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P78543 (BTG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein BTG2
Alternative name(s):
BTG family member 2
NGF-inducible anti-proliferative protein PC3
Gene names
Name:BTG2
Synonyms:PC3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Anti-proliferative protein; the function is mediated by association with deadenylase subunits of the CCR4-NOT complex. Activates mRNA deadenyltion 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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Subunit structure

Interacts with PRKCABP By similarity. Interacts with CNOT7 and CNOT8; indicative for an asscociation with the CCR4-NOT complex. Interacts with PIN1, inducing mitochondrial depolarization. Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.13

Post-translational modification

Phosphorylated at Ser-147 by MAPK1/ERK2 and MAPK3/ERK1, and at Ser-149 by MAPK14, leading to PIN1-binding and mitochondrial depolarization. Ref.9

Sequence similarities

Belongs to the BTG family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Coding sequence diversityPolymorphism
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement Ref.1. Source: ProtInc

anterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

associative learning

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from direct assay Ref.1. Source: MGI

central nervous system neuron development

Inferred from electronic annotation. Source: Ensembl

dentate gyrus development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.12. Source: UniProtKB

negative regulation of neural precursor cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of translation

Inferred from direct assay Ref.12. Source: UniProtKB

neuron projection development

Inferred from mutant phenotype Ref.11. Source: UniProtKB

positive regulation of nuclear-transcribed mRNA poly(A) tail shortening

Inferred from direct assay Ref.10. Source: MGI

protein methylation

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

skeletal muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 158158Protein BTG2
PRO_0000143804

Amino acid modifications

Modified residue1471Phosphoserine; by MAPK1 and MAPK3 Ref.9
Modified residue1491Phosphoserine; by MAPK14 Ref.9

Natural variations

Natural variant1531V → M.
Corresponds to variant rs12039961 [ dbSNP | Ensembl ].
VAR_048437

Experimental info

Mutagenesis531H → A: Impairs interaction with CNOT7 and CNOT8. Ref.12
Mutagenesis651Y → A: Abolishes interaction with CNOT7 and CNOT8. Ref.12 Ref.13
Mutagenesis751D → A: Abolishes interaction with CNOT7 and CNOT8. Ref.12
Mutagenesis1031W → A: Abolishes interaction with CNOT7 and CNOT8; impairs anti-proliferative activity. Ref.12 Ref.13
Mutagenesis1051D → A: Impairs interaction with CNOT7 and CNOT8. Ref.12
Mutagenesis1151E → A: Impairs interaction with CNOT7. Inhibits CNOT7 mRNA deadenylase activity. Ref.13
Mutagenesis1471S → A: Impairs phosphorylation by MAPK1 and MAPK3, and decreases PIN1-binding. Ref.9
Mutagenesis1481P → A: Impairs PIN1-binding. Ref.9
Mutagenesis1491S → A: Impairs phosphorylation by MAPK14, and decreases PIN1-binding. Ref.9

Secondary structure

.................... 158
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P78543 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: FFAA1844CC360209

FASTA15817,416
        10         20         30         40         50         60 
MSHGKGTDML PEIAAAVGFL SSLLRTRGCV SEQRLKVFSG ALQEALTEHY KHHWFPEKPS 

        70         80         90        100        110        120 
KGSGYRCIRI NHKMDPIISR VASQIGLSQP QLHQLLPSEL TLWVDPYEVS YRIGEDGSIC 

       130        140        150 
VLYEEAPLAA SCGLLTCKNQ VLLGRSSPSK NYVMAVSS 

« Hide

References

« Hide 'large scale' references
[1]"Identification of BTG2, an antiproliferative p53-dependent component of the DNA damage cellular response pathway."
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.
Nat. Genet. 14:482-486(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The gene PC3(TIS21/BTG2), prototype member of the PC3/BTG/TOB family: regulator in control of cell growth, differentiation, and DNA repair?"
Tirone F.
J. Cell. Physiol. 187:155-165(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal liver.
[3]"The human BTG2/TIS21/PC3 gene: genomic structure, transcriptional regulation and evaluation as a candidate tumor suppressor gene."
Duriez C., Falette N., Audoynaud C., Moyret-Lalle C., Bensaad K., Courtois S., Wang Q., Soussi T., Puisieux A.
Gene 282:207-214(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Interaction of BTG1 and p53-regulated BTG2 gene products with mCaf1, the murine homolog of a component of the yeast CCR4 transcriptional regulatory complex."
Rouault J.P., Prevot D., Berthet C., Birot A.M., Billaud M., Magaud J.P., Corbo L.
J. Biol. Chem. 273:22563-22569(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CNOT7.
[7]"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."
Prevot D., Morel A.P., Voeltzel T., Rostan M.C., Rimokh R., Magaud J.P., Corbo L.
J. Biol. Chem. 276:9640-9648(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CNOT8.
[8]"BTG2 antiproliferative protein interacts with the human CCR4 complex existing in vivo in three cell-cycle-regulated forms."
Morel A.-P., Sentis S., Bianchin C., Le Romancer M., Jonard L., Rostan M.-C., Rimokh R., Corbo L.
J. Cell Sci. 116:2929-2936(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH THE CCR4-NOT COMPLEX.
[9]"Phosphorylation of serine 147 of tis21/BTG2/pc3 by p-Erk1/2 induces Pin-1 binding in cytoplasm and cell death."
Hong J.W., Ryu M.S., Lim I.K.
J. Biol. Chem. 280:21256-21263(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-147 AND SER-149, MUTAGENESIS OF SER-147; PRO-148 AND SER-149, INTERACTION WITH PIN1, FUNCTION.
[10]"The BTG2 protein is a general activator of mRNA deadenylation."
Mauxion F., Faux C., Seraphin B.
EMBO J. 27:1039-1048(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"PRMT1 and Btg2 regulates neurite outgrowth of Neuro2a cells."
Miyata S., Mori Y., Tohyama M.
Neurosci. Lett. 445:162-165(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"The anti-proliferative activity of BTG/TOB proteins is mediated via the Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not complex."
Doidge R., Mittal S., Aslam A., Winkler G.S.
PLoS ONE 7:E51331-E51331(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CNOT7 AND CNOT8, MUTAGENESIS OF HIS-53; TYR-65; ASP-75; TRP-103 AND ASP-105.
[13]"Crystal structures of human BTG2 and mouse TIS21 involved in suppression of CAF1 deadenylase activity."
Yang X., Morita M., Wang H., Suzuki T., Yang W., Luo Y., Zhao C., Yu Y., Bartlam M., Yamamoto T., Rao Z.
Nucleic Acids Res. 36:6872-6881(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 7-128, INTERACTION WITH CNOT7, MUTAGENESIS OF TYR-65; TRP-103 AND GLU-115.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U72649 mRNA. Translation: AAB37580.1.
Y09943 mRNA. Translation: CAA71074.1.
AF361937 Genomic DNA. Translation: AAL05626.1.
AL513326 Genomic DNA. Translation: CAH70451.1.
BC105948 mRNA. Translation: AAI05949.1.
BC105949 mRNA. Translation: AAI05950.1.
RefSeqNP_006754.1. NM_006763.2.
UniGeneHs.519162.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DJUX-ray2.26B7-128[»]
3E9VX-ray1.70A8-127[»]
ProteinModelPortalP78543.
SMRP78543. Positions 8-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113593. 20 interactions.
IntActP78543. 5 interactions.
MINTMINT-155716.
STRING9606.ENSP00000290551.

PTM databases

PhosphoSiteP78543.

Polymorphism databases

DMDM3023409.

Proteomic databases

PaxDbP78543.
PRIDEP78543.

Protocols and materials databases

DNASU7832.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290551; ENSP00000290551; ENSG00000159388.
ENST00000475157; ENSP00000433553; ENSG00000159388.
GeneID7832.
KEGGhsa:7832.
UCSCuc001gzq.3. human.

Organism-specific databases

CTD7832.
GeneCardsGC01P203274.
HGNCHGNC:1131. BTG2.
HPAHPA002355.
MIM601597. gene.
neXtProtNX_P78543.
PharmGKBPA25451.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287298.
HOGENOMHOG000290200.
HOVERGENHBG004907.
InParanoidP78543.
KOK14443.
OMATCKNQMM.
OrthoDBEOG72RN0S.
PhylomeDBP78543.
TreeFamTF105272.

Gene expression databases

BgeeP78543.
CleanExHS_BTG2.
GenevestigatorP78543.

Family and domain databases

InterProIPR002087. Anti_prolifrtn.
[Graphical view]
PfamPF07742. BTG. 1 hit.
[Graphical view]
PRINTSPR00310. ANTIPRLFBTG1.
SMARTSM00099. btg1. 1 hit.
[Graphical view]
PROSITEPS00960. BTG_1. 1 hit.
PS01203. BTG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP78543.
GeneWikiBTG2.
GenomeRNAi7832.
NextBio30230.
PROP78543.
SOURCESearch...

Entry information

Entry nameBTG2_HUMAN
AccessionPrimary (citable) accession number: P78543
Secondary accession number(s): Q3KR25, Q5VUT0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM