ID 2ABB_HUMAN Reviewed; 443 AA. AC Q00005; A6NEJ2; A8K102; B3KPD0; B7Z2F2; B7Z304; D3DQF7; D3DQF8; G3V149; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 27-MAR-2024, entry version 217. DE RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform; DE AltName: Full=PP2A subunit B isoform B55-beta; DE AltName: Full=PP2A subunit B isoform PR55-beta; DE AltName: Full=PP2A subunit B isoform R2-beta; DE AltName: Full=PP2A subunit B isoform beta; GN Name=PPP2R2B; 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 1). RC TISSUE=Fetal brain; RX PubMed=1849734; DOI=10.1021/bi00229a001; RA Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J., RA Merlevede W., Hofsteenge J., Hemmings B.A.; RT "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: RT evidence for a neuronal-specific isoform."; RL Biochemistry 30:3589-3597(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-433 (ISOFORM 7). RC TISSUE=Brain, and Corpus callosum; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-131 (ISOFORM 6). RC TISSUE=Brain, and Hypothalamus; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-197 (ISOFORM 2). RA Strausberg R.L.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [7] RP INVOLVEMENT IN SCA12. RX PubMed=10581021; DOI=10.1038/70493; RA Holmes S.E., O'Hearn E.E., McInnis M.G., Gorelick-Feldman D.A., RA Kleiderlein J.J., Callahan C., Kwak N.G., Ingersoll-Ashworth R.G., RA Sherr M., Sumner A.J., Sharp A.H., Ananth U., Seltzer W.K., Boss M.A., RA Vieria-Saecker A.-M., Epplen J.T., Riess O., Ross C.A., Margolis R.L.; RT "Expansion of a novel CAG trinucleotide repeat in the 5' region of PPP2R2B RT is associated with SCA12."; RL Nat. Genet. 23:391-392(1999). RN [8] 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). RN [9] RP INTERACTION WITH IER5. RX PubMed=26496226; DOI=10.1016/j.febslet.2015.10.013; RA Kawabata S., Ishita Y., Ishikawa Y., Sakurai H.; RT "Immediate-early response 5 (IER5) interacts with protein phosphatase 2A RT and regulates the phosphorylation of ribosomal protein S6 kinase and heat RT shock factor 1."; RL FEBS Lett. 589:3679-3685(2015). RN [10] RP VARIANT PRO-138. RX PubMed=25356899; DOI=10.1371/journal.pgen.1004772; RA Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C., Patry L., RA Massicotte C., Ambalavanan A., Spiegelman D., Diallo O., Henrion E., RA Dionne-Laporte A., Fougerat A., Pshezhetsky A.V., Venkateswaran S., RA Rouleau G.A., Michaud J.L.; RT "De novo mutations in moderate or severe intellectual disability."; RL PLoS Genet. 10:E1004772-E1004772(2014). 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. Within the CC PP2A holoenzyme complex, isoform 2 is required to promote proapoptotic CC activity (By similarity). Isoform 2 regulates neuronal survival through CC the mitochondrial fission and fusion balance (By similarity). CC {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 (By CC similarity). Interacts with TOMM22 (By similarity). Interacts with IER5 CC (via N- and C-terminal regions) (PubMed:25816751, PubMed:26496226). CC {ECO:0000250, ECO:0000250|UniProtKB:P36877, CC ECO:0000269|PubMed:25816751, ECO:0000269|PubMed:26496226}. CC -!- INTERACTION: CC Q00005; P05067: APP; NbExp=3; IntAct=EBI-1052159, EBI-77613; CC Q00005; O15530: PDPK1; NbExp=8; IntAct=EBI-1052159, EBI-717097; CC Q00005; P30153: PPP2R1A; NbExp=10; IntAct=EBI-1052159, EBI-302388; CC Q00005; P23443: RPS6KB1; NbExp=2; IntAct=EBI-1052159, EBI-1775921; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000250}. Cytoplasm, CC cytoskeleton {ECO:0000250}. Membrane {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250}. CC Mitochondrion {ECO:0000250}. Mitochondrion outer membrane CC {ECO:0000250}. Note=Under basal conditions, localizes to both cytosolic CC and mitochondrial compartments. Relocalizes from the cytosolic to the CC mitochondrial compartment during apoptosis. Its targeting to the outer CC mitochondrial membrane (OMM) involves an association with import CC receptors of the TOM complex and is required to promote proapoptotic CC activity (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=Bbeta, Bbeta1; CC IsoId=Q00005-1; Sequence=Displayed; CC Name=2; Synonyms=Bbeta2; CC IsoId=Q00005-2; Sequence=VSP_037976; CC Name=3; CC IsoId=Q00005-3; Sequence=VSP_037977; CC Name=4; CC IsoId=Q00005-4; Sequence=VSP_037978; CC Name=5; CC IsoId=Q00005-5; Sequence=VSP_037979; CC Name=6; CC IsoId=Q00005-6; Sequence=VSP_044923; CC Name=7; CC IsoId=Q00005-7; Sequence=VSP_045748; CC -!- TISSUE SPECIFICITY: Brain. CC -!- DOMAIN: The N-terminal 26 residues of isoform 2 constitute a cryptic CC mitochondrial matrix import signal with critical basic and hydrophobic CC residues, that is necessary and sufficient for targeting the PP2A CC holoenzyme to the outer mitochondrial membrane (OMM) and does not CC affect holoenzyme formation or catalytic activity. {ECO:0000250}. CC -!- DOMAIN: The last WD repeat of isoform 2 constitutes a mitochondrial CC stop-transfer domain that confers resistance to the unfolding step CC process required for import and therefore prevents PPP2R2B matrix CC translocation and signal sequence cleavage. {ECO:0000250}. CC -!- DISEASE: Spinocerebellar ataxia 12 (SCA12) [MIM:604326]: CC Spinocerebellar ataxia is a clinically and genetically heterogeneous CC group of cerebellar disorders. Patients show progressive incoordination CC of gait and often poor coordination of hands, speech and eye movements, CC due to degeneration of the cerebellum with variable involvement of the CC brainstem and spinal cord. SCA12 is an autosomal dominant cerebellar CC ataxia (ADCA). {ECO:0000269|PubMed:10581021}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 1]: Conserved additional ATG codons are found CC 5' of the putative initiator codon in transcripts supporting isoform 1. CC They may initiate the translation of upstream short open reading frames CC altering the expression of that isoform as described in PubMed:1849734. CC -!- MISCELLANEOUS: [Isoform 2]: Contains a cryptic mitochondrial transit CC peptide at positions 1-26. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH31790.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG51642.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG51642.1; Type=Erroneous termination; Note=Truncated C-terminus.; 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; M64930; AAA36493.1; -; mRNA. DR EMBL; AK056192; BAG51642.1; ALT_SEQ; mRNA. DR EMBL; AK289717; BAF82406.1; -; mRNA. DR EMBL; AK294659; BAH11838.1; -; mRNA. DR EMBL; AK295347; BAH12040.1; -; mRNA. DR EMBL; AC008728; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC009186; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC010251; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC011386; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC011357; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC091919; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC091924; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471062; EAW61829.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61831.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61832.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61833.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61834.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61835.1; -; Genomic_DNA. DR EMBL; BC031790; AAH31790.1; ALT_INIT; mRNA. DR EMBL; BI490027; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BI669304; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS4283.1; -. [Q00005-2] DR CCDS; CCDS4284.2; -. [Q00005-5] DR CCDS; CCDS43380.1; -. [Q00005-6] DR CCDS; CCDS64281.1; -. [Q00005-4] DR CCDS; CCDS64282.1; -. [Q00005-3] DR CCDS; CCDS93800.1; -. [Q00005-1] DR PIR; B38351; B38351. DR RefSeq; NP_001258828.1; NM_001271899.1. [Q00005-3] DR RefSeq; NP_001258829.1; NM_001271900.1. [Q00005-4] DR RefSeq; NP_001258877.1; NM_001271948.1. [Q00005-6] DR RefSeq; NP_858060.2; NM_181674.2. [Q00005-5] DR RefSeq; NP_858061.2; NM_181675.3. [Q00005-1] DR RefSeq; NP_858062.1; NM_181676.2. [Q00005-2] DR RefSeq; NP_858063.1; NM_181677.2. DR RefSeq; NP_858064.1; NM_181678.2. [Q00005-6] DR AlphaFoldDB; Q00005; -. DR SMR; Q00005; -. DR BioGRID; 111513; 239. DR IntAct; Q00005; 184. DR MINT; Q00005; -. DR STRING; 9606.ENSP00000377936; -. DR GlyGen; Q00005; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q00005; -. DR PhosphoSitePlus; Q00005; -. DR SwissPalm; Q00005; -. DR BioMuta; PPP2R2B; -. DR DMDM; 231446; -. DR EPD; Q00005; -. DR jPOST; Q00005; -. DR MassIVE; Q00005; -. DR MaxQB; Q00005; -. DR PaxDb; 9606-ENSP00000377936; -. DR PeptideAtlas; Q00005; -. DR PRIDE; Q00005; -. DR ProteomicsDB; 32258; -. DR ProteomicsDB; 57832; -. DR ProteomicsDB; 57833; -. [Q00005-2] DR ProteomicsDB; 57834; -. [Q00005-3] DR ProteomicsDB; 57835; -. [Q00005-4] DR ProteomicsDB; 57836; -. [Q00005-5] DR Antibodypedia; 27589; 273 antibodies from 32 providers. DR DNASU; 5521; -. DR Ensembl; ENST00000336640.10; ENSP00000336591.6; ENSG00000156475.19. [Q00005-2] DR Ensembl; ENST00000394409.7; ENSP00000377931.4; ENSG00000156475.19. [Q00005-1] DR Ensembl; ENST00000394411.9; ENSP00000377933.3; ENSG00000156475.19. [Q00005-1] DR Ensembl; ENST00000394413.7; ENSP00000377935.4; ENSG00000156475.19. [Q00005-4] DR Ensembl; ENST00000394414.5; ENSP00000377936.1; ENSG00000156475.19. [Q00005-5] DR Ensembl; ENST00000453001.5; ENSP00000398779.2; ENSG00000156475.19. [Q00005-6] DR Ensembl; ENST00000504198.5; ENSP00000421396.1; ENSG00000156475.19. [Q00005-3] DR Ensembl; ENST00000508545.6; ENSP00000431320.1; ENSG00000156475.19. [Q00005-6] DR GeneID; 5521; -. DR KEGG; hsa:5521; -. DR MANE-Select; ENST00000394411.9; ENSP00000377933.3; NM_181675.4; NP_858061.3. DR UCSC; uc003loe.6; human. [Q00005-1] DR AGR; HGNC:9305; -. DR CTD; 5521; -. DR DisGeNET; 5521; -. DR GeneCards; PPP2R2B; -. DR HGNC; HGNC:9305; PPP2R2B. DR HPA; ENSG00000156475; Tissue enhanced (brain, retina). DR MalaCards; PPP2R2B; -. DR MIM; 604325; gene. DR MIM; 604326; phenotype. DR neXtProt; NX_Q00005; -. DR OpenTargets; ENSG00000156475; -. DR Orphanet; 98762; Spinocerebellar ataxia type 12. DR PharmGKB; PA33669; -. DR VEuPathDB; HostDB:ENSG00000156475; -. DR eggNOG; KOG1354; Eukaryota. DR GeneTree; ENSGT00950000182864; -. DR HOGENOM; CLU_021713_3_3_1; -. DR InParanoid; Q00005; -. DR OMA; VNMESAP; -. DR OrthoDB; 397100at2759; -. DR PhylomeDB; Q00005; -. DR TreeFam; TF105553; -. DR PathwayCommons; Q00005; -. DR SignaLink; Q00005; -. DR SIGNOR; Q00005; -. DR BioGRID-ORCS; 5521; 14 hits in 1150 CRISPR screens. DR ChiTaRS; PPP2R2B; human. DR GeneWiki; PPP2R2B; -. DR GenomeRNAi; 5521; -. DR Pharos; Q00005; Tbio. DR PRO; PR:Q00005; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q00005; Protein. DR Bgee; ENSG00000156475; Expressed in sperm and 169 other cell types or tissues. DR ExpressionAtlas; Q00005; baseline and differential. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central. DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR000009; PP2A_PR55. DR InterPro; IPR018067; PP2A_PR55_CS. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR11871; PROTEIN PHOSPHATASE PP2A REGULATORY SUBUNIT B; 1. DR PANTHER; PTHR11871:SF1; SERINE_THREONINE-PROTEIN PHOSPHATASE 2A 55 KDA REGULATORY SUBUNIT B BETA ISOFORM; 1. DR PIRSF; PIRSF037309; PP2A_PR55; 1. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR Genevisible; Q00005; HS. PE 1: Evidence at protein level; KW Alternative splicing; Apoptosis; Cytoplasm; Cytoskeleton; Disease variant; KW Membrane; Mitochondrion; Mitochondrion outer membrane; Neurodegeneration; KW Phosphoprotein; Reference proteome; Repeat; Spinocerebellar ataxia; KW WD repeat. FT CHAIN 1..443 FT /note="Serine/threonine-protein phosphatase 2A 55 kDa FT regulatory subunit B beta isoform" FT /id="PRO_0000071421" FT REPEAT 22..61 FT /note="WD 1" FT REPEAT 87..128 FT /note="WD 2" FT REPEAT 171..209 FT /note="WD 3" FT REPEAT 220..260 FT /note="WD 4" FT REPEAT 279..317 FT /note="WD 5" FT REPEAT 334..375 FT /note="WD 6" FT REPEAT 410..442 FT /note="WD 7" FT MOD_RES 275 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P36877" FT MOD_RES 295 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P36877" FT MOD_RES 298 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P36877" FT VAR_SEQ 1..23 FT /note="MEEDIDTRKINNSFLRDHSYATE -> MNYPDENTYGNK (in isoform FT 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_044923" FT VAR_SEQ 1..21 FT /note="MEEDIDTRKINNSFLRDHSYA -> MKCFSRYLPYIFRPPNTILSSSCH FT (in isoform 2)" FT /evidence="ECO:0000303|Ref.6" FT /id="VSP_037976" FT VAR_SEQ 1..21 FT /note="MEEDIDTRKINNSFLRDHSYA -> MIPGIGTLTQDTLWCFSQVKGTIEIGT FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037977" FT VAR_SEQ 1 FT /note="M -> MVLQPSERHYRDWNHRRLGPWCSPTGSPAPLSCETGCGEGSWILVCR FT LLVPTQVSLLSM (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_037978" FT VAR_SEQ 1 FT /note="M -> MLLSLPALHLQTSEHHPFFQLPHRRLGPWCSPTGSPAPLSCETGCGE FT GSWILVCRLLVPTQVSLLSM (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_037979" FT VAR_SEQ 1 FT /note="M -> MHQPPPASCSSSSSSSSSSCECARVGVRVSALAPAAAPCPAPRQLPY FT PRLPEPPSRGTSTLIPARLGPWCSPTGSPAPLSCETGCGEGSWILVCRLLVPTQVSLLS FT M (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045748" FT VARIANT 36 FT /note="G -> V (in dbSNP:rs11547494)" FT /id="VAR_051738" FT VARIANT 138 FT /note="R -> P (found in a patient with moderate FT intellectual disability, autism and intractable epilepsy; FT uncertain significance)" FT /evidence="ECO:0000269|PubMed:25356899" FT /id="VAR_078654" FT CONFLICT 22 FT /note="T -> A (in Ref. 2; BAH11838)" FT /evidence="ECO:0000305" FT CONFLICT 62 FT /note="H -> N (in Ref. 5; BI669304)" FT /evidence="ECO:0000305" FT CONFLICT 109 FT /note="S -> F (in Ref. 2; BAH12040)" FT /evidence="ECO:0000305" FT CONFLICT 163 FT /note="T -> S (in Ref. 6; BI490027)" FT /evidence="ECO:0000305" FT CONFLICT 164 FT /note="P -> S (in Ref. 2; BAF82406)" FT /evidence="ECO:0000305" FT CONFLICT 292 FT /note="S -> R (in Ref. 2; BAH12040)" FT /evidence="ECO:0000305" SQ SEQUENCE 443 AA; 51710 MW; C383C834B2852B8F CRC64; MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN //