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Protein BTG2 (BTG family member 2) (NGF-inducible anti-proliferative protein PC3)

 BTG2_HUMAN              Reviewed;         158 AA.
P78543; A0A024R986; Q3KR25; Q5VUT0;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
22-NOV-2017, entry version 151.
RecName: Full=Protein BTG2;
AltName: Full=BTG family member 2;
AltName: Full=NGF-inducible anti-proliferative protein PC3;
Name=BTG2; Synonyms=PC3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8944033; DOI=10.1038/ng1296-482;
Rouault J.-P., Falette N., Guehenneux F., Guillot C., Rimokh R.,
Wang Q., Berthet C., Moyret-Lalle C., Savatier P., Pain B., Shaw P.,
Berger R., Samarut J., Magaud J.-P., Ozturk M., Samarut C.,
Puisieux A.;
"Identification of BTG2, an antiproliferative p53-dependent component
of the DNA damage cellular response pathway.";
Nat. Genet. 14:482-486(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal liver;
PubMed=11267995; DOI=10.1002/jcp.1062;
Tirone F.;
"The gene PC3(TIS21/BTG2), prototype member of the PC3/BTG/TOB family:
regulator in control of cell growth, differentiation, and DNA
repair?";
J. Cell. Physiol. 187:155-165(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11814693; DOI=10.1016/S0378-1119(01)00825-3;
Duriez C., Falette N., Audoynaud C., Moyret-Lalle C., Bensaad K.,
Courtois S., Wang Q., Soussi T., Puisieux A.;
"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional
regulation and evaluation as a candidate tumor suppressor gene.";
Gene 282:207-214(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH CNOT7.
PubMed=9712883; DOI=10.1074/jbc.273.35.22563;
Rouault J.P., Prevot D., Berthet C., Birot A.M., Billaud M.,
Magaud J.P., Corbo L.;
"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1,
the murine homolog of a component of the yeast CCR4 transcriptional
regulatory complex.";
J. Biol. Chem. 273:22563-22569(1998).
[8]
INTERACTION WITH CNOT8.
PubMed=11136725; DOI=10.1074/jbc.M008201200;
Prevot D., Morel A.P., Voeltzel T., Rostan M.C., Rimokh R.,
Magaud J.P., Corbo L.;
"Relationships of the antiproliferative proteins BTG1 and BTG2 with
CAF1, the human homolog of a component of the yeast CCR4
transcriptional complex: involvement in estrogen receptor alpha
signaling pathway.";
J. Biol. Chem. 276:9640-9648(2001).
[9]
FUNCTION, AND INTERACTION WITH THE CCR4-NOT COMPLEX.
PubMed=12771185; DOI=10.1242/jcs.00480;
Morel A.-P., Sentis S., Bianchin C., Le Romancer M., Jonard L.,
Rostan M.-C., Rimokh R., Corbo L.;
"BTG2 antiproliferative protein interacts with the human CCR4 complex
existing in vivo in three cell-cycle-regulated forms.";
J. Cell Sci. 116:2929-2936(2003).
[10]
PHOSPHORYLATION AT SER-147 AND SER-149, MUTAGENESIS OF SER-147;
PRO-148 AND SER-149, INTERACTION WITH PIN1, AND FUNCTION.
PubMed=15788397; DOI=10.1074/jbc.M500318200;
Hong J.W., Ryu M.S., Lim I.K.;
"Phosphorylation of serine 147 of tis21/BTG2/pc3 by p-Erk1/2 induces
Pin-1 binding in cytoplasm and cell death.";
J. Biol. Chem. 280:21256-21263(2005).
[11]
FUNCTION.
PubMed=18337750; DOI=10.1038/emboj.2008.43;
Mauxion F., Faux C., Seraphin B.;
"The BTG2 protein is a general activator of mRNA deadenylation.";
EMBO J. 27:1039-1048(2008).
[12]
FUNCTION.
PubMed=18773938; DOI=10.1016/j.neulet.2008.08.065;
Miyata S., Mori Y., Tohyama M.;
"PRMT1 and Btg2 regulates neurite outgrowth of Neuro2a cells.";
Neurosci. Lett. 445:162-165(2008).
[13]
FUNCTION, INTERACTION WITH CNOT7 AND CNOT8, AND MUTAGENESIS OF HIS-53;
TYR-65; ASP-75; TRP-103 AND ASP-105.
PubMed=23236473; DOI=10.1371/journal.pone.0051331;
Doidge R., Mittal S., Aslam A., Winkler G.S.;
"The anti-proliferative activity of BTG/TOB proteins is mediated via
the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-
not complex.";
PLoS ONE 7:E51331-E51331(2012).
[14]
X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 7-128, INTERACTION WITH
CNOT7, AND MUTAGENESIS OF TYR-65; TRP-103 AND GLU-115.
PubMed=18974182; DOI=10.1093/nar/gkn825;
Yang X., Morita M., Wang H., Suzuki T., Yang W., Luo Y., Zhao C.,
Yu Y., Bartlam M., Yamamoto T., Rao Z.;
"Crystal structures of human BTG2 and mouse TIS21 involved in
suppression of CAF1 deadenylase activity.";
Nucleic Acids Res. 36:6872-6881(2008).
-!- FUNCTION: Anti-proliferative protein; the function is mediated by
association with deadenylase subunits of the CCR4-NOT complex.
Activates mRNA deadenylation in a CNOT6 and CNOT7-dependent
manner. In vitro can inhibit deadenylase activity of CNOT7 and
CNOT8. Involved in cell cycle regulation. Could be involved in the
growth arrest and differentiation of the neuronal precursors (By
similarity). Modulates transcription regulation mediated by ESR1.
Involved in mitochondrial depolarization and neurite outgrowth.
{ECO:0000250, ECO:0000269|PubMed:12771185,
ECO:0000269|PubMed:15788397, ECO:0000269|PubMed:18337750,
ECO:0000269|PubMed:18773938, ECO:0000269|PubMed:23236473}.
-!- SUBUNIT: Interacts with PRKCABP (By similarity). Interacts with
CNOT7 and CNOT8; indicative for an association with the CCR4-NOT
complex. Interacts with PIN1, inducing mitochondrial
depolarization. {ECO:0000250, ECO:0000269|PubMed:11136725,
ECO:0000269|PubMed:12771185, ECO:0000269|PubMed:15788397,
ECO:0000269|PubMed:18974182, ECO:0000269|PubMed:23236473,
ECO:0000269|PubMed:9712883}.
-!- INTERACTION:
Q9UFF9:-; NbExp=5; IntAct=EBI-1047576, EBI-742299;
P10275:AR; NbExp=4; IntAct=EBI-1047576, EBI-608057;
Q9UIV1:CNOT7; NbExp=7; IntAct=EBI-1047576, EBI-2105113;
Q60809:Cnot7 (xeno); NbExp=5; IntAct=EBI-1047576, EBI-2104739;
-!- PTM: Phosphorylated at Ser-147 by MAPK1/ERK2 and MAPK3/ERK1, and
at Ser-149 by MAPK14, leading to PIN1-binding and mitochondrial
depolarization. {ECO:0000269|PubMed:15788397}.
-!- SIMILARITY: Belongs to the BTG family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U72649; AAB37580.1; -; mRNA.
EMBL; Y09943; CAA71074.1; -; mRNA.
EMBL; AF361937; AAL05626.1; -; Genomic_DNA.
EMBL; AL513326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91475.1; -; Genomic_DNA.
EMBL; CH471067; EAW91476.1; -; Genomic_DNA.
EMBL; BC105948; AAI05949.1; -; mRNA.
EMBL; BC105949; AAI05950.1; -; mRNA.
CCDS; CCDS1437.1; -.
RefSeq; NP_006754.1; NM_006763.2.
UniGene; Hs.519162; -.
PDB; 3DJU; X-ray; 2.26 A; B=7-128.
PDB; 3E9V; X-ray; 1.70 A; A=8-127.
PDBsum; 3DJU; -.
PDBsum; 3E9V; -.
ProteinModelPortal; P78543; -.
SMR; P78543; -.
BioGrid; 113593; 18.
ELM; P78543; -.
IntAct; P78543; 5.
MINT; MINT-155716; -.
STRING; 9606.ENSP00000290551; -.
iPTMnet; P78543; -.
PhosphoSitePlus; P78543; -.
BioMuta; BTG2; -.
DMDM; 3023409; -.
MaxQB; P78543; -.
PaxDb; P78543; -.
PeptideAtlas; P78543; -.
PRIDE; P78543; -.
DNASU; 7832; -.
Ensembl; ENST00000290551; ENSP00000290551; ENSG00000159388.
Ensembl; ENST00000475157; ENSP00000433553; ENSG00000159388.
GeneID; 7832; -.
KEGG; hsa:7832; -.
UCSC; uc001gzq.4; human.
CTD; 7832; -.
DisGeNET; 7832; -.
EuPathDB; HostDB:ENSG00000159388.5; -.
GeneCards; BTG2; -.
HGNC; HGNC:1131; BTG2.
HPA; HPA002355; -.
MIM; 601597; gene.
neXtProt; NX_P78543; -.
OpenTargets; ENSG00000159388; -.
PharmGKB; PA25451; -.
eggNOG; KOG4006; Eukaryota.
eggNOG; ENOG410ZZC0; LUCA.
GeneTree; ENSGT00550000074461; -.
HOGENOM; HOG000290200; -.
HOVERGEN; HBG004907; -.
InParanoid; P78543; -.
KO; K14443; -.
OMA; PSKNYIM; -.
OrthoDB; EOG091G0RS0; -.
PhylomeDB; P78543; -.
TreeFam; TF105272; -.
Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
SIGNOR; P78543; -.
ChiTaRS; BTG2; human.
EvolutionaryTrace; P78543; -.
GeneWiki; BTG2; -.
GenomeRNAi; 7832; -.
PRO; PR:P78543; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000159388; -.
CleanEx; HS_BTG2; -.
Genevisible; P78543; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
GO; GO:0008306; P:associative learning; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl.
GO; GO:0021542; P:dentate gyrus development; IEA:Ensembl.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IDA:MGI.
GO; GO:0006479; P:protein methylation; IEA:Ensembl.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR002087; Anti_prolifrtn.
InterPro; IPR036054; BTG-like_sf.
InterPro; IPR033328; BTG2.
PANTHER; PTHR22978:SF29; PTHR22978:SF29; 1.
Pfam; PF07742; BTG; 1.
PRINTS; PR00310; ANTIPRLFBTG1.
SMART; SM00099; btg1; 1.
SUPFAM; SSF160696; SSF160696; 1.
PROSITE; PS00960; BTG_1; 1.
PROSITE; PS01203; BTG_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 158 Protein BTG2.
/FTId=PRO_0000143804.
MOD_RES 147 147 Phosphoserine; by MAPK1 and MAPK3.
{ECO:0000269|PubMed:15788397}.
MOD_RES 149 149 Phosphoserine; by MAPK14.
{ECO:0000269|PubMed:15788397}.
VARIANT 153 153 V -> M (in dbSNP:rs12039961).
/FTId=VAR_048437.
MUTAGEN 53 53 H->A: Impairs interaction with CNOT7 and
CNOT8. {ECO:0000269|PubMed:23236473}.
MUTAGEN 65 65 Y->A: Abolishes interaction with CNOT7
and CNOT8. {ECO:0000269|PubMed:18974182,
ECO:0000269|PubMed:23236473}.
MUTAGEN 75 75 D->A: Abolishes interaction with CNOT7
and CNOT8. {ECO:0000269|PubMed:23236473}.
MUTAGEN 103 103 W->A: Abolishes interaction with CNOT7
and CNOT8; impairs anti-proliferative
activity. {ECO:0000269|PubMed:18974182,
ECO:0000269|PubMed:23236473}.
MUTAGEN 105 105 D->A: Impairs interaction with CNOT7 and
CNOT8. {ECO:0000269|PubMed:23236473}.
MUTAGEN 115 115 E->A: Impairs interaction with CNOT7.
Inhibits CNOT7 mRNA deadenylase activity.
{ECO:0000269|PubMed:18974182}.
MUTAGEN 147 147 S->A: Impairs phosphorylation by MAPK1
and MAPK3, and decreases PIN1-binding.
{ECO:0000269|PubMed:15788397}.
MUTAGEN 148 148 P->A: Impairs PIN1-binding.
{ECO:0000269|PubMed:15788397}.
MUTAGEN 149 149 S->A: Impairs phosphorylation by MAPK14,
and decreases PIN1-binding.
{ECO:0000269|PubMed:15788397}.
HELIX 10 27 {ECO:0000244|PDB:3E9V}.
HELIX 32 50 {ECO:0000244|PDB:3E9V}.
TURN 59 62 {ECO:0000244|PDB:3E9V}.
HELIX 63 66 {ECO:0000244|PDB:3E9V}.
STRAND 71 73 {ECO:0000244|PDB:3E9V}.
HELIX 76 84 {ECO:0000244|PDB:3E9V}.
HELIX 89 95 {ECO:0000244|PDB:3E9V}.
STRAND 100 105 {ECO:0000244|PDB:3E9V}.
STRAND 108 114 {ECO:0000244|PDB:3E9V}.
STRAND 119 124 {ECO:0000244|PDB:3E9V}.
SEQUENCE 158 AA; 17416 MW; FFAA1844CC360209 CRC64;
MSHGKGTDML PEIAAAVGFL SSLLRTRGCV SEQRLKVFSG ALQEALTEHY KHHWFPEKPS
KGSGYRCIRI NHKMDPIISR VASQIGLSQP QLHQLLPSEL TLWVDPYEVS YRIGEDGSIC
VLYEEAPLAA SCGLLTCKNQ VLLGRSSPSK NYVMAVSS


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