ID CMTA1_HUMAN Reviewed; 1673 AA. AC Q9Y6Y1; A7MBM4; G3V3Z7; Q5VUE1; Q6V701; Q8WYI3; Q96S92; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 4. DT 27-MAR-2024, entry version 180. DE RecName: Full=Calmodulin-binding transcription activator 1 {ECO:0000312|HGNC:HGNC:18806}; GN Name=CAMTA1 {ECO:0000312|HGNC:HGNC:18806}; GN Synonyms=KIAA0833 {ECO:0000312|EMBL:BAA74856.3}; GN ORFNames=MSTP023 {ECO:0000312|EMBL:AAL39006.1}; 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] {ECO:0000312|EMBL:BAA74856.3} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [2] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Li N., Zhang M., Wan T., Zhang W., Cao X.; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4). RC TISSUE=Skin; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1422-1673 (ISOFORM 2). RC TISSUE=Heart; RA Xu Y.Y., Sun L.Z., Wu Q.Y., Liu Y.Q., Liu B., Zhao B., Wang X.Y., Song L., RA Ye J., Sheng H., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Sun Y.H., RA Jiang Y.X., Zhao X.W., Liu S., Liu L.S., Ding J.F., Gao R.L., Qiang B.Q., RA Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1437-1673 (ISOFORM 2). RA Li H., Li S., Yu R., Shen C., Zhou G., Ke R., Lin L., Yang S.; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=11925432; DOI=10.1074/jbc.m200268200; RA Bouche N., Scharlat A., Snedden W., Bouchez D., Fromm H.; RT "A novel family of calmodulin-binding transcription activators in RT multicellular organisms."; RL J. Biol. Chem. 277:21851-21861(2002). RN [10] RP INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=15138581; RA Nakatani K., Nishioka J., Itakura T., Nakanishi Y., Horinouchi J., Abe Y., RA Wada H., Nobori T.; RT "Cell cycle-dependent transcriptional regulation of calmodulin-binding RT transcription activator 1 in neuroblastoma cells."; RL Int. J. Oncol. 24:1407-1412(2004). RN [11] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=15709179; DOI=10.1158/1078-0432.1119.11.3; RA Barbashina V., Salazar P., Holland E.C., Rosenblum M.K., Ladanyi M.; RT "Allelic losses at 1p36 and 19q13 in gliomas: correlation with histologic RT classification, definition of a 150-kb minimal deleted region on 1p36, and RT evaluation of CAMTA1 as a candidate tumor suppressor gene."; RL Clin. Cancer Res. 11:1119-1128(2005). RN [12] RP INVOLVEMENT IN CECBA. RX PubMed=22693284; DOI=10.1136/jmedgenet-2012-100856; RA Thevenon J., Lopez E., Keren B., Heron D., Mignot C., Altuzarra C., RA Beri-Dexheimer M., Bonnet C., Magnin E., Burglen L., Minot D., Vigneron J., RA Morle S., Anheim M., Charles P., Brice A., Gallagher L., Amiel J., RA Haffen E., Mach C., Depienne C., Doummar D., Bonnet M., Duplomb L., RA Carmignac V., Callier P., Marle N., Mosca-Boidron A.L., Roze V., Aral B., RA Razavi F., Jonveaux P., Faivre L., Thauvin-Robinet C.; RT "Intragenic CAMTA1 rearrangements cause non-progressive congenital ataxia RT with or without intellectual disability."; RL J. Med. Genet. 49:400-408(2012). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 872-953. RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure of the TIG domain of human calmodulin-binding RT transcription activator 1 (CAMTA1)."; RL Submitted (DEC-2005) to the PDB data bank. RN [14] RP VARIANTS LYS-1177; THR-1218 AND ILE-1336. RX PubMed=17222547; DOI=10.1016/j.ejca.2006.09.023; RA Henrich K.-O., Claas A., Praml C., Benner A., Mollenhauer J., Poustka A., RA Schwab M., Westermann F.; RT "Allelic variants of CAMTA1 and FLJ10737 within a commonly deleted region RT at 1p36 in neuroblastoma."; RL Eur. J. Cancer 43:607-616(2007). RN [15] RP VARIANT THR-1473. RX PubMed=33798445; DOI=10.1016/j.ajhg.2021.03.013; RA Courage C., Oliver K.L., Park E.J., Cameron J.M., Grabinska K.A., Muona M., RA Canafoglia L., Gambardella A., Said E., Afawi Z., Baykan B., Brandt C., RA di Bonaventura C., Chew H.B., Criscuolo C., Dibbens L.M., Castellotti B., RA Riguzzi P., Labate A., Filla A., Giallonardo A.T., Berecki G., RA Jackson C.B., Joensuu T., Damiano J.A., Kivity S., Korczyn A., Palotie A., RA Striano P., Uccellini D., Giuliano L., Andermann E., Scheffer I.E., RA Michelucci R., Bahlo M., Franceschetti S., Sessa W.C., Berkovic S.F., RA Lehesjoki A.E.; RT "Progressive myoclonus epilepsies-Residual unsolved cases have marked RT genetic heterogeneity including dolichol-dependent protein glycosylation RT pathway genes."; RL Am. J. Hum. Genet. 108:722-738(2021). CC -!- FUNCTION: Transcriptional activator. {ECO:0000269|PubMed:11925432}. CC -!- SUBUNIT: May interact with calmodulin. {ECO:0000305|PubMed:11925432}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:11925432}. Cytoplasm CC {ECO:0000305|PubMed:15138581}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9Y6Y1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y6Y1-2; Sequence=VSP_035936, VSP_035937; CC Name=3; CC IsoId=Q9Y6Y1-3; Sequence=VSP_043842, VSP_043843; CC Name=4; CC IsoId=Q9Y6Y1-4; Sequence=VSP_046358, VSP_046359; CC -!- TISSUE SPECIFICITY: Normally expressed in non-neoplastic adult central CC nervous system tissues: detected in whole brain, cerebellum, brain CC cortex, occipital lobe, frontal lobe, temporal lobe, putamen. CC Expression levels are low in oligodendroglial tumors, and are reduced CC by half in oligodendroglioma and astrocytoma cases with 1p loss of CC heterozygosity. Detected in neuroblastic-type cultured neuroblastoma CC cells. Expressed in heart and kidney. {ECO:0000269|PubMed:11925432, CC ECO:0000269|PubMed:15138581, ECO:0000269|PubMed:15709179}. CC -!- INDUCTION: Detected at low levels at interphase and in resting cells. CC Up-regulated during S phase and mitosis. Levels decrease at the end of CC mitosis. {ECO:0000269|PubMed:15138581}. CC -!- DISEASE: Cerebellar dysfunction with variable cognitive and behavioral CC abnormalities (CECBA) [MIM:614756]: An autosomal dominant CC neurodevelopmental disorder characterized by mildly delayed psychomotor CC development, early onset of cerebellar ataxia, and intellectual CC disability later in childhood and adult life. Other features may CC include neonatal hypotonia, dysarthria, and dysmetria. Brain imaging in CC some patients shows cerebellar atrophy. Dysmorphic facial features are CC variable. {ECO:0000269|PubMed:22693284}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: A very small segment of 1p36 located within CAMTA1 is CC deleted in all oligodendroglial tumors with 1p LOH. This minimal CC deleted region (MDR) also overlaps the neuroblastoma 1p36 MDR. CAMTA1 CC shows no evidence of inactivation by somatic mutations. CC -!- SIMILARITY: Belongs to the CAMTA family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL39006.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA74856.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=EAW71580.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/908/CAMTA1"; 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; AB020640; BAA74856.3; ALT_INIT; mRNA. DR EMBL; AY037153; AAK67633.1; -; mRNA. DR EMBL; AL359881; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL365194; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590128; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL596210; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z97635; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z98052; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z98884; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471130; EAW71580.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC116457; AAI16458.1; -; mRNA. DR EMBL; BC151835; AAI51836.1; -; mRNA. DR EMBL; CD103791; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AF111804; AAL39006.1; ALT_INIT; mRNA. DR EMBL; AY349360; AAQ56724.1; -; mRNA. DR CCDS; CCDS30576.1; -. [Q9Y6Y1-1] DR CCDS; CCDS55574.1; -. [Q9Y6Y1-3] DR CCDS; CCDS55575.1; -. [Q9Y6Y1-4] DR RefSeq; NP_001182492.1; NM_001195563.1. [Q9Y6Y1-3] DR RefSeq; NP_001229630.1; NM_001242701.1. [Q9Y6Y1-4] DR RefSeq; NP_056030.1; NM_015215.3. [Q9Y6Y1-1] DR PDB; 2CXK; X-ray; 1.85 A; A/B/C/D/E=872-953. DR PDBsum; 2CXK; -. DR AlphaFoldDB; Q9Y6Y1; -. DR SMR; Q9Y6Y1; -. DR BioGRID; 116863; 9. DR IntAct; Q9Y6Y1; 4. DR STRING; 9606.ENSP00000306522; -. DR GlyGen; Q9Y6Y1; 1 site. DR iPTMnet; Q9Y6Y1; -. DR PhosphoSitePlus; Q9Y6Y1; -. DR BioMuta; CAMTA1; -. DR DMDM; 97046872; -. DR MassIVE; Q9Y6Y1; -. DR PaxDb; 9606-ENSP00000306522; -. DR PeptideAtlas; Q9Y6Y1; -. DR ProteomicsDB; 33093; -. DR ProteomicsDB; 86825; -. [Q9Y6Y1-1] DR ProteomicsDB; 86826; -. [Q9Y6Y1-2] DR ProteomicsDB; 86827; -. [Q9Y6Y1-3] DR Antibodypedia; 49059; 86 antibodies from 18 providers. DR DNASU; 23261; -. DR Ensembl; ENST00000303635.12; ENSP00000306522.6; ENSG00000171735.21. [Q9Y6Y1-1] DR Ensembl; ENST00000473578.5; ENSP00000451388.1; ENSG00000171735.21. [Q9Y6Y1-3] DR Ensembl; ENST00000557126.5; ENSP00000451510.1; ENSG00000171735.21. [Q9Y6Y1-4] DR GeneID; 23261; -. DR KEGG; hsa:23261; -. DR MANE-Select; ENST00000303635.12; ENSP00000306522.6; NM_015215.4; NP_056030.1. DR UCSC; uc001aoh.4; human. [Q9Y6Y1-1] DR AGR; HGNC:18806; -. DR CTD; 23261; -. DR DisGeNET; 23261; -. DR GeneCards; CAMTA1; -. DR HGNC; HGNC:18806; CAMTA1. DR HPA; ENSG00000171735; Low tissue specificity. DR MalaCards; CAMTA1; -. DR MIM; 611501; gene. DR MIM; 614756; phenotype. DR neXtProt; NX_Q9Y6Y1; -. DR OpenTargets; ENSG00000171735; -. DR Orphanet; 157791; Epithelioid hemangioendothelioma. DR Orphanet; 314647; Non-progressive cerebellar ataxia with intellectual disability. DR PharmGKB; PA38688; -. DR VEuPathDB; HostDB:ENSG00000171735; -. DR eggNOG; KOG0520; Eukaryota. DR GeneTree; ENSGT00940000155203; -. DR HOGENOM; CLU_003170_1_0_1; -. DR InParanoid; Q9Y6Y1; -. DR OMA; GCANYSA; -. DR OrthoDB; 470813at2759; -. DR PhylomeDB; Q9Y6Y1; -. DR TreeFam; TF323452; -. DR PathwayCommons; Q9Y6Y1; -. DR SignaLink; Q9Y6Y1; -. DR SIGNOR; Q9Y6Y1; -. DR BioGRID-ORCS; 23261; 8 hits in 1175 CRISPR screens. DR ChiTaRS; CAMTA1; human. DR EvolutionaryTrace; Q9Y6Y1; -. DR GeneWiki; CAMTA1; -. DR GenomeRNAi; 23261; -. DR Pharos; Q9Y6Y1; Tbio. DR PRO; PR:Q9Y6Y1; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9Y6Y1; Protein. DR Bgee; ENSG00000171735; Expressed in parotid gland and 195 other cell types or tissues. DR ExpressionAtlas; Q9Y6Y1; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central. DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl. DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IMP:BHF-UCL. DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 1.20.5.190; -; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR005559; CG-1_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR002909; IPT_dom. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR23335:SF11; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR 1; 1. DR PANTHER; PTHR23335; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR CAMTA; 1. DR Pfam; PF12796; Ank_2; 1. DR Pfam; PF03859; CG-1; 1. DR Pfam; PF00612; IQ; 1. DR Pfam; PF01833; TIG; 1. DR SMART; SM01076; CG-1; 1. DR SUPFAM; SSF48403; Ankyrin repeat; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. DR PROSITE; PS51437; CG_1; 1. DR PROSITE; PS50096; IQ; 1. DR Genevisible; Q9Y6Y1; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; ANK repeat; Cytoplasm; KW Intellectual disability; Nucleus; Reference proteome; Repeat; KW Transcription; Transcription regulation. FT CHAIN 1..1673 FT /note="Calmodulin-binding transcription activator 1" FT /id="PRO_0000235820" FT DOMAIN 875..953 FT /note="IPT/TIG" FT /evidence="ECO:0007744|PDB:2CXK" FT REPEAT 1064..1093 FT /note="ANK 1" FT REPEAT 1109..1129 FT /note="ANK 2" FT REPEAT 1143..1172 FT /note="ANK 3" FT DOMAIN 1547..1576 FT /note="IQ 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT DOMAIN 1577..1599 FT /note="IQ 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT DOMAIN 1600..1622 FT /note="IQ 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT DNA_BIND 63..188 FT /note="CG-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00767" FT REGION 283..375 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 990..1021 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1215..1246 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1264..1317 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 112..119 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00767" FT COMPBIAS 305..331 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 337..370 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 991..1021 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1222..1236 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1269..1288 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 79..101 FT /note="EIAAYLITFEKHEEWLTTSPKTR -> ALTTHLFMGAAKKRDPQSWSHEG FT (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_046358" FT VAR_SEQ 79..80 FT /note="EI -> RS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_043842" FT VAR_SEQ 81..1673 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_043843" FT VAR_SEQ 102..1673 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_046359" FT VAR_SEQ 1458..1471 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.7, ECO:0000303|Ref.8" FT /id="VSP_035936" FT VAR_SEQ 1653..1673 FT /note="SPLVDHRLYKRSERIEKGQGT -> RVKELKKAKELEDIQQHPLAM (in FT isoform 2)" FT /evidence="ECO:0000303|Ref.7, ECO:0000303|Ref.8" FT /id="VSP_035937" FT VARIANT 1177 FT /note="N -> K (in dbSNP:rs41278952)" FT /evidence="ECO:0000269|PubMed:17222547" FT /id="VAR_047824" FT VARIANT 1218 FT /note="N -> T (in dbSNP:rs41278954)" FT /evidence="ECO:0000269|PubMed:17222547" FT /id="VAR_047825" FT VARIANT 1336 FT /note="T -> I (in dbSNP:rs137974312)" FT /evidence="ECO:0000269|PubMed:17222547" FT /id="VAR_047826" FT VARIANT 1473 FT /note="S -> T (found in patients with late onset FT progressive myoclonus epilepsy; uncertain significance; FT dbSNP:rs776553769)" FT /evidence="ECO:0000269|PubMed:33798445" FT /id="VAR_085043" FT STRAND 875..877 FT /evidence="ECO:0007829|PDB:2CXK" FT STRAND 879..881 FT /evidence="ECO:0007829|PDB:2CXK" FT STRAND 888..894 FT /evidence="ECO:0007829|PDB:2CXK" FT STRAND 902..906 FT /evidence="ECO:0007829|PDB:2CXK" FT STRAND 909..912 FT /evidence="ECO:0007829|PDB:2CXK" FT STRAND 914..917 FT /evidence="ECO:0007829|PDB:2CXK" FT STRAND 920..924 FT /evidence="ECO:0007829|PDB:2CXK" FT STRAND 930..939 FT /evidence="ECO:0007829|PDB:2CXK" FT STRAND 948..952 FT /evidence="ECO:0007829|PDB:2CXK" SQ SEQUENCE 1673 AA; 183672 MW; 008AA6A906374C00 CRC64; MWRAEGKWLP KTSRKSVSQS VFCGTSTYCV LNTVPPIEDD HGNSNSSHVK IFLPKKLLEC LPKCSSLPKE RHRWNTNEEI AAYLITFEKH EEWLTTSPKT RPQNGSMILY NRKKVKYRKD GYCWKKRKDG KTTREDHMKL KVQGVECLYG CYVHSSIIPT FHRRCYWLLQ NPDIVLVHYL NVPAIEDCGK PCGPILCSIN TDKKEWAKWT KEELIGQLKP MFHGIKWTCS NGNSSSGFSV EQLVQQILDS HQTKPQPRTH NCLCTGSLGA GGSVHHKCNS AKHRIISPKV EPRTGGYGSH SEVQHNDVSE GKHEHSHSKG SSREKRNGKV AKPVLLHQSS TEVSSTNQVE VPDTTQSSPV SISSGLNSDP DMVDSPVVTG VSGMAVASVM GSLSQSATVF MSEVTNEAVY TMSPTAGPNH HLLSPDASQG LVLAVSSDGH KFAFPTTGSS ESLSMLPTNV SEELVLSTTL DGGRKIPETT MNFDPDCFLN NPKQGQTYGG GGLKAEMVSS NIRHSPPGER SFSFTTVLTK EIKTEDTSFE QQMAKEAYSS SAAAVAASSL TLTAGSSLLP SGGGLSPSTT LEQMDFSAID SNKDYTSSFS QTGHSPHIHQ TPSPSFFLQD ASKPLPVEQN THSSLSDSGG TFVMPTVKTE ASSQTSSCSG HVETRIESTS SLHLMQFQAN FQAMTAEGEV TMETSQAAEG SEVLLKSGEL QACSSEHYLQ PETNGVIRSA GGVPILPGNV VQGLYPVAQP SLGNASNMEL SLDHFDISFS NQFSDLINDF ISVEGGSSTI YGHQLVSGDS TALSQSEDGA RAPFTQAEMC LPCCSPQQGS LQLSSSEGGA STMAYMHVAE VVSAASAQGT LGMLQQSGRV FMVTDYSPEW SYPEGGVKVL ITGPWQEASN NYSCLFDQIS VPASLIQPGV LRCYCPAHDT GLVTLQVAFN NQIISNSVVF EYKARALPTL PSSQHDWLSL DDNQFRMSIL ERLEQMERRM AEMTGSQQHK QASGGGSSGG GSGSGNGGSQ AQCASGTGAL GSCFESRVVV VCEKMMSRAC WAKSKHLIHS KTFRGMTLLH LAAAQGYATL IQTLIKWRTK HADSIDLELE VDPLNVDHFS CTPLMWACAL GHLEAAVVLY KWDRRAISIP DSLGRLPLGI ARSRGHVKLA ECLEHLQRDE QAQLGQNPRI HCPASEEPST ESWMAQWHSE AISSPEIPKG VTVIASTNPE LRRPRSEPSN YYSSESHKDY PAPKKHKLNP EYFQTRQEKL LPTALSLEEP NIRKQSPSSK QSVPETLSPS EGVRDFSREL SPPTPETAAF QASGSQPVGK WNSKDLYIGV STVQVTGNPK GTSVGKEAAP SQVRPREPMS VLMMANREVV NTELGSYRDS AENEECGQPM DDIQVNMMTL AEHIIEATPD RIKQENFVPM ESSGLERTDP ATISSTMSWL ASYLADADCL PSAAQIRSAY NEPLTPSSNT SLSPVGSPVS EIAFEKPNLP SAADWSEFLS ASTSEKVENE FAQLTLSDHE QRELYEAARL VQTAFRKYKG RPLREQQEVA AAVIQRCYRK YKQYALYKKM TQAAILIQSK FRSYYEQKKF QQSRRAAVLI QKYYRSYKKC GKRRQARRTA VIVQQKLRSS LLTKKQDQAA RKIMRFLRRC RHSPLVDHRL YKRSERIEKG QGT //