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Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (PP2A B subunit isoform B'-gamma) (PP2A B subunit isoform B56-gamma) (PP2A B subunit isoform PR61-gamma) (PP2A B subunit isoform R5-gamma) (Renal carcinoma antigen NY-REN-29)

 2A5G_HUMAN              Reviewed;         524 AA.
Q13362; B4DYJ8; B5BUA5; F5GWP3; Q14391; Q15060; Q15174; Q6ZN33;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
12-SEP-2018, entry version 183.
RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform;
AltName: Full=PP2A B subunit isoform B'-gamma;
AltName: Full=PP2A B subunit isoform B56-gamma;
AltName: Full=PP2A B subunit isoform PR61-gamma;
AltName: Full=PP2A B subunit isoform R5-gamma;
AltName: Full=Renal carcinoma antigen NY-REN-29;
Name=PPP2R5C; Synonyms=KIAA0044;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-3).
TISSUE=Umbilical vein;
PubMed=8617797; DOI=10.1074/jbc.271.9.5164;
Tehrani M.A., Mumby M.C., Kamibayashi C.;
"Identification of a novel protein phosphatase 2A regulatory subunit
highly expressed in muscle.";
J. Biol. Chem. 271:5164-5170(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-1).
TISSUE=Fetal retina;
PubMed=8694763; DOI=10.1042/bj3170187;
Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I.,
Merlevede W., Goris J., Hemmings B.A.;
"The variable subunit associated with protein phosphatase 2A0 defines
a novel multimember family of regulatory subunits.";
Biochem. J. 317:187-194(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND PARTIAL
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Hippocampus, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-3).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-524 (ISOFORM GAMMA-2).
TISSUE=Bone marrow;
PubMed=7584044; DOI=10.1093/dnares/1.5.223;
Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S.,
Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. II.
The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 1:223-229(1994).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 11-524 (ISOFORM GAMMA-1).
PubMed=7592815; DOI=10.1074/jbc.270.44.26123;
McCright B., Virshup D.M.;
"Identification of a new family of protein phosphatase 2A regulatory
subunits.";
J. Biol. Chem. 270:26123-26128(1995).
[9]
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=8703017; DOI=10.1074/jbc.271.36.22081;
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).
[10]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[11]
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SGO1, AND
SUBCELLULAR LOCATION.
PubMed=16580887; DOI=10.1016/j.devcel.2006.03.010;
Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.;
"PP2A is required for centromeric localization of Sgo1 and proper
chromosome segregation.";
Dev. Cell 10:575-585(2006).
[12]
FUNCTION, INTERACTION WITH IER3 AND ERK KINASES, AND PHOSPHORYLATION.
PubMed=16456541; DOI=10.1038/sj.emboj.7600980;
Letourneux C., Rocher G., Porteu F.;
"B56-containing PP2A dephosphorylate ERK and their activity is
controlled by the early gene IEX-1 and ERK.";
EMBO J. 25:727-738(2006).
[13]
INTERACTION WITH SGO1.
PubMed=16541025; DOI=10.1038/nature04663;
Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
Kawashima S.A., Watanabe Y.;
"Shugoshin collaborates with protein phosphatase 2A to protect
cohesin.";
Nature 441:46-52(2006).
[14]
FUNCTION, INTERACTION WITH TP53, AND INDUCTION.
PubMed=17245430; DOI=10.1038/sj.emboj.7601519;
Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.;
"A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-
induced dephosphorylation of p53 at Thr55.";
EMBO J. 26:402-411(2007).
[15]
INTERACTION WITH TP53.
PubMed=17967874; DOI=10.1128/MCB.00983-07;
Shouse G.P., Cai X., Liu X.;
"Serine 15 phosphorylation of p53 directs its interaction with
B56gamma and the tumor suppressor activity of B56gamma-specific
protein phosphatase 2A.";
Mol. Cell. Biol. 28:448-456(2008).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-442 IN COMPLEX WITH PPP2CA
AND PPP2R1A.
PubMed=17174897; DOI=10.1016/j.cell.2006.11.033;
Xu Y., Xing Y., Chen Y., Chao Y., Lin Z., Fan E., Yu J.W., Strack S.,
Jeffrey P.D., Shi Y.;
"Structure of the protein phosphatase 2A holoenzyme.";
Cell 127:1239-1251(2006).
[18]
X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 30-436 IN COMPLEX WITH
PPP2CA AND PPP2R1A.
PubMed=17086192; DOI=10.1038/nature05351;
Cho U.S., Xu W.;
"Crystal structure of a protein phosphatase 2A heterotrimeric
holoenzyme.";
Nature 445:53-57(2007).
[19]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 34-436 IN COMPLEX WITH
PPP2CA; PPP2R1A AND SGO1.
PubMed=19716788; DOI=10.1016/j.molcel.2009.06.031;
Xu Z., Cetin B., Anger M., Cho U.S., Helmhart W., Nasmyth K., Xu W.;
"Structure and function of the PP2A-shugoshin interaction.";
Mol. Cell 35:426-441(2009).
[20]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 11-380.
PubMed=18618707; DOI=10.1002/prot.22150;
Magnusdottir A., Stenmark P., Flodin S., Nyman T., Kotenyova T.,
Graeslund S., Ogg D., Nordlund P.;
"The structure of the PP2A regulatory subunit B56 gamma: the remaining
piece of the PP2A jigsaw puzzle.";
Proteins 74:212-221(2009).
[21]
INTERACTION WITH CIP2A.
PubMed=28174209; DOI=10.15252/embr.201642788;
Wang J., Okkeri J., Pavic K., Wang Z., Kauko O., Halonen T., Sarek G.,
Ojala P.M., Rao Z., Xu W., Westermarck J.;
"Oncoprotein CIP2A is stabilized via interaction with tumor suppressor
PP2A/B56.";
EMBO Rep. 18:437-450(2017).
-!- FUNCTION: The B regulatory subunit might modulate substrate
selectivity and catalytic activity, and also might direct the
localization of the catalytic enzyme to a particular subcellular
compartment. The PP2A-PPP2R5C holoenzyme may specifically
dephosphorylate and activate TP53 and play a role in DNA damage-
induced inhibition of cell proliferation. PP2A-PPP2R5C may also
regulate the ERK signaling pathway through ERK dephosphorylation.
{ECO:0000269|PubMed:16456541, ECO:0000269|PubMed:17245430}.
-!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme,
composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and
PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A),
that associates with a variety of regulatory subunits. Proteins
that associate with the core dimer include three families of
regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59
and R5/B'/B56 families), the 48 kDa variable regulatory subunit,
viral proteins, and cell signaling molecules. Interacts with
PPP2CA AND PPP2R1A; the interaction is direct. Interacts with
SGO1; the interaction is direct. Isoform 1 and isoform 2 interact
with TP53 (phosphorylated at Ser-15 by ATM); increased upon DNA
damage it drives PP2A-mediated dephosphorylation of TP53 at Thr-
55. Interacts with IER3 and/or ERK kinases; regulates ERK
dephosphorylation. Interacts with CIP2A; this interaction
stabilizes CIP2A (PubMed:28174209). {ECO:0000269|PubMed:16456541,
ECO:0000269|PubMed:16541025, ECO:0000269|PubMed:16580887,
ECO:0000269|PubMed:17086192, ECO:0000269|PubMed:17174897,
ECO:0000269|PubMed:17245430, ECO:0000269|PubMed:17967874,
ECO:0000269|PubMed:19716788, ECO:0000269|PubMed:28174209}.
-!- INTERACTION:
O96017:CHEK2; NbExp=4; IntAct=EBI-1266176, EBI-1180783;
P46695:IER3; NbExp=2; IntAct=EBI-1266156, EBI-1748945;
Q00987:MDM2; NbExp=5; IntAct=EBI-1266156, EBI-389668;
P67775:PPP2CA; NbExp=9; IntAct=EBI-1266156, EBI-712311;
P30153:PPP2R1A; NbExp=10; IntAct=EBI-1266156, EBI-302388;
P30154:PPP2R1B; NbExp=2; IntAct=EBI-1266156, EBI-357094;
P04049:RAF1; NbExp=2; IntAct=EBI-1266156, EBI-365996;
P04637:TP53; NbExp=4; IntAct=EBI-1266156, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=Gamma-3;
IsoId=Q13362-1; Sequence=Displayed;
Name=Gamma-1;
IsoId=Q13362-2; Sequence=VSP_005112;
Name=Gamma-2;
IsoId=Q13362-3; Sequence=VSP_005113;
Name=4;
IsoId=Q13362-4; Sequence=VSP_043645, VSP_005113;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q13362-5; Sequence=VSP_046768;
Note=Ref.3 (BAG63760) sequence is in conflict in position:
3:N->K. No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Highest levels in heart, skeletal muscle and
brain. Lower levels in pancreas, kidney, lung and placenta. Very
low levels in liver.
-!- INDUCTION: Up-regulated upon DNA damage.
{ECO:0000269|PubMed:17245430}.
-!- PTM: Isoform Gamma-3 is phosphorylated on serine residues. Isoform
Gamma-1 phosphorylation by ERK2 is IER3-dependent and inhibits ERK
dephosphorylation by PP2A-PPP2R5C. {ECO:0000269|PubMed:16456541,
ECO:0000269|PubMed:8703017}.
-!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC50387.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG63760.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; U37352; AAC50387.1; ALT_INIT; mRNA.
EMBL; Z69030; CAA93154.1; -; mRNA.
EMBL; AK131391; BAD18542.1; -; mRNA.
EMBL; AK302470; BAG63760.1; ALT_INIT; mRNA.
EMBL; AB451341; BAG70155.1; -; mRNA.
EMBL; AL118558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL137779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW81756.1; -; Genomic_DNA.
EMBL; D26445; BAA05465.1; -; mRNA.
EMBL; L42375; AAC37603.1; -; mRNA.
CCDS; CCDS45163.1; -. [Q13362-2]
CCDS; CCDS53911.1; -. [Q13362-4]
CCDS; CCDS53912.1; -. [Q13362-5]
CCDS; CCDS9964.1; -. [Q13362-1]
CCDS; CCDS9965.1; -. [Q13362-3]
RefSeq; NP_001155197.1; NM_001161725.1. [Q13362-5]
RefSeq; NP_001155198.1; NM_001161726.1. [Q13362-4]
RefSeq; NP_002710.2; NM_002719.3. [Q13362-1]
RefSeq; NP_848701.1; NM_178586.2. [Q13362-3]
RefSeq; NP_848702.1; NM_178587.2. [Q13362-2]
RefSeq; XP_005267884.1; XM_005267827.1.
RefSeq; XP_011535222.1; XM_011536920.1.
UniGene; Hs.368264; -.
PDB; 2IAE; X-ray; 3.50 A; B/E=30-436.
PDB; 2JAK; X-ray; 2.60 A; A=11-380.
PDB; 2NPP; X-ray; 3.30 A; B/E=1-442.
PDB; 2NYL; X-ray; 3.80 A; B/E=38-425.
PDB; 2NYM; X-ray; 3.60 A; B/E=38-425.
PDB; 3FGA; X-ray; 2.70 A; B=34-436.
PDB; 5JJA; X-ray; 2.35 A; A/B=30-380.
PDB; 5K6S; X-ray; 2.79 A; A=31-380.
PDB; 5SW9; X-ray; 2.85 A; A=31-380.
PDB; 5SWF; X-ray; 2.82 A; A=31-380.
PDBsum; 2IAE; -.
PDBsum; 2JAK; -.
PDBsum; 2NPP; -.
PDBsum; 2NYL; -.
PDBsum; 2NYM; -.
PDBsum; 3FGA; -.
PDBsum; 5JJA; -.
PDBsum; 5K6S; -.
PDBsum; 5SW9; -.
PDBsum; 5SWF; -.
ProteinModelPortal; Q13362; -.
SMR; Q13362; -.
BioGrid; 111519; 41.
DIP; DIP-39401N; -.
ELM; Q13362; -.
IntAct; Q13362; 21.
MINT; Q13362; -.
STRING; 9606.ENSP00000412324; -.
iPTMnet; Q13362; -.
PhosphoSitePlus; Q13362; -.
BioMuta; PPP2R5C; -.
DMDM; 116241235; -.
EPD; Q13362; -.
MaxQB; Q13362; -.
PaxDb; Q13362; -.
PeptideAtlas; Q13362; -.
PRIDE; Q13362; -.
DNASU; 5527; -.
Ensembl; ENST00000328724; ENSP00000329009; ENSG00000078304. [Q13362-4]
Ensembl; ENST00000334743; ENSP00000333905; ENSG00000078304. [Q13362-1]
Ensembl; ENST00000350249; ENSP00000262239; ENSG00000078304. [Q13362-3]
Ensembl; ENST00000422945; ENSP00000412324; ENSG00000078304. [Q13362-5]
Ensembl; ENST00000445439; ENSP00000408389; ENSG00000078304. [Q13362-2]
GeneID; 5527; -.
KEGG; hsa:5527; -.
UCSC; uc001ykk.4; human. [Q13362-1]
CTD; 5527; -.
DisGeNET; 5527; -.
EuPathDB; HostDB:ENSG00000078304.19; -.
GeneCards; PPP2R5C; -.
HGNC; HGNC:9311; PPP2R5C.
HPA; HPA027553; -.
MIM; 601645; gene.
neXtProt; NX_Q13362; -.
OpenTargets; ENSG00000078304; -.
PharmGKB; PA33674; -.
eggNOG; KOG2085; Eukaryota.
eggNOG; ENOG410XQJW; LUCA.
GeneTree; ENSGT00550000074525; -.
HOGENOM; HOG000067326; -.
HOVERGEN; HBG000009; -.
InParanoid; Q13362; -.
KO; K11584; -.
OMA; DIYTMKA; -.
OrthoDB; EOG091G06HU; -.
PhylomeDB; Q13362; -.
TreeFam; TF105556; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
Reactome; R-HSA-432142; Platelet sensitization by LDL.
Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-HSA-5339716; Misspliced GSK3beta mutants stabilize beta-catenin.
Reactome; R-HSA-5358747; S33 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358749; S37 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358751; S45 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358752; T41 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-5673000; RAF activation.
Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-68877; Mitotic Prometaphase.
SignaLink; Q13362; -.
SIGNOR; Q13362; -.
ChiTaRS; PPP2R5C; human.
EvolutionaryTrace; Q13362; -.
GeneWiki; PPP2R5C; -.
GenomeRNAi; 5527; -.
PMAP-CutDB; Q13362; -.
PRO; PR:Q13362; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000078304; Expressed in 232 organ(s), highest expression level in sperm.
CleanEx; HS_PPP2R5C; -.
ExpressionAtlas; Q13362; baseline and differential.
Genevisible; Q13362; HS.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
GO; GO:0019888; F:protein phosphatase regulator activity; IDA:UniProtKB.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IDA:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:MGI.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002554; PP2A_B56.
PANTHER; PTHR10257; PTHR10257; 1.
Pfam; PF01603; B56; 1.
PIRSF; PIRSF028043; PP2A_B56; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Centromere;
Chromosome; Complete proteome; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 524 Serine/threonine-protein phosphatase 2A
56 kDa regulatory subunit gamma isoform.
/FTId=PRO_0000071457.
MOTIF 416 422 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
VAR_SEQ 1 31 MLTCNKAGSRMVVDAANSNGPFQPVVLLHIR -> MPNKNK
KEKESPKAGKSGKSSKEGQDTVESEQISVRKNSLVAVPSTV
SAKIKVPVSQPIVKKDKRQNSSRFSASNNRELQKLPSLK
(in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043645.
VAR_SEQ 1 30 MLTCNKAGSRMVVDAANSNGPFQPVVLLHI -> MPNKNKK
EKESPKAGKSGKSSKEGQDTVESEGTSPEEPSSPKVPPPLL
PELLVLIFGGLQG (in isoform 5).
{ECO:0000305}.
/FTId=VSP_046768.
VAR_SEQ 443 524 YTVYSQASTMSIPVAMETDGPLFEDVQMLRKTVKDEAHQAQ
KDPKKDRPLARRKSELPQDPHTKKALEAHCRADELASQDGR
-> VLKKRIT (in isoform Gamma-1).
{ECO:0000303|PubMed:7592815,
ECO:0000303|PubMed:8694763}.
/FTId=VSP_005112.
VAR_SEQ 443 481 Missing (in isoform Gamma-2 and isoform
4). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:7584044}.
/FTId=VSP_005113.
VARIANT 515 515 A -> P (in dbSNP:rs3742424).
/FTId=VAR_051745.
CONFLICT 494 494 R -> L (in Ref. 1; AAC50387).
{ECO:0000305}.
HELIX 30 32 {ECO:0000244|PDB:5JJA}.
TURN 35 37 {ECO:0000244|PDB:5JJA}.
HELIX 38 48 {ECO:0000244|PDB:5JJA}.
STRAND 55 57 {ECO:0000244|PDB:5JJA}.
TURN 59 62 {ECO:0000244|PDB:5JJA}.
HELIX 63 82 {ECO:0000244|PDB:5JJA}.
STRAND 83 85 {ECO:0000244|PDB:5SWF}.
HELIX 91 103 {ECO:0000244|PDB:5JJA}.
STRAND 115 118 {ECO:0000244|PDB:2NPP}.
HELIX 120 122 {ECO:0000244|PDB:3FGA}.
HELIX 131 146 {ECO:0000244|PDB:5JJA}.
HELIX 152 155 {ECO:0000244|PDB:5JJA}.
TURN 156 158 {ECO:0000244|PDB:5JJA}.
HELIX 161 169 {ECO:0000244|PDB:5JJA}.
HELIX 170 172 {ECO:0000244|PDB:5JJA}.
HELIX 176 192 {ECO:0000244|PDB:5JJA}.
HELIX 194 196 {ECO:0000244|PDB:5JJA}.
HELIX 197 213 {ECO:0000244|PDB:5JJA}.
HELIX 221 233 {ECO:0000244|PDB:5JJA}.
HELIX 241 249 {ECO:0000244|PDB:5JJA}.
TURN 250 252 {ECO:0000244|PDB:5JJA}.
HELIX 253 256 {ECO:0000244|PDB:5JJA}.
HELIX 260 262 {ECO:0000244|PDB:5JJA}.
HELIX 264 277 {ECO:0000244|PDB:5JJA}.
HELIX 279 281 {ECO:0000244|PDB:5JJA}.
HELIX 282 292 {ECO:0000244|PDB:5JJA}.
HELIX 301 313 {ECO:0000244|PDB:5JJA}.
HELIX 317 335 {ECO:0000244|PDB:5JJA}.
HELIX 340 347 {ECO:0000244|PDB:5JJA}.
HELIX 348 351 {ECO:0000244|PDB:5JJA}.
HELIX 353 360 {ECO:0000244|PDB:5JJA}.
HELIX 363 370 {ECO:0000244|PDB:5JJA}.
TURN 372 374 {ECO:0000244|PDB:5JJA}.
HELIX 384 398 {ECO:0000244|PDB:3FGA}.
HELIX 409 430 {ECO:0000244|PDB:3FGA}.
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


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