2A5G_MOUSE
ID 2A5G_MOUSE Reviewed; 524 AA.
AC Q60996; O35708; Q6TQF7; Q99KW8; Q99N67; Q99N68;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform;
DE AltName: Full=PP2A B subunit isoform B'-alpha-3;
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;
GN Name=Ppp2r5c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-524 (ISOFORMS 2 AND 3).
RX PubMed=12507892; DOI=10.1016/s0002-9440(10)63800-x;
RA Ito A., Koma Y., Watabe K., Nagano T., Endo Y., Nojima H., Kitamura Y.;
RT "A truncated isoform of the protein phosphatase 2A B56gamma regulatory
RT subunit may promote genetic instability and cause tumor progression.";
RL Am. J. Pathol. 162:81-91(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-524 (ISOFORM 1).
RC TISSUE=T-cell;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-524 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=8752144;
RA Francia G., Mitchell S.D., Moss S.E., Hanby A.M., Marshall J.F., Hart I.R.;
RT "Identification by differential display of annexin-VI, a gene
RT differentially expressed during melanoma progression.";
RL Cancer Res. 56:3855-3858(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 326-524 (ISOFORM 4), AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=15051958; DOI=10.1159/000076823;
RA Ortega-Lazaro J.C., del Mazo J.;
RT "Expression of the B56delta subunit of protein phosphatase 2A and Mea1 in
RT mouse spermatogenesis. Identification of a new B56gamma subunit (B56gamma4)
RT specifically expressed in testis.";
RL Cytogenet. Genome Res. 103:345-351(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 activate TP53 and play a role in DNA damage-
CC induced inhibition of cell proliferation. PP2A-PPP2R5C may also
CC regulate the ERK signaling pathway through ERK dephosphorylation (By
CC similarity). {ECO:0000250}.
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 SGO1 (By similarity). Interacts with SGO1;
CC the interaction is direct. May interact with TP53 (By similarity).
CC Interacts with IER3 and/or ERK kinases; regulates ERK dephosphorylation
CC (By similarity). Interacts with CIP2A; this interaction stabilizes
CC CIP2A (By similarity). {ECO:0000250|UniProtKB:Q13362}.
CC -!- INTERACTION:
CC Q60996-3; P30153: PPP2R1A; Xeno; NbExp=2; IntAct=EBI-1369292, EBI-302388;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=2; Synonyms=Gamma-2;
CC IsoId=Q60996-1; Sequence=Displayed;
CC Name=1; Synonyms=Gamma-1;
CC IsoId=Q60996-2; Sequence=VSP_014719, VSP_014720;
CC Name=3; Synonyms=Gamma-3;
CC IsoId=Q60996-3; Sequence=VSP_014718;
CC Name=4; Synonyms=Gamma-4;
CC IsoId=Q60996-4; Sequence=VSP_038641, VSP_038642;
CC -!- TISSUE SPECIFICITY: Highest levels in heart, liver and brain. Lower
CC levels in skeletal muscle, spleen, kidney and lung. Isoform 4 is
CC testis-specific. {ECO:0000269|PubMed:15051958}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
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DR EMBL; BC003979; AAH03979.1; -; mRNA.
DR EMBL; AB055635; BAB32447.1; -; mRNA.
DR EMBL; AB055636; BAB32448.1; -; mRNA.
DR EMBL; U37353; AAC52435.1; -; mRNA.
DR EMBL; U59418; AAB70857.1; -; mRNA.
DR EMBL; AY389498; AAR26474.1; -; mRNA.
DR CCDS; CCDS36557.1; -. [Q60996-1]
DR CCDS; CCDS36558.1; -. [Q60996-3]
DR CCDS; CCDS88403.1; -. [Q60996-4]
DR CCDS; CCDS88404.1; -. [Q60996-2]
DR RefSeq; NP_001074926.1; NM_001081457.2. [Q60996-3]
DR RefSeq; NP_001074927.1; NM_001081458.2. [Q60996-2]
DR RefSeq; NP_036153.2; NM_012023.3. [Q60996-1]
DR RefSeq; XP_017170571.1; XM_017315082.1.
DR AlphaFoldDB; Q60996; -.
DR SMR; Q60996; -.
DR BioGRID; 205070; 20.
DR DIP; DIP-24181N; -.
DR IntAct; Q60996; 6.
DR MINT; Q60996; -.
DR STRING; 10090.ENSMUSP00000082053; -.
DR iPTMnet; Q60996; -.
DR PhosphoSitePlus; Q60996; -.
DR EPD; Q60996; -.
DR MaxQB; Q60996; -.
DR PaxDb; Q60996; -.
DR PeptideAtlas; Q60996; -.
DR PRIDE; Q60996; -.
DR ProteomicsDB; 285984; -. [Q60996-1]
DR ProteomicsDB; 285985; -. [Q60996-2]
DR ProteomicsDB; 285986; -. [Q60996-3]
DR ProteomicsDB; 285987; -. [Q60996-4]
DR Antibodypedia; 27667; 252 antibodies from 29 providers.
DR DNASU; 26931; -.
DR Ensembl; ENSMUST00000084985; ENSMUSP00000082053; ENSMUSG00000017843. [Q60996-1]
DR Ensembl; ENSMUST00000109832; ENSMUSP00000105458; ENSMUSG00000017843. [Q60996-3]
DR Ensembl; ENSMUST00000221074; ENSMUSP00000152282; ENSMUSG00000017843. [Q60996-4]
DR Ensembl; ENSMUST00000221715; ENSMUSP00000152865; ENSMUSG00000017843. [Q60996-2]
DR GeneID; 26931; -.
DR KEGG; mmu:26931; -.
DR UCSC; uc007pbk.1; mouse. [Q60996-2]
DR UCSC; uc007pbl.2; mouse. [Q60996-1]
DR UCSC; uc007pbm.2; mouse. [Q60996-3]
DR CTD; 5527; -.
DR MGI; MGI:1349475; Ppp2r5c.
DR VEuPathDB; HostDB:ENSMUSG00000017843; -.
DR eggNOG; KOG2085; Eukaryota.
DR GeneTree; ENSGT01030000234620; -.
DR HOGENOM; CLU_012437_3_2_1; -.
DR InParanoid; Q60996; -.
DR OMA; FMEINQR; -.
DR OrthoDB; 890437at2759; -.
DR PhylomeDB; Q60996; -.
DR TreeFam; TF105556; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
DR Reactome; R-MMU-432142; Platelet sensitization by LDL.
DR Reactome; R-MMU-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-5673000; RAF activation.
DR Reactome; R-MMU-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 26931; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ppp2r5c; mouse.
DR PRO; PR:Q60996; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q60996; protein.
DR Bgee; ENSMUSG00000017843; Expressed in retinal neural layer and 262 other tissues.
DR ExpressionAtlas; Q60996; baseline and differential.
DR Genevisible; Q60996; MM.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISO:MGI.
DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; ISO:MGI.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:MGI.
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; 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 Acetylation; Alternative splicing; Centromere; Chromosome; Nucleus;
KW Reference proteome.
FT CHAIN 1..524
FT /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT regulatory subunit gamma isoform"
FT /id="PRO_0000071458"
FT REGION 476..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13362"
FT VAR_SEQ 442..480
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12507892"
FT /id="VSP_014718"
FT VAR_SEQ 443..452
FT /note="YAVYSQASAV -> VLKKRVTREC (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8617797, ECO:0000303|PubMed:8752144"
FT /id="VSP_014719"
FT VAR_SEQ 453..524
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8617797, ECO:0000303|PubMed:8752144"
FT /id="VSP_014720"
FT VAR_SEQ 482..496
FT /note="AQKELKKDRPLVRRK -> LVGRKAMTATQVRKV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15051958"
FT /id="VSP_038641"
FT VAR_SEQ 497..524
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15051958"
FT /id="VSP_038642"
FT CONFLICT 17..19
FT /note="SSN -> APT (in Ref. 2; BAB32447/BAB32448)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="D -> N (in Ref. 4; AAB70857)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="A -> S (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 60824 MW; A22DFD34A1FFBD01 CRC64;
MLTCNKAGSG MVVDAASSNG PFQPVALLHI RDVPPADQEK LFIQKLRQCC VLFDFVSDPL
SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEAVHMFA 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 PQYAVYSQAS AVSIPVAMET DGPQFEDVQM LKKTVSDEAR
QAQKELKKDR PLVRRKSELP QDPHTEKALE AHCRASELLS QDGR
