2A5D_HUMAN
ID 2A5D_HUMAN Reviewed; 602 AA.
AC Q14738; A8K3I9; B5BUA6; O00494; O00696; Q15171; Q5TC39;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform;
DE AltName: Full=PP2A B subunit isoform B'-delta;
DE AltName: Full=PP2A B subunit isoform B56-delta;
DE AltName: Full=PP2A B subunit isoform PR61-delta;
DE AltName: Full=PP2A B subunit isoform R5-delta;
GN Name=PPP2R5D;
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 [MRNA] (ISOFORM DELTA-1).
RC TISSUE=Fetal brain;
RX PubMed=8703017; DOI=10.1074/jbc.271.36.22081;
RA McCright B., Rivers A.M., Audlin S., Virshup D.M.;
RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits
RT encodes differentiation-induced phosphoproteins that target PP2A to both
RT nucleus and cytoplasm.";
RL J. Biol. Chem. 271:22081-22089(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DELTA-1 AND DELTA-3).
RC TISSUE=Brain cortex;
RX PubMed=9180267; DOI=10.1016/s0014-5793(97)00392-x;
RA Tanabe O., Gomez G.A., Nishito Y., Usui H., Takeda M.;
RT "Molecular heterogeneity of the cDNA encoding a 74-kDa regulatory subunit
RT (B'' or delta) of human protein phosphatase 2A.";
RL FEBS Lett. 408:52-56(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA-2), AND PROTEIN SEQUENCE OF
RP 501-508; 550-559; 573-580 AND 584-601 (DELTA-1).
RC TISSUE=Bone marrow, and Brain cortex;
RX PubMed=8566219; DOI=10.1016/0014-5793(95)01500-0;
RA Tanabe O., Nagase T., Murakami T., Nozaki H., Usui H., Nishito Y.,
RA Hayashi H., Kagamiyama H., Takeda M.;
RT "Molecular cloning of a 74-kDa regulatory subunit (B'' or delta) of human
RT protein phosphatase 2A.";
RL FEBS Lett. 379:107-111(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA-2).
RC TISSUE=Heart;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA-1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS DELTA-1 AND DELTA-2).
RC TISSUE=Colon, Eye, and Kidney;
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 [9]
RP INTERACTION WITH SGO1.
RX PubMed=16541025; DOI=10.1038/nature04663;
RA Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
RA Kawashima S.A., Watanabe Y.;
RT "Shugoshin collaborates with protein phosphatase 2A to protect cohesin.";
RL Nature 441:46-52(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP INTERACTION WITH ADCY8.
RX PubMed=22976297; DOI=10.1242/jcs.111427;
RA Willoughby D., Halls M.L., Everett K.L., Ciruela A., Skroblin P.,
RA Klussmann E., Cooper D.M.;
RT "A key phosphorylation site in AC8 mediates regulation of Ca(2+)-dependent
RT cAMP dynamics by an AC8-AKAP79-PKA signalling complex.";
RL J. Cell Sci. 125:5850-5859(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-63; SER-88; SER-89; SER-90
RP AND SER-573, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP INVOLVEMENT IN MRD35, AND VARIANTS MRD35 LYS-198 AND ARG-201.
RX PubMed=25533962; DOI=10.1038/nature14135;
RG Deciphering Developmental Disorders Study;
RT "Large-scale discovery of novel genetic causes of developmental
RT disorders.";
RL Nature 519:223-228(2015).
RN [17]
RP VARIANT SER-53.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
RN [18]
RP VARIANTS MRD35 LYS-198; LYS-200; ARG-201 AND ARG-207, VARIANT SER-53,
RP CHARACTERIZATION OF VARIANTS MRD35 LYS-198; LYS-200; ARG-201 AND ARG-207,
RP AND CHARACTERIZATION OF VARIANT SER-53.
RX PubMed=26168268; DOI=10.1172/jci79860;
RA Houge G., Haesen D., Vissers L.E., Mehta S., Parker M.J., Wright M.,
RA Vogt J., McKee S., Tolmie J.L., Cordeiro N., Kleefstra T., Willemsen M.H.,
RA Reijnders M.R., Berland S., Hayman E., Lahat E., Brilstra E.H.,
RA van Gassen K.L., Zonneveld-Huijssoon E., de Bie C.I., Hoischen A.,
RA Eichler E.E., Holdhus R., Steen V.M., Doeskeland S.O., Hurles M.E.,
RA FitzPatrick D.R., Janssens V.;
RT "B56delta-related protein phosphatase 2A dysfunction identified in patients
RT with intellectual disability.";
RL J. Clin. Invest. 125:3051-3062(2015).
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.
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 SGO1. Interacts with ADCY8 (PubMed:22976297).
CC {ECO:0000269|PubMed:16541025, ECO:0000269|PubMed:22976297}.
CC -!- INTERACTION:
CC Q14738; Q8WWB3: DYDC1; NbExp=3; IntAct=EBI-396563, EBI-740680;
CC Q14738; A1L4K1: FSD2; NbExp=3; IntAct=EBI-396563, EBI-5661036;
CC Q14738; Q13136: PPFIA1; NbExp=5; IntAct=EBI-396563, EBI-745426;
CC Q14738; P30153: PPP2R1A; NbExp=12; IntAct=EBI-396563, EBI-302388;
CC Q14738; P30154: PPP2R1B; NbExp=3; IntAct=EBI-396563, EBI-357094;
CC Q14738; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-396563, EBI-739895;
CC Q14738; O08785: Clock; Xeno; NbExp=2; IntAct=EBI-396563, EBI-79859;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nuclear in interphase,
CC nuclear during mitosis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Delta-1;
CC IsoId=Q14738-1; Sequence=Displayed;
CC Name=Delta-2;
CC IsoId=Q14738-2; Sequence=VSP_005111;
CC Name=Delta-3;
CC IsoId=Q14738-3; Sequence=VSP_005110;
CC -!- TISSUE SPECIFICITY: Isoform Delta-2 is widely expressed. Isoform Delta-
CC 1 is highly expressed in brain.
CC -!- INDUCTION: By retinoic acid; in neuroblastoma cell lines.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 35
CC (MRD35) [MIM:616355]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC {ECO:0000269|PubMed:25533962, ECO:0000269|PubMed:26168268}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
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DR EMBL; L76702; AAB69751.1; -; mRNA.
DR EMBL; AB000634; BAA20381.1; -; mRNA.
DR EMBL; AB000635; BAA20382.1; -; mRNA.
DR EMBL; D78360; BAA11372.1; -; mRNA.
DR EMBL; AK290604; BAF83293.1; -; mRNA.
DR EMBL; AB451342; BAG70156.1; -; mRNA.
DR EMBL; AB451357; BAG70171.1; -; mRNA.
DR EMBL; AL136304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04133.1; -; Genomic_DNA.
DR EMBL; BC010692; AAH10692.1; -; mRNA.
DR EMBL; BC001095; AAH01095.1; -; mRNA.
DR EMBL; BC001175; AAH01175.1; -; mRNA.
DR CCDS; CCDS43464.1; -. [Q14738-3]
DR CCDS; CCDS4878.1; -. [Q14738-1]
DR CCDS; CCDS55002.1; -. [Q14738-2]
DR PIR; S68686; S68686.
DR RefSeq; NP_001257405.1; NM_001270476.1.
DR RefSeq; NP_006236.1; NM_006245.3. [Q14738-1]
DR RefSeq; NP_851307.1; NM_180976.2. [Q14738-2]
DR RefSeq; NP_851308.1; NM_180977.2. [Q14738-3]
DR AlphaFoldDB; Q14738; -.
DR SMR; Q14738; -.
DR BioGRID; 111520; 151.
DR DIP; DIP-29961N; -.
DR ELM; Q14738; -.
DR IntAct; Q14738; 57.
DR MINT; Q14738; -.
DR STRING; 9606.ENSP00000417963; -.
DR GlyGen; Q14738; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14738; -.
DR MetOSite; Q14738; -.
DR PhosphoSitePlus; Q14738; -.
DR BioMuta; PPP2R5D; -.
DR DMDM; 7387495; -.
DR EPD; Q14738; -.
DR jPOST; Q14738; -.
DR MassIVE; Q14738; -.
DR MaxQB; Q14738; -.
DR PaxDb; Q14738; -.
DR PeptideAtlas; Q14738; -.
DR PRIDE; Q14738; -.
DR ProteomicsDB; 60149; -.
DR ProteomicsDB; 60150; -. [Q14738-2]
DR ProteomicsDB; 60151; -. [Q14738-3]
DR Antibodypedia; 30209; 378 antibodies from 39 providers.
DR DNASU; 5528; -.
DR Ensembl; ENST00000394110.7; ENSP00000377669.3; ENSG00000112640.16. [Q14738-2]
DR Ensembl; ENST00000461010.5; ENSP00000420674.1; ENSG00000112640.16. [Q14738-3]
DR Ensembl; ENST00000485511.6; ENSP00000417963.1; ENSG00000112640.16. [Q14738-1]
DR GeneID; 5528; -.
DR KEGG; hsa:5528; -.
DR MANE-Select; ENST00000485511.6; ENSP00000417963.1; NM_006245.4; NP_006236.1.
DR UCSC; uc003oth.5; human. [Q14738-1]
DR CTD; 5528; -.
DR DisGeNET; 5528; -.
DR GeneCards; PPP2R5D; -.
DR GeneReviews; PPP2R5D; -.
DR HGNC; HGNC:9312; PPP2R5D.
DR HPA; ENSG00000112640; Low tissue specificity.
DR MalaCards; PPP2R5D; -.
DR MIM; 601646; gene.
DR MIM; 616355; phenotype.
DR neXtProt; NX_Q14738; -.
DR OpenTargets; ENSG00000112640; -.
DR Orphanet; 457279; Intellectual disability-macrocephaly-hypotonia-behavioral abnormalities syndrome.
DR PharmGKB; PA33676; -.
DR VEuPathDB; HostDB:ENSG00000112640; -.
DR eggNOG; KOG2085; Eukaryota.
DR GeneTree; ENSGT01030000234620; -.
DR HOGENOM; CLU_012437_3_1_1; -.
DR InParanoid; Q14738; -.
DR OMA; CSHEYNE; -.
DR PhylomeDB; Q14738; -.
DR TreeFam; TF105556; -.
DR PathwayCommons; Q14738; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-163685; Integration of energy metabolism.
DR Reactome; R-HSA-163767; PP2A-mediated dephosphorylation of key metabolic factors.
DR Reactome; R-HSA-180024; DARPP-32 events.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-HSA-198753; ERK/MAPK targets.
DR Reactome; R-HSA-202670; ERKs are inactivated.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
DR Reactome; R-HSA-432142; Platelet sensitization by LDL.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-HSA-5339716; Signaling by GSK3beta mutants.
DR Reactome; R-HSA-5358747; CTNNB1 S33 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358749; CTNNB1 S37 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358751; CTNNB1 S45 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358752; CTNNB1 T41 mutants aren't phosphorylated.
DR Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
DR Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
DR Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-5673000; RAF activation.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9634600; Regulation of glycolysis by fructose 2,6-bisphosphate metabolism.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q14738; -.
DR SIGNOR; Q14738; -.
DR BioGRID-ORCS; 5528; 17 hits in 1078 CRISPR screens.
DR ChiTaRS; PPP2R5D; human.
DR GeneWiki; PPP2R5D; -.
DR GenomeRNAi; 5528; -.
DR Pharos; Q14738; Tbio.
DR PRO; PR:Q14738; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q14738; protein.
DR Bgee; ENSG00000112640; Expressed in ganglionic eminence and 207 other tissues.
DR ExpressionAtlas; Q14738; baseline and differential.
DR Genevisible; Q14738; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; TAS:ProtInc.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IEA:Ensembl.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Disease variant; Intellectual disability; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..602
FT /note="Serine/threonine-protein phosphatase 2A 56 kDa
FT regulatory subunit delta isoform"
FT /id="PRO_0000071452"
FT REPEAT 37..38
FT /note="1"
FT REPEAT 39..40
FT /note="2"
FT REPEAT 41..42
FT /note="3"
FT REPEAT 43..44
FT /note="4"
FT REPEAT 45..46
FT /note="5"
FT REPEAT 47..48
FT /note="6; approximate"
FT REPEAT 49..50
FT /note="7; approximate"
FT REPEAT 51..52
FT /note="8"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..52
FT /note="8 X 2 AA approximate tandem repeats of Q-P"
FT MOTIF 523..530
FT /note="SH3-binding; class I"
FT /evidence="ECO:0000255"
FT MOTIF 548..565
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 63
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VAR_SEQ 11..116
FT /note="Missing (in isoform Delta-3)"
FT /evidence="ECO:0000303|PubMed:9180267"
FT /id="VSP_005110"
FT VAR_SEQ 85..116
FT /note="Missing (in isoform Delta-2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8566219"
FT /id="VSP_005111"
FT VARIANT 53
FT /note="P -> S (found in a patient with delayed psychomotor
FT development, no speech and cataracts; no effect on binding
FT to subunit PPP2CA; no effect on binding to subunit PPP2R1A;
FT dbSNP:rs757369209)"
FT /evidence="ECO:0000269|PubMed:23033978,
FT ECO:0000269|PubMed:26168268"
FT /id="VAR_069414"
FT VARIANT 198
FT /note="E -> K (in MRD35; decreases binding to subunit
FT PPP2CA; decreases binding to subunit PPP2R1A;
FT dbSNP:rs863225082)"
FT /evidence="ECO:0000269|PubMed:25533962,
FT ECO:0000269|PubMed:26168268"
FT /id="VAR_073708"
FT VARIANT 200
FT /note="E -> K (in MRD35; decreases binding to subunit
FT PPP2CA; decreases binding to subunit PPP2R1A;
FT dbSNP:rs863225079)"
FT /evidence="ECO:0000269|PubMed:26168268"
FT /id="VAR_074491"
FT VARIANT 201
FT /note="P -> R (in MRD35; decreases binding to subunit
FT PPP2CA; decreases binding to subunit PPP2R1A;
FT dbSNP:rs876657383)"
FT /evidence="ECO:0000269|PubMed:25533962,
FT ECO:0000269|PubMed:26168268"
FT /id="VAR_073709"
FT VARIANT 207
FT /note="W -> R (in MRD35; decreases binding to subunit
FT PPP2CA; decreases binding to subunit PPP2R1A;
FT dbSNP:rs869320691)"
FT /evidence="ECO:0000269|PubMed:26168268"
FT /id="VAR_074492"
SQ 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
