2AAB_MOUSE
ID 2AAB_MOUSE Reviewed; 601 AA.
AC Q7TNP2; E9QNJ1;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 135.
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 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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Lung, 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 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. {ECO:0000250}.
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 (By similarity). Interacts with SGO1 (By
CC similarity). Interacts with RAF1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q7TNP2; Q8K1S3: Unc5b; NbExp=2; IntAct=EBI-4396871, EBI-4396886;
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}.
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DR EMBL; AC103406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC123614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056218; AAH56218.1; -; mRNA.
DR CCDS; CCDS40626.1; -.
DR RefSeq; NP_082890.2; NM_028614.3.
DR AlphaFoldDB; Q7TNP2; -.
DR SMR; Q7TNP2; -.
DR BioGRID; 216197; 2.
DR IntAct; Q7TNP2; 1.
DR STRING; 10090.ENSMUSP00000034560; -.
DR iPTMnet; Q7TNP2; -.
DR PhosphoSitePlus; Q7TNP2; -.
DR SwissPalm; Q7TNP2; -.
DR EPD; Q7TNP2; -.
DR jPOST; Q7TNP2; -.
DR MaxQB; Q7TNP2; -.
DR PaxDb; Q7TNP2; -.
DR PRIDE; Q7TNP2; -.
DR ProteomicsDB; 285890; -.
DR Antibodypedia; 3416; 312 antibodies from 36 providers.
DR DNASU; 73699; -.
DR Ensembl; ENSMUST00000114437; ENSMUSP00000110080; ENSMUSG00000032058.
DR GeneID; 73699; -.
DR KEGG; mmu:73699; -.
DR UCSC; uc009pkv.2; mouse.
DR CTD; 5519; -.
DR MGI; MGI:1920949; Ppp2r1b.
DR VEuPathDB; HostDB:ENSMUSG00000032058; -.
DR eggNOG; KOG0211; Eukaryota.
DR GeneTree; ENSGT00950000183066; -.
DR InParanoid; Q7TNP2; -.
DR OrthoDB; 447572at2759; -.
DR Reactome; R-MMU-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-180024; DARPP-32 events.
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-198753; ERK/MAPK targets.
DR Reactome; R-MMU-202670; ERKs are inactivated.
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-69231; Cyclin D associated events in G1.
DR Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 73699; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ppp2r1b; mouse.
DR PRO; PR:Q7TNP2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q7TNP2; protein.
DR Bgee; ENSMUSG00000032058; Expressed in metanephric ureteric bud and 252 other tissues.
DR ExpressionAtlas; Q7TNP2; baseline and differential.
DR Genevisible; Q7TNP2; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; ISO:MGI.
DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; 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; IPR000357; HEAT.
DR InterPro; IPR021133; HEAT_type_2.
DR Pfam; PF02985; HEAT; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 12.
PE 1: Evidence at protein level;
KW Acetylation; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P30154"
FT CHAIN 2..601
FT /note="Serine/threonine-protein phosphatase 2A 65 kDa
FT regulatory subunit A beta isoform"
FT /id="PRO_0000071404"
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:0000250|UniProtKB:P30154"
FT CONFLICT 154
FT /note="T -> M (in Ref. 2; AAH56218)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="V -> E (in Ref. 2; AAH56218)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="M -> I (in Ref. 2; AAH56218)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="N -> S (in Ref. 2; AAH56218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 65934 MW; 801D903C90D1F15A CRC64;
MAGAAGPGSG PGAAGGDGDD SLYPIAVLID ELRNEDVQLR LNSIKKLSTI ALALGVERTR
TELLPFLTDT IYDEDEVLLA LAEQLGNFTG LVGGPDFAHC LLPPLESLAT VEETVVRDKA
VESLRQISQE HTPVALEAHF VPLVKRLASG DWFTSRTSAC GLFSVCYPRA SNAVKAEIRQ
HFRSLCSDDT PMVRRAAASK LGEFAKVLEL DSVKTEIVPL FTNLASDEQD SVRLLAVEAC
VSIAQLLSQE DLEALVMPTL RQAAEDKSWR VRYMVADKFS ELQKAVGPKI ALSDLIPAFQ
SLLRDCEAEV RAAAAHKVRE LCENLPAEGR ETVIMNQILP YIKELVSDTN QHVKSALASV
IMGLSTVLGK ENTIEHLLPL FLAQLKDECP EVRLNIISNL DCVNEVIGIR QLSQSLLPAI
VELAEDAKWR VRLAIIEYMP LLAGQLGVEF FDEKLNSLCM AWLVDHVYAI REAATNNLMK
LVQKFGTEWA QNTIVPKVLV MANDPNYLHR MTTLFCINAL SEACGKEITT KQMLPIVLKM
AGDQVANVRF NVAKSLQKIG PILDTNALQG EVKPVLQKLG QDEDMDVKYF AQEAISVLAL
A
