ID   BEX1_HUMAN              Reviewed;         125 AA.
AC   Q9HBH7; A0AVN1; A8K4J3; Q9NZ33;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Protein BEX1;
DE   AltName: Full=Brain-expressed X-linked protein 1;
GN   Name=BEX1;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Fetal brain;
RX   PubMed=11989783; DOI=10.1023/a:1014565320998;
RA   Yang Q.-S., Xia F., Gu S.-H., Yuan H.-L., Chen J.-Z., Yang Q.-S., Ying K.,
RA   Xie Y., Mao Y.-M.;
RT   "Cloning and expression pattern of a spermatogenesis-related gene, BEX1,
RT   mapped to chromosome Xq22.";
RL   Biochem. Genet. 40:1-12(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=15958283; DOI=10.1016/j.gene.2005.05.012;
RA   Alvarez E., Zhou W., Witta S.E., Freed C.R.;
RT   "Characterization of the Bex gene family in humans, mice, and rats.";
RL   Gene 357:18-28(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Adrenal gland, and Hypothalamus;
RX   PubMed=10931946; DOI=10.1073/pnas.160270997;
RA   Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA   Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA   Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA   Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA   Chen M.-D., Chen J.-L.;
RT   "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT   and full-length cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   TISSUE SPECIFICITY.
RX   PubMed=15920485; DOI=10.1038/sj.leu.2403820;
RA   Quentmeier H., Tonelli R., Geffers R., Pession A., Uphoff C.C.,
RA   Drexler H.G.;
RT   "Expression of BEX1 in acute myeloid leukemia with MLL rearrangements.";
RL   Leukemia 19:1488-1489(2005).
CC   -!- FUNCTION: Signaling adapter molecule involved in p75NTR/NGFR signaling.
CC       Plays a role in cell cycle progression and neuronal differentiation.
CC       Inhibits neuronal differentiation in response to nerve growth factor
CC       (NGF). May act as a link between the cell cycle and neurotrophic factor
CC       signaling, possibly by functioning as an upstream modulator of receptor
CC       signaling, coordinating biological responses to external signals with
CC       internal cellular states (By similarity). In absence of reductive
CC       stress, acts as a pseudosubstrate for the CRL2(FEM1B) complex:
CC       associates with FEM1B via zinc, thereby preventing association between
CC       FEM1B and its substrates (By similarity).
CC       {ECO:0000250|UniProtKB:Q3MKQ2, ECO:0000250|UniProtKB:Q9R224}.
CC   -!- SUBUNIT: Interacts with neurotrophin receptor p75NTR/NGFR (By
CC       similarity). Interacts with OMP (By similarity).
CC       {ECO:0000250|UniProtKB:Q3MKQ2, ECO:0000250|UniProtKB:Q9R224}.
CC   -!- INTERACTION:
CC       Q9HBH7; Q9NZN8: CNOT2; NbExp=3; IntAct=EBI-7162175, EBI-743033;
CC       Q9HBH7; P78358: CTAG1B; NbExp=5; IntAct=EBI-7162175, EBI-1188472;
CC       Q9HBH7; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-7162175, EBI-3867333;
CC       Q9HBH7; Q9BS75: KLHL20; NbExp=3; IntAct=EBI-7162175, EBI-10693436;
CC       Q9HBH7; Q15323: KRT31; NbExp=3; IntAct=EBI-7162175, EBI-948001;
CC       Q9HBH7; O76011: KRT34; NbExp=3; IntAct=EBI-7162175, EBI-1047093;
CC       Q9HBH7; P43356: MAGEA2B; NbExp=3; IntAct=EBI-7162175, EBI-5650739;
CC       Q9HBH7; Q99750: MDFI; NbExp=6; IntAct=EBI-7162175, EBI-724076;
CC       Q9HBH7; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-7162175, EBI-16439278;
CC       Q9HBH7; Q5XKR4: OTP; NbExp=3; IntAct=EBI-7162175, EBI-12865884;
CC       Q9HBH7; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-7162175, EBI-79165;
CC       Q9HBH7; Q8IYF3: TEX11; NbExp=3; IntAct=EBI-7162175, EBI-742397;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3MKQ2}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q3MKQ2}. Note=Shuttles between the cytoplasm and
CC       the nucleus. Predominantly nuclear. {ECO:0000250|UniProtKB:Q3MKQ2}.
CC   -!- TISSUE SPECIFICITY: Expressed in central nervous system, with high
CC       level in pituitary, cerebellum and temporal lobe. Expressed in lung,
CC       skeletal muscle, peripheral blood leukocyte, stomach, lymph node,
CC       trachea and bone marrow. Highly expressed in acute myeloid leukemia.
CC       {ECO:0000269|PubMed:11989783, ECO:0000269|PubMed:15920485,
CC       ECO:0000269|PubMed:15958283}.
CC   -!- DOMAIN: The histidine cluster (His cluster) and Cys-122 mediate zinc-
CC       binding. {ECO:0000250|UniProtKB:Q9WTZ9}.
CC   -!- PTM: Phosphorylated. Phosphorylation of Ser-102 protects it from the
CC       proteasome. {ECO:0000250|UniProtKB:Q3MKQ2}.
CC   -!- PTM: Ubiquitinated. Degraded by the proteasome.
CC       {ECO:0000250|UniProtKB:Q3MKQ2}.
CC   -!- SIMILARITY: Belongs to the BEX family. {ECO:0000305}.
CC   -!- CAUTION: Was named BEX2 by some authors. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/44161/bex1-(brain-expressed-x-linked-1)";
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DR   EMBL; AF237783; AAG09752.1; -; mRNA.
DR   EMBL; AY833561; AAX40679.1; -; mRNA.
DR   EMBL; AF183416; AAG09685.1; -; mRNA.
DR   EMBL; AF220189; AAF67654.1; -; mRNA.
DR   EMBL; AK290958; BAF83647.1; -; mRNA.
DR   EMBL; AL008708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC126427; AAI26428.1; -; mRNA.
DR   EMBL; BC126429; AAI26430.1; -; mRNA.
DR   CCDS; CCDS35354.1; -.
DR   RefSeq; NP_060946.3; NM_018476.3.
DR   AlphaFoldDB; Q9HBH7; -.
DR   BioGRID; 120961; 53.
DR   IntAct; Q9HBH7; 25.
DR   MINT; Q9HBH7; -.
DR   STRING; 9606.ENSP00000361813; -.
DR   iPTMnet; Q9HBH7; -.
DR   PhosphoSitePlus; Q9HBH7; -.
DR   BioMuta; BEX1; -.
DR   DMDM; 91208332; -.
DR   MassIVE; Q9HBH7; -.
DR   PaxDb; 9606-ENSP00000361813; -.
DR   PeptideAtlas; Q9HBH7; -.
DR   ProteomicsDB; 81553; -.
DR   Antibodypedia; 28967; 159 antibodies from 21 providers.
DR   DNASU; 55859; -.
DR   Ensembl; ENST00000372728.4; ENSP00000361813.3; ENSG00000133169.6.
DR   GeneID; 55859; -.
DR   KEGG; hsa:55859; -.
DR   MANE-Select; ENST00000372728.4; ENSP00000361813.3; NM_018476.4; NP_060946.3.
DR   UCSC; uc004ejt.2; human.
DR   AGR; HGNC:1036; -.
DR   CTD; 55859; -.
DR   DisGeNET; 55859; -.
DR   GeneCards; BEX1; -.
DR   HGNC; HGNC:1036; BEX1.
DR   HPA; ENSG00000133169; Tissue enhanced (brain, pituitary gland).
DR   MIM; 300690; gene.
DR   neXtProt; NX_Q9HBH7; -.
DR   OpenTargets; ENSG00000133169; -.
DR   PharmGKB; PA25340; -.
DR   VEuPathDB; HostDB:ENSG00000133169; -.
DR   eggNOG; ENOG502RW3Y; Eukaryota.
DR   GeneTree; ENSGT00940000153412; -.
DR   HOGENOM; CLU_123122_1_0_1; -.
DR   InParanoid; Q9HBH7; -.
DR   OMA; GKPQARM; -.
DR   OrthoDB; 5261636at2759; -.
DR   PhylomeDB; Q9HBH7; -.
DR   TreeFam; TF337909; -.
DR   PathwayCommons; Q9HBH7; -.
DR   SignaLink; Q9HBH7; -.
DR   SIGNOR; Q9HBH7; -.
DR   BioGRID-ORCS; 55859; 11 hits in 773 CRISPR screens.
DR   ChiTaRS; BEX1; human.
DR   GeneWiki; BEX1; -.
DR   GenomeRNAi; 55859; -.
DR   Pharos; Q9HBH7; Tbio.
DR   PRO; PR:Q9HBH7; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9HBH7; Protein.
DR   Bgee; ENSG00000133169; Expressed in endothelial cell and 171 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140678; F:molecular function inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   InterPro; IPR007623; BEX.
DR   InterPro; IPR021156; TF_A-like/BEX.
DR   PANTHER; PTHR19430:SF3; PROTEIN BEX1; 1.
DR   PANTHER; PTHR19430; PROTEIN BEX1-RELATED; 1.
DR   Pfam; PF04538; BEX; 1.
DR   PIRSF; PIRSF008633; BEX; 1.
DR   Genevisible; Q9HBH7; HS.
PE   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Differentiation; Metal-binding;
KW   Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation;
KW   Zinc.
FT   CHAIN           1..125
FT                   /note="Protein BEX1"
FT                   /id="PRO_0000229772"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..118
FT                   /note="His cluster"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTZ9"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared with FEM1B"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTZ9"
FT   MOD_RES         102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3MKQ2"
FT   VARIANT         9
FT                   /note="V -> L (in dbSNP:rs3174500)"
FT                   /id="VAR_042667"
FT   VARIANT         11
FT                   /note="S -> N (in dbSNP:rs1045058)"
FT                   /id="VAR_042668"
FT   VARIANT         13
FT                   /note="S -> I (in dbSNP:rs1045061)"
FT                   /id="VAR_042669"
FT   VARIANT         14
FT                   /note="M -> V (in dbSNP:rs1045063)"
FT                   /id="VAR_042670"
FT   VARIANT         17
FT                   /note="A -> V (in dbSNP:rs1045065)"
FT                   /id="VAR_042671"
FT   VARIANT         40
FT                   /note="A -> V (in dbSNP:rs709036)"
FT                   /id="VAR_025756"
FT   VARIANT         66
FT                   /note="M -> I (in dbSNP:rs1045082)"
FT                   /id="VAR_025757"
FT   CONFLICT        7
FT                   /note="R -> L (in Ref. 1; AAG09752)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88
FT                   /note="E -> G (in Ref. 1; AAG09752)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="Q -> R (in Ref. 4; BAF83647)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   125 AA;  14860 MW;  2406DD71F7E663D2 CRC64;
     MESKEKRAVN SLSMENANQE NEEKEQVANK GEPLALPLDA GEYCVPRGNR RRFRVRQPIL
     QYRWDMMHRL GEPQARMREE NMERIGEEVR QLMEKLREKQ LSHSLRAVST DPPHHDHHDE
     FCLMP
//