ID EI2BB_HUMAN Reviewed; 351 AA.
AC P49770; O43201;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 27-MAR-2024, entry version 195.
DE RecName: Full=Translation initiation factor eIF2B subunit beta;
DE AltName: Full=S20I15;
DE AltName: Full=S20III15;
DE AltName: Full=eIF2B GDP-GTP exchange factor subunit beta;
GN Name=EIF2B2; Synonyms=EIF2BB;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7596406; DOI=10.1038/375754a0;
RA Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., Ikeda M.,
RA Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F.,
RA Bruni A.C., Montesi M.P., Sorbi S., Rainero I., Pinessi L., Nee L.,
RA Chumakov I., Pollen D., Brookes A., Sanseau P., Polinsky R.J., Wasco W.,
RA da Silva H.A.R., Haines J.L., Pericak-Vance M.A., Tanzi R.E., Roses A.D.,
RA Fraser P.E., Rommens J.M., St George-Hyslop P.H.;
RT "Cloning of a gene bearing missense mutations in early-onset familial
RT Alzheimer's disease.";
RL Nature 375:754-760(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP IDENTIFICATION IN THE EIF2B COMPLEX.
RX PubMed=25858979; DOI=10.1126/science.aaa6986;
RA Sekine Y., Zyryanova A., Crespillo-Casado A., Fischer P.M., Harding H.P.,
RA Ron D.;
RT "Stress responses. Mutations in a translation initiation factor identify
RT the target of a memory-enhancing compound.";
RL Science 348:1027-1030(2015).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN THE EIF2B COMPLEX.
RX PubMed=27023709; DOI=10.1007/s10969-016-9203-3;
RA Kashiwagi K., Shigeta T., Imataka H., Ito T., Yokoyama S.;
RT "Expression, purification, and crystallization of Schizosaccharomyces pombe
RT eIF2B.";
RL J. Struct. Funct. Genomics 17:33-38(2016).
RN [9] {ECO:0007744|PDB:6K71, ECO:0007744|PDB:6K72}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS) IN COMPLEX WITH THE EIF2
RP COMPLEX, FUNCTION, SUBUNIT, AND IDENTIFICATION IN THE EIF2B COMPLEX.
RX PubMed=31048492; DOI=10.1126/science.aaw4104;
RA Kashiwagi K., Yokoyama T., Nishimoto M., Takahashi M., Sakamoto A.,
RA Yonemochi M., Shirouzu M., Ito T.;
RT "Structural basis for eIF2B inhibition in integrated stress response.";
RL Science 364:495-499(2019).
RN [10]
RP VARIANTS VWM2 GLY-213; ARG-273; ASP-316 AND VAL-329.
RX PubMed=11704758; DOI=10.1038/ng764;
RA Leegwater P.A.J., Vermeulen G., Koenst A.A.M., Naidu S., Mulders J.,
RA Visser A., Kersbergen P., Mobach D., Fonds D., van Berkel C.G.M.,
RA Lemmers R.J.L.F., Frants R.R., Oudejans C.B.M., Schutgens R.B.H.,
RA Pronk J.C., van der Knaap M.S.;
RT "Subunits of the translation initiation factor eIF2B are mutant in
RT leukoencephalopathy with vanishing white matter.";
RL Nat. Genet. 29:383-388(2001).
RN [11]
RP VARIANTS VWM2 PHE-171 AND GLY-213.
RX PubMed=12707859; DOI=10.1086/375404;
RA Fogli A., Rodriguez D., Eymard-Pierre E., Bouhour F., Labauge P.,
RA Meaney B.F., Zeesman S., Kaneski C.R., Schiffmann R., Boespflug-Tanguy O.;
RT "Ovarian failure related to eukaryotic initiation factor 2B mutations.";
RL Am. J. Hum. Genet. 72:1544-1550(2003).
RN [12]
RP VARIANTS VWM2 PHE-171; SER-196; VAL-200 AND GLY-213.
RX PubMed=15776425; DOI=10.1002/humu.9325;
RA Ohlenbusch A., Henneke M., Brockmann K., Goerg M., Hanefeld F.,
RA Kohlschutter A., Gartner J.;
RT "Identification of ten novel mutations in patients with eIF2B-related
RT disorders.";
RL Hum. Mutat. 25:411-411(2005).
RN [13]
RP VARIANT VWM2 GLU-85.
RX PubMed=21484434; DOI=10.1007/s10048-011-0284-7;
RA Matsukawa T., Wang X., Liu R., Wortham N.C., Onuki Y., Kubota A., Hida A.,
RA Kowa H., Fukuda Y., Ishiura H., Mitsui J., Takahashi Y., Aoki S.,
RA Takizawa S., Shimizu J., Goto J., Proud C.G., Tsuji S.;
RT "Adult-onset leukoencephalopathies with vanishing white matter with novel
RT missense mutations in EIF2B2, EIF2B3, and EIF2B5.";
RL Neurogenetics 12:259-261(2011).
RN [14]
RP VARIANT VWM2 TYR-268.
RX PubMed=22285377; DOI=10.1016/j.gene.2011.12.047;
RA Alsalem A., Shaheen R., Alkuraya F.S.;
RT "Vanishing white matter disease caused by EIF2B2 mutation with the
RT presentation of an adrenoleukodystrophy phenotype.";
RL Gene 496:141-143(2012).
RN [15]
RP VARIANT VWM2 GLY-213.
RX PubMed=22729508; DOI=10.1007/s10072-012-1129-3;
RA Sambati L., Agati R., Bacci A., Bianchi S., Capellari S.;
RT "Vanishing white matter disease: an Italian case with A638G mutation in
RT exon 5 of EIF2B2 gene, an unusual early onset and a long course.";
RL Neurol. Sci. 34:1235-1238(2013).
RN [16]
RP VARIANT VAL-127.
RX PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568;
RA Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I.,
RA Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P.,
RA Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C.,
RA Gyllensten U., Pinto D., Maciel P.;
RT "Identification of novel genetic causes of Rett syndrome-like phenotypes.";
RL J. Med. Genet. 53:190-199(2016).
CC -!- FUNCTION: Acts as a component of the translation initiation factor 2B
CC (eIF2B) complex, which catalyzes the exchange of GDP for GTP on
CC eukaryotic initiation factor 2 (eIF2) gamma subunit (PubMed:25858979,
CC PubMed:27023709, PubMed:31048492). Its guanine nucleotide exchange
CC factor activity is repressed when bound to eIF2 complex phosphorylated
CC on the alpha subunit, thereby limiting the amount of methionyl-
CC initiator methionine tRNA available to the ribosome and consequently
CC global translation is repressed (PubMed:25858979, PubMed:31048492).
CC {ECO:0000269|PubMed:25858979, ECO:0000269|PubMed:27023709,
CC ECO:0000269|PubMed:31048492}.
CC -!- ACTIVITY REGULATION: Activated by the chemical integrated stress
CC response (ISR) inhibitor ISRIB which stimulates guanine nucleotide
CC exchange factor activity for both phosphorylated and unphosphorylated
CC eIF2. {ECO:0000269|PubMed:25858979}.
CC -!- SUBUNIT: Component of the translation initiation factor 2B (eIF2B)
CC complex which is a heterodecamer of two sets of five different
CC subunits: alpha, beta, gamma, delta and epsilon. Subunits alpha, beta
CC and delta comprise a regulatory subcomplex and subunits epsilon and
CC gamma comprise a catalytic subcomplex (PubMed:25858979,
CC PubMed:27023709, PubMed:31048492). Within the complex, the hexameric
CC regulatory complex resides at the center, with the two heterodimeric
CC catalytic subcomplexes bound on opposite sides (PubMed:31048492).
CC {ECO:0000269|PubMed:25858979, ECO:0000269|PubMed:27023709,
CC ECO:0000269|PubMed:31048492}.
CC -!- INTERACTION:
CC P49770; Q96LT7: C9orf72; NbExp=6; IntAct=EBI-718773, EBI-2961725;
CC P49770; Q9UI10: EIF2B4; NbExp=7; IntAct=EBI-718773, EBI-2340132;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9UT76}.
CC -!- DISEASE: Leukoencephalopathy with vanishing white matter 2 (VWM2)
CC [MIM:620312]: An autosomal recessive brain disease characterized by
CC neurological features including progressive cerebellar ataxia,
CC spasticity, and cognitive deficits. Brain imaging shows abnormal white
CC matter that vanishes over time and is replaced by cerebrospinal fluid.
CC Disease severity ranges from fatal infantile forms to adult forms
CC without neurological deterioration. The disease is progressive with, in
CC most individuals, additional episodes of rapid deterioration following
CC febrile infections or minor head trauma. Death may occurs after a
CC variable period after disease onset, usually following an episode of
CC fever and coma. A subset of affected females with milder forms of the
CC disease who survive to adolescence exhibit ovarian dysfunction. This
CC variant of the disorder is called ovarioleukodystrophy.
CC {ECO:0000269|PubMed:11704758, ECO:0000269|PubMed:12707859,
CC ECO:0000269|PubMed:15776425, ECO:0000269|PubMed:21484434,
CC ECO:0000269|PubMed:22285377, ECO:0000269|PubMed:22729508}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC42002.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mendelian genes eukaryotic translation initiation
CC factor 2B, subunit 2 beta, 39kDa (EIF2B2); Note=Leiden Open Variation
CC Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/EIF2B2";
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DR EMBL; AF035280; AAB88176.1; -; mRNA.
DR EMBL; L40395; AAC42002.1; ALT_FRAME; mRNA.
DR EMBL; AC006530; AAD30183.1; -; Genomic_DNA.
DR EMBL; BC011750; AAH11750.1; -; mRNA.
DR CCDS; CCDS9836.1; -.
DR RefSeq; NP_055054.1; NM_014239.3.
DR PDB; 6CAJ; EM; 2.80 A; C/D=2-351.
DR PDB; 6EZO; EM; 4.10 A; C/D=5-351.
DR PDB; 6K71; EM; 4.30 A; C/D=1-351.
DR PDB; 6K72; EM; 4.60 A; C/D=1-351.
DR PDB; 6O81; EM; 3.21 A; C/D=2-351.
DR PDB; 6O85; EM; 3.03 A; C/D=2-351.
DR PDB; 6O9Z; EM; 3.03 A; C/D=2-351.
DR PDB; 7D43; EM; 4.30 A; C/D=1-351.
DR PDB; 7D44; EM; 4.00 A; C/D=1-351.
DR PDB; 7D45; EM; 3.80 A; C/D=1-351.
DR PDB; 7D46; EM; 4.00 A; C/D=1-351.
DR PDB; 7F64; EM; 2.42 A; C/D=1-351.
DR PDB; 7F66; EM; 2.76 A; C/D=1-351.
DR PDB; 7F67; EM; 3.59 A; C/D=1-351.
DR PDB; 7KMF; EM; 2.91 A; C/D=1-351.
DR PDB; 7L70; EM; 2.80 A; C/D=2-351.
DR PDB; 7L7G; EM; 3.00 A; C/D=2-351.
DR PDB; 7RLO; EM; 2.60 A; C/D=1-351.
DR PDB; 7TRJ; EM; 2.80 A; C/D=1-351.
DR PDB; 7VLK; EM; 2.27 A; C/D=1-351.
DR PDB; 8TQO; EM; 3.10 A; D=2-351.
DR PDB; 8TQZ; EM; 2.90 A; C/D=2-351.
DR PDBsum; 6CAJ; -.
DR PDBsum; 6EZO; -.
DR PDBsum; 6K71; -.
DR PDBsum; 6K72; -.
DR PDBsum; 6O81; -.
DR PDBsum; 6O85; -.
DR PDBsum; 6O9Z; -.
DR PDBsum; 7D43; -.
DR PDBsum; 7D44; -.
DR PDBsum; 7D45; -.
DR PDBsum; 7D46; -.
DR PDBsum; 7F64; -.
DR PDBsum; 7F66; -.
DR PDBsum; 7F67; -.
DR PDBsum; 7KMF; -.
DR PDBsum; 7L70; -.
DR PDBsum; 7L7G; -.
DR PDBsum; 7RLO; -.
DR PDBsum; 7TRJ; -.
DR PDBsum; 7VLK; -.
DR PDBsum; 8TQO; -.
DR PDBsum; 8TQZ; -.
DR AlphaFoldDB; P49770; -.
DR EMDB; EMD-0649; -.
DR EMDB; EMD-0651; -.
DR EMDB; EMD-0664; -.
DR EMDB; EMD-22924; -.
DR EMDB; EMD-23209; -.
DR EMDB; EMD-24535; -.
DR EMDB; EMD-26098; -.
DR EMDB; EMD-30568; -.
DR EMDB; EMD-30569; -.
DR EMDB; EMD-30570; -.
DR EMDB; EMD-30571; -.
DR EMDB; EMD-31472; -.
DR EMDB; EMD-31474; -.
DR EMDB; EMD-31475; -.
DR EMDB; EMD-32023; -.
DR EMDB; EMD-4162; -.
DR EMDB; EMD-7442; -.
DR EMDB; EMD-9840; -.
DR EMDB; EMD-9841; -.
DR EMDB; EMD-9842; -.
DR SMR; P49770; -.
DR BioGRID; 114409; 135.
DR CORUM; P49770; -.
DR IntAct; P49770; 45.
DR MINT; P49770; -.
DR STRING; 9606.ENSP00000266126; -.
DR iPTMnet; P49770; -.
DR PhosphoSitePlus; P49770; -.
DR SwissPalm; P49770; -.
DR BioMuta; EIF2B2; -.
DR DMDM; 6226858; -.
DR EPD; P49770; -.
DR jPOST; P49770; -.
DR MassIVE; P49770; -.
DR PaxDb; 9606-ENSP00000266126; -.
DR PeptideAtlas; P49770; -.
DR ProteomicsDB; 56113; -.
DR Pumba; P49770; -.
DR Antibodypedia; 57; 213 antibodies from 30 providers.
DR DNASU; 8892; -.
DR Ensembl; ENST00000266126.10; ENSP00000266126.5; ENSG00000119718.11.
DR GeneID; 8892; -.
DR KEGG; hsa:8892; -.
DR MANE-Select; ENST00000266126.10; ENSP00000266126.5; NM_014239.4; NP_055054.1.
DR AGR; HGNC:3258; -.
DR CTD; 8892; -.
DR DisGeNET; 8892; -.
DR GeneCards; EIF2B2; -.
DR GeneReviews; EIF2B2; -.
DR HGNC; HGNC:3258; EIF2B2.
DR HPA; ENSG00000119718; Low tissue specificity.
DR MalaCards; EIF2B2; -.
DR MIM; 606454; gene.
DR MIM; 620312; phenotype.
DR neXtProt; NX_P49770; -.
DR OpenTargets; ENSG00000119718; -.
DR Orphanet; 157713; Congenital or early infantile CACH syndrome.
DR Orphanet; 99854; Cree leukoencephalopathy.
DR Orphanet; 157719; Juvenile or adult CACH syndrome.
DR Orphanet; 157716; Late infantile CACH syndrome.
DR Orphanet; 99853; Ovarioleukodystrophy.
DR PharmGKB; PA27689; -.
DR VEuPathDB; HostDB:ENSG00000119718; -.
DR eggNOG; KOG1465; Eukaryota.
DR GeneTree; ENSGT00550000074908; -.
DR HOGENOM; CLU_016218_4_3_1; -.
DR InParanoid; P49770; -.
DR OMA; SHSCAVA; -.
DR OrthoDB; 169494at2759; -.
DR PhylomeDB; P49770; -.
DR TreeFam; TF101506; -.
DR PathwayCommons; P49770; -.
DR Reactome; R-HSA-72731; Recycling of eIF2:GDP.
DR SignaLink; P49770; -.
DR SIGNOR; P49770; -.
DR BioGRID-ORCS; 8892; 844 hits in 1176 CRISPR screens.
DR ChiTaRS; EIF2B2; human.
DR GeneWiki; EIF2B2; -.
DR GenomeRNAi; 8892; -.
DR Pharos; P49770; Tbio.
DR PRO; PR:P49770; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P49770; Protein.
DR Bgee; ENSG00000119718; Expressed in left lobe of thyroid gland and 209 other cell types or tissues.
DR ExpressionAtlas; P49770; baseline and differential.
DR Genevisible; P49770; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; IMP:UniProtKB.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IDA:UniProtKB.
DR GO; GO:0042552; P:myelination; IMP:UniProtKB.
DR GO; GO:0014003; P:oligodendrocyte development; IMP:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; IMP:UniProtKB.
DR GO; GO:0006446; P:regulation of translational initiation; TAS:UniProtKB.
DR GO; GO:0009749; P:response to glucose; ISS:UniProtKB.
DR GO; GO:0009408; P:response to heat; ISS:UniProtKB.
DR GO; GO:0043434; P:response to peptide hormone; ISS:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR PANTHER; PTHR45859; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT BETA; 1.
DR PANTHER; PTHR45859:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT BETA; 1.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; Initiation factor;
KW Leukodystrophy; Protein biosynthesis; Reference proteome.
FT CHAIN 1..351
FT /note="Translation initiation factor eIF2B subunit beta"
FT /id="PRO_0000156061"
FT VARIANT 85
FT /note="V -> E (in VWM2; dbSNP:rs397514648)"
FT /evidence="ECO:0000269|PubMed:21484434"
FT /id="VAR_068451"
FT VARIANT 127
FT /note="A -> V (found in a patient with Rett syndrome-like
FT phenotype; uncertain significance; dbSNP:rs150617429)"
FT /evidence="ECO:0000269|PubMed:26740508"
FT /id="VAR_079034"
FT VARIANT 171
FT /note="S -> F (in VWM2; with ovarian failure;
FT dbSNP:rs104894428)"
FT /evidence="ECO:0000269|PubMed:12707859,
FT ECO:0000269|PubMed:15776425"
FT /id="VAR_016842"
FT VARIANT 196
FT /note="P -> S (in VWM2; dbSNP:rs113994011)"
FT /evidence="ECO:0000269|PubMed:15776425"
FT /id="VAR_068452"
FT VARIANT 200
FT /note="G -> V (in VWM2; dbSNP:rs113994012)"
FT /evidence="ECO:0000269|PubMed:15776425"
FT /id="VAR_068453"
FT VARIANT 213
FT /note="E -> G (in VWM2; with and without ovarian failure;
FT dbSNP:rs104894425)"
FT /evidence="ECO:0000269|PubMed:11704758,
FT ECO:0000269|PubMed:12707859, ECO:0000269|PubMed:15776425,
FT ECO:0000269|PubMed:22729508"
FT /id="VAR_012289"
FT VARIANT 268
FT /note="C -> Y (in VWM2)"
FT /evidence="ECO:0000269|PubMed:22285377"
FT /id="VAR_068454"
FT VARIANT 273
FT /note="K -> R (in VWM2; dbSNP:rs113994016)"
FT /evidence="ECO:0000269|PubMed:11704758"
FT /id="VAR_012321"
FT VARIANT 316
FT /note="V -> D (in VWM2; dbSNP:rs104894426)"
FT /evidence="ECO:0000269|PubMed:11704758"
FT /id="VAR_012290"
FT VARIANT 329
FT /note="G -> V (in VWM2; dbSNP:rs113994020)"
FT /evidence="ECO:0000269|PubMed:11704758"
FT /id="VAR_012322"
FT CONFLICT 6
FT /note="A -> K (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="K -> T (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="S -> R (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="A -> V (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="S -> R (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT CONFLICT 95..101
FT /note="RLHGRSD -> DSMDAAT (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="H -> D (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT HELIX 9..24
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:7RLO"
FT HELIX 31..48
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 76..97
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:7VLK"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:7VLK"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:7L70"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:7VLK"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:6CAJ"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:7VLK"
SQ SEQUENCE 351 AA; 38990 MW; C29FE477143F545A CRC64;
MPGSAAKGSE LSERIESFVE TLKRGGGPRS SEEMARETLG LLRQIITDHR WSNAGELMEL
IRREGRRMTA AQPSETTVGN MVRRVLKIIR EEYGRLHGRS DESDQQESLH KLLTSGGLNE
DFSFHYAQLQ SNIIEAINEL LVELEGTMEN IAAQALEHIH SNEVIMTIGF SRTVEAFLKE
AARKRKFHVI VAECAPFCQG HEMAVNLSKA GIETTVMTDA AIFAVMSRVN KVIIGTKTIL
ANGALRAVTG THTLALAAKH HSTPLIVCAP MFKLSPQFPN EEDSFHKFVA PEEVLPFTEG
DILEKVSVHC PVFDYVPPEL ITLFISNIGG NAPSYIYRLM SELYHPDDHV L
//
