BEX4_RAT
ID BEX4_RAT Reviewed; 118 AA.
AC Q3MKP9; A1A5L0;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein BEX4 {ECO:0000305};
DE AltName: Full=Brain-expressed X-linked protein 4 {ECO:0000312|RGD:1564749};
GN Name=Bex4 {ECO:0000303|PubMed:15958283, ECO:0000312|RGD:1564749};
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], SUBCELLULAR LOCATION, AND DEGRADATION BY THE
RP PROTEASOME.
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 [2]
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).
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:0000250|UniProtKB:Q9NWD9}.
CC -!- SUBUNIT: Interacts with alpha-tubulin. Interacts with SIRT2.
CC {ECO:0000250|UniProtKB:Q9NWD9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q9NWD9}. Nucleus {ECO:0000269|PubMed:15958283}.
CC Cytoplasm {ECO:0000269|PubMed:15958283}. Note=Also localizes to
CC microtubules. {ECO:0000250|UniProtKB:Q9NWD9}.
CC -!- PTM: Ubiquitinated and degraded by the proteasome.
CC {ECO:0000305|PubMed:15958283}.
CC -!- SIMILARITY: Belongs to the BEX family. {ECO:0000305}.
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DR EMBL; AY833557; AAX40675.1; -; mRNA.
DR EMBL; BC128698; AAI28699.1; -; mRNA.
DR RefSeq; NP_001032643.1; NM_001037554.1.
DR AlphaFoldDB; Q3MKP9; -.
DR SMR; Q3MKP9; -.
DR STRING; 10116.ENSRNOP00000035429; -.
DR PaxDb; Q3MKP9; -.
DR Ensembl; ENSRNOT00000102634; ENSRNOP00000086315; ENSRNOG00000062806.
DR GeneID; 501624; -.
DR KEGG; rno:501624; -.
DR UCSC; RGD:1564749; rat.
DR CTD; 56271; -.
DR RGD; 1564749; Bex4.
DR eggNOG; ENOG502TDUR; Eukaryota.
DR GeneTree; ENSGT00940000162932; -.
DR HOGENOM; CLU_123122_0_0_1; -.
DR InParanoid; Q3MKP9; -.
DR OMA; NIDHNEM; -.
DR OrthoDB; 1525516at2759; -.
DR PhylomeDB; Q3MKP9; -.
DR TreeFam; TF337909; -.
DR PRO; PR:Q3MKP9; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000060103; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q3MKP9; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:1904428; P:negative regulation of tubulin deacetylation; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:RGD.
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 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..118
FT /note="Protein BEX4"
FT /id="PRO_0000229786"
FT REGION 14..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..118
FT /note="Interaction with alpha-tubulin"
FT /evidence="ECO:0000250|UniProtKB:Q9NWD9"
FT REGION 30..88
FT /note="Interaction with SIRT2"
FT /evidence="ECO:0000250|UniProtKB:Q9NWD9"
FT COMPBIAS 14..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 118 AA; 13721 MW; 362873538A36E62C CRC64;
MASKVKQVIL DLTVEKDKKN KKGGKASKQS EEESHHLEEV ENKKPGGNVR RKVRRLVPNF
LWAIPNRHVD HSEGGEEVGR FVGQVMEAKR KSKEQQMRPY TRFRTPEPDN HYDFCLIP
