2A5G_HUMAN
ID 2A5G_HUMAN Reviewed; 524 AA.
AC Q13362; B4DYJ8; B5BUA5; F5GWP3; Q14391; Q15060; Q15174; Q6ZN33;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform;
DE AltName: Full=PP2A B subunit isoform B'-gamma;
DE AltName: Full=PP2A B subunit isoform B56-gamma;
DE AltName: Full=PP2A B subunit isoform PR61-gamma;
DE AltName: Full=PP2A B subunit isoform R5-gamma;
DE AltName: Full=Renal carcinoma antigen NY-REN-29;
GN Name=PPP2R5C; Synonyms=KIAA0044;
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 GAMMA-3).
RC TISSUE=Umbilical vein;
RX PubMed=8617797; DOI=10.1074/jbc.271.9.5164;
RA Tehrani M.A., Mumby M.C., Kamibayashi C.;
RT "Identification of a novel protein phosphatase 2A regulatory subunit highly
RT expressed in muscle.";
RL J. Biol. Chem. 271:5164-5170(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-1).
RC TISSUE=Fetal retina;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND PARTIAL NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Hippocampus, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-3).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-524 (ISOFORM GAMMA-2).
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-524 (ISOFORM GAMMA-1).
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 [9]
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 [10]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SGO1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16580887; DOI=10.1016/j.devcel.2006.03.010;
RA Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.;
RT "PP2A is required for centromeric localization of Sgo1 and proper
RT chromosome segregation.";
RL Dev. Cell 10:575-585(2006).
RN [12]
RP FUNCTION, INTERACTION WITH IER3 AND ERK KINASES, AND PHOSPHORYLATION.
RX PubMed=16456541; DOI=10.1038/sj.emboj.7600980;
RA Letourneux C., Rocher G., Porteu F.;
RT "B56-containing PP2A dephosphorylate ERK and their activity is controlled
RT by the early gene IEX-1 and ERK.";
RL EMBO J. 25:727-738(2006).
RN [13]
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 [14]
RP FUNCTION, INTERACTION WITH TP53, AND INDUCTION.
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-induced
RT dephosphorylation of p53 at Thr55.";
RL EMBO J. 26:402-411(2007).
RN [15]
RP INTERACTION WITH TP53.
RX PubMed=17967874; DOI=10.1128/mcb.00983-07;
RA Shouse G.P., Cai X., Liu X.;
RT "Serine 15 phosphorylation of p53 directs its interaction with B56gamma and
RT the tumor suppressor activity of B56gamma-specific protein phosphatase
RT 2A.";
RL Mol. Cell. Biol. 28:448-456(2008).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [17]
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-442 IN COMPLEX WITH PPP2CA AND
RP PPP2R1A.
RX PubMed=17174897; DOI=10.1016/j.cell.2006.11.033;
RA Xu Y., Xing Y., Chen Y., Chao Y., Lin Z., Fan E., Yu J.W., Strack S.,
RA Jeffrey P.D., Shi Y.;
RT "Structure of the protein phosphatase 2A holoenzyme.";
RL Cell 127:1239-1251(2006).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 30-436 IN COMPLEX WITH PPP2CA AND
RP PPP2R1A.
RX PubMed=17086192; DOI=10.1038/nature05351;
RA Cho U.S., Xu W.;
RT "Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme.";
RL Nature 445:53-57(2007).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 34-436 IN COMPLEX WITH PPP2CA;
RP PPP2R1A AND SGO1.
RX PubMed=19716788; DOI=10.1016/j.molcel.2009.06.031;
RA Xu Z., Cetin B., Anger M., Cho U.S., Helmhart W., Nasmyth K., Xu W.;
RT "Structure and function of the PP2A-shugoshin interaction.";
RL Mol. Cell 35:426-441(2009).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 11-380.
RX PubMed=18618707; DOI=10.1002/prot.22150;
RA Magnusdottir A., Stenmark P., Flodin S., Nyman T., Kotenyova T.,
RA Graeslund S., Ogg D., Nordlund P.;
RT "The structure of the PP2A regulatory subunit B56 gamma: the remaining
RT piece of the PP2A jigsaw puzzle.";
RL Proteins 74:212-221(2009).
RN [21]
RP INTERACTION WITH CIP2A.
RX PubMed=28174209; DOI=10.15252/embr.201642788;
RA Wang J., Okkeri J., Pavic K., Wang Z., Kauko O., Halonen T., Sarek G.,
RA Ojala P.M., Rao Z., Xu W., Westermarck J.;
RT "Oncoprotein CIP2A is stabilized via interaction with tumor suppressor
RT PP2A/B56.";
RL EMBO Rep. 18:437-450(2017).
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. The PP2A-
CC PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53
CC and play a role in DNA damage-induced inhibition of cell proliferation.
CC PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK
CC dephosphorylation. {ECO:0000269|PubMed:16456541,
CC ECO:0000269|PubMed:17245430}.
CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed
CC of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa
CC constant regulatory subunit (PR65 or subunit A), that associates with a
CC variety of regulatory subunits. Proteins that associate with the core
CC dimer include three families of regulatory subunits B (the
CC R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48
CC kDa variable regulatory subunit, viral proteins, and cell signaling
CC molecules. Interacts with PPP2CA AND PPP2R1A; the interaction is
CC direct. Interacts with SGO1; the interaction is direct. Isoform 1 and
CC isoform 2 interact with TP53 (phosphorylated at Ser-15 by ATM);
CC increased upon DNA damage it drives PP2A-mediated dephosphorylation of
CC TP53 at Thr-55. Interacts with IER3 and/or ERK kinases; regulates ERK
CC dephosphorylation. Interacts with CIP2A; this interaction stabilizes
CC CIP2A (PubMed:28174209). {ECO:0000269|PubMed:16456541,
CC ECO:0000269|PubMed:16541025, ECO:0000269|PubMed:16580887,
CC ECO:0000269|PubMed:17086192, ECO:0000269|PubMed:17174897,
CC ECO:0000269|PubMed:17245430, ECO:0000269|PubMed:17967874,
CC ECO:0000269|PubMed:19716788, ECO:0000269|PubMed:28174209}.
CC -!- INTERACTION:
CC Q13362; P46695: IER3; NbExp=2; IntAct=EBI-1266156, EBI-1748945;
CC Q13362; Q00987: MDM2; NbExp=5; IntAct=EBI-1266156, EBI-389668;
CC Q13362; P67775: PPP2CA; NbExp=10; IntAct=EBI-1266156, EBI-712311;
CC Q13362; P30153: PPP2R1A; NbExp=10; IntAct=EBI-1266156, EBI-302388;
CC Q13362; P30154: PPP2R1B; NbExp=2; IntAct=EBI-1266156, EBI-357094;
CC Q13362; P04049: RAF1; NbExp=2; IntAct=EBI-1266156, EBI-365996;
CC Q13362; P04637: TP53; NbExp=4; IntAct=EBI-1266156, EBI-366083;
CC Q13362-1; O96017: CHEK2; NbExp=3; IntAct=EBI-1266170, EBI-1180783;
CC Q13362-1; P30153: PPP2R1A; NbExp=5; IntAct=EBI-1266170, EBI-302388;
CC Q13362-2; O96017: CHEK2; NbExp=2; IntAct=EBI-1266173, EBI-1180783;
CC Q13362-2; P30153: PPP2R1A; NbExp=4; IntAct=EBI-1266173, EBI-302388;
CC Q13362-3; O96017: CHEK2; NbExp=4; IntAct=EBI-1266176, EBI-1180783;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=Gamma-3;
CC IsoId=Q13362-1; Sequence=Displayed;
CC Name=Gamma-1;
CC IsoId=Q13362-2; Sequence=VSP_005112;
CC Name=Gamma-2;
CC IsoId=Q13362-3; Sequence=VSP_005113;
CC Name=4;
CC IsoId=Q13362-4; Sequence=VSP_043645, VSP_005113;
CC Name=5;
CC IsoId=Q13362-5; Sequence=VSP_046768;
CC -!- TISSUE SPECIFICITY: Highest levels in heart, skeletal muscle and brain.
CC Lower levels in pancreas, kidney, lung and placenta. Very low levels in
CC liver.
CC -!- INDUCTION: Up-regulated upon DNA damage. {ECO:0000269|PubMed:17245430}.
CC -!- PTM: Isoform Gamma-3 is phosphorylated on serine residues. Isoform
CC Gamma-1 phosphorylation by ERK2 is IER3-dependent and inhibits ERK
CC dephosphorylation by PP2A-PPP2R5C. {ECO:0000269|PubMed:16456541,
CC ECO:0000269|PubMed:8703017}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50387.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG63760.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U37352; AAC50387.1; ALT_INIT; mRNA.
DR EMBL; Z69030; CAA93154.1; -; mRNA.
DR EMBL; AK131391; BAD18542.1; -; mRNA.
DR EMBL; AK302470; BAG63760.1; ALT_INIT; mRNA.
DR EMBL; AB451341; BAG70155.1; -; mRNA.
DR EMBL; AL118558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81756.1; -; Genomic_DNA.
DR EMBL; D26445; BAA05465.1; -; mRNA.
DR EMBL; L42375; AAC37603.1; -; mRNA.
DR CCDS; CCDS45163.1; -. [Q13362-2]
DR CCDS; CCDS53911.1; -. [Q13362-4]
DR CCDS; CCDS53912.1; -. [Q13362-5]
DR CCDS; CCDS9964.1; -. [Q13362-1]
DR CCDS; CCDS9965.1; -. [Q13362-3]
DR RefSeq; NP_001155197.1; NM_001161725.1. [Q13362-5]
DR RefSeq; NP_001155198.1; NM_001161726.1. [Q13362-4]
DR RefSeq; NP_002710.2; NM_002719.3. [Q13362-1]
DR RefSeq; NP_848701.1; NM_178586.2. [Q13362-3]
DR RefSeq; NP_848702.1; NM_178587.2. [Q13362-2]
DR RefSeq; XP_005267884.1; XM_005267827.1.
DR RefSeq; XP_011535222.1; XM_011536920.1.
DR PDB; 2IAE; X-ray; 3.50 A; B/E=30-436.
DR PDB; 2JAK; X-ray; 2.60 A; A=11-380.
DR PDB; 2NPP; X-ray; 3.30 A; B/E=1-442.
DR PDB; 2NYL; X-ray; 3.80 A; B/E=38-425.
DR PDB; 2NYM; X-ray; 3.60 A; B/E=38-425.
DR PDB; 3FGA; X-ray; 2.70 A; B=34-436.
DR PDB; 5JJA; X-ray; 2.35 A; A/B=30-380.
DR PDB; 5K6S; X-ray; 2.79 A; A=31-380.
DR PDB; 5SW9; X-ray; 2.85 A; A=31-380.
DR PDB; 5SWF; X-ray; 2.82 A; A=31-380.
DR PDB; 6OYL; X-ray; 3.15 A; A=31-380.
DR PDB; 6TOQ; X-ray; 3.16 A; AAA=11-380.
DR PDB; 6VOY; EM; 3.70 A; E/F=30-372.
DR PDB; 6VRO; X-ray; 2.45 A; A=31-380.
DR PDB; 7OUF; EM; 3.00 A; C/F=11-380.
DR PDB; 7OUG; EM; 3.10 A; C/F=11-380.
DR PDB; 7OUH; EM; 3.50 A; C/F=11-380.
DR PDB; 7PEL; EM; 3.34 A; C/F=11-380.
DR PDBsum; 2IAE; -.
DR PDBsum; 2JAK; -.
DR PDBsum; 2NPP; -.
DR PDBsum; 2NYL; -.
DR PDBsum; 2NYM; -.
DR PDBsum; 3FGA; -.
DR PDBsum; 5JJA; -.
DR PDBsum; 5K6S; -.
DR PDBsum; 5SW9; -.
DR PDBsum; 5SWF; -.
DR PDBsum; 6OYL; -.
DR PDBsum; 6TOQ; -.
DR PDBsum; 6VOY; -.
DR PDBsum; 6VRO; -.
DR PDBsum; 7OUF; -.
DR PDBsum; 7OUG; -.
DR PDBsum; 7OUH; -.
DR PDBsum; 7PEL; -.
DR AlphaFoldDB; Q13362; -.
DR SMR; Q13362; -.
DR BioGRID; 111519; 70.
DR DIP; DIP-39401N; -.
DR ELM; Q13362; -.
DR IntAct; Q13362; 36.
DR MINT; Q13362; -.
DR STRING; 9606.ENSP00000412324; -.
DR DrugBank; DB06905; (2S,3S,4E,6E,8S,9S)-3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid.
DR DrugBank; DB02506; 2,6,8-Trimethyl-3-Amino-9-Benzyl-9-Methoxynonanoic Acid.
DR GlyGen; Q13362; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13362; -.
DR PhosphoSitePlus; Q13362; -.
DR SwissPalm; Q13362; -.
DR BioMuta; PPP2R5C; -.
DR DMDM; 116241235; -.
DR EPD; Q13362; -.
DR jPOST; Q13362; -.
DR MassIVE; Q13362; -.
DR MaxQB; Q13362; -.
DR PaxDb; Q13362; -.
DR PeptideAtlas; Q13362; -.
DR PRIDE; Q13362; -.
DR ProteomicsDB; 24176; -.
DR ProteomicsDB; 59345; -.
DR ProteomicsDB; 59346; -. [Q13362-2]
DR ProteomicsDB; 59347; -. [Q13362-3]
DR ProteomicsDB; 59348; -. [Q13362-4]
DR Antibodypedia; 27667; 252 antibodies from 29 providers.
DR DNASU; 5527; -.
DR Ensembl; ENST00000328724.9; ENSP00000329009.5; ENSG00000078304.19. [Q13362-4]
DR Ensembl; ENST00000334743.9; ENSP00000333905.4; ENSG00000078304.19. [Q13362-1]
DR Ensembl; ENST00000350249.7; ENSP00000262239.5; ENSG00000078304.19. [Q13362-3]
DR Ensembl; ENST00000422945.6; ENSP00000412324.2; ENSG00000078304.19. [Q13362-5]
DR Ensembl; ENST00000445439.7; ENSP00000408389.3; ENSG00000078304.19. [Q13362-2]
DR GeneID; 5527; -.
DR KEGG; hsa:5527; -.
DR UCSC; uc001ykk.4; human. [Q13362-1]
DR CTD; 5527; -.
DR DisGeNET; 5527; -.
DR GeneCards; PPP2R5C; -.
DR HGNC; HGNC:9311; PPP2R5C.
DR HPA; ENSG00000078304; Low tissue specificity.
DR MIM; 601645; gene.
DR neXtProt; NX_Q13362; -.
DR OpenTargets; ENSG00000078304; -.
DR PharmGKB; PA33674; -.
DR VEuPathDB; HostDB:ENSG00000078304; -.
DR eggNOG; KOG2085; Eukaryota.
DR GeneTree; ENSGT01030000234620; -.
DR HOGENOM; CLU_012437_3_2_1; -.
DR InParanoid; Q13362; -.
DR OMA; FMEINQR; -.
DR OrthoDB; 890437at2759; -.
DR PhylomeDB; Q13362; -.
DR TreeFam; TF105556; -.
DR PathwayCommons; Q13362; -.
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-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-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q13362; -.
DR SIGNOR; Q13362; -.
DR BioGRID-ORCS; 5527; 32 hits in 1085 CRISPR screens.
DR ChiTaRS; PPP2R5C; human.
DR EvolutionaryTrace; Q13362; -.
DR GeneWiki; PPP2R5C; -.
DR GenomeRNAi; 5527; -.
DR Pharos; Q13362; Tbio.
DR PRO; PR:Q13362; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q13362; protein.
DR Bgee; ENSG00000078304; Expressed in sperm and 202 other tissues.
DR ExpressionAtlas; Q13362; baseline and differential.
DR Genevisible; Q13362; HS.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:UniProtKB.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IDA:UniProtKB.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
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 Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..524
FT /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT regulatory subunit gamma isoform"
FT /id="PRO_0000071457"
FT REGION 476..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 416..422
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1..31
FT /note="MLTCNKAGSRMVVDAANSNGPFQPVVLLHIR -> MPNKNKKEKESPKAGKS
FT GKSSKEGQDTVESEQISVRKNSLVAVPSTVSAKIKVPVSQPIVKKDKRQNSSRFSASNN
FT RELQKLPSLK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043645"
FT VAR_SEQ 1..30
FT /note="MLTCNKAGSRMVVDAANSNGPFQPVVLLHI -> MPNKNKKEKESPKAGKSG
FT KSSKEGQDTVESEGTSPEEPSSPKVPPPLLPELLVLIFGGLQG (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_046768"
FT VAR_SEQ 443..524
FT /note="YTVYSQASTMSIPVAMETDGPLFEDVQMLRKTVKDEAHQAQKDPKKDRPLAR
FT RKSELPQDPHTKKALEAHCRADELASQDGR -> VLKKRIT (in isoform
FT Gamma-1)"
FT /evidence="ECO:0000303|PubMed:7592815,
FT ECO:0000303|PubMed:8694763"
FT /id="VSP_005112"
FT VAR_SEQ 443..481
FT /note="Missing (in isoform Gamma-2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:7584044"
FT /id="VSP_005113"
FT VARIANT 515
FT /note="A -> P (in dbSNP:rs3742424)"
FT /id="VAR_051745"
FT CONFLICT 494
FT /note="R -> L (in Ref. 1; AAC50387)"
FT /evidence="ECO:0000305"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:5JJA"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:5JJA"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:5JJA"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 63..82
FT /evidence="ECO:0007829|PDB:5JJA"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5SWF"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:5JJA"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:2NPP"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 131..146
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:5JJA"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 176..192
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 197..213
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 241..249
FT /evidence="ECO:0007829|PDB:5JJA"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 264..277
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 282..292
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 301..313
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 317..335
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 340..347
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 353..360
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 363..370
FT /evidence="ECO:0007829|PDB:5JJA"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:5JJA"
FT HELIX 384..398
FT /evidence="ECO:0007829|PDB:3FGA"
FT HELIX 409..430
FT /evidence="ECO:0007829|PDB:3FGA"
FT CONFLICT Q13362-5:3
FT /note="N -> K (in Ref. 3; BAG63760)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 61061 MW; B9CBF54550D713F8 CRC64;
MLTCNKAGSR MVVDAANSNG PFQPVVLLHI RDVPPADQEK LFIQKLRQCC VLFDFVSDPL
SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEVVHMFA VNMFRTLPPS SNPTGAEFDP
EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLQLLEL FDSEDPRERD
FLKTTLHRIY GKFLGLRAYI RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK
EEHKIFLLKV LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK
EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS
DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QFKAEKLKEK
LKMKEREEAW VKIENLAKAN PQYTVYSQAS TMSIPVAMET DGPLFEDVQM LRKTVKDEAH
QAQKDPKKDR PLARRKSELP QDPHTKKALE AHCRADELAS QDGR
