TRA2B_RAT
ID TRA2B_RAT Reviewed; 288 AA.
AC P62997; O15449; Q15815; Q64283;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Transformer-2 protein homolog beta {ECO:0000305};
DE Short=TRA-2 beta;
DE Short=TRA2-beta;
DE AltName: Full=RA301;
DE AltName: Full=Splicing factor, arginine/serine-rich 10;
DE AltName: Full=Transformer-2 protein homolog B;
GN Name=Tra2b {ECO:0000312|RGD:619886}; Synonyms=Sfrs10;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Astrocyte;
RX PubMed=7499316; DOI=10.1074/jbc.270.47.28216;
RA Matsuo N., Ogawa S., Imai Y., Takagi T., Tohyama M., Stern D., Wanaka A.;
RT "Cloning of a novel RNA binding polypeptide (RA301) induced by
RT hypoxia/reoxygenation.";
RL J. Biol. Chem. 270:28216-28222(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH SAFB/SAFB1.
RX PubMed=9671816; DOI=10.1093/nar/26.15.3542;
RA Nayler O., Straetling W., Bourquin J.-P., Stagljar I., Lindemann L.,
RA Jasper H., Hartmann A.M., Fackelmeyer F.O., Ullrich A., Stamm S.;
RT "SAF-B couples transcription and pre-mRNA splicing to SAR/MAR elements.";
RL Nucleic Acids Res. 26:3542-3549(1998).
RN [4]
RP INTERACTION WITH RBMX.
RX PubMed=19282290; DOI=10.1074/jbc.m901026200;
RA Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M.,
RA Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R.,
RA Stamm S.;
RT "Heterogeneous nuclear ribonucleoprotein G regulates splice site selection
RT by binding to CC(A/C)-rich regions in pre-mRNA.";
RL J. Biol. Chem. 284:14303-14315(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-4; SER-14; SER-29;
RP THR-33; SER-95; SER-97; SER-99 AND THR-201, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Sequence-specific RNA-binding protein which participates in
CC the control of pre-mRNA splicing. Can either activate or suppress exon
CC inclusion. Acts additively with RBMX to promote exon 7 inclusion of the
CC survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10.
CC Alters pre-mRNA splicing patterns by antagonizing the effects of
CC splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the
CC SMN exon 7 RNA. Binds to pre-mRNA (By similarity).
CC {ECO:0000250|UniProtKB:P62995}.
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 RNPS1 and phosphorylated SFRS13A (By similarity). Interacts with RBMX
CC and SAFB/SAFB1 (PubMed:9671816, PubMed:19282290). Interacts with ILDR1
CC (via C-terminus) and ILDR2 (By similarity).
CC {ECO:0000250|UniProtKB:P62995, ECO:0000250|UniProtKB:P62996,
CC ECO:0000269|PubMed:19282290, ECO:0000269|PubMed:9671816}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62995}.
CC -!- INDUCTION: Induced by reoxygenation following hypoxia and by exposure
CC to silica. Repressed by interferon gamma, LPS and TPA.
CC {ECO:0000269|PubMed:7499316}.
CC -!- PTM: Phosphorylated in the RS domains. {ECO:0000250|UniProtKB:P62995}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; D49708; BAA08556.1; -; mRNA.
DR EMBL; BC070948; AAH70948.1; -; mRNA.
DR RefSeq; NP_476460.1; NM_057119.1.
DR AlphaFoldDB; P62997; -.
DR BMRB; P62997; -.
DR SMR; P62997; -.
DR IntAct; P62997; 3.
DR STRING; 10116.ENSRNOP00000002429; -.
DR iPTMnet; P62997; -.
DR PhosphoSitePlus; P62997; -.
DR SwissPalm; P62997; -.
DR jPOST; P62997; -.
DR PaxDb; P62997; -.
DR PRIDE; P62997; -.
DR GeneID; 117259; -.
DR KEGG; rno:117259; -.
DR UCSC; RGD:619886; rat.
DR CTD; 6434; -.
DR RGD; 619886; Tra2b.
DR VEuPathDB; HostDB:ENSRNOG00000001783; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_050438_3_0_1; -.
DR InParanoid; P62997; -.
DR OMA; FGFVNMV; -.
DR OrthoDB; 1524134at2759; -.
DR PhylomeDB; P62997; -.
DR TreeFam; TF106265; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-RNO-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-RNO-9013422; RHOBTB1 GTPase cycle.
DR PRO; PR:P62997; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001783; Expressed in thymus and 20 other tissues.
DR Genevisible; P62997; RN.
DR GO; GO:0005637; C:nuclear inner membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005681; C:spliceosomal complex; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0036002; F:pre-mRNA binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:0021796; P:cerebral cortex regionalization; ISO:RGD.
DR GO; GO:1990403; P:embryonic brain development; ISO:RGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
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 GO; GO:0000302; P:response to reactive oxygen species; IEP:RGD.
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 1: Evidence at protein 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_0000081985"
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:0007744|PubMed:22673903"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
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
