; -.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0031430; C:M band; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:ProtInc.
DR GO; GO:0090005; P:negative regulation of establishment of protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0090219; P:negative regulation of lipid kinase activity; IMP:BHF-UCL.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; Centromere; Chromosome; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 486 Serine/threonine-protein phosphatase 2A
FT 56 kDa regulatory subunit alpha isoform.
FT /FTId=PRO_0000071448.
FT COMPBIAS 2 5 Poly-Ser.
FT MOD_RES 41 41 Phosphoserine.
FT MOD_RES 42 42 Phosphoserine.
FT VAR_SEQ 1 61 MSSSSPPAGAASAAISASEKVDGFTRKSVRKAQRQKRSQGS
FT SQFRSQGSQAELHPLPQLKD -> MIMN (in isoform
FT 2).
FT /FTId=VSP_042889.
FT CONFLICT 52 52 E -> F (in Ref. 6; AA sequence).
FT CONFLICT 54 54 H -> S (in Ref. 6; AA sequence).
FT CONFLICT 176 176 Q -> R (in Ref. 5; AAH22474).
FT CONFLICT 389 389 D -> N (in Ref. 5; AAH22474).
FT CONFLICT 451 451 R -> E (in Ref. 6; AA sequence).
SQ SEQUENCE 486 AA; 56194 MW; D31407F7032A6D44 CRC64;
MSSSSPPAGA ASAAISASEK VDGFTRKSVR KAQRQKRSQG SSQFRSQGSQ AELHPLPQLK
DATSNEQQEL FCQKLQQCCI LFDFMDSVSD LKSKEIKRAT LNELVEYVST NRGVIVESAY
SDIVKMISAN IFRTLPPSDN PDFDPEEDEP TLEASWPHIQ LVYEFFLRFL ESPDFQPSIA
KRYIDQKFVQ QLLELFDSED PRERDFLKTV LHRIYGKFLG LRAFIRKQIN NIFLRFIYET
EHFNGVAELL EILGSIINGF ALPLKAEHKQ FLMKVLIPMH TAKGLALFHA QLAYCVVQFL
EKDTTLTEPV IRGLLKFWPK TCSQKEVMFL GEIEEILDVI EPTQFKKIEE PLFKQISKCV
SSSHFQVAER ALYFWNNEYI LSLIEENIDK ILPIMFASLY KISKEHWNPT IVALVYNVLK
TLMEMNGKLF DDLTSSYKAE RQREKKKELE REELWKKLEE LKLKKALEKQ NSAYNMHSIL
SNTSAE
//
MIM
601643
*RECORD*
*FIELD* NO
601643
*FIELD* TI
*601643 PROTEIN PHOSPHATASE 2, REGULATORY SUBUNIT B (B56), ALPHA; PPP2R5A
*FIELD* TX
read more
DESCRIPTION
Protein phosphorylation is a regulatory mechanism commonly employed in
cellular processes such as cell cycle progression, growth factor
signaling, and cell transformation. Protein phosphatase 2A (PP2A), a
heterotrimeric serine/threonine phosphatase, has been implicated in a
variety of regulatory processes including cell growth and division,
muscle contraction, and gene transcription. PP2A is a trimeric enzyme
composed of a 36-kD catalytic subunit (176915), a highly homologous
65-kD structural subunit (605983), and any of several different
regulatory subunits which control its specificity. According to McCright
et al. (1996), the B56 family of regulatory subunits is encoded by at
least 5 homologous but distinct genes, termed B56-alpha (PPP2R5A), -beta
(601644), -gamma (601645), -delta (601646), and -epsilon (601647).
GENE FUNCTION
McCright and Virshup (1995) noted that the B56 alpha subunit gene
encodes a cytoplasmic phosphoprotein. The alpha and gamma subunits are
expressed at highest levels in skeletal and cardiac muscle.
MAPPING
McCright et al. (1996) mapped the gene for the alpha subunit, designated
PPP2R5A, to chromosome 1q41 by fluorescence in situ hybridization.
*FIELD* RF
1. 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.
2. 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.
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* CD
Alan F. Scott: 1/23/1997
*FIELD* ED
alopez: 03/08/2012
alopez: 4/27/2010
mark: 2/10/1997
mark: 2/7/1997
jenny: 1/28/1997
mark: 1/23/1997
*RECORD*
*FIELD* NO
601643
*FIELD* TI
*601643 PROTEIN PHOSPHATASE 2, REGULATORY SUBUNIT B (B56), ALPHA; PPP2R5A
*FIELD* TX
read more
DESCRIPTION
Protein phosphorylation is a regulatory mechanism commonly employed in
cellular processes such as cell cycle progression, growth factor
signaling, and cell transformation. Protein phosphatase 2A (PP2A), a
heterotrimeric serine/threonine phosphatase, has been implicated in a
variety of regulatory processes including cell growth and division,
muscle contraction, and gene transcription. PP2A is a trimeric enzyme
composed of a 36-kD catalytic subunit (176915), a highly homologous
65-kD structural subunit (605983), and any of several different
regulatory subunits which control its specificity. According to McCright
et al. (1996), the B56 family of regulatory subunits is encoded by at
least 5 homologous but distinct genes, termed B56-alpha (PPP2R5A), -beta
(601644), -gamma (601645), -delta (601646), and -epsilon (601647).
GENE FUNCTION
McCright and Virshup (1995) noted that the B56 alpha subunit gene
encodes a cytoplasmic phosphoprotein. The alpha and gamma subunits are
expressed at highest levels in skeletal and cardiac muscle.
MAPPING
McCright et al. (1996) mapped the gene for the alpha subunit, designated
PPP2R5A, to chromosome 1q41 by fluorescence in situ hybridization.
*FIELD* RF
1. 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.
2. 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.
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* CD
Alan F. Scott: 1/23/1997
*FIELD* ED
alopez: 03/08/2012
alopez: 4/27/2010
mark: 2/10/1997
mark: 2/7/1997
jenny: 1/28/1997
mark: 1/23/1997