2ABD_MOUSE
ID 2ABD_MOUSE Reviewed; 453 AA.
AC Q925E7; Q6ZPN5;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform;
DE AltName: Full=PP2A subunit B isoform B55-delta;
DE AltName: Full=PP2A subunit B isoform PR55-delta;
DE AltName: Full=PP2A subunit B isoform R2-delta;
DE AltName: Full=PP2A subunit B isoform delta;
GN Name=Ppp2r2d; Synonyms=D7Ertd753e, Kiaa1541;
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 [MRNA].
RC STRAIN=C57BL/6J;
RA Chang H., Lee S., Park K.;
RT "Analysis of mDRA (Mouse Down-regulated in Adenoma) interaction in yeast
RT two-hybrid system.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Natural killer cell;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Spleen;
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: B regulatory subunit of protein phosphatase 2A (PP2A) that
CC plays a key role in cell cycle by controlling mitosis entry and exit.
CC The activity of PP2A complexes containing PPP2R2D (PR55-delta)
CC fluctuate during the cell cycle: the activity is high in interphase and
CC low in mitosis. During mitosis, activity of PP2A is inhibited via
CC interaction with phosphorylated ENSA and ARPP19 inhibitors. Within the
CC PP2A complexes, the B regulatory subunits modulate substrate
CC selectivity and catalytic activity, and also may direct the
CC localization of the catalytic enzyme to a particular subcellular
CC compartment (By similarity). {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 ENSA (when phosphorylated at 'Ser-67') and ARPP19 (when
CC phosphorylated at 'Ser-62'), leading to inhibit PP2A activity (By
CC similarity). Interacts with IER5 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q66LE6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98196.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF366393; AAK53703.1; -; mRNA.
DR EMBL; AK129386; BAC98196.2; ALT_INIT; mRNA.
DR EMBL; BC066022; AAH66022.1; -; mRNA.
DR CCDS; CCDS21950.1; -.
DR RefSeq; NP_080667.1; NM_026391.2.
DR AlphaFoldDB; Q925E7; -.
DR SMR; Q925E7; -.
DR BioGRID; 206582; 40.
DR IntAct; Q925E7; 15.
DR MINT; Q925E7; -.
DR STRING; 10090.ENSMUSP00000040321; -.
DR PhosphoSitePlus; Q925E7; -.
DR SwissPalm; Q925E7; -.
DR EPD; Q925E7; -.
DR jPOST; Q925E7; -.
DR MaxQB; Q925E7; -.
DR PaxDb; Q925E7; -.
DR PeptideAtlas; Q925E7; -.
DR PRIDE; Q925E7; -.
DR ProteomicsDB; 285532; -.
DR Antibodypedia; 55293; 65 antibodies from 15 providers.
DR DNASU; 52432; -.
DR Ensembl; ENSMUST00000041097; ENSMUSP00000040321; ENSMUSG00000041769.
DR GeneID; 52432; -.
DR KEGG; mmu:52432; -.
DR UCSC; uc009kfe.1; mouse.
DR CTD; 55844; -.
DR MGI; MGI:1289252; Ppp2r2d.
DR VEuPathDB; HostDB:ENSMUSG00000041769; -.
DR eggNOG; KOG1354; Eukaryota.
DR GeneTree; ENSGT00950000182864; -.
DR HOGENOM; CLU_021713_3_3_1; -.
DR InParanoid; Q925E7; -.
DR OMA; LSHHDTI; -.
DR OrthoDB; 810409at2759; -.
DR PhylomeDB; Q925E7; -.
DR TreeFam; TF105553; -.
DR BioGRID-ORCS; 52432; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Ppp2r2d; mouse.
DR PRO; PR:Q925E7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q925E7; protein.
DR Bgee; ENSMUSG00000041769; Expressed in internal carotid artery and 255 other tissues.
DR ExpressionAtlas; Q925E7; baseline and differential.
DR Genevisible; Q925E7; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; ISS:UniProtKB.
DR GO; GO:0019888; F:protein phosphatase regulator activity; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR000009; PP2A_PR55.
DR InterPro; IPR018067; PP2A_PR55_CS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR11871; PTHR11871; 1.
DR PIRSF; PIRSF037309; PP2A_PR55; 1.
DR PRINTS; PR00600; PP2APR55.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS01024; PR55_1; 1.
DR PROSITE; PS01025; PR55_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Mitosis; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..453
FT /note="Serine/threonine-protein phosphatase 2A 55 kDa
FT regulatory subunit B delta isoform"
FT /id="PRO_0000071434"
FT REPEAT 32..71
FT /note="WD 1"
FT REPEAT 97..138
FT /note="WD 2"
FT REPEAT 181..219
FT /note="WD 3"
FT REPEAT 230..270
FT /note="WD 4"
FT REPEAT 289..327
FT /note="WD 5"
FT REPEAT 344..385
FT /note="WD 6"
FT REPEAT 420..452
FT /note="WD 7"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36877"
FT MOD_RES 305
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P36877"
FT MOD_RES 308
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P36877"
SQ SEQUENCE 453 AA; 51957 MW; C4B474AA28397576 CRC64;
MAGAGGGGCP AGGNDFQWCF SQVKGAVDED VAEADIISTV EFNYSGDLLA TGDKGGRVVI
FQREQENKGR AHSRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAHFLLST
NDKTIKLWKI SERDKRAEGY NLKDEDGRLR DPFRITALRV PILKPMDLMV EASPRRIFAN
AHTYHINSIS VNSDHETYLS ADDLRINLWH LEITDRSFNI VDIKPANMEE LTEVITAAEF
HPHQCNVFVY SSSKGTIRLC DMRSSALCDR HAKFFEEPED PSSRSFFSEI ISSISDVKFS
HSGRYMMTRD YLSVKVWDLN MEGRPVETHQ VHEYLRSKLC SLYENDCIFD KFECCWNGSD
SAIMTGSYNN FFRMFDRNTR RDVTLEASRE NSKPRASLKP RKVCTGGKRK KDEISVDSLD
FNKKILHTAW HPMESIIAVA ATNNLYIFQD KIN
