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Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta)

 2ABB_HUMAN              Reviewed;         443 AA.
Q00005; A6NEJ2; A8K102; B3KPD0; B7Z2F2; B7Z304; D3DQF7; D3DQF8;
G3V149;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
23-MAY-2018, entry version 184.
RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform;
AltName: Full=PP2A subunit B isoform B55-beta;
AltName: Full=PP2A subunit B isoform PR55-beta;
AltName: Full=PP2A subunit B isoform R2-beta;
AltName: Full=PP2A subunit B isoform beta;
Name=PPP2R2B;
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 1).
TISSUE=Fetal brain;
PubMed=1849734; DOI=10.1021/bi00229a001;
Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J.,
Merlevede W., Hofsteenge J., Hemmings B.A.;
"Structure of the 55-kDa regulatory subunit of protein phosphatase 2A:
evidence for a neuronal-specific isoform.";
Biochemistry 30:3589-3597(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-433 (ISOFORM 7).
TISSUE=Brain, and Corpus callosum;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-131 (ISOFORM 6).
TISSUE=Brain, and Hypothalamus;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-197 (ISOFORM 2).
Strausberg R.L.;
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[7]
INVOLVEMENT IN SCA12.
PubMed=10581021; DOI=10.1038/70493;
Holmes S.E., O'Hearn E.E., McInnis M.G., Gorelick-Feldman D.A.,
Kleiderlein J.J., Callahan C., Kwak N.G., Ingersoll-Ashworth R.G.,
Sherr M., Sumner A.J., Sharp A.H., Ananth U., Seltzer W.K., Boss M.A.,
Vieria-Saecker A.-M., Epplen J.T., Riess O., Ross C.A., Margolis R.L.;
"Expansion of a novel CAG trinucleotide repeat in the 5' region of
PPP2R2B is associated with SCA12.";
Nat. Genet. 23:391-392(1999).
[8]
INTERACTION WITH IER5.
PubMed=25816751; DOI=10.1016/j.febslet.2015.03.019;
Ishikawa Y., Kawabata S., Sakurai H.;
"HSF1 transcriptional activity is modulated by IER5 and PP2A/B55.";
FEBS Lett. 589:1150-1155(2015).
[9]
INTERACTION WITH IER5.
PubMed=26496226; DOI=10.1016/j.febslet.2015.10.013;
Kawabata S., Ishita Y., Ishikawa Y., Sakurai H.;
"Immediate-early response 5 (IER5) interacts with protein phosphatase
2A and regulates the phosphorylation of ribosomal protein S6 kinase
and heat shock factor 1.";
FEBS Lett. 589:3679-3685(2015).
[10]
VARIANT PRO-138.
PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C.,
Patry L., Massicotte C., Ambalavanan A., Spiegelman D., Diallo O.,
Henrion E., Dionne-Laporte A., Fougerat A., Pshezhetsky A.V.,
Venkateswaran S., Rouleau G.A., Michaud J.L.;
"De novo mutations in moderate or severe intellectual disability.";
PLoS Genet. 10:E1004772-E1004772(2014).
-!- 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. Within the PP2A holoenzyme complex, isoform 2 is
required to promote proapoptotic activity (By similarity). Isoform
2 regulates neuronal survival through the mitochondrial fission
and fusion balance (By similarity). {ECO:0000250}.
-!- 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 (By similarity). Interacts with
TOMM22 (By similarity). Interacts with IER5 (via N- and C-terminal
regions) (PubMed:25816751, PubMed:26496226). {ECO:0000250,
ECO:0000250|UniProtKB:P36877, ECO:0000269|PubMed:25816751,
ECO:0000269|PubMed:26496226}.
-!- INTERACTION:
O15530:PDPK1; NbExp=8; IntAct=EBI-1052159, EBI-717097;
P30153:PPP2R1A; NbExp=10; IntAct=EBI-1052159, EBI-302388;
P23443:RPS6KB1; NbExp=2; IntAct=EBI-1052159, EBI-1775921;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000250}.
Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000250}.
Mitochondrion {ECO:0000250}. Mitochondrion outer membrane
{ECO:0000250}. Note=Under basal conditions, localizes to both
cytosolic and mitochondrial compartments. Relocalizes from the
cytosolic to the mitochondrial compartment during apoptosis. Its
targeting to the outer mitochondrial membrane (OMM) involves an
association with import receptors of the TOM complex and is
required to promote proapoptotic activity (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=Bbeta, Bbeta1;
IsoId=Q00005-1; Sequence=Displayed;
Note=Conserved additional ATG codons are found 5' of the
putative initiator codon in transcripts supporting isoform 1.
They may initiate the translation of upstream short open reading
frames altering the expression of that isoform as described in
PubMed:1849734.;
Name=2; Synonyms=Bbeta2;
IsoId=Q00005-2; Sequence=VSP_037976;
Note=Contains a cryptic mitochondrial transit peptide at
positions 1-26. {ECO:0000250};
Name=3;
IsoId=Q00005-3; Sequence=VSP_037977;
Name=4;
IsoId=Q00005-4; Sequence=VSP_037978;
Name=5;
IsoId=Q00005-5; Sequence=VSP_037979;
Name=6;
IsoId=Q00005-6; Sequence=VSP_044923;
Name=7;
IsoId=Q00005-7; Sequence=VSP_045748;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Brain.
-!- DOMAIN: The N-terminal 26 residues of isoform 2 constitute a
cryptic mitochondrial matrix import signal with critical basic and
hydrophobic residues, that is necessary and sufficient for
targeting the PP2A holoenzyme to the outer mitochondrial membrane
(OMM) and does not affect holoenzyme formation or catalytic
activity. {ECO:0000250}.
-!- DOMAIN: The last WD repeat of isoform 2 constitutes a
mitochondrial stop-transfer domain that confers resistance to the
unfolding step process required for import and therefore prevents
PPP2R2B matrix translocation and signal sequence cleavage.
{ECO:0000250}.
-!- DISEASE: Spinocerebellar ataxia 12 (SCA12) [MIM:604326]:
Spinocerebellar ataxia is a clinically and genetically
heterogeneous group of cerebellar disorders. Patients show
progressive incoordination of gait and often poor coordination of
hands, speech and eye movements, due to degeneration of the
cerebellum with variable involvement of the brainstem and spinal
cord. SCA12 is an autosomal dominant cerebellar ataxia (ADCA).
{ECO:0000269|PubMed:10581021}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH31790.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG51642.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG51642.1; Type=Erroneous termination; Positions=116; Note=Translated as Lys.; Evidence={ECO:0000305};
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EMBL; M64930; AAA36493.1; -; mRNA.
EMBL; AK056192; BAG51642.1; ALT_SEQ; mRNA.
EMBL; AK289717; BAF82406.1; -; mRNA.
EMBL; AK294659; BAH11838.1; -; mRNA.
EMBL; AK295347; BAH12040.1; -; mRNA.
EMBL; AC008728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC009186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC091919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC091924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW61829.1; -; Genomic_DNA.
EMBL; CH471062; EAW61831.1; -; Genomic_DNA.
EMBL; CH471062; EAW61832.1; -; Genomic_DNA.
EMBL; CH471062; EAW61833.1; -; Genomic_DNA.
EMBL; CH471062; EAW61834.1; -; Genomic_DNA.
EMBL; CH471062; EAW61835.1; -; Genomic_DNA.
EMBL; BC031790; AAH31790.1; ALT_INIT; mRNA.
EMBL; BI490027; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BI669304; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS4283.1; -. [Q00005-2]
CCDS; CCDS4284.2; -. [Q00005-5]
CCDS; CCDS43380.1; -. [Q00005-6]
CCDS; CCDS64281.1; -. [Q00005-4]
CCDS; CCDS64282.1; -. [Q00005-3]
PIR; B38351; B38351.
RefSeq; NP_001258828.1; NM_001271899.1. [Q00005-3]
RefSeq; NP_001258829.1; NM_001271900.1. [Q00005-4]
RefSeq; NP_001258877.1; NM_001271948.1. [Q00005-6]
RefSeq; NP_858060.2; NM_181674.2. [Q00005-5]
RefSeq; NP_858061.2; NM_181675.3. [Q00005-7]
RefSeq; NP_858062.1; NM_181676.2. [Q00005-2]
RefSeq; NP_858063.1; NM_181677.2.
RefSeq; NP_858064.1; NM_181678.2. [Q00005-6]
UniGene; Hs.627618; -.
UniGene; Hs.655213; -.
ProteinModelPortal; Q00005; -.
SMR; Q00005; -.
BioGrid; 111513; 50.
IntAct; Q00005; 179.
STRING; 9606.ENSP00000336591; -.
iPTMnet; Q00005; -.
PhosphoSitePlus; Q00005; -.
BioMuta; PPP2R2B; -.
DMDM; 231446; -.
EPD; Q00005; -.
MaxQB; Q00005; -.
PaxDb; Q00005; -.
PeptideAtlas; Q00005; -.
PRIDE; Q00005; -.
DNASU; 5521; -.
Ensembl; ENST00000336640; ENSP00000336591; ENSG00000156475. [Q00005-2]
Ensembl; ENST00000394409; ENSP00000377931; ENSG00000156475. [Q00005-1]
Ensembl; ENST00000394411; ENSP00000377933; ENSG00000156475. [Q00005-1]
Ensembl; ENST00000394413; ENSP00000377935; ENSG00000156475. [Q00005-4]
Ensembl; ENST00000394414; ENSP00000377936; ENSG00000156475. [Q00005-5]
Ensembl; ENST00000453001; ENSP00000398779; ENSG00000156475. [Q00005-6]
Ensembl; ENST00000504198; ENSP00000421396; ENSG00000156475. [Q00005-3]
Ensembl; ENST00000508545; ENSP00000431320; ENSG00000156475. [Q00005-6]
GeneID; 5521; -.
KEGG; hsa:5521; -.
UCSC; uc003loe.6; human. [Q00005-1]
CTD; 5521; -.
DisGeNET; 5521; -.
EuPathDB; HostDB:ENSG00000156475.18; -.
GeneCards; PPP2R2B; -.
GeneReviews; PPP2R2B; -.
HGNC; HGNC:9305; PPP2R2B.
HPA; HPA038118; -.
HPA; HPA042122; -.
HPA; HPA042770; -.
MalaCards; PPP2R2B; -.
MIM; 604325; gene.
MIM; 604326; phenotype.
neXtProt; NX_Q00005; -.
OpenTargets; ENSG00000156475; -.
Orphanet; 98762; Spinocerebellar ataxia type 12.
PharmGKB; PA33669; -.
eggNOG; KOG1354; Eukaryota.
eggNOG; COG5170; LUCA.
GeneTree; ENSGT00390000006311; -.
HOVERGEN; HBG000012; -.
InParanoid; Q00005; -.
KO; K04354; -.
OMA; YSNAHAY; -.
OrthoDB; EOG091G09BB; -.
PhylomeDB; Q00005; -.
TreeFam; TF105553; -.
SignaLink; Q00005; -.
SIGNOR; Q00005; -.
ChiTaRS; PPP2R2B; human.
GeneWiki; PPP2R2B; -.
GenomeRNAi; 5521; -.
PRO; PR:Q00005; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000156475; -.
CleanEx; HS_PPP2R2B; -.
ExpressionAtlas; Q00005; baseline and differential.
Genevisible; Q00005; HS.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0032502; P:developmental process; IBA:GO_Central.
GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
GO; GO:0070262; P:peptidyl-serine dephosphorylation; IBA:GO_Central.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR000009; PP2A_PR55.
InterPro; IPR018067; PP2A_PR55_CS.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR11871; PTHR11871; 1.
PIRSF; PIRSF037309; PP2A_PR55; 1.
PRINTS; PR00600; PP2APR55.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 3.
PROSITE; PS01024; PR55_1; 1.
PROSITE; PS01025; PR55_2; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Complete proteome; Cytoplasm;
Cytoskeleton; Disease mutation; Membrane; Mitochondrion;
Mitochondrion outer membrane; Neurodegeneration; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Spinocerebellar ataxia;
WD repeat.
CHAIN 1 443 Serine/threonine-protein phosphatase 2A
55 kDa regulatory subunit B beta isoform.
/FTId=PRO_0000071421.
REPEAT 22 61 WD 1.
REPEAT 87 128 WD 2.
REPEAT 171 209 WD 3.
REPEAT 220 260 WD 4.
REPEAT 279 317 WD 5.
REPEAT 334 375 WD 6.
REPEAT 410 442 WD 7.
MOD_RES 275 275 Phosphoserine.
{ECO:0000250|UniProtKB:P36877}.
MOD_RES 295 295 Phosphotyrosine.
{ECO:0000250|UniProtKB:P36877}.
MOD_RES 298 298 Phosphothreonine.
{ECO:0000250|UniProtKB:P36877}.
VAR_SEQ 1 23 MEEDIDTRKINNSFLRDHSYATE -> MNYPDENTYGNK
(in isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044923.
VAR_SEQ 1 21 MEEDIDTRKINNSFLRDHSYA -> MKCFSRYLPYIFRPPN
TILSSSCH (in isoform 2).
{ECO:0000303|Ref.6}.
/FTId=VSP_037976.
VAR_SEQ 1 21 MEEDIDTRKINNSFLRDHSYA -> MIPGIGTLTQDTLWCF
SQVKGTIEIGT (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037977.
VAR_SEQ 1 1 M -> MVLQPSERHYRDWNHRRLGPWCSPTGSPAPLSCETG
CGEGSWILVCRLLVPTQVSLLSM (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037978.
VAR_SEQ 1 1 M -> MLLSLPALHLQTSEHHPFFQLPHRRLGPWCSPTGSP
APLSCETGCGEGSWILVCRLLVPTQVSLLSM (in
isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_037979.
VAR_SEQ 1 1 M -> MHQPPPASCSSSSSSSSSSCECARVGVRVSALAPAA
APCPAPRQLPYPRLPEPPSRGTSTLIPARLGPWCSPTGSPA
PLSCETGCGEGSWILVCRLLVPTQVSLLSM (in
isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045748.
VARIANT 36 36 G -> V (in dbSNP:rs11547494).
/FTId=VAR_051738.
VARIANT 138 138 R -> P (probable disease-associated
mutation found in a patient with moderate
intellectual disability, authism and
intractable epilepsy).
{ECO:0000269|PubMed:25356899}.
/FTId=VAR_078654.
CONFLICT 22 22 T -> A (in Ref. 2; BAH11838).
{ECO:0000305}.
CONFLICT 62 62 H -> N (in Ref. 5; BI669304).
{ECO:0000305}.
CONFLICT 109 109 S -> F (in Ref. 2; BAH12040).
{ECO:0000305}.
CONFLICT 163 163 T -> S (in Ref. 6; BI490027).
{ECO:0000305}.
CONFLICT 164 164 P -> S (in Ref. 2; BAF82406).
{ECO:0000305}.
CONFLICT 292 292 S -> R (in Ref. 2; BAH12040).
{ECO:0000305}.
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


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