BEX4_HUMAN
ID BEX4_HUMAN Reviewed; 120 AA.
AC Q9NWD9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein BEX4 {ECO:0000305};
DE AltName: Full=BEX1-like protein 1 {ECO:0000312|HGNC:HGNC:25475};
DE AltName: Full=Brain-expressed X-linked protein 4 {ECO:0000303|PubMed:15958283, ECO:0000312|HGNC:HGNC:25475};
DE AltName: Full=Nerve growth factor receptor-associated protein 3 {ECO:0000303|PubMed:15958283};
GN Name=BEX4 {ECO:0000303|PubMed:15958283, ECO:0000312|HGNC:HGNC:25475};
GN Synonyms=BEXL1 {ECO:0000312|HGNC:HGNC:25475},
GN NADE3 {ECO:0000303|PubMed:15958283};
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 [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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 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 [4]
RP FUNCTION, INTERACTION WITH ALPHA-TUBULIN AND SIRT2, SUBCELLULAR LOCATION,
RP AND REGION.
RX PubMed=27512957; DOI=10.1038/cddis.2016.240;
RA Lee J.K., Lee J., Go H., Lee C.G., Kim S., Kim H.S., Cho H., Choi K.S.,
RA Ha G.H., Lee C.W.;
RT "Oncogenic microtubule hyperacetylation through BEX4-mediated sirtuin 2
RT inhibition.";
RL Cell Death Dis. 7:E2336-E2336(2016).
CC -!- FUNCTION: May play a role in microtubule deacetylation by negatively
CC regulating the SIRT2 deacetylase activity toward alpha-tubulin and
CC thereby participate in the control of cell cycle progression and
CC genomic stability. {ECO:0000269|PubMed:27512957}.
CC -!- SUBUNIT: Interacts with alpha-tubulin (PubMed:27512957). Interacts with
CC SIRT2 (PubMed:27512957). {ECO:0000269|PubMed:27512957}.
CC -!- INTERACTION:
CC Q9NWD9; Q15777: MPPED2; NbExp=3; IntAct=EBI-15105944, EBI-2350461;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:27512957}. Nucleus {ECO:0000269|PubMed:27512957}.
CC Cytoplasm {ECO:0000269|PubMed:27512957}. Note=Also localizes to
CC microtubules. {ECO:0000269|PubMed:27512957}.
CC -!- TISSUE SPECIFICITY: Very high expression in heart, skeletal muscle,
CC liver, and kidney. The levels of expression are uniform throughout the
CC brain. {ECO:0000269|PubMed:15958283}.
CC -!- PTM: Ubiquitinated and degraded by the proteasome.
CC {ECO:0000250|UniProtKB:Q3MKP9}.
CC -!- SIMILARITY: Belongs to the BEX family. {ECO:0000305}.
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DR EMBL; AK000959; BAA91443.1; -; mRNA.
DR EMBL; AY833563; AAX40681.1; -; mRNA.
DR EMBL; AL035494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS35355.1; -.
DR RefSeq; NP_001073894.1; NM_001080425.3.
DR RefSeq; NP_001121160.1; NM_001127688.2.
DR AlphaFoldDB; Q9NWD9; -.
DR BioGRID; 121131; 16.
DR IntAct; Q9NWD9; 3.
DR MINT; Q9NWD9; -.
DR STRING; 9606.ENSP00000361780; -.
DR iPTMnet; Q9NWD9; -.
DR PhosphoSitePlus; Q9NWD9; -.
DR BioMuta; BEX4; -.
DR DMDM; 74753015; -.
DR MassIVE; Q9NWD9; -.
DR PaxDb; Q9NWD9; -.
DR PeptideAtlas; Q9NWD9; -.
DR PRIDE; Q9NWD9; -.
DR ProteomicsDB; 82929; -.
DR Antibodypedia; 29002; 111 antibodies from 15 providers.
DR DNASU; 56271; -.
DR Ensembl; ENST00000372691.3; ENSP00000361776.3; ENSG00000102409.10.
DR Ensembl; ENST00000372695.6; ENSP00000361780.5; ENSG00000102409.10.
DR GeneID; 56271; -.
DR KEGG; hsa:56271; -.
DR MANE-Select; ENST00000372695.6; ENSP00000361780.5; NM_001080425.4; NP_001073894.1.
DR UCSC; uc004ejv.5; human.
DR CTD; 56271; -.
DR DisGeNET; 56271; -.
DR GeneCards; BEX4; -.
DR HGNC; HGNC:25475; BEX4.
DR HPA; ENSG00000102409; Low tissue specificity.
DR MIM; 300692; gene.
DR neXtProt; NX_Q9NWD9; -.
DR OpenTargets; ENSG00000102409; -.
DR PharmGKB; PA162377543; -.
DR VEuPathDB; HostDB:ENSG00000102409; -.
DR eggNOG; ENOG502TDUR; Eukaryota.
DR GeneTree; ENSGT00940000162932; -.
DR HOGENOM; CLU_123122_0_0_1; -.
DR InParanoid; Q9NWD9; -.
DR OMA; ESFNMED; -.
DR OrthoDB; 1525516at2759; -.
DR PhylomeDB; Q9NWD9; -.
DR TreeFam; TF337909; -.
DR PathwayCommons; Q9NWD9; -.
DR SignaLink; Q9NWD9; -.
DR BioGRID-ORCS; 56271; 5 hits in 706 CRISPR screens.
DR ChiTaRS; BEX4; human.
DR GenomeRNAi; 56271; -.
DR Pharos; Q9NWD9; Tbio.
DR PRO; PR:Q9NWD9; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NWD9; protein.
DR Bgee; ENSG00000102409; Expressed in prefrontal cortex and 205 other tissues.
DR Genevisible; Q9NWD9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:1904428; P:negative regulation of tubulin deacetylation; IMP:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR InterPro; IPR007623; BEX.
DR InterPro; IPR021156; TF_A-like/BEX.
DR PANTHER; PTHR13987; PTHR13987; 1.
DR Pfam; PF04538; BEX; 1.
DR PIRSF; PIRSF008633; BEX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..120
FT /note="Protein BEX4"
FT /id="PRO_0000229783"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..120
FT /note="Interaction with alpha-tubulin"
FT /evidence="ECO:0000269|PubMed:27512957"
FT REGION 31..90
FT /note="Interaction with SIRT2"
FT /evidence="ECO:0000269|PubMed:27512957"
FT COMPBIAS 9..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 120 AA; 14067 MW; AD9527B5587622D4 CRC64;
MESKEELAAN NLNGENAQQE NEGGEQAPTQ NEEESRHLGG GEGQKPGGNI RRGRVRRLVP
NFRWAIPNRH IEHNEARDDV ERFVGQMMEI KRKTREQQMR HYMRFQTPEP DNHYDFCLIP
