BEX1_RAT
ID BEX1_RAT Reviewed; 128 AA.
AC Q3MKQ2; Q6XUZ8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein BEX1;
DE AltName: Full=Brain-expressed X-linked protein 1 homolog;
DE AltName: Full=EG2RVC;
GN Name=Bex1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD Charles River;
RX PubMed=15033532; DOI=10.1016/j.gene.2003.12.021;
RA Feng Y., Liang H.L., Wong-Riley M.;
RT "Differential gene expressions in the visual cortex of postnatal day 1
RT versus day 21 rats revealed by suppression subtractive hybridization.";
RL Gene 329:93-101(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-19
RP AND LYS-45.
RC STRAIN=Sprague-Dawley;
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP PHOSPHORYLATION AT SER-105, UBIQUITINATION, INTERACTION WITH NGFR, AND
RP MUTAGENESIS OF 53-ARG--ARG-55 AND SER-105.
RX PubMed=16498402; DOI=10.1038/sj.emboj.7601017;
RA Vilar M., Murillo-Carretero M., Mira H., Magnusson K., Besset V.,
RA Ibanez C.F.;
RT "Bex1, a novel interactor of the p75 neurotrophin receptor, links
RT neurotrophin signaling to the cell cycle.";
RL EMBO J. 25:1219-1230(2006).
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. {ECO:0000269|PubMed:16498402}.
CC -!- SUBUNIT: Interacts with OMP (By similarity). Interacts with
CC neurotrophin receptor p75NTR/NGFR. {ECO:0000250,
CC ECO:0000269|PubMed:16498402}.
CC -!- INTERACTION:
CC Q3MKQ2; P07174: Ngfr; NbExp=4; IntAct=EBI-8089575, EBI-1038810;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the
CC cytoplasm and the nucleus. Predominantly nuclear.
CC -!- TISSUE SPECIFICITY: Expressed in the central nervous system. Expressed
CC in Schwann cells from newborn sciatic nerve.
CC {ECO:0000269|PubMed:16498402}.
CC -!- DEVELOPMENTAL STAGE: Oscillates during the cell cycle, being lowest at
CC G1 and highest at S phase (at protein level).
CC {ECO:0000269|PubMed:16498402}.
CC -!- PTM: Phosphorylated. Phosphorylation of Ser-105 protects it from the
CC proteasome. {ECO:0000269|PubMed:16498402}.
CC -!- PTM: Ubiquitinated (Probable). Degraded by the proteasome (By
CC similarity). {ECO:0000250, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BEX family. {ECO:0000305}.
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DR EMBL; AY208292; AAP81280.1; -; mRNA.
DR EMBL; AY833554; AAX40672.1; -; mRNA.
DR RefSeq; NP_001032442.1; NM_001037365.1.
DR AlphaFoldDB; Q3MKQ2; -.
DR BioGRID; 272932; 1.
DR IntAct; Q3MKQ2; 1.
DR MINT; Q3MKQ2; -.
DR STRING; 10116.ENSRNOP00000039471; -.
DR iPTMnet; Q3MKQ2; -.
DR PhosphoSitePlus; Q3MKQ2; -.
DR jPOST; Q3MKQ2; -.
DR PRIDE; Q3MKQ2; -.
DR GeneID; 501625; -.
DR KEGG; rno:501625; -.
DR CTD; 55859; -.
DR RGD; 1564643; Bex1.
DR eggNOG; ENOG502RW3Y; Eukaryota.
DR InParanoid; Q3MKQ2; -.
DR PhylomeDB; Q3MKQ2; -.
DR TreeFam; TF337909; -.
DR PRO; PR:Q3MKQ2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IGI:MGI.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR007623; BEX.
DR InterPro; IPR021156; TF_A-like/BEX.
DR PANTHER; PTHR19430; PTHR19430; 1.
DR Pfam; PF04538; BEX; 1.
DR PIRSF; PIRSF008633; BEX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Differentiation; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..128
FT /note="Protein BEX1"
FT /id="PRO_0000229775"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 105
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:16498402"
FT MUTAGEN 19
FT /note="K->E: Does not affect subcellular location."
FT /evidence="ECO:0000269|PubMed:15958283"
FT MUTAGEN 45
FT /note="K->E: Does not affect subcellular location."
FT /evidence="ECO:0000269|PubMed:15958283"
FT MUTAGEN 53..55
FT /note="RRR->AAA: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:16498402"
FT MUTAGEN 105
FT /note="S->A: Abolishes phosphorylation, leading to
FT degradation by the proteasome."
FT /evidence="ECO:0000269|PubMed:16498402"
FT CONFLICT 63
FT /note="A -> S (in Ref. 2; AAX40672)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="P -> A (in Ref. 2; AAX40672)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="E -> D (in Ref. 2; AAX40672)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="Q -> H (in Ref. 2; AAX40672)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="E -> G (in Ref. 2; AAX40672)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="H -> N (in Ref. 2; AAX40672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 15248 MW; 13F8CCF5021C9D49 CRC64;
MESKDQGAKN LNMENDHQKK EEKEEKPQDT IKREPVVAPT FEAGKNCAPR GGRRRFRVRQ
PIAHYRWDLM HRVGEPQGRM REENVQRFGE DMRQLMEKLR ERQLSHSLRA VSTDPPHHDH
HDEFCLMP
