BEX4_PONAB
ID BEX4_PONAB Reviewed; 119 AA.
AC Q5R590;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Protein BEX4 {ECO:0000305};
DE AltName: Full=Brain-expressed X-linked protein 4 homolog {ECO:0000250|UniProtKB:Q9NWD9};
GN Name=BEX4 {ECO:0000250|UniProtKB:Q9NWD9};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9NWD9}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q9NWD9}. Note=Also localizes to
CC microtubules. {ECO:0000250|UniProtKB:Q9NWD9}.
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; CR860974; CAH93076.1; -; mRNA.
DR EMBL; CR860614; CAH92735.1; -; mRNA.
DR RefSeq; NP_001126822.1; NM_001133350.1.
DR AlphaFoldDB; Q5R590; -.
DR SMR; Q5R590; -.
DR STRING; 9601.ENSPPYP00000023031; -.
DR Ensembl; ENSPPYT00000024000; ENSPPYP00000023031; ENSPPYG00000020575.
DR GeneID; 100173827; -.
DR KEGG; pon:100173827; -.
DR CTD; 56271; -.
DR eggNOG; ENOG502TDUR; Eukaryota.
DR GeneTree; ENSGT00940000162932; -.
DR HOGENOM; CLU_123122_1_0_1; -.
DR InParanoid; Q5R590; -.
DR OrthoDB; 1525516at2759; -.
DR Proteomes; UP000001595; Chromosome X.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; ISS:UniProtKB.
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; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
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..119
FT /note="Protein BEX4"
FT /id="PRO_0000229785"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..119
FT /note="Interaction with alpha-tubulin"
FT /evidence="ECO:0000250|UniProtKB:Q9NWD9"
FT REGION 31..89
FT /note="Interaction with SIRT2"
FT /evidence="ECO:0000250|UniProtKB:Q9NWD9"
FT COMPBIAS 9..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 119 AA; 14051 MW; B56DF36FF4AEC87E CRC64;
MESKEELAAN NLNGENAQQE NEGREQAPTQ NEETRHLGGG EGQKPGGNIR RGRVRRLVPN
FRWAIPNRHI EHNEARDDVE RFVGQMMEIK RKTREQQMRH YMRFQTPEPD NHYDFCLIP
