2A5A_HUMAN
ID 2A5A_HUMAN Reviewed; 486 AA.
AC Q15172; B2R6D2; B7Z7L2; D3DT99; Q2NL72; Q5VVB2; Q8TBI9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 198.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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; DOI=10.1042/bj3170187;
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 a
RT 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 both
RT nucleus and cytoplasm.";
RL J. Biol. Chem. 271:22081-22089(1996).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SGO1.
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 cohesin.";
RL Nature 441:46-52(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-42 AND SER-49, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: The B regulatory subunit might modulate substrate selectivity
CC and catalytic activity, and also might direct the localization of the
CC catalytic enzyme to a particular subcellular compartment.
CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC of a 36 kDa catalytic subunit (subunit C) and a 65 kDa constant
CC regulatory subunit (PR65 or subunit A), that associates with a variety
CC of regulatory subunits. Proteins that associate with the core dimer
CC include 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 variable
CC regulatory subunit, viral proteins, and cell signaling molecules.
CC Interacts with SGO1. {ECO:0000269|PubMed:16541025}.
CC -!- INTERACTION:
CC Q15172; P05067: APP; NbExp=3; IntAct=EBI-641666, EBI-77613;
CC Q15172; Q9Y2T1: AXIN2; NbExp=3; IntAct=EBI-641666, EBI-4400025;
CC Q15172; Q9H246: C1orf21; NbExp=5; IntAct=EBI-641666, EBI-10305393;
CC Q15172; O96017: CHEK2; NbExp=2; IntAct=EBI-641666, EBI-1180783;
CC Q15172; Q86YF9: DZIP1; NbExp=4; IntAct=EBI-641666, EBI-998108;
CC Q15172; A6NGS2: ERICH4; NbExp=3; IntAct=EBI-641666, EBI-18398448;
CC Q15172; Q9BVP2: GNL3; NbExp=3; IntAct=EBI-641666, EBI-641642;
CC Q15172; P00540: MOS; NbExp=5; IntAct=EBI-641666, EBI-1757866;
CC Q15172; Q13136: PPFIA1; NbExp=3; IntAct=EBI-641666, EBI-745426;
CC Q15172; P67775: PPP2CA; NbExp=6; IntAct=EBI-641666, EBI-712311;
CC Q15172; P30153: PPP2R1A; NbExp=6; IntAct=EBI-641666, EBI-302388;
CC Q15172; P30154: PPP2R1B; NbExp=2; IntAct=EBI-641666, EBI-357094;
CC Q15172; Q5FBB7: SGO1; NbExp=3; IntAct=EBI-641666, EBI-989069;
CC Q15172; Q9NUL5-4: SHFL; NbExp=3; IntAct=EBI-641666, EBI-11955083;
CC Q15172; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-641666, EBI-5235340;
CC Q15172; P45379-11: TNNT2; NbExp=3; IntAct=EBI-641666, EBI-17559309;
CC Q15172; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-641666, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8703017}. Nucleus
CC {ECO:0000269|PubMed:8703017}. Chromosome, centromere
CC {ECO:0000269|PubMed:16541025}. Note=From mitotic prophase to metaphase,
CC localizes at the inner centromere between a pair of sister
CC kinetochores. Decreased expression at the onset of anaphase.
CC {ECO:0000269|PubMed:16541025}.
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 -!- TISSUE SPECIFICITY: Widely expressed with the highest expression in
CC heart and skeletal muscle.
CC -!- PTM: Phosphorylated on serine residues. {ECO:0000269|PubMed:8703017}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
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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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL360091; -; NOT_ANNOTATED_CDS; 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 CCDS; CCDS1503.1; -. [Q15172-1]
DR CCDS; CCDS55686.1; -. [Q15172-2]
DR PIR; I55449; I55449.
DR RefSeq; NP_001186685.1; NM_001199756.1. [Q15172-2]
DR RefSeq; NP_006234.1; NM_006243.3. [Q15172-1]
DR PDB; 6NTS; EM; 3.63 A; B=1-486.
DR PDBsum; 6NTS; -.
DR AlphaFoldDB; Q15172; -.
DR SMR; Q15172; -.
DR BioGRID; 111517; 69.
DR CORUM; Q15172; -.
DR DIP; DIP-459N; -.
DR ELM; Q15172; -.
DR IntAct; Q15172; 42.
DR MINT; Q15172; -.
DR STRING; 9606.ENSP00000261461; -.
DR BindingDB; Q15172; -.
DR ChEMBL; CHEMBL4763; -.
DR iPTMnet; Q15172; -.
DR PhosphoSitePlus; Q15172; -.
DR BioMuta; PPP2R5A; -.
DR DMDM; 7387496; -.
DR OGP; Q15172; -.
DR EPD; Q15172; -.
DR jPOST; Q15172; -.
DR MassIVE; Q15172; -.
DR MaxQB; Q15172; -.
DR PaxDb; Q15172; -.
DR PeptideAtlas; Q15172; -.
DR PRIDE; Q15172; -.
DR ProteomicsDB; 60481; -.
DR ProteomicsDB; 60482; -. [Q15172-2]
DR Antibodypedia; 34606; 268 antibodies from 37 providers.
DR DNASU; 5525; -.
DR Ensembl; ENST00000261461.7; ENSP00000261461.2; ENSG00000066027.12. [Q15172-1]
DR Ensembl; ENST00000537030.3; ENSP00000442866.1; ENSG00000066027.12. [Q15172-2]
DR GeneID; 5525; -.
DR KEGG; hsa:5525; -.
DR MANE-Select; ENST00000261461.7; ENSP00000261461.2; NM_006243.4; NP_006234.1.
DR UCSC; uc001hjb.3; human. [Q15172-1]
DR CTD; 5525; -.
DR DisGeNET; 5525; -.
DR GeneCards; PPP2R5A; -.
DR HGNC; HGNC:9309; PPP2R5A.
DR HPA; ENSG00000066027; Low tissue specificity.
DR MIM; 601643; gene.
DR neXtProt; NX_Q15172; -.
DR OpenTargets; ENSG00000066027; -.
DR PharmGKB; PA33672; -.
DR VEuPathDB; HostDB:ENSG00000066027; -.
DR eggNOG; KOG2085; Eukaryota.
DR GeneTree; ENSGT01030000234620; -.
DR HOGENOM; CLU_012437_4_0_1; -.
DR InParanoid; Q15172; -.
DR OMA; NHEDQER; -.
DR OrthoDB; 890437at2759; -.
DR PhylomeDB; Q15172; -.
DR TreeFam; TF105556; -.
DR PathwayCommons; Q15172; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
DR Reactome; R-HSA-432142; Platelet sensitization by LDL.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-HSA-5339716; Signaling by GSK3beta mutants.
DR Reactome; R-HSA-5358747; CTNNB1 S33 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358749; CTNNB1 S37 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358751; CTNNB1 S45 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358752; CTNNB1 T41 mutants aren't phosphorylated.
DR Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
DR Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
DR Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-5673000; RAF activation.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q15172; -.
DR SIGNOR; Q15172; -.
DR BioGRID-ORCS; 5525; 17 hits in 1085 CRISPR screens.
DR ChiTaRS; PPP2R5A; human.
DR GeneWiki; PPP2R5A; -.
DR GenomeRNAi; 5525; -.
DR Pharos; Q15172; Tchem.
DR PRO; PR:Q15172; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15172; protein.
DR Bgee; ENSG00000066027; Expressed in monocyte and 203 other tissues.
DR Genevisible; Q15172; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031430; C:M band; ISS:BHF-UCL.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR GO; GO:0019900; F:kinase binding; IPI:BHF-UCL.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; TAS:ProtInc.
DR GO; GO:0090219; P:negative regulation of lipid kinase activity; IMP:BHF-UCL.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:BHF-UCL.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
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 3D-structure; Acetylation; Alternative splicing; Centromere; Chromosome;
KW Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..486
FT /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT regulatory subunit alpha isoform"
FT /id="PRO_0000071448"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..61
FT /note="MSSSSPPAGAASAAISASEKVDGFTRKSVRKAQRQKRSQGSSQFRSQGSQAE
FT LHPLPQLKD -> MIMN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042889"
FT CONFLICT 52
FT /note="E -> F (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="H -> S (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="Q -> R (in Ref. 5; AAH22474)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="D -> N (in Ref. 5; AAH22474)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="R -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
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
