2AAB_HUMAN
ID 2AAB_HUMAN Reviewed; 601 AA.
AC P30154; A8MY67; B0YJ69; B4DGQ6; B4DK91; B4DWW5; F8W8G1; O75620; Q8NHV8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform;
DE AltName: Full=PP2A subunit A isoform PR65-beta;
DE AltName: Full=PP2A subunit A isoform R1-beta;
GN Name=PPP2R1B;
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 [GENOMIC DNA].
RX PubMed=9795170; DOI=10.1016/s0378-1119(98)00350-3;
RA Baysal B.E., Farr J.E., Goss J.R., Devlin B., Richard C.W. III;
RT "Genomic organization and precise physical location of protein phosphatase
RT 2A regulatory subunit A beta isoform gene on chromosome band 11q23.";
RL Gene 217:107-116(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-8; SER-65; ASP-90;
RP PRO-101; GLU-343; ALA-448; GLY-504 AND ALA-545.
RX PubMed=9765152; DOI=10.1126/science.282.5387.284;
RA Wang S.S., Esplin E.D., Li J.L., Huang L., Gazdar A., Minna J., Evans G.A.;
RT "Alterations of the PPP2R1B gene in human lung and colon cancer.";
RL Science 282:284-287(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11313745; DOI=10.1038/sj.ejhg.5200585;
RA Baysal B.E., Willett-Brozick J.E., Taschner P.E.M., Dauwerse J.G.,
RA Devilee P., Devlin B.;
RT "A high-resolution integrated map spanning the SDHD gene at 11q23: a 1.1-Mb
RT BAC contig, a partial transcript map and 15 new repeat polymorphisms in a
RT tumour-suppressor region.";
RL Eur. J. Hum. Genet. 9:121-129(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
RC TISSUE=Brain, Testis, and Thalamus;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-601 (ISOFORM 1).
RX PubMed=2159327; DOI=10.1021/bi00465a002;
RA Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J.,
RA Merlevede W., Hofsteenge J., Stone S.R.;
RT "Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have
RT a similar 39 amino acid repeating structure.";
RL Biochemistry 29:3166-3173(1990).
RN [10]
RP INTERACTION WITH RAF1.
RX PubMed=10801873; DOI=10.1074/jbc.m003259200;
RA Abraham D., Podar K., Pacher M., Kubicek M., Welzel N., Hemmings B.A.,
RA Dilworth S.M., Mischak H., Kolch W., Baccarini M.;
RT "Raf-1-associated protein phosphatase 2A as a positive regulator of kinase
RT activation.";
RL J. Biol. Chem. 275:22300-22304(2000).
RN [11]
RP INTERACTION WITH IPO9.
RX PubMed=12670497; DOI=10.1016/s0006-291x(03)00434-0;
RA Lubert E.J., Sarge K.D.;
RT "Interaction between protein phosphatase 2A and members of the importin
RT beta superfamily.";
RL Biochem. Biophys. Res. Commun. 303:908-913(2003).
RN [12]
RP 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 [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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).
RN [16]
RP VARIANT ASP-90.
RX PubMed=10597236; DOI=10.1038/sj.onc.1203070;
RA Campbell I.G., Manolitsas T.;
RT "Absence of PPP2R1B gene alterations in primary ovarian cancers.";
RL Oncogene 18:6367-6369(1999).
RN [17]
RP VARIANTS ALA-15; PRO-365; GLU-498; ILE-499 AND GLY-500.
RX PubMed=10896920; DOI=10.1136/gut.47.2.268;
RA Takagi Y., Futamura M., Yamaguchi K., Aoki S., Takahashi T., Saji S.;
RT "Alterations of the PPP2R1B gene located at 11q23 in human colorectal
RT cancers.";
RL Gut 47:268-271(2000).
RN [18]
RP VARIANT ASP-90.
RX PubMed=11996789; DOI=10.1016/s0165-4608(01)00597-0;
RA Hemmer S., Wasenius V.M., Haglund C., Zhu Y., Knuutila S., Franssila K.,
RA Joensuu H.;
RT "Alterations in the suppressor gene PPP2R1B in parathyroid hyperplasias and
RT adenomas.";
RL Cancer Genet. Cytogenet. 134:13-17(2002).
CC -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a
CC scaffolding molecule to coordinate the assembly of the catalytic
CC subunit and a variable regulatory B subunit.
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 IPO9. Interacts with SGO1. Interacts with RAF1.
CC {ECO:0000269|PubMed:10801873, ECO:0000269|PubMed:12670497,
CC ECO:0000269|PubMed:16541025}.
CC -!- INTERACTION:
CC P30154; P67775: PPP2CA; NbExp=8; IntAct=EBI-357094, EBI-712311;
CC P30154; P30153: PPP2R1A; NbExp=2; IntAct=EBI-357094, EBI-302388;
CC P30154; P63151: PPP2R2A; NbExp=5; IntAct=EBI-357094, EBI-1048931;
CC P30154; Q15172: PPP2R5A; NbExp=2; IntAct=EBI-357094, EBI-641666;
CC P30154; Q13362: PPP2R5C; NbExp=2; IntAct=EBI-357094, EBI-1266156;
CC P30154; Q14738: PPP2R5D; NbExp=3; IntAct=EBI-357094, EBI-396563;
CC P30154; Q16537: PPP2R5E; NbExp=3; IntAct=EBI-357094, EBI-968374;
CC P30154; P11233: RALA; NbExp=6; IntAct=EBI-357094, EBI-1036803;
CC P30154; O08785: Clock; Xeno; NbExp=2; IntAct=EBI-357094, EBI-79859;
CC P30154; O08722: Unc5b; Xeno; NbExp=4; IntAct=EBI-357094, EBI-4404185;
CC P30154-2; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-11058011, EBI-12593112;
CC P30154-2; O14901: KLF11; NbExp=3; IntAct=EBI-11058011, EBI-948266;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P30154-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30154-2; Sequence=VSP_036460;
CC Name=3;
CC IsoId=P30154-3; Sequence=VSP_043379, VSP_036460;
CC Name=4;
CC IsoId=P30154-4; Sequence=VSP_045275;
CC Name=5;
CC IsoId=P30154-5; Sequence=VSP_046684;
CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices joined
CC by a hydrophilic region, the intrarepeat loop. The repeat units may be
CC arranged laterally to form a rod-like structure.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA59983.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=BAG59103.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF083439; AAC63525.1; -; Genomic_DNA.
DR EMBL; AF083425; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF083426; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF083427; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF083428; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF083429; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF083430; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF083431; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF083432; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF083433; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF083434; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF083435; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF083436; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF083437; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF083438; AAC63525.1; JOINED; Genomic_DNA.
DR EMBL; AF087438; AAC69624.1; -; mRNA.
DR EMBL; AF163473; AAG39644.1; -; mRNA.
DR EMBL; AK294716; BAG57867.1; -; mRNA.
DR EMBL; AK296455; BAG59103.1; ALT_FRAME; mRNA.
DR EMBL; AK301705; BAG63177.1; -; mRNA.
DR EMBL; EF445011; ACA06046.1; -; Genomic_DNA.
DR EMBL; EF445011; ACA06047.1; -; Genomic_DNA.
DR EMBL; AP000925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP001781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67150.1; -; Genomic_DNA.
DR EMBL; CH471065; EAW67151.1; -; Genomic_DNA.
DR EMBL; BC027596; AAH27596.1; -; mRNA.
DR EMBL; M65254; AAA59983.1; ALT_SEQ; mRNA.
DR CCDS; CCDS53706.1; -. [P30154-3]
DR CCDS; CCDS53707.1; -. [P30154-5]
DR CCDS; CCDS53708.1; -. [P30154-4]
DR CCDS; CCDS8348.1; -. [P30154-2]
DR CCDS; CCDS8349.1; -. [P30154-1]
DR PIR; B34541; B34541.
DR RefSeq; NP_001171033.1; NM_001177562.1. [P30154-4]
DR RefSeq; NP_001171034.1; NM_001177563.1. [P30154-5]
DR RefSeq; NP_002707.3; NM_002716.4. [P30154-1]
DR RefSeq; NP_859050.1; NM_181699.2. [P30154-2]
DR RefSeq; NP_859051.1; NM_181700.1. [P30154-3]
DR AlphaFoldDB; P30154; -.
DR SMR; P30154; -.
DR BioGRID; 111511; 174.
DR CORUM; P30154; -.
DR DIP; DIP-36616N; -.
DR IntAct; P30154; 107.
DR MINT; P30154; -.
DR STRING; 9606.ENSP00000311344; -.
DR GlyGen; P30154; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P30154; -.
DR MetOSite; P30154; -.
DR PhosphoSitePlus; P30154; -.
DR SwissPalm; P30154; -.
DR BioMuta; PPP2R1B; -.
DR DMDM; 116241236; -.
DR EPD; P30154; -.
DR jPOST; P30154; -.
DR MassIVE; P30154; -.
DR MaxQB; P30154; -.
DR PaxDb; P30154; -.
DR PeptideAtlas; P30154; -.
DR PRIDE; P30154; -.
DR ProteomicsDB; 2377; -.
DR ProteomicsDB; 30144; -.
DR ProteomicsDB; 54637; -.
DR ProteomicsDB; 54638; -. [P30154-2]
DR ProteomicsDB; 54639; -. [P30154-3]
DR Antibodypedia; 3416; 312 antibodies from 36 providers.
DR DNASU; 5519; -.
DR Ensembl; ENST00000311129.9; ENSP00000311344.5; ENSG00000137713.16. [P30154-2]
DR Ensembl; ENST00000341980.10; ENSP00000343317.6; ENSG00000137713.16. [P30154-4]
DR Ensembl; ENST00000393055.6; ENSP00000376775.2; ENSG00000137713.16. [P30154-5]
DR Ensembl; ENST00000426998.6; ENSP00000410671.2; ENSG00000137713.16. [P30154-3]
DR Ensembl; ENST00000527614.6; ENSP00000437193.1; ENSG00000137713.16. [P30154-1]
DR GeneID; 5519; -.
DR KEGG; hsa:5519; -.
DR MANE-Select; ENST00000527614.6; ENSP00000437193.1; NM_002716.5; NP_002707.3.
DR UCSC; uc001plw.2; human. [P30154-1]
DR CTD; 5519; -.
DR DisGeNET; 5519; -.
DR GeneCards; PPP2R1B; -.
DR HGNC; HGNC:9303; PPP2R1B.
DR HPA; ENSG00000137713; Tissue enhanced (liver).
DR MalaCards; PPP2R1B; -.
DR MIM; 603113; gene.
DR neXtProt; NX_P30154; -.
DR OpenTargets; ENSG00000137713; -.
DR PharmGKB; PA33667; -.
DR VEuPathDB; HostDB:ENSG00000137713; -.
DR eggNOG; KOG0211; Eukaryota.
DR GeneTree; ENSGT00950000183066; -.
DR HOGENOM; CLU_015533_2_1_1; -.
DR InParanoid; P30154; -.
DR OMA; SSLCMSW; -.
DR OrthoDB; 447572at2759; -.
DR PhylomeDB; P30154; -.
DR TreeFam; TF105552; -.
DR PathwayCommons; P30154; -.
DR Reactome; R-HSA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-163685; Integration of energy metabolism.
DR Reactome; R-HSA-163767; PP2A-mediated dephosphorylation of key metabolic factors.
DR Reactome; R-HSA-180024; DARPP-32 events.
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-198753; ERK/MAPK targets.
DR Reactome; R-HSA-202670; ERKs are inactivated.
DR Reactome; R-HSA-2465910; MASTL Facilitates Mitotic Progression.
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-6804757; Regulation of TP53 Degradation.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-HSA-9634600; Regulation of glycolysis by fructose 2,6-bisphosphate metabolism.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; P30154; -.
DR SIGNOR; P30154; -.
DR BioGRID-ORCS; 5519; 15 hits in 1083 CRISPR screens.
DR ChiTaRS; PPP2R1B; human.
DR GeneWiki; PPP2R1B; -.
DR GenomeRNAi; 5519; -.
DR Pharos; P30154; Tbio.
DR PRO; PR:P30154; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P30154; protein.
DR Bgee; ENSG00000137713; Expressed in sperm and 195 other tissues.
DR ExpressionAtlas; P30154; baseline and differential.
DR Genevisible; P30154; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; IMP:UniProtKB.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR Pfam; PF02985; HEAT; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 12.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..601
FT /note="Serine/threonine-protein phosphatase 2A 65 kDa
FT regulatory subunit A beta isoform"
FT /id="PRO_0000071403"
FT REPEAT 20..58
FT /note="HEAT 1"
FT REPEAT 59..96
FT /note="HEAT 2"
FT REPEAT 97..135
FT /note="HEAT 3"
FT REPEAT 136..173
FT /note="HEAT 4"
FT REPEAT 174..212
FT /note="HEAT 5"
FT REPEAT 213..251
FT /note="HEAT 6"
FT REPEAT 252..290
FT /note="HEAT 7"
FT REPEAT 291..333
FT /note="HEAT 8"
FT REPEAT 334..372
FT /note="HEAT 9"
FT REPEAT 373..411
FT /note="HEAT 10"
FT REPEAT 412..450
FT /note="HEAT 11"
FT REPEAT 451..489
FT /note="HEAT 12"
FT REPEAT 490..528
FT /note="HEAT 13"
FT REPEAT 529..567
FT /note="HEAT 14"
FT REPEAT 568..601
FT /note="HEAT 15"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 39..102
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043379"
FT VAR_SEQ 103..229
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046684"
FT VAR_SEQ 344..388
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045275"
FT VAR_SEQ 598..601
FT /note="LALA -> VAQRLRKLEFPVKDSGEPSVPRADKNHFPRPTVPGEDMGKGPVY
FT QLRGDTRDTLAQLGIAELVHFSQSTD (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036460"
FT VARIANT 8
FT /note="G -> R (in a lung cancer patient;
FT dbSNP:rs142771326)"
FT /evidence="ECO:0000269|PubMed:9765152"
FT /id="VAR_022895"
FT VARIANT 15
FT /note="G -> A (in a colorectal cancer patient)"
FT /evidence="ECO:0000269|PubMed:10896920"
FT /id="VAR_022896"
FT VARIANT 65
FT /note="P -> S (in a lung cancer patient)"
FT /evidence="ECO:0000269|PubMed:9765152"
FT /id="VAR_022897"
FT VARIANT 90
FT /note="G -> D (in a lung cancer patient; dbSNP:rs1805076)"
FT /evidence="ECO:0000269|PubMed:10597236,
FT ECO:0000269|PubMed:11996789, ECO:0000269|PubMed:9765152"
FT /id="VAR_006384"
FT VARIANT 101
FT /note="L -> P (in a colon adenocarcinoma)"
FT /evidence="ECO:0000269|PubMed:9765152"
FT /id="VAR_022898"
FT VARIANT 343
FT /note="K -> E (in a lung cancer patient)"
FT /evidence="ECO:0000269|PubMed:9765152"
FT /id="VAR_022899"
FT VARIANT 365
FT /note="S -> P (in a colorectal cancer patient;
FT dbSNP:rs1442893893)"
FT /evidence="ECO:0000269|PubMed:10896920"
FT /id="VAR_022900"
FT VARIANT 448
FT /note="V -> A (in a colon adenocarcinoma)"
FT /evidence="ECO:0000269|PubMed:9765152"
FT /id="VAR_022901"
FT VARIANT 498
FT /note="V -> E (in a colorectal cancer patient)"
FT /evidence="ECO:0000269|PubMed:10896920"
FT /id="VAR_022902"
FT VARIANT 499
FT /note="L -> I (in a colorectal cancer patient)"
FT /evidence="ECO:0000269|PubMed:10896920"
FT /id="VAR_022903"
FT VARIANT 500
FT /note="V -> G (in a colorectal cancer patient)"
FT /evidence="ECO:0000269|PubMed:10896920"
FT /id="VAR_022904"
FT VARIANT 504
FT /note="D -> G (in a lung cancer patient;
FT dbSNP:rs973682124)"
FT /evidence="ECO:0000269|PubMed:9765152"
FT /id="VAR_022905"
FT VARIANT 545
FT /note="V -> A (in a colon adenocarcinoma;
FT dbSNP:rs1318084062)"
FT /evidence="ECO:0000269|PubMed:9765152"
FT /id="VAR_022906"
FT CONFLICT 74
FT /note="E -> V (in Ref. 9; AAA59983)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="I -> T (in Ref. 1; AAC63525, 3; AAG39644 and 9;
FT AAA59983)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="D -> G (in Ref. 4; BAG57867)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="Q -> R (in Ref. 9; AAA59983)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="N -> S (in Ref. 4; BAG57867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 66214 MW; 86AB20D7505210B0 CRC64;
MAGASELGTG PGAAGGDGDD SLYPIAVLID ELRNEDVQLR LNSIKKLSTI ALALGVERTR
SELLPFLTDT IYDEDEVLLA LAEQLGNFTG LVGGPDFAHC LLPPLENLAT VEETVVRDKA
VESLRQISQE HTPVALEAYF VPLVKRLASG DWFTSRTSAC GLFSVCYPRA SNAVKAEIRQ
QFRSLCSDDT PMVRRAAASK LGEFAKVLEL DSVKSEIVPL FTSLASDEQD SVRLLAVEAC
VSIAQLLSQD DLETLVMPTL RQAAEDKSWR VRYMVADRFS ELQKAMGPKI TLNDLIPAFQ
NLLKDCEAEV RAAAAHKVKE LGENLPIEDR ETIIMNQILP YIKELVSDTN QHVKSALASV
IMGLSTILGK ENTIEHLLPL FLAQLKDECP DVRLNIISNL DCVNEVIGIR QLSQSLLPAI
VELAEDAKWR VRLAIIEYMP LLAGQLGVEF FDEKLNSLCM AWLVDHVYAI REAATNNLMK
LVQKFGTEWA QNTIVPKVLV MANDPNYLHR MTTLFCINAL SEACGQEITT KQMLPIVLKM
AGDQVANVRF NVAKSLQKIG PILDTNALQG EVKPVLQKLG QDEDMDVKYF AQEAISVLAL
A
