2ABD_HUMAN
ID 2ABD_HUMAN Reviewed; 453 AA.
AC Q66LE6; A8KAK0; Q5SQJ2; Q9P1Y7;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 163.
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=KIAA1541;
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 [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-453.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [5]
RP INTERACTION WITH IER5.
RX PubMed=25816751; DOI=10.1016/j.febslet.2015.03.019;
RA Ishikawa Y., Kawabata S., Sakurai H.;
RT "HSF1 transcriptional activity is modulated by IER5 and PP2A/B55.";
RL FEBS Lett. 589:1150-1155(2015).
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 (PubMed:25816751). {ECO:0000250,
CC ECO:0000269|PubMed:25816751}.
CC -!- INTERACTION:
CC Q66LE6; Q76S40: ORF2; Xeno; NbExp=2; IntAct=EBI-717262, EBI-14032793;
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=BAA96065.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK293065; BAF85754.1; -; mRNA.
DR EMBL; AL732395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047379; AAH47379.1; -; mRNA.
DR EMBL; AB040974; BAA96065.1; ALT_INIT; mRNA.
DR CCDS; CCDS73224.1; -.
DR RefSeq; NP_001278239.1; NM_001291310.1.
DR RefSeq; NP_060931.2; NM_018461.4.
DR AlphaFoldDB; Q66LE6; -.
DR SMR; Q66LE6; -.
DR BioGRID; 120946; 160.
DR IntAct; Q66LE6; 101.
DR MINT; Q66LE6; -.
DR STRING; 9606.ENSP00000399970; -.
DR iPTMnet; Q66LE6; -.
DR PhosphoSitePlus; Q66LE6; -.
DR BioMuta; PPP2R2D; -.
DR DMDM; 74736328; -.
DR EPD; Q66LE6; -.
DR jPOST; Q66LE6; -.
DR MassIVE; Q66LE6; -.
DR MaxQB; Q66LE6; -.
DR PaxDb; Q66LE6; -.
DR PeptideAtlas; Q66LE6; -.
DR PRIDE; Q66LE6; -.
DR ProteomicsDB; 65964; -.
DR Antibodypedia; 55293; 65 antibodies from 15 providers.
DR DNASU; 55844; -.
DR Ensembl; ENST00000455566.6; ENSP00000399970.2; ENSG00000175470.20.
DR GeneID; 55844; -.
DR KEGG; hsa:55844; -.
DR MANE-Select; ENST00000455566.6; ENSP00000399970.2; NM_018461.5; NP_060931.2.
DR UCSC; uc031wxk.2; human.
DR CTD; 55844; -.
DR DisGeNET; 55844; -.
DR GeneCards; PPP2R2D; -.
DR HGNC; HGNC:23732; PPP2R2D.
DR HPA; ENSG00000175470; Tissue enhanced (pancreas).
DR MIM; 613992; gene.
DR neXtProt; NX_Q66LE6; -.
DR OpenTargets; ENSG00000175470; -.
DR PharmGKB; PA134899040; -.
DR VEuPathDB; HostDB:ENSG00000175470; -.
DR eggNOG; KOG1354; Eukaryota.
DR GeneTree; ENSGT00950000182864; -.
DR HOGENOM; CLU_021713_3_3_1; -.
DR InParanoid; Q66LE6; -.
DR OMA; LSHHDTI; -.
DR OrthoDB; 810409at2759; -.
DR PhylomeDB; Q66LE6; -.
DR TreeFam; TF105553; -.
DR PathwayCommons; Q66LE6; -.
DR Reactome; R-HSA-2465910; MASTL Facilitates Mitotic Progression.
DR SignaLink; Q66LE6; -.
DR SIGNOR; Q66LE6; -.
DR BioGRID-ORCS; 55844; 3 hits in 213 CRISPR screens.
DR ChiTaRS; PPP2R2D; human.
DR GenomeRNAi; 55844; -.
DR Pharos; Q66LE6; Tbio.
DR PRO; PR:Q66LE6; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q66LE6; protein.
DR Bgee; ENSG00000175470; Expressed in body of pancreas and 173 other tissues.
DR ExpressionAtlas; Q66LE6; baseline and differential.
DR Genevisible; Q66LE6; HS.
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_0000071433"
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"
FT VARIANT 358
FT /note="G -> S (in dbSNP:rs34473884)"
FT /id="VAR_057127"
FT CONFLICT 290
FT /note="I -> V (in Ref. 1; BAF85754)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="Y -> H (in Ref. 1; BAF85754)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="M -> T (in Ref. 1; BAF85754)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="Q -> R (in Ref. 1; BAF85754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 52042 MW; 0669CDB80AF4400E CRC64;
MAGAGGGGCP AGGNDFQWCF SQVKGAIDED VAEADIISTV EFNYSGDLLA TGDKGGRVVI
FQREQENKSR PHSRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAHFLLST
NDKTIKLWKI SERDKRAEGY NLKDEDGRLR DPFRITALRV PILKPMDLMV EASPRRIFAN
AHTYHINSIS VNSDHETYLS ADDLRINLWH LEITDRSFNI VDIKPANMEE LTEVITAAEF
HPHQCNVFVY SSSKGTIRLC DMRSSALCDR HSKFFEEPED PSSRSFFSEI ISSISDVKFS
HSGRYMMTRD YLSVKVWDLN MESRPVETHQ VHEYLRSKLC SLYENDCIFD KFECCWNGSD
SAIMTGSYNN FFRMFDRDTR RDVTLEASRE SSKPRASLKP RKVCTGGKRR KDEISVDSLD
FNKKILHTAW HPVDNVIAVA ATNNLYIFQD KIN
