ID BEX5_HUMAN Reviewed; 111 AA. AC Q5H9J7; Q569J0; Q56A74; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 15-FEB-2005, sequence version 1. DT 24-JAN-2024, entry version 130. DE RecName: Full=Protein BEX5; DE AltName: Full=Brain-expressed X-linked protein 5; DE AltName: Full=NGFRAP1-like protein 1; DE AltName: Full=Nerve growth factor receptor-associated protein 2; GN Name=BEX5; Synonyms=NADE2, NGFRAP1L1; 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], SUBCELLULAR LOCATION, AND DEGRADATION BY THE RP PROTEASOME. 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 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 [3] 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 [4] RP CAUTION. RX PubMed=15861462; DOI=10.1002/cne.20486; RA Koo J.H., Saraswati M., Margolis F.L.; RT "Immunolocalization of Bex protein in the mouse brain and olfactory RT system."; RL J. Comp. Neurol. 487:1-14(2005). CC -!- INTERACTION: CC Q5H9J7; Q13515: BFSP2; NbExp=3; IntAct=EBI-10243741, EBI-10229433; CC Q5H9J7; Q9H9Q2: COPS7B; NbExp=3; IntAct=EBI-10243741, EBI-2510162; CC Q5H9J7; G5E9A7: DMWD; NbExp=3; IntAct=EBI-10243741, EBI-10976677; CC Q5H9J7; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-10243741, EBI-21603100; CC Q5H9J7; Q9Y6C2: EMILIN1; NbExp=4; IntAct=EBI-10243741, EBI-744586; CC Q5H9J7; O95363: FARS2; NbExp=3; IntAct=EBI-10243741, EBI-2513774; CC Q5H9J7; P22607: FGFR3; NbExp=3; IntAct=EBI-10243741, EBI-348399; CC Q5H9J7; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-10243741, EBI-10226858; CC Q5H9J7; Q6VB84: FOXD4L3; NbExp=3; IntAct=EBI-10243741, EBI-11961494; CC Q5H9J7; Q9P2W3: GNG13; NbExp=3; IntAct=EBI-10243741, EBI-11427343; CC Q5H9J7; Q08AF8: GOLGA8G; NbExp=3; IntAct=EBI-10243741, EBI-10181260; CC Q5H9J7; P06396: GSN; NbExp=3; IntAct=EBI-10243741, EBI-351506; CC Q5H9J7; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-10243741, EBI-1054873; CC Q5H9J7; A0A0C4DG38: ING3; NbExp=3; IntAct=EBI-10243741, EBI-10263367; CC Q5H9J7; O15116: LSM1; NbExp=3; IntAct=EBI-10243741, EBI-347619; CC Q5H9J7; P43361: MAGEA8; NbExp=7; IntAct=EBI-10243741, EBI-10182930; CC Q5H9J7; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-10243741, EBI-10288852; CC Q5H9J7; Q15014: MORF4L2; NbExp=3; IntAct=EBI-10243741, EBI-399257; CC Q5H9J7; O14561: NDUFAB1; NbExp=3; IntAct=EBI-10243741, EBI-1246261; CC Q5H9J7; P35240-4: NF2; NbExp=3; IntAct=EBI-10243741, EBI-1014514; CC Q5H9J7; Q8N7B6-2: PACRGL; NbExp=3; IntAct=EBI-10243741, EBI-10694433; CC Q5H9J7; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-10243741, EBI-5235340; CC Q5H9J7; Q13148: TARDBP; NbExp=6; IntAct=EBI-10243741, EBI-372899; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15958283}. CC -!- PTM: Ubiquitinated (PubMed:15958283). Degraded by the proteasome CC (PubMed:15958283). {ECO:0000269|PubMed:15958283}. CC -!- MISCELLANEOUS: The mouse orthologous protein seems not to exist. A CC publication described a sequence that they named Bex5, but it probably CC represents a pseudogene (PubMed:15861462). CC {ECO:0000305|PubMed:15861462}. CC -!- SIMILARITY: Belongs to the BEX family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY833564; AAX40682.1; -; mRNA. DR EMBL; Z70719; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC042818; AAH42818.1; -; mRNA. DR EMBL; BC092450; AAH92450.1; -; mRNA. DR EMBL; BC106955; AAI06956.1; -; mRNA. DR CCDS; CCDS35350.1; -. DR RefSeq; NP_001012996.1; NM_001012978.2. DR RefSeq; NP_001153032.1; NM_001159560.1. DR AlphaFoldDB; Q5H9J7; -. DR SMR; Q5H9J7; -. DR BioGRID; 131069; 28. DR IntAct; Q5H9J7; 25. DR STRING; 9606.ENSP00000446054; -. DR iPTMnet; Q5H9J7; -. DR PhosphoSitePlus; Q5H9J7; -. DR BioMuta; BEX5; -. DR DMDM; 74755456; -. DR MassIVE; Q5H9J7; -. DR PaxDb; 9606-ENSP00000446054; -. DR PeptideAtlas; Q5H9J7; -. DR ProteomicsDB; 62890; -. DR Antibodypedia; 28852; 38 antibodies from 9 providers. DR DNASU; 340542; -. DR Ensembl; ENST00000333643.4; ENSP00000328030.3; ENSG00000184515.11. DR Ensembl; ENST00000543160.5; ENSP00000446054.1; ENSG00000184515.11. DR Ensembl; ENST00000708878.1; ENSP00000517394.1; ENSG00000291824.1. DR Ensembl; ENST00000708879.1; ENSP00000517395.1; ENSG00000291824.1. DR GeneID; 340542; -. DR KEGG; hsa:340542; -. DR MANE-Select; ENST00000333643.4; ENSP00000328030.3; NM_001012978.3; NP_001012996.1. DR UCSC; uc004eir.4; human. DR AGR; HGNC:27990; -. DR CTD; 340542; -. DR DisGeNET; 340542; -. DR GeneCards; BEX5; -. DR HGNC; HGNC:27990; BEX5. DR HPA; ENSG00000184515; Tissue enhanced (brain, pituitary gland). DR MIM; 300693; gene. DR neXtProt; NX_Q5H9J7; -. DR OpenTargets; ENSG00000184515; -. DR PharmGKB; PA162377554; -. DR VEuPathDB; HostDB:ENSG00000184515; -. DR eggNOG; ENOG502R12Q; Eukaryota. DR GeneTree; ENSGT00940000153412; -. DR HOGENOM; CLU_123122_0_0_1; -. DR InParanoid; Q5H9J7; -. DR OMA; NMENVPQ; -. DR OrthoDB; 4868729at2759; -. DR PhylomeDB; Q5H9J7; -. DR TreeFam; TF337909; -. DR PathwayCommons; Q5H9J7; -. DR SignaLink; Q5H9J7; -. DR BioGRID-ORCS; 340542; 12 hits in 770 CRISPR screens. DR ChiTaRS; BEX5; human. DR GenomeRNAi; 340542; -. DR Pharos; Q5H9J7; Tdark. DR PRO; PR:Q5H9J7; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q5H9J7; Protein. DR Bgee; ENSG00000184515; Expressed in endothelial cell and 164 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central. 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:SF0; PROTEIN BEX5; 1. DR Pfam; PF04538; BEX; 1. DR PIRSF; PIRSF008633; BEX; 1. DR Genevisible; Q5H9J7; HS. PE 1: Evidence at protein level; KW Cytoplasm; Metal-binding; Reference proteome; Ubl conjugation; Zinc. FT CHAIN 1..111 FT /note="Protein BEX5" FT /id="PRO_0000229788" FT REGION 1..37 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 100..104 FT /note="His cluster" FT /evidence="ECO:0000250|UniProtKB:Q9WTZ9" FT BINDING 108 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared with FEM1B" FT /evidence="ECO:0000250|UniProtKB:Q9WTZ9" FT CONFLICT 27 FT /note="E -> G (in Ref. 3; AAH92450)" FT /evidence="ECO:0000305" FT CONFLICT 42 FT /note="P -> H (in Ref. 3; AAH42818)" FT /evidence="ECO:0000305" SQ SEQUENCE 111 AA; 12602 MW; 1FCB30E1BAA20725 CRC64; MENVPKENKV VEKAPVQNEA PALGGGEYQE PGGNVKGVWA PPAPGFGEDV PNRLVDNIDM IDGDGDDMER FMEEMRELRR KIRELQLRYS LRILIGDPPH HDHHDEFCLM P //