TRA2B_MOUSE
ID TRA2B_MOUSE Reviewed; 288 AA.
AC P62996; 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 162.
DE RecName: Full=Transformer-2 protein homolog beta {ECO:0000305};
DE Short=TRA-2 beta;
DE Short=TRA2-beta;
DE AltName: Full=Silica-induced gene 41 protein;
DE Short=SIG-41;
DE AltName: Full=Splicing factor, arginine/serine-rich 10;
DE AltName: Full=Transformer-2 protein homolog B;
GN Name=Tra2b {ECO:0000312|MGI:MGI:106016}; Synonyms=Sfrs10, Silg41;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RC TISSUE=Macrophage;
RX PubMed=7868905;
RA Segade F., Claudio E., Wrobel K., Ramos S., Lazo P.S.;
RT "Isolation of nine gene sequences induced by silica in murine
RT macrophages.";
RL J. Immunol. 154:2384-2392(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=8674539; DOI=10.1016/0014-5793(96)00496-6;
RA Segade F., Hurle B., Claudio E., Ramos S., Lazo P.S.;
RT "Molecular cloning of a mouse homologue for the Drosophila splicing
RT regulator Tra2.";
RL FEBS Lett. 387:152-156(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-241, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [7]
RP FUNCTION, INTERACTION WITH ILDR1 AND ILDR2, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=28785060; DOI=10.1038/s41598-017-07530-z;
RA Liu Y., Nie H., Liu C., Zhai X., Sang Q., Wang Y., Shi D., Wang L., Xu Z.;
RT "Angulin proteins ILDR1 and ILDR2 regulate alternative pre-mRNA splicing
RT through binding to splicing factors TRA2A, TRA2B, or SRSF1.";
RL Sci. Rep. 7:7466-7466(2017).
CC -!- FUNCTION: Sequence-specific RNA-binding protein which participates in
CC the control of pre-mRNA splicing (PubMed:28785060). 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:0000269|PubMed:28785060}.
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 (PubMed:28785060). {ECO:0000250|UniProtKB:P62995,
CC ECO:0000250|UniProtKB:P62997, ECO:0000269|PubMed:28785060}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28785060}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62996-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62996-2; Sequence=VSP_011509, VSP_011510;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in uterus and
CC brain. Expressed in inner ear (PubMed:28785060).
CC {ECO:0000269|PubMed:28785060, ECO:0000269|PubMed:8674539}.
CC -!- INDUCTION: Induced by reoxygenation following hypoxia and by exposure
CC to silica. Repressed by interferon gamma, LPS and TPA.
CC {ECO:0000269|PubMed:7868905}.
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; X80232; CAA56518.1; -; mRNA.
DR EMBL; AK049573; BAC33819.1; -; mRNA.
DR EMBL; AK077418; BAC36791.1; -; mRNA.
DR EMBL; AK080378; BAC37898.1; -; mRNA.
DR EMBL; BC061177; AAH61177.1; -; mRNA.
DR CCDS; CCDS37297.1; -. [P62996-1]
DR PIR; S68798; S68798.
DR RefSeq; NP_001317483.1; NM_001330554.1.
DR RefSeq; NP_001317484.1; NM_001330555.1.
DR RefSeq; NP_033212.1; NM_009186.5. [P62996-1]
DR AlphaFoldDB; P62996; -.
DR BMRB; P62996; -.
DR SMR; P62996; -.
DR BioGRID; 203252; 19.
DR IntAct; P62996; 6.
DR MINT; P62996; -.
DR STRING; 10090.ENSMUSP00000124846; -.
DR iPTMnet; P62996; -.
DR PhosphoSitePlus; P62996; -.
DR SwissPalm; P62996; -.
DR EPD; P62996; -.
DR jPOST; P62996; -.
DR MaxQB; P62996; -.
DR PaxDb; P62996; -.
DR PeptideAtlas; P62996; -.
DR PRIDE; P62996; -.
DR ProteomicsDB; 259300; -. [P62996-1]
DR ProteomicsDB; 259301; -. [P62996-2]
DR Antibodypedia; 3190; 176 antibodies from 26 providers.
DR DNASU; 20462; -.
DR Ensembl; ENSMUST00000161286; ENSMUSP00000124846; ENSMUSG00000022858. [P62996-1]
DR GeneID; 20462; -.
DR KEGG; mmu:20462; -.
DR UCSC; uc007ysc.1; mouse. [P62996-1]
DR CTD; 6434; -.
DR MGI; MGI:106016; Tra2b.
DR VEuPathDB; HostDB:ENSMUSG00000022858; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00950000183009; -.
DR HOGENOM; CLU_050438_3_0_1; -.
DR InParanoid; P62996; -.
DR OMA; FGFVNMV; -.
DR OrthoDB; 1524134at2759; -.
DR PhylomeDB; P62996; -.
DR TreeFam; TF106265; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR BioGRID-ORCS; 20462; 13 hits in 75 CRISPR screens.
DR ChiTaRS; Tra2b; mouse.
DR PRO; PR:P62996; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P62996; protein.
DR Bgee; ENSMUSG00000022858; Expressed in embryonic post-anal tail and 181 other tissues.
DR ExpressionAtlas; P62996; baseline and differential.
DR Genevisible; P62996; MM.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0036002; F:pre-mRNA binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0021796; P:cerebral cortex regionalization; IMP:MGI.
DR GO; GO:1990403; P:embryonic brain development; IMP:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP: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 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Isopeptide bond; Methylation;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; 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_0000081984"
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:0007744|PubMed:24129315"
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:0007744|PubMed:24129315"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62995"
FT VAR_SEQ 23..38
FT /note="AHGSGKSARHTPARSR -> RHLTSFINEYLKLRNK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011509"
FT VAR_SEQ 39..288
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011510"
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
