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BTG2_MOUSE
ID   BTG2_MOUSE              Reviewed;         158 AA.
AC   Q04211;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Protein BTG2;
DE   AltName: Full=BTG family member 2;
DE   AltName: Full=NGF-inducible protein TIS21;
GN   Name=Btg2; Synonyms=Tis21;
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 [GENOMIC DNA], AND INDUCTION.
RX   PubMed=1713584; DOI=10.1016/s0021-9258(18)98716-8;
RA   Fletcher B.S., Lim R.W., Varnum B.C., Kujubu D.A., Koski R.A.,
RA   Herschman H.R.;
RT   "Structure and expression of TIS21, a primary response gene induced by
RT   growth factors and tumor promoters.";
RL   J. Biol. Chem. 266:14511-14518(1991).
CC   -!- FUNCTION: Anti-proliferative protein; the function is mediated by
CC       association with deadenylase subunits of the CCR4-NOT complex.
CC       Activates mRNA deadenylation in a CNOT6 and CNOT7-dependent manner. In
CC       vitro can inhibit deadenylase activity of CNOT7 and CNOT8. Involved in
CC       cell cycle regulation. Could be involved in the growth arrest and
CC       differentiation of the neuronal precursors. Modulates transcription
CC       regulation mediated by ESR1. Involved in mitochondrial depolarization
CC       and neurite outgrowth (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PRKCABP. Interacts with CNOT7 and CNOT8;
CC       indicative for an association with the CCR4-NOT complex. Interacts with
CC       PIN1, inducing mitochondrial depolarization (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q04211; Q60809: Cnot7; NbExp=2; IntAct=EBI-7847081, EBI-2104739;
CC       Q04211; Q9D8X5: Cnot8; NbExp=3; IntAct=EBI-7847081, EBI-16204625;
CC   -!- INDUCTION: By nerve growth factor and tumors promoters.
CC       {ECO:0000269|PubMed:1713584}.
CC   -!- PTM: Phosphorylated at Ser-147 by MAPK1/ERK2 and MAPK3/ERK1, and at
CC       Ser-149 by MAPK14, leading to PIN1-binding and mitochondrial
CC       depolarization. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BTG family. {ECO:0000305}.
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DR   EMBL; M64292; AAA40449.1; -; Genomic_DNA.
DR   CCDS; CCDS15302.1; -.
DR   PIR; A40761; A40761.
DR   RefSeq; NP_031596.1; NM_007570.2.
DR   PDB; 3DJN; X-ray; 2.20 A; B=8-125.
DR   PDBsum; 3DJN; -.
DR   AlphaFoldDB; Q04211; -.
DR   SMR; Q04211; -.
DR   BioGRID; 198398; 3.
DR   DIP; DIP-41601N; -.
DR   IntAct; Q04211; 3.
DR   MINT; Q04211; -.
DR   STRING; 10090.ENSMUSP00000020692; -.
DR   iPTMnet; Q04211; -.
DR   PhosphoSitePlus; Q04211; -.
DR   PaxDb; Q04211; -.
DR   PRIDE; Q04211; -.
DR   ProteomicsDB; 265386; -.
DR   Antibodypedia; 1189; 330 antibodies from 29 providers.
DR   DNASU; 12227; -.
DR   Ensembl; ENSMUST00000020692; ENSMUSP00000020692; ENSMUSG00000020423.
DR   GeneID; 12227; -.
DR   KEGG; mmu:12227; -.
DR   UCSC; uc007cre.1; mouse.
DR   CTD; 7832; -.
DR   MGI; MGI:108384; Btg2.
DR   VEuPathDB; HostDB:ENSMUSG00000020423; -.
DR   eggNOG; KOG4006; Eukaryota.
DR   GeneTree; ENSGT00950000182952; -.
DR   HOGENOM; CLU_079660_4_0_1; -.
DR   InParanoid; Q04211; -.
DR   OMA; SYGMLTC; -.
DR   OrthoDB; 1439942at2759; -.
DR   PhylomeDB; Q04211; -.
DR   TreeFam; TF105272; -.
DR   Reactome; R-MMU-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR   BioGRID-ORCS; 12227; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Btg2; mouse.
DR   EvolutionaryTrace; Q04211; -.
DR   PRO; PR:Q04211; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q04211; protein.
DR   Bgee; ENSMUSG00000020423; Expressed in granulocyte and 260 other tissues.
DR   ExpressionAtlas; Q04211; baseline and differential.
DR   Genevisible; Q04211; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR   GO; GO:0008306; P:associative learning; IMP:MGI.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR   GO; GO:0021954; P:central nervous system neuron development; IMP:MGI.
DR   GO; GO:0021542; P:dentate gyrus development; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR   GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR   GO; GO:0030182; P:neuron differentiation; ISO:MGI.
DR   GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR   GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISO:MGI.
DR   GO; GO:0006479; P:protein methylation; IDA:MGI.
DR   GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR   Gene3D; 3.90.640.90; -; 1.
DR   InterPro; IPR002087; Anti_prolifrtn.
DR   InterPro; IPR033332; BTG.
DR   InterPro; IPR036054; BTG-like_sf.
DR   InterPro; IPR033328; BTG2.
DR   PANTHER; PTHR22978; PTHR22978; 1.
DR   PANTHER; PTHR22978:SF29; PTHR22978:SF29; 1.
DR   Pfam; PF07742; BTG; 1.
DR   PRINTS; PR00310; ANTIPRLFBTG1.
DR   SMART; SM00099; btg1; 1.
DR   SUPFAM; SSF160696; SSF160696; 1.
DR   PROSITE; PS00960; BTG_1; 1.
DR   PROSITE; PS01203; BTG_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..158
FT                   /note="Protein BTG2"
FT                   /id="PRO_0000143805"
FT   MOD_RES         147
FT                   /note="Phosphoserine; by MAPK1 and MAPK3"
FT                   /evidence="ECO:0000250|UniProtKB:P78543"
FT   MOD_RES         149
FT                   /note="Phosphoserine; by MAPK14"
FT                   /evidence="ECO:0000250|UniProtKB:P78543"
FT   HELIX           10..28
FT                   /evidence="ECO:0007829|PDB:3DJN"
FT   HELIX           32..50
FT                   /evidence="ECO:0007829|PDB:3DJN"
FT   TURN            59..62
FT                   /evidence="ECO:0007829|PDB:3DJN"
FT   HELIX           63..66
FT                   /evidence="ECO:0007829|PDB:3DJN"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:3DJN"
FT   HELIX           76..84
FT                   /evidence="ECO:0007829|PDB:3DJN"
FT   HELIX           89..95
FT                   /evidence="ECO:0007829|PDB:3DJN"
FT   STRAND          98..105
FT                   /evidence="ECO:0007829|PDB:3DJN"
FT   STRAND          108..114
FT                   /evidence="ECO:0007829|PDB:3DJN"
FT   STRAND          120..124
FT                   /evidence="ECO:0007829|PDB:3DJN"
SQ   SEQUENCE   158 AA;  17682 MW;  5B91563BAE4CB74C CRC64;
     MSHGKRTDML PEIAAAVGFL SSLLRTRGCV SEQRLKVFSR ALQDALTDHY KHHWFPEKPS
     KGSGYRCIRI NHKMDPIISK VASQIGLSQP QLHRLLPSEL TLWVDPYEVS YRIGEDGSIC
     VLYEEAPVAA SYGLLTCKNQ MMLGRSSPSK NYVMAVSS
 
 
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