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BEX4_MOUSE
ID   BEX4_MOUSE              Reviewed;         118 AA.
AC   Q9CWT2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Protein BEX4 {ECO:0000305};
DE   AltName: Full=Brain-expressed X-linked protein 4 {ECO:0000312|MGI:MGI:3606746};
GN   Name=Bex4 {ECO:0000303|PubMed:15958283, ECO:0000312|MGI:MGI:3606746};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
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   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY CADMIUM.
RX   PubMed=28295929; DOI=10.1002/jbt.21908;
RA   Yu W., Yaping L., Mingjun W., Jie H., Xiaogang L., Gang L.;
RT   "BEX4 upregulation alters Sertoli cell growth properties and protein
RT   expression profiles: An explanation for cadmium-induced testicular Sertoli
RT   cell injury.";
RL   J. Biochem. Mol. Toxicol. 31:0-0(2017).
RN   [4]
RP   INDUCTION BY CURCUMIN.
RX   PubMed=28145533; DOI=10.1038/srep41420;
RA   Sidhar H., Giri R.K.;
RT   "Induction of Bex genes by curcumin is associated with apoptosis and
RT   activation of p53 in N2a neuroblastoma cells.";
RL   Sci. Rep. 7:41420-41420(2017).
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:0000269|PubMed:28295929}. Note=Also localizes to
CC       microtubules. {ECO:0000250|UniProtKB:Q9NWD9}.
CC   -!- TISSUE SPECIFICITY: Expressed in both Sertoli and germ cells as well as
CC       interstitial area of the testis (at protein level).
CC       {ECO:0000269|PubMed:28295929}.
CC   -!- INDUCTION: Up-regulated by cadmium in testis (at protein level)
CC       (PubMed:28295929). Up-regulated by curcumin (PubMed:28145533).
CC       {ECO:0000269|PubMed:28145533, ECO:0000269|PubMed:28295929}.
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; AY833558; AAX40676.1; -; mRNA.
DR   EMBL; AK010400; BAB26911.1; -; mRNA.
DR   CCDS; CCDS30414.1; -.
DR   RefSeq; NP_997622.1; NM_212457.2.
DR   AlphaFoldDB; Q9CWT2; -.
DR   SMR; Q9CWT2; -.
DR   STRING; 10090.ENSMUSP00000112226; -.
DR   iPTMnet; Q9CWT2; -.
DR   PhosphoSitePlus; Q9CWT2; -.
DR   MaxQB; Q9CWT2; -.
DR   PaxDb; Q9CWT2; -.
DR   PRIDE; Q9CWT2; -.
DR   ProteomicsDB; 273672; -.
DR   Ensembl; ENSMUST00000116527; ENSMUSP00000112226; ENSMUSG00000047844.
DR   GeneID; 406217; -.
DR   KEGG; mmu:406217; -.
DR   UCSC; uc009uic.2; mouse.
DR   CTD; 56271; -.
DR   MGI; MGI:3606746; Bex4.
DR   VEuPathDB; HostDB:ENSMUSG00000047844; -.
DR   eggNOG; ENOG502TDUR; Eukaryota.
DR   GeneTree; ENSGT00940000162932; -.
DR   HOGENOM; CLU_123122_0_0_1; -.
DR   InParanoid; Q9CWT2; -.
DR   OMA; NIDHNEM; -.
DR   OrthoDB; 1525516at2759; -.
DR   PhylomeDB; Q9CWT2; -.
DR   TreeFam; TF337909; -.
DR   BioGRID-ORCS; 406217; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Bex4; mouse.
DR   PRO; PR:Q9CWT2; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q9CWT2; protein.
DR   Bgee; ENSMUSG00000047844; Expressed in yolk sac and 70 other tissues.
DR   ExpressionAtlas; Q9CWT2; baseline and differential.
DR   Genevisible; Q9CWT2; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISO:MGI.
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:MGI.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; 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..118
FT                   /note="Protein BEX4"
FT                   /id="PRO_0000229784"
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;  13820 MW;  80557188C3419CD7 CRC64;
     MASKFKQVIL DLTVEKDKKD KKGGKASKQS EEEPHHLEEV ENKKPGGNVR RKVRRLVPNF
     LWAIPNRHVD RNEGGEDVGR FVVQGTEVKR KTTEQQVRPY RRFRTPEPDN HYDFCLIP
 
 
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