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Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform (PP2A B subunit isoform B'-delta) (PP2A B subunit isoform B56-delta) (PP2A B subunit isoform PR61-delta) (PP2A B subunit isoform R5-delta)

 2A5D_HUMAN              Reviewed;         602 AA.
Q14738; A8K3I9; B5BUA6; O00494; O00696; Q15171; Q5TC39;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-DEC-2018, entry version 195.
RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform;
AltName: Full=PP2A B subunit isoform B'-delta;
AltName: Full=PP2A B subunit isoform B56-delta;
AltName: Full=PP2A B subunit isoform PR61-delta;
AltName: Full=PP2A B subunit isoform R5-delta;
Name=PPP2R5D;
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 DELTA-1).
TISSUE=Fetal brain;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DELTA-1 AND DELTA-3).
TISSUE=Brain cortex;
PubMed=9180267; DOI=10.1016/S0014-5793(97)00392-X;
Tanabe O., Gomez G.A., Nishito Y., Usui H., Takeda M.;
"Molecular heterogeneity of the cDNA encoding a 74-kDa regulatory
subunit (B'' or delta) of human protein phosphatase 2A.";
FEBS Lett. 408:52-56(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA-2), AND PROTEIN SEQUENCE OF
501-508; 550-559; 573-580 AND 584-601 (DELTA-1).
TISSUE=Bone marrow, and Brain cortex;
PubMed=8566219; DOI=10.1016/0014-5793(95)01500-0;
Tanabe O., Nagase T., Murakami T., Nozaki H., Usui H., Nishito Y.,
Hayashi H., Kagamiyama H., Takeda M.;
"Molecular cloning of a 74-kDa regulatory subunit (B'' or delta) of
human protein phosphatase 2A.";
FEBS Lett. 379:107-111(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA-2).
TISSUE=Heart;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA-1).
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS DELTA-1 AND DELTA-2).
TISSUE=Colon, Eye, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
INTERACTION WITH ADCY8.
PubMed=22976297; DOI=10.1242/jcs.111427;
Willoughby D., Halls M.L., Everett K.L., Ciruela A., Skroblin P.,
Klussmann E., Cooper D.M.;
"A key phosphorylation site in AC8 mediates regulation of Ca(2+)-
dependent cAMP dynamics by an AC8-AKAP79-PKA signalling complex.";
J. Cell Sci. 125:5850-5859(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63; SER-88; SER-89;
SER-90 AND SER-573, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
INVOLVEMENT IN MRD35, AND VARIANTS MRD35 LYS-198 AND ARG-201.
PubMed=25533962; DOI=10.1038/nature14135;
Deciphering Developmental Disorders Study;
"Large-scale discovery of novel genetic causes of developmental
disorders.";
Nature 519:223-228(2015).
[17]
VARIANT SER-53.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
[18]
VARIANTS MRD35 LYS-198; LYS-200; ARG-201 AND ARG-207, VARIANT SER-53,
CHARACTERIZATION OF VARIANTS MRD35 LYS-198; LYS-200; ARG-201 AND
ARG-207, AND CHARACTERIZATION OF VARIANT SER-53.
PubMed=26168268; DOI=10.1172/JCI79860;
Houge G., Haesen D., Vissers L.E., Mehta S., Parker M.J., Wright M.,
Vogt J., McKee S., Tolmie J.L., Cordeiro N., Kleefstra T.,
Willemsen M.H., Reijnders M.R., Berland S., Hayman E., Lahat E.,
Brilstra E.H., van Gassen K.L., Zonneveld-Huijssoon E., de Bie C.I.,
Hoischen A., Eichler E.E., Holdhus R., Steen V.M., Doeskeland S.O.,
Hurles M.E., FitzPatrick D.R., Janssens V.;
"B56delta-related protein phosphatase 2A dysfunction identified in
patients with intellectual disability.";
J. Clin. Invest. 125:3051-3062(2015).
-!- 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.
-!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme,
composed of a 36 kDa catalytic subunit (subunit C) and 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 SGO1. Interacts with
ADCY8 (PubMed:22976297). {ECO:0000269|PubMed:16541025,
ECO:0000269|PubMed:22976297}.
-!- INTERACTION:
O08785:Clock (xeno); NbExp=2; IntAct=EBI-396563, EBI-79859;
A1L4K1:FSD2; NbExp=3; IntAct=EBI-396563, EBI-5661036;
Q13136:PPFIA1; NbExp=3; IntAct=EBI-396563, EBI-745426;
P30153:PPP2R1A; NbExp=11; IntAct=EBI-396563, EBI-302388;
P30154:PPP2R1B; NbExp=3; IntAct=EBI-396563, EBI-357094;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-396563, EBI-739895;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nuclear in
interphase, nuclear during mitosis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Delta-1;
IsoId=Q14738-1; Sequence=Displayed;
Name=Delta-2;
IsoId=Q14738-2; Sequence=VSP_005111;
Name=Delta-3;
IsoId=Q14738-3; Sequence=VSP_005110;
-!- TISSUE SPECIFICITY: Isoform Delta-2 is widely expressed. Isoform
Delta-1 is highly expressed in brain.
-!- INDUCTION: By retinoic acid; in neuroblastoma cell lines.
-!- DISEASE: Mental retardation, autosomal dominant 35 (MRD35)
[MIM:616355]: A form of mental retardation, a disorder
characterized by significantly below average general intellectual
functioning associated with impairments in adaptive behavior and
manifested during the developmental period.
{ECO:0000269|PubMed:25533962, ECO:0000269|PubMed:26168268}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
family. {ECO:0000305}.
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EMBL; L76702; AAB69751.1; -; mRNA.
EMBL; AB000634; BAA20381.1; -; mRNA.
EMBL; AB000635; BAA20382.1; -; mRNA.
EMBL; D78360; BAA11372.1; -; mRNA.
EMBL; AK290604; BAF83293.1; -; mRNA.
EMBL; AB451342; BAG70156.1; -; mRNA.
EMBL; AB451357; BAG70171.1; -; mRNA.
EMBL; AL136304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX04133.1; -; Genomic_DNA.
EMBL; BC010692; AAH10692.1; -; mRNA.
EMBL; BC001095; AAH01095.1; -; mRNA.
EMBL; BC001175; AAH01175.1; -; mRNA.
CCDS; CCDS43464.1; -. [Q14738-3]
CCDS; CCDS4878.1; -. [Q14738-1]
CCDS; CCDS55002.1; -. [Q14738-2]
PIR; S68686; S68686.
RefSeq; NP_001257405.1; NM_001270476.1.
RefSeq; NP_006236.1; NM_006245.3. [Q14738-1]
RefSeq; NP_851307.1; NM_180976.2. [Q14738-2]
RefSeq; NP_851308.1; NM_180977.2. [Q14738-3]
UniGene; Hs.533308; -.
ProteinModelPortal; Q14738; -.
SMR; Q14738; -.
BioGrid; 111520; 84.
DIP; DIP-29961N; -.
ELM; Q14738; -.
IntAct; Q14738; 36.
MINT; Q14738; -.
STRING; 9606.ENSP00000417963; -.
iPTMnet; Q14738; -.
PhosphoSitePlus; Q14738; -.
BioMuta; PPP2R5D; -.
DMDM; 7387495; -.
EPD; Q14738; -.
MaxQB; Q14738; -.
PaxDb; Q14738; -.
PeptideAtlas; Q14738; -.
PRIDE; Q14738; -.
DNASU; 5528; -.
Ensembl; ENST00000394110; ENSP00000377669; ENSG00000112640. [Q14738-2]
Ensembl; ENST00000461010; ENSP00000420674; ENSG00000112640. [Q14738-3]
Ensembl; ENST00000485511; ENSP00000417963; ENSG00000112640. [Q14738-1]
GeneID; 5528; -.
KEGG; hsa:5528; -.
UCSC; uc003oth.5; human. [Q14738-1]
CTD; 5528; -.
DisGeNET; 5528; -.
EuPathDB; HostDB:ENSG00000112640.14; -.
GeneCards; PPP2R5D; -.
HGNC; HGNC:9312; PPP2R5D.
HPA; HPA029045; -.
HPA; HPA029046; -.
MalaCards; PPP2R5D; -.
MIM; 601646; gene.
MIM; 616355; phenotype.
neXtProt; NX_Q14738; -.
OpenTargets; ENSG00000112640; -.
Orphanet; 457279; Intellectual disability-macrocephaly-hypotonia-behavioral abnormalities syndrome.
PharmGKB; PA33676; -.
eggNOG; KOG2085; Eukaryota.
eggNOG; ENOG410XQJW; LUCA.
GeneTree; ENSGT00940000153459; -.
HOVERGEN; HBG000009; -.
InParanoid; Q14738; -.
KO; K11584; -.
OMA; DECSHEY; -.
OrthoDB; EOG091G06HU; -.
PhylomeDB; Q14738; -.
TreeFam; TF105556; -.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-163685; Integration of energy metabolism.
Reactome; R-HSA-163767; PP2A-mediated dephosphorylation of key metabolic factors.
Reactome; R-HSA-180024; DARPP-32 events.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
Reactome; R-HSA-198753; ERK/MAPK targets.
Reactome; R-HSA-202670; ERKs are inactivated.
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-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-70171; Glycolysis.
SignaLink; Q14738; -.
SIGNOR; Q14738; -.
GeneWiki; PPP2R5D; -.
GenomeRNAi; 5528; -.
PRO; PR:Q14738; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112640; Expressed in 227 organ(s), highest expression level in dorsal plus ventral thalamus.
CleanEx; HS_PPP2R5D; -.
ExpressionAtlas; Q14738; baseline and differential.
Genevisible; Q14738; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
GO; GO:0019888; F:protein phosphatase regulator activity; TAS:ProtInc.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; TAS:Reactome.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IEA:Ensembl.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0031952; P:regulation of protein autophosphorylation; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
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;
Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Mental retardation;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat.
CHAIN 1 602 Serine/threonine-protein phosphatase 2A
56 kDa regulatory subunit delta isoform.
/FTId=PRO_0000071452.
REPEAT 37 38 1.
REPEAT 39 40 2.
REPEAT 41 42 3.
REPEAT 43 44 4.
REPEAT 45 46 5.
REPEAT 47 48 6; approximate.
REPEAT 49 50 7; approximate.
REPEAT 51 52 8.
REGION 37 52 8 X 2 AA approximate tandem repeats of Q-
P.
MOTIF 523 530 SH3-binding; class I. {ECO:0000255}.
MOTIF 548 565 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 63 63 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 573 573 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 598 598 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
VAR_SEQ 11 116 Missing (in isoform Delta-3).
{ECO:0000303|PubMed:9180267}.
/FTId=VSP_005110.
VAR_SEQ 85 116 Missing (in isoform Delta-2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8566219}.
/FTId=VSP_005111.
VARIANT 53 53 P -> S (found in a patient with delayed
psychomotor development, no speech and
cataracts; no effect on binding to
subunit PPP2CA; no effect on binding to
subunit PPP2R1A; dbSNP:rs757369209).
{ECO:0000269|PubMed:23033978,
ECO:0000269|PubMed:26168268}.
/FTId=VAR_069414.
VARIANT 198 198 E -> K (in MRD35; decreases binding to
subunit PPP2CA; decreases binding to
subunit PPP2R1A; dbSNP:rs863225082).
{ECO:0000269|PubMed:25533962,
ECO:0000269|PubMed:26168268}.
/FTId=VAR_073708.
VARIANT 200 200 E -> K (in MRD35; decreases binding to
subunit PPP2CA; decreases binding to
subunit PPP2R1A; dbSNP:rs863225079).
{ECO:0000269|PubMed:26168268}.
/FTId=VAR_074491.
VARIANT 201 201 P -> R (in MRD35; decreases binding to
subunit PPP2CA; decreases binding to
subunit PPP2R1A; dbSNP:rs876657383).
{ECO:0000269|PubMed:25533962,
ECO:0000269|PubMed:26168268}.
/FTId=VAR_073709.
VARIANT 207 207 W -> R (in MRD35; decreases binding to
subunit PPP2CA; decreases binding to
subunit PPP2R1A; dbSNP:rs869320691).
{ECO:0000269|PubMed:26168268}.
/FTId=VAR_074492.
SEQUENCE 602 AA; 69992 MW; F15F71AF4E565387 CRC64;
MPYKLKKEKE PPKVAKCTAK PSSSGKDGGG ENTEEAQPQP QPQPQPQAQS QPPSSNKRPS
NSTPPPTQLS KIKYSGGPQI VKKERRQSSS RFNLSKNREL QKLPALKDSP TQEREELFIQ
KLRQCCVLFD FVSDPLSDLK FKEVKRAGLN EMVEYITHSR DVVTEAIYPE AVTMFSVNLF
RTLPPSSNPT GAEFDPEEDE PTLEAAWPHL QLVYEFFLRF LESPDFQPNI AKKYIDQKFV
LALLDLFDSE DPRERDFLKT ILHRIYGKFL GLRAYIRRQI NHIFYRFIYE TEHHNGIAEL
LEILGSIING FALPLKEEHK MFLIRVLLPL HKVKSLSVYH PQLAYCVVQF LEKESSLTEP
VIVGLLKFWP KTHSPKEVMF LNELEEILDV IEPSEFSKVM EPLFRQLAKC VSSPHFQVAE
RALYYWNNEY IMSLISDNAA RVLPIMFPAL YRNSKSHWNK TIHGLIYNAL KLFMEMNQKL
FDDCTQQYKA EKQKGRFRMK EREEMWQKIE ELARLNPQYP MFRAPPPLPP VYSMETETPT
AEDIQLLKRT VETEAVQMLK DIKKEKVLLR RKSELPQDVY TIKALEAHKR AEEFLTASQE
AL


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