ID A0A2K6AX12_MACNE Unreviewed; 345 AA.
AC A0A2K6AX12;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Transducer of ERBB2, 1 {ECO:0000313|Ensembl:ENSMNEP00000003701.1};
GN Name=TOB1 {ECO:0000313|Ensembl:ENSMNEP00000003701.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000003701.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000003701.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the BTG family. {ECO:0000256|ARBA:ARBA00007989}.
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DR RefSeq; XP_011723908.1; XM_011725606.1.
DR AlphaFoldDB; A0A2K6AX12; -.
DR SMR; A0A2K6AX12; -.
DR STRING; 9545.ENSMNEP00000003701; -.
DR Ensembl; ENSMNET00000018895.1; ENSMNEP00000003701.1; ENSMNEG00000017321.1.
DR GeneID; 105472397; -.
DR KEGG; mni:105472397; -.
DR CTD; 10140; -.
DR GeneTree; ENSGT00940000154208; -.
DR OMA; FPNVQGQ; -.
DR OrthoDB; 11568at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000017321; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0030014; C:CCR4-NOT complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
DR GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0060212; P:negative regulation of nuclear-transcribed mRNA poly(A) tail shortening; IEA:Ensembl.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl.
DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:Ensembl.
DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IEA:Ensembl.
DR GO; GO:0060390; P:regulation of SMAD protein signal transduction; IEA:Ensembl.
DR Gene3D; 3.90.640.90; Anti-proliferative protein, N-terminal domain; 1.
DR InterPro; IPR002087; Anti_prolifrtn.
DR InterPro; IPR036054; BTG-like_sf.
DR InterPro; IPR015676; Tob1/2.
DR PANTHER; PTHR17537:SF6; PROTEIN TOB1; 1.
DR PANTHER; PTHR17537; TRANSDUCER OF ERBB2 TOB; 1.
DR Pfam; PF07742; BTG; 1.
DR PRINTS; PR00310; ANTIPRLFBTG1.
DR SMART; SM00099; btg1; 1.
DR SUPFAM; SSF160696; BTG domain-like; 1.
DR PROSITE; PS00960; BTG_1; 1.
DR PROSITE; PS01203; BTG_2; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120}.
FT DOMAIN 40..60
FT /note="Anti-proliferative protein"
FT /evidence="ECO:0000259|PROSITE:PS00960"
FT DOMAIN 86..105
FT /note="Anti-proliferative protein"
FT /evidence="ECO:0000259|PROSITE:PS01203"
FT REGION 144..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 38155 MW; 3C8AC51B49E1E69F CRC64;
MQLEIQVALN FIISYLYNKL PRRRVNIFGE ELERLLKKKY EGHWYPEKPY KGSGFRCIHI
GEKVDPVIEQ ASKESGLDID DVRGNLPQDL SVWIDPFEVS YQIGEKGPVK VLYVDDNNEN
GCELDKEIKN SFNPEAQVFM PISDPASSVS SSPSPPFGHS AAVSPTFMPR STQPLTFTTA
TFAATKFGST KMKNSGRSNK VARTSPINLG LNVNDLLKQK AISSSMHSLY GLGLGSQQQP
QQQQQPAQPP PPPPPPQQQQ QQKTSALSPN AKEFIFPNMQ GQGSSTNGMF PGDSPLNLSP
LQYSNAFDVF AAYGGLNEKS FVDGLNFSLN NMQYSNQQFQ PVMAN
//