TRA2B_BOVIN
ID TRA2B_BOVIN Reviewed; 288 AA.
AC Q3ZBT6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Transformer-2 protein homolog beta;
DE Short=TRA-2 beta;
DE Short=TRA2-beta;
DE AltName: Full=Splicing factor, arginine/serine-rich 10;
DE AltName: Full=Transformer-2 protein homolog B;
GN Name=TRA2B; Synonyms=SFRS10;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sequence-specific RNA-binding protein which participates in
CC the control of pre-mRNA splicing (By similarity). Can either activate
CC or suppress exon inclusion. Acts additively with RBMX to promote exon 7
CC inclusion of the survival motor neuron SMN2. Activates the splicing of
CC MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the
CC effects of splicing regulators, like RBMX. Binds to the AG-rich SE2
CC domain in the SMN exon 7 RNA. Binds to pre-mRNA (By similarity).
CC {ECO:0000250|UniProtKB:P62995, ECO:0000250|UniProtKB:P62996}.
CC -!- SUBUNIT: Found in a pre-mRNA exonic splicing enhancer (ESE) complex
CC with TRA2B/SFRS10, SNRNP70, SNRPA1 and SRRM1. Binds to A3 enhancer
CC proteins SFRS4, SFRS5, SFRS6 and SFRS9. Interacts with CPSF6, RBMY1A1,
CC RBMX, RNPS1 and phosphorylated SFRS13A (By similarity). Interacts with
CC SAFB/SAFB1 (By similarity). Interacts with ILDR1 (via C-terminus) and
CC ILDR2 (By similarity). {ECO:0000250|UniProtKB:P62995,
CC ECO:0000250|UniProtKB:P62996, ECO:0000250|UniProtKB:P62997}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62996}.
CC -!- PTM: Phosphorylated in the RS domains. {ECO:0000250|UniProtKB:P62995}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC103113; AAI03114.1; -; mRNA.
DR RefSeq; NP_001029948.1; NM_001034776.2.
DR AlphaFoldDB; Q3ZBT6; -.
DR BMRB; Q3ZBT6; -.
DR SMR; Q3ZBT6; -.
DR STRING; 9913.ENSBTAP00000002225; -.
DR PaxDb; Q3ZBT6; -.
DR PRIDE; Q3ZBT6; -.
DR Ensembl; ENSBTAT00000002225; ENSBTAP00000002225; ENSBTAG00000001697.
DR GeneID; 615156; -.
DR KEGG; bta:615156; -.
DR CTD; 6434; -.
DR VEuPathDB; HostDB:ENSBTAG00000001697; -.
DR VGNC; VGNC:36268; TRA2B.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00950000183009; -.
DR HOGENOM; CLU_050438_3_0_1; -.
DR InParanoid; Q3ZBT6; -.
DR OMA; FGFVNMV; -.
DR OrthoDB; 1524134at2759; -.
DR TreeFam; TF106265; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000001697; Expressed in thymus and 105 other tissues.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0036002; F:pre-mRNA binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0021796; P:cerebral cortex regionalization; IEA:Ensembl.
DR GO; GO:1990403; P:embryonic brain development; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Isopeptide bond; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT CHAIN 2..288
FT /note="Transformer-2 protein homolog beta"
FT /id="PRO_0000287722"
FT DOMAIN 118..196
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..230
FT /note="Linker"
FT REGION 196..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..105
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62997"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62997"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 241
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 241
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 241
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62995"
SQ SEQUENCE 288 AA; 33666 MW; 60B310C8BA443E28 CRC64;
MSDSGEQNYG ERESRSASRS GSAHGSGKSA RHTPARSRSK EDSRRSRSKS RSRSESRSRS
RRSSRRHYTR SRSRSRSHRR SRSRSYSRDY RRRHSHSHSP MSTRRRHVGN RANPDPNCCL
GVFGLSLYTT ERDLREVFSK YGPIADVSIV YDQQSRRSRG FAFVYFENVD DAKEAKERAN
GMELDGRRIR VDFSITKRPH TPTPGIYMGR PTYGSSRRRD YYDRGYDRGY DDRDYYSRSY
RGGGGGGGGW RAAQDRDQIY RRRSPSPYYS RGGYRSRSRS RSYSPRRY
