ID   BEX2_HUMAN              Reviewed;         128 AA.
AC   Q9BXY8; B2R574; D3DXA2; F5H7H5; Q5JVV9;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Protein BEX2;
DE   AltName: Full=Brain-expressed X-linked protein 2;
DE            Short=hBex2;
GN   Name=BEX2;
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.
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Mao Y., Xie Y., Zhou Z., Zhao W., Zhao S., Wang W., Huang Y., Wang S.,
RA   Tang R., Chen X., Wu C.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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   [4]
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   [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   SUBCELLULAR LOCATION, AND INTERACTION WITH LMO2.
RX   PubMed=16314316; DOI=10.1093/nar/gki964;
RA   Han C., Liu H., Liu J., Yin K., Xie Y., Shen X., Wang Y., Yuan J.,
RA   Qiang B., Liu Y.-J., Peng X.;
RT   "Human Bex2 interacts with LMO2 and regulates the transcriptional activity
RT   of a novel DNA-binding complex.";
RL   Nucleic Acids Res. 33:6555-6565(2005).
RN   [8]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=19711341; DOI=10.1002/ijc.24866;
RA   Naderi A., Liu J., Bennett I.C.;
RT   "BEX2 regulates mitochondrial apoptosis and G1 cell cycle in breast
RT   cancer.";
RL   Int. J. Cancer 126:1596-1610(2010).
CC   -!- FUNCTION: Regulator of mitochondrial apoptosis and G1 cell cycle in
CC       breast cancer (PubMed:19711341). Protects the breast cancer cells
CC       against mitochondrial apoptosis and this effect is mediated through the
CC       modulation of BCL2 protein family, which involves the positive
CC       regulation of anti-apoptotic member BCL2 and the negative regulation of
CC       pro-apoptotic members BAD, BAK1 and PUMA (PubMed:19711341). Required
CC       for the normal cell cycle progression during G1 in breast cancer cells
CC       through the regulation of CCND1 and CDKN1A (PubMed:19711341). Regulates
CC       the level of PP2A regulatory subunit B and PP2A phosphatase activity
CC       (PubMed:19711341). In absence of reductive stress, acts as a
CC       pseudosubstrate for the CRL2(FEM1B) complex: associates with FEM1B via
CC       zinc, thereby preventing association between FEM1B and its substrates
CC       (By similarity). {ECO:0000250|UniProtKB:Q9WTZ8,
CC       ECO:0000269|PubMed:19711341}.
CC   -!- SUBUNIT: Interacts with LMO2, possibly leading to regulate the
CC       transcriptional activity of a DNA-binding complex containing LMO2
CC       (PubMed:16314316). Interacts with OMP (By similarity).
CC       {ECO:0000250|UniProtKB:Q9WTZ8, ECO:0000269|PubMed:16314316}.
CC   -!- INTERACTION:
CC       Q9BXY8; Q6PJH3: AKAP9; NbExp=3; IntAct=EBI-745073, EBI-11745576;
CC       Q9BXY8; Q9H2G9: BLZF1; NbExp=6; IntAct=EBI-745073, EBI-2548012;
CC       Q9BXY8; Q96GS4: BORCS6; NbExp=3; IntAct=EBI-745073, EBI-10193358;
CC       Q9BXY8; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-745073, EBI-739580;
CC       Q9BXY8; Q8NCU1: CCDC197; NbExp=3; IntAct=EBI-745073, EBI-750686;
CC       Q9BXY8; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-745073, EBI-10961624;
CC       Q9BXY8; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-745073, EBI-347573;
CC       Q9BXY8; Q01850: CDR2; NbExp=3; IntAct=EBI-745073, EBI-1181367;
CC       Q9BXY8; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-745073, EBI-739624;
CC       Q9BXY8; Q9H9E3: COG4; NbExp=3; IntAct=EBI-745073, EBI-368382;
CC       Q9BXY8; P78358: CTAG1B; NbExp=5; IntAct=EBI-745073, EBI-1188472;
CC       Q9BXY8; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-745073, EBI-3867333;
CC       Q9BXY8; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-745073, EBI-356015;
CC       Q9BXY8; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-745073, EBI-742102;
CC       Q9BXY8; A1L4K1: FSD2; NbExp=3; IntAct=EBI-745073, EBI-5661036;
CC       Q9BXY8; P19883: FST; NbExp=3; IntAct=EBI-745073, EBI-1571188;
CC       Q9BXY8; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-745073, EBI-11519926;
CC       Q9BXY8; O75031: HSF2BP; NbExp=3; IntAct=EBI-745073, EBI-7116203;
CC       Q9BXY8; Q16082: HSPB2; NbExp=3; IntAct=EBI-745073, EBI-739395;
CC       Q9BXY8; Q9BS75: KLHL20; NbExp=3; IntAct=EBI-745073, EBI-10693436;
CC       Q9BXY8; Q92876: KLK6; NbExp=3; IntAct=EBI-745073, EBI-2432309;
CC       Q9BXY8; Q9Y448: KNSTRN; NbExp=3; IntAct=EBI-745073, EBI-373334;
CC       Q9BXY8; P19012: KRT15; NbExp=3; IntAct=EBI-745073, EBI-739566;
CC       Q9BXY8; P08727: KRT19; NbExp=3; IntAct=EBI-745073, EBI-742756;
CC       Q9BXY8; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-745073, EBI-3044087;
CC       Q9BXY8; Q15323: KRT31; NbExp=6; IntAct=EBI-745073, EBI-948001;
CC       Q9BXY8; O76011: KRT34; NbExp=3; IntAct=EBI-745073, EBI-1047093;
CC       Q9BXY8; O76015: KRT38; NbExp=3; IntAct=EBI-745073, EBI-1047263;
CC       Q9BXY8; Q6A163: KRT39; NbExp=3; IntAct=EBI-745073, EBI-11958242;
CC       Q9BXY8; Q6A162: KRT40; NbExp=3; IntAct=EBI-745073, EBI-10171697;
CC       Q9BXY8; P02538: KRT6A; NbExp=3; IntAct=EBI-745073, EBI-702198;
CC       Q9BXY8; O95678: KRT75; NbExp=3; IntAct=EBI-745073, EBI-2949715;
CC       Q9BXY8; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-745073, EBI-10171774;
CC       Q9BXY8; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-745073, EBI-1052037;
CC       Q9BXY8; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-745073, EBI-10176379;
CC       Q9BXY8; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-745073, EBI-14065470;
CC       Q9BXY8; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-745073, EBI-18395721;
CC       Q9BXY8; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-745073, EBI-3957694;
CC       Q9BXY8; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-745073, EBI-3958099;
CC       Q9BXY8; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-745073, EBI-11962084;
CC       Q9BXY8; P80188: LCN2; NbExp=3; IntAct=EBI-745073, EBI-11911016;
CC       Q9BXY8; O95751: LDOC1; NbExp=3; IntAct=EBI-745073, EBI-740738;
CC       Q9BXY8; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-745073, EBI-741037;
CC       Q9BXY8; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-745073, EBI-10178634;
CC       Q9BXY8; P43356: MAGEA2B; NbExp=3; IntAct=EBI-745073, EBI-5650739;
CC       Q9BXY8; Q1RN33: MAGEA4; NbExp=3; IntAct=EBI-745073, EBI-10194128;
CC       Q9BXY8; Q99750: MDFI; NbExp=4; IntAct=EBI-745073, EBI-724076;
CC       Q9BXY8; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-745073, EBI-2548751;
CC       Q9BXY8; Q13064: MKRN3; NbExp=6; IntAct=EBI-745073, EBI-2340269;
CC       Q9BXY8; Q6PF18: MORN3; NbExp=3; IntAct=EBI-745073, EBI-9675802;
CC       Q9BXY8; Q96DV4: MRPL38; NbExp=3; IntAct=EBI-745073, EBI-720441;
CC       Q9BXY8; Q4VC12: MSS51; NbExp=3; IntAct=EBI-745073, EBI-11599933;
CC       Q9BXY8; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-745073, EBI-11522433;
CC       Q9BXY8; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-745073, EBI-10172876;
CC       Q9BXY8; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-745073, EBI-10271199;
CC       Q9BXY8; O43482: OIP5; NbExp=3; IntAct=EBI-745073, EBI-536879;
CC       Q9BXY8; O15496: PLA2G10; NbExp=3; IntAct=EBI-745073, EBI-726466;
CC       Q9BXY8; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-745073, EBI-949255;
CC       Q9BXY8; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-745073, EBI-302345;
CC       Q9BXY8; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-745073, EBI-3957793;
CC       Q9BXY8; Q96C74: ROPN1L; NbExp=3; IntAct=EBI-745073, EBI-9033237;
CC       Q9BXY8; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-745073, EBI-748621;
CC       Q9BXY8; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-745073, EBI-5235340;
CC       Q9BXY8; O43610: SPRY3; NbExp=3; IntAct=EBI-745073, EBI-12290641;
CC       Q9BXY8; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-745073, EBI-2212028;
CC       Q9BXY8; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-745073, EBI-6872807;
CC       Q9BXY8; Q9Y6A5: TACC3; NbExp=3; IntAct=EBI-745073, EBI-2554984;
CC       Q9BXY8; Q13077: TRAF1; NbExp=3; IntAct=EBI-745073, EBI-359224;
CC       Q9BXY8; Q12933: TRAF2; NbExp=6; IntAct=EBI-745073, EBI-355744;
CC       Q9BXY8; P14373: TRIM27; NbExp=3; IntAct=EBI-745073, EBI-719493;
CC       Q9BXY8; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-745073, EBI-5235829;
CC       Q9BXY8; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-745073, EBI-11525489;
CC       Q9BXY8; Q86UV6-2: TRIM74; NbExp=3; IntAct=EBI-745073, EBI-10259086;
CC       Q9BXY8; Q15654: TRIP6; NbExp=3; IntAct=EBI-745073, EBI-742327;
CC       Q9BXY8; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-745073, EBI-739895;
CC       Q9BXY8; Q9UK41-2: VPS28; NbExp=3; IntAct=EBI-745073, EBI-12146727;
CC       Q9BXY8; P17023: ZNF19; NbExp=3; IntAct=EBI-745073, EBI-12884200;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3MKQ1}. Nucleus
CC       {ECO:0000269|PubMed:16314316}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BXY8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BXY8-2; Sequence=VSP_046808;
CC   -!- TISSUE SPECIFICITY: Expressed in central nervous system, with high
CC       level in pituitary, cerebellum and temporal lobe. Widely expressed in
CC       breast cancer cell lines. {ECO:0000269|PubMed:15958283,
CC       ECO:0000269|PubMed:19711341}.
CC   -!- DOMAIN: The histidine cluster (His cluster) and Cys-125 mediate zinc-
CC       binding. {ECO:0000250|UniProtKB:Q9WTZ9}.
CC   -!- SIMILARITY: Belongs to the BEX family. {ECO:0000305}.
CC   -!- CAUTION: Was named BEX1 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/44162/BEX2";
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DR   EMBL; AY833560; AAX40678.1; -; mRNA.
DR   EMBL; AF251053; AAK34943.1; -; mRNA.
DR   EMBL; AK312085; BAG35021.1; -; mRNA.
DR   EMBL; AL133348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z70233; CAD24039.1; -; Genomic_DNA.
DR   EMBL; CH471190; EAW54715.1; -; Genomic_DNA.
DR   EMBL; CH471190; EAW54716.1; -; Genomic_DNA.
DR   EMBL; BC015522; AAH15522.1; -; mRNA.
DR   CCDS; CCDS14505.1; -. [Q9BXY8-1]
DR   CCDS; CCDS55467.1; -. [Q9BXY8-2]
DR   RefSeq; NP_001161871.1; NM_001168399.1. [Q9BXY8-2]
DR   RefSeq; NP_001161872.1; NM_001168400.1.
DR   RefSeq; NP_001161873.1; NM_001168401.1. [Q9BXY8-1]
DR   RefSeq; NP_116010.1; NM_032621.3. [Q9BXY8-1]
DR   AlphaFoldDB; Q9BXY8; -.
DR   BioGRID; 124218; 109.
DR   CORUM; Q9BXY8; -.
DR   IntAct; Q9BXY8; 89.
DR   MINT; Q9BXY8; -.
DR   STRING; 9606.ENSP00000442521; -.
DR   iPTMnet; Q9BXY8; -.
DR   PhosphoSitePlus; Q9BXY8; -.
DR   SwissPalm; Q9BXY8; -.
DR   BioMuta; BEX2; -.
DR   DMDM; 74752443; -.
DR   MassIVE; Q9BXY8; -.
DR   PaxDb; 9606-ENSP00000442521; -.
DR   PeptideAtlas; Q9BXY8; -.
DR   Antibodypedia; 44280; 106 antibodies from 20 providers.
DR   DNASU; 84707; -.
DR   Ensembl; ENST00000372674.5; ENSP00000361759.1; ENSG00000133134.12. [Q9BXY8-1]
DR   Ensembl; ENST00000372677.8; ENSP00000361762.3; ENSG00000133134.12. [Q9BXY8-1]
DR   Ensembl; ENST00000536889.1; ENSP00000442521.1; ENSG00000133134.12. [Q9BXY8-2]
DR   GeneID; 84707; -.
DR   KEGG; hsa:84707; -.
DR   MANE-Select; ENST00000372677.8; ENSP00000361762.3; NM_032621.4; NP_116010.1.
DR   UCSC; uc004eka.4; human. [Q9BXY8-1]
DR   AGR; HGNC:30933; -.
DR   CTD; 84707; -.
DR   DisGeNET; 84707; -.
DR   GeneCards; BEX2; -.
DR   HGNC; HGNC:30933; BEX2.
DR   HPA; ENSG00000133134; Tissue enhanced (brain, pituitary gland).
DR   MIM; 300691; gene.
DR   neXtProt; NX_Q9BXY8; -.
DR   OpenTargets; ENSG00000133134; -.
DR   PharmGKB; PA134977614; -.
DR   VEuPathDB; HostDB:ENSG00000133134; -.
DR   eggNOG; ENOG502RW3Y; Eukaryota.
DR   GeneTree; ENSGT00940000153412; -.
DR   HOGENOM; CLU_123122_1_0_1; -.
DR   InParanoid; Q9BXY8; -.
DR   OMA; HRVGEPQ; -.
DR   OrthoDB; 5261636at2759; -.
DR   PhylomeDB; Q9BXY8; -.
DR   TreeFam; TF337909; -.
DR   PathwayCommons; Q9BXY8; -.
DR   SignaLink; Q9BXY8; -.
DR   BioGRID-ORCS; 84707; 17 hits in 745 CRISPR screens.
DR   ChiTaRS; BEX2; human.
DR   GeneWiki; BEX2; -.
DR   GenomeRNAi; 84707; -.
DR   Pharos; Q9BXY8; Tbio.
DR   PRO; PR:Q9BXY8; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9BXY8; Protein.
DR   Bgee; ENSG00000133134; Expressed in endothelial cell and 184 other cell types or tissues.
DR   ExpressionAtlas; Q9BXY8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   InterPro; IPR007623; BEX.
DR   InterPro; IPR021156; TF_A-like/BEX.
DR   PANTHER; PTHR19430; PROTEIN BEX1-RELATED; 1.
DR   PANTHER; PTHR19430:SF2; PROTEIN BEX2; 1.
DR   Pfam; PF04538; BEX; 1.
DR   PIRSF; PIRSF008633; BEX; 1.
DR   Genevisible; Q9BXY8; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cell cycle; Cytoplasm; Metal-binding;
KW   Methylation; Nucleus; Reference proteome; Zinc.
FT   CHAIN           1..128
FT                   /note="Protein BEX2"
FT                   /id="PRO_0000229777"
FT   REGION          107..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..121
FT                   /note="His cluster"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTZ9"
FT   BINDING         125
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         50
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTZ8"
FT   VAR_SEQ         1
FT                   /note="M -> MQKMVVCGAKCCGDAPHVENREEETARIGPGVM (in isoform
FT                   2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046808"
SQ   SEQUENCE   128 AA;  15321 MW;  F6302EC28F71D2A8 CRC64;
     MESKEERALN NLIVENVNQE NDEKDEKEQV ANKGEPLALP LNVSEYCVPR GNRRRFRVRQ
     PILQYRWDIM HRLGEPQARM REENMERIGE EVRQLMEKLR EKQLSHSLRA VSTDPPHHDH
     HDEFCLMP
//