PRIC1_HUMAN
ID PRIC1_HUMAN Reviewed; 831 AA.
AC Q96MT3; Q14C83; Q71QF8; Q96N00;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Prickle-like protein 1;
DE AltName: Full=REST/NRSF-interacting LIM domain protein 1;
DE Flags: Precursor;
GN Name=PRICKLE1; Synonyms=RILP;
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], TISSUE SPECIFICITY, ISOPRENYLATION AT CYS-828,
RP MUTAGENESIS OF 828-CYS--SER-831, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP REST.
RC TISSUE=Brain;
RX PubMed=14645515; DOI=10.1128/mcb.23.24.9025-9031.2003;
RA Shimojo M., Hersh L.B.;
RT "REST/NRSF-interacting LIM domain protein, a putative nuclear translocation
RT receptor.";
RL Mol. Cell. Biol. 23:9025-9031(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
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 [4]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=12525887;
RA Katoh M., Katoh M.;
RT "Identification and characterization of human PRICKLE1 and PRICKLE2 genes
RT as well as mouse Prickle1 and Prickle2 genes homologous to Drosophila
RT tissue polarity gene prickle.";
RL Int. J. Mol. Med. 11:249-256(2003).
RN [5]
RP INTERACTION WITH REST.
RX PubMed=16442230; DOI=10.1016/j.neulet.2005.12.080;
RA Shimojo M.;
RT "Characterization of the nuclear targeting signal of REST/NRSF.";
RL Neurosci. Lett. 398:161-166(2006).
RN [6]
RP ISOPRENYLATION AT CYS-828.
RX PubMed=17411337; DOI=10.1371/journal.pcbi.0030066;
RA Maurer-Stroh S., Koranda M., Benetka W., Schneider G., Sirota F.L.,
RA Eisenhaber F.;
RT "Towards complete sets of farnesylated and geranylgeranylated proteins.";
RL PLoS Comput. Biol. 3:634-648(2007).
RN [7]
RP TISSUE SPECIFICITY, VARIANT EPM1B GLN-104, AND CHARACTERIZATION OF VARIANT
RP EPM1B GLN-104.
RX PubMed=18976727; DOI=10.1016/j.ajhg.2008.10.003;
RA Bassuk A.G., Wallace R.H., Buhr A., Buller A.R., Afawi Z., Shimojo M.,
RA Miyata S., Chen S., Gonzalez-Alegre P., Griesbach H.L., Wu S.,
RA Nashelsky M., Vladar E.K., Antic D., Ferguson P.J., Cirak S., Voit T.,
RA Scott M.P., Axelrod J.D., Gurnett C., Daoud A.S., Kivity S., Neufeld M.Y.,
RA Mazarib A., Straussberg R., Walid S., Korczyn A.D., Slusarski D.C.,
RA Berkovic S.F., El-Shanti H.I.;
RT "A homozygous mutation in human PRICKLE1 causes an autosomal-recessive
RT progressive myoclonus epilepsy-ataxia syndrome.";
RL Am. J. Hum. Genet. 83:572-581(2008).
RN [8]
RP FUNCTION, POSSIBLE INVOLVEMENT IN NTD, AND VARIANTS THR-69; HIS-81;
RP ILE-121; THR-124; MET-275; CYS-682; PHE-739; ASN-771 AND CYS-799.
RX PubMed=21901791; DOI=10.1002/humu.21589;
RA Bosoi C.M., Capra V., Allache R., Trinh V.Q., De Marco P., Merello E.,
RA Drapeau P., Bassuk A.G., Kibar Z.;
RT "Identification and characterization of novel rare mutations in the planar
RT cell polarity gene PRICKLE1 in human neural tube defects.";
RL Hum. Mutat. 32:1371-1375(2011).
RN [9]
RP IDENTIFICATION BY 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 [10]
RP VARIANTS EPM1B GLN-104; HIS-144 AND HIS-472.
RX PubMed=21276947; DOI=10.1016/j.ajhg.2010.12.012;
RA Tao H., Manak J.R., Sowers L., Mei X., Kiyonari H., Abe T., Dahdaleh N.S.,
RA Yang T., Wu S., Chen S., Fox M.H., Gurnett C., Montine T., Bird T.,
RA Shaffer L.G., Rosenfeld J.A., McConnell J., Madan-Khetarpal S.,
RA Berry-Kravis E., Griesbach H., Saneto R.P., Scott M.P., Antic D., Reed J.,
RA Boland R., Ehaideb S.N., El-Shanti H., Mahajan V.B., Ferguson P.J.,
RA Axelrod J.D., Lehesjoki A.E., Fritzsch B., Slusarski D.C., Wemmie J.,
RA Ueno N., Bassuk A.G.;
RT "Mutations in prickle orthologs cause seizures in flies, mice, and
RT humans.";
RL Am. J. Hum. Genet. 88:138-149(2011).
CC -!- FUNCTION: Involved in the planar cell polarity pathway that controls
CC convergent extension during gastrulation and neural tube closure.
CC Convergent extension is a complex morphogenetic process during which
CC cells elongate, move mediolaterally, and intercalate between
CC neighboring cells, leading to convergence toward the mediolateral axis
CC and extension along the anteroposterior axis. Necessary for nuclear
CC localization of REST. May serve as nuclear receptor.
CC {ECO:0000269|PubMed:21901791}.
CC -!- SUBUNIT: Interacts with REST. {ECO:0000269|PubMed:14645515,
CC ECO:0000269|PubMed:16442230}.
CC -!- INTERACTION:
CC Q96MT3; Q13895: BYSL; NbExp=3; IntAct=EBI-2348662, EBI-358049;
CC Q96MT3; Q92997: DVL3; NbExp=3; IntAct=EBI-2348662, EBI-739789;
CC Q96MT3; O75564-2: JRK; NbExp=3; IntAct=EBI-2348662, EBI-17181882;
CC Q96MT3; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-2348662, EBI-8472129;
CC Q96MT3; Q8WWY3: PRPF31; NbExp=6; IntAct=EBI-2348662, EBI-1567797;
CC Q96MT3; Q08E77: UTP14C; NbExp=3; IntAct=EBI-2348662, EBI-10225961;
CC Q96MT3; Q8VIG1: Rest; Xeno; NbExp=4; IntAct=EBI-2348662, EBI-2312802;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:14645515}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:14645515}. Note=A smaller amount
CC is detected in the cytosol.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in placenta and at
CC lower levels in lung, liver, kidney and pancreas. Expressed in
CC thalamus, hippocampus, cerebral cortex, and cerebellum (in neurons
CC rather than glia). {ECO:0000269|PubMed:12525887,
CC ECO:0000269|PubMed:14645515, ECO:0000269|PubMed:18976727}.
CC -!- DISEASE: Epilepsy, progressive myoclonic 1B (EPM1B) [MIM:612437]: A
CC form of progressive myoclonic epilepsy, a clinically and genetically
CC heterogeneous group of disorders defined by the combination of action
CC and reflex myoclonus, other types of epileptic seizures, and
CC progressive neurodegeneration and neurocognitive impairment. EPM1B is
CC an autosomal recessive form characterized by myoclonus that progressed
CC in severity over time, tonic-clonic seizures and ataxia.
CC {ECO:0000269|PubMed:18976727, ECO:0000269|PubMed:21276947}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Neural tube defects (NTD) [MIM:182940]: Congenital
CC malformations of the central nervous system and adjacent structures
CC related to defective neural tube closure during the first trimester of
CC pregnancy. Failure of neural tube closure can occur at any level of the
CC embryonic axis. Common NTD forms include anencephaly, myelomeningocele
CC and spina bifida, which result from the failure of fusion in the
CC cranial and spinal region of the neural tube. NTDs have a
CC multifactorial etiology encompassing both genetic and environmental
CC components. {ECO:0000269|PubMed:21901791}. Note=Disease susceptibility
CC is associated with variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
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DR EMBL; AF399844; AAQ03035.1; -; mRNA.
DR EMBL; AK056189; BAB71116.1; -; mRNA.
DR EMBL; AK056499; BAB71198.1; -; mRNA.
DR EMBL; BC114939; AAI14940.1; -; mRNA.
DR EMBL; BC114940; AAI14941.1; -; mRNA.
DR CCDS; CCDS8742.1; -.
DR RefSeq; NP_001138353.1; NM_001144881.1.
DR RefSeq; NP_001138354.1; NM_001144882.1.
DR RefSeq; NP_001138355.1; NM_001144883.1.
DR RefSeq; NP_694571.2; NM_153026.2.
DR RefSeq; XP_011536248.1; XM_011537946.1.
DR RefSeq; XP_011536249.1; XM_011537947.2.
DR RefSeq; XP_016874327.1; XM_017018838.1.
DR RefSeq; XP_016874328.1; XM_017018839.1.
DR RefSeq; XP_016874329.1; XM_017018840.1.
DR AlphaFoldDB; Q96MT3; -.
DR SMR; Q96MT3; -.
DR BioGRID; 126835; 23.
DR IntAct; Q96MT3; 12.
DR STRING; 9606.ENSP00000345064; -.
DR GlyConnect; 2062; 1 N-Linked glycan (1 site).
DR GlyGen; Q96MT3; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q96MT3; -.
DR PhosphoSitePlus; Q96MT3; -.
DR BioMuta; PRICKLE1; -.
DR DMDM; 59800163; -.
DR EPD; Q96MT3; -.
DR jPOST; Q96MT3; -.
DR MassIVE; Q96MT3; -.
DR MaxQB; Q96MT3; -.
DR PaxDb; Q96MT3; -.
DR PeptideAtlas; Q96MT3; -.
DR PRIDE; Q96MT3; -.
DR ProteomicsDB; 77402; -.
DR Antibodypedia; 13204; 140 antibodies from 23 providers.
DR DNASU; 144165; -.
DR Ensembl; ENST00000345127.9; ENSP00000345064.3; ENSG00000139174.12.
DR Ensembl; ENST00000445766.7; ENSP00000398947.2; ENSG00000139174.12.
DR Ensembl; ENST00000455697.6; ENSP00000401060.1; ENSG00000139174.12.
DR Ensembl; ENST00000548696.6; ENSP00000448359.1; ENSG00000139174.12.
DR Ensembl; ENST00000552240.6; ENSP00000449819.1; ENSG00000139174.12.
DR Ensembl; ENST00000639566.1; ENSP00000492332.1; ENSG00000139174.12.
DR Ensembl; ENST00000639589.1; ENSP00000491051.1; ENSG00000139174.12.
DR Ensembl; ENST00000639958.1; ENSP00000492644.1; ENSG00000139174.12.
DR Ensembl; ENST00000640055.1; ENSP00000492763.1; ENSG00000139174.12.
DR Ensembl; ENST00000640132.1; ENSP00000491228.1; ENSG00000139174.12.
DR GeneID; 144165; -.
DR KEGG; hsa:144165; -.
DR MANE-Select; ENST00000345127.9; ENSP00000345064.3; NM_153026.3; NP_694571.2.
DR UCSC; uc001rnl.4; human.
DR CTD; 144165; -.
DR DisGeNET; 144165; -.
DR GeneCards; PRICKLE1; -.
DR GeneReviews; PRICKLE1; -.
DR HGNC; HGNC:17019; PRICKLE1.
DR HPA; ENSG00000139174; Low tissue specificity.
DR MalaCards; PRICKLE1; -.
DR MIM; 182940; phenotype.
DR MIM; 608500; gene.
DR MIM; 612437; phenotype.
DR neXtProt; NX_Q96MT3; -.
DR OpenTargets; ENSG00000139174; -.
DR Orphanet; 308; Progressive myoclonic epilepsy type 1.
DR PharmGKB; PA134906946; -.
DR VEuPathDB; HostDB:ENSG00000139174; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00940000157529; -.
DR HOGENOM; CLU_008937_5_0_1; -.
DR InParanoid; Q96MT3; -.
DR OMA; PFCCNCF; -.
DR OrthoDB; 997264at2759; -.
DR PhylomeDB; Q96MT3; -.
DR TreeFam; TF313265; -.
DR PathwayCommons; Q96MT3; -.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR SignaLink; Q96MT3; -.
DR SIGNOR; Q96MT3; -.
DR BioGRID-ORCS; 144165; 15 hits in 1075 CRISPR screens.
DR ChiTaRS; PRICKLE1; human.
DR GenomeRNAi; 144165; -.
DR Pharos; Q96MT3; Tbio.
DR PRO; PR:Q96MT3; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96MT3; protein.
DR Bgee; ENSG00000139174; Expressed in buccal mucosa cell and 182 other tissues.
DR ExpressionAtlas; Q96MT3; baseline and differential.
DR Genevisible; Q96MT3; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:2000691; P:negative regulation of cardiac muscle cell myoblast differentiation; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
DR CDD; cd09418; LIM2_Prickle; 1.
DR CDD; cd09420; LIM3_Prickle; 1.
DR CDD; cd09827; PET_Prickle; 1.
DR InterPro; IPR033726; LIM2_prickle.
DR InterPro; IPR033727; LIM3_prickle.
DR InterPro; IPR010442; PET_domain.
DR InterPro; IPR033723; PET_prickle.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 3.
DR Pfam; PF06297; PET; 1.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS51303; PET; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disease variant; Epilepsy; LIM domain; Lipoprotein; Membrane;
KW Metal-binding; Methylation; Neurodegeneration; Nucleus; Phosphoprotein;
KW Prenylation; Reference proteome; Repeat; Zinc.
FT CHAIN 1..828
FT /note="Prickle-like protein 1"
FT /id="PRO_0000075889"
FT PROPEP 829..831
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396712"
FT DOMAIN 14..122
FT /note="PET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT DOMAIN 124..189
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 189..249
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 249..313
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 313..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..831
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U5C7"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U5C7"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U5C7"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U5C7"
FT MOD_RES 828
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 828
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:14645515,
FT ECO:0000269|PubMed:17411337"
FT VARIANT 69
FT /note="I -> T (may be associated with NTD;
FT dbSNP:rs141795695)"
FT /evidence="ECO:0000269|PubMed:21901791"
FT /id="VAR_066850"
FT VARIANT 81
FT /note="N -> H (may be associated with NTD;
FT dbSNP:rs796052934)"
FT /evidence="ECO:0000269|PubMed:21901791"
FT /id="VAR_066851"
FT VARIANT 104
FT /note="R -> Q (in EPM1B; affects interaction with REST;
FT dbSNP:rs113994140)"
FT /evidence="ECO:0000269|PubMed:18976727,
FT ECO:0000269|PubMed:21276947"
FT /id="VAR_054663"
FT VARIANT 121
FT /note="V -> I (may be associated with NTD;
FT dbSNP:rs371720624)"
FT /evidence="ECO:0000269|PubMed:21901791"
FT /id="VAR_066852"
FT VARIANT 124
FT /note="A -> T (in dbSNP:rs79087668)"
FT /evidence="ECO:0000269|PubMed:21901791"
FT /id="VAR_066853"
FT VARIANT 144
FT /note="R -> H (in EPM1B; dbSNP:rs281865563)"
FT /evidence="ECO:0000269|PubMed:21276947"
FT /id="VAR_065580"
FT VARIANT 275
FT /note="T -> M (may be associated with NTD;
FT dbSNP:rs559947948)"
FT /evidence="ECO:0000269|PubMed:21901791"
FT /id="VAR_066854"
FT VARIANT 472
FT /note="Y -> H (in EPM1B; dbSNP:rs281865564)"
FT /evidence="ECO:0000269|PubMed:21276947"
FT /id="VAR_065581"
FT VARIANT 682
FT /note="R -> C (may be associated with NTD;
FT dbSNP:rs768954477)"
FT /evidence="ECO:0000269|PubMed:21901791"
FT /id="VAR_066855"
FT VARIANT 739
FT /note="S -> F (may be associated with NTD;
FT dbSNP:rs138452760)"
FT /evidence="ECO:0000269|PubMed:21901791"
FT /id="VAR_066856"
FT VARIANT 746
FT /note="P -> S (in dbSNP:rs3827522)"
FT /id="VAR_056164"
FT VARIANT 771
FT /note="D -> N (may be associated with NTD;
FT dbSNP:rs146670726)"
FT /evidence="ECO:0000269|PubMed:21901791"
FT /id="VAR_066857"
FT VARIANT 799
FT /note="S -> C (may be associated with NTD)"
FT /evidence="ECO:0000269|PubMed:21901791"
FT /id="VAR_066858"
FT MUTAGEN 828..831
FT /note="Missing: Abolishes localization to the nuclear
FT membrane."
FT /evidence="ECO:0000269|PubMed:14645515"
FT CONFLICT 739
FT /note="S -> P (in Ref. 2; BAB71198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 831 AA; 94300 MW; 753D68BD5A4D0935 CRC64;
MPLEMEPKMS KLAFGCQRSS TSDDDSGCAL EEYAWVPPGL RPEQIQLYFA CLPEEKVPYV
NSPGEKHRIK QLLYQLPPHD NEVRYCQSLS EEEKKELQVF SAQRKKEALG RGTIKLLSRA
VMHAVCEQCG LKINGGEVAV FASRAGPGVC WHPSCFVCFT CNELLVDLIY FYQDGKIHCG
RHHAELLKPR CSACDEIIFA DECTEAEGRH WHMKHFCCLE CETVLGGQRY IMKDGRPFCC
GCFESLYAEY CETCGEHIGV DHAQMTYDGQ HWHATEACFS CAQCKASLLG CPFLPKQGQI
YCSKTCSLGE DVHASDSSDS AFQSARSRDS RRSVRMGKSS RSADQCRQSL LLSPALNYKF
PGLSGNADDT LSRKLDDLSL SRQGTSFASE EFWKGRVEQE TPEDPEEWAD HEDYMTQLLL
KFGDKSLFQP QPNEMDIRAS EHWISDNMVK SKTELKQNNQ SLASKKYQSD MYWAQSQDGL
GDSAYGSHPG PASSRRLQEL ELDHGASGYN HDETQWYEDS LECLSDLKPE QSVRDSMDSL
ALSNITGASV DGENKPRPSL YSLQNFEEME TEDCEKMSNM GTLNSSMLHR SAESLKSLSS
ELCPEKILPE EKPVHLPVLR RSKSQSRPQQ VKFSDDVIDN GNYDIEIRQP PMSERTRRRV
YNFEERGSRS HHHRRRRSRK SRSDNALNLV TERKYSPKDR LRLYTPDNYE KFIQNKSARE
IQAYIQNADL YGQYAHATSD YGLQNPGMNR FLGLYGEDDD SWCSSSSSSS DSEEEGYFLG
QPIPQPRPQR FAYYTDDLSS PPSALPTPQF GQRTTKSKKK KGHKGKNCII S
