TRA2A_MOUSE
ID TRA2A_MOUSE Reviewed; 281 AA.
AC Q6PFR5;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Transformer-2 protein homolog alpha {ECO:0000305};
DE Short=TRA-2 alpha;
DE Short=TRA2-alpha;
DE AltName: Full=Transformer-2 protein homolog A;
GN Name=Tra2a {ECO:0000312|MGI:MGI:1933972};
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 [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-233, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [5]
RP INTERACTION WITH ILDR1, SUBCELLULAR LOCATION, AND 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. {ECO:0000250|UniProtKB:Q13595}.
CC -!- SUBUNIT: Binds to A3 enhancer proteins SRp75, SRp55, SRp40 and SRp30
CC (Probable). Interacts with ILDR1 (via C-terminus) and ILDR2
CC (PubMed:28785060). {ECO:0000269|PubMed:28785060, ECO:0000305}.
CC -!- INTERACTION:
CC Q6PFR5; Q9D1X0: Nol3; NbExp=4; IntAct=EBI-913075, EBI-913097;
CC Q6PFR5; Q8BL97: Srsf7; NbExp=4; IntAct=EBI-913075, EBI-913123;
CC Q6PFR5; Q6PFR5: Tra2a; NbExp=2; IntAct=EBI-913075, EBI-913075;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28785060}.
CC -!- TISSUE SPECIFICITY: Expressed in inner ear.
CC {ECO:0000269|PubMed:28785060}.
CC -!- PTM: Phosphorylated in the RS domains. {ECO:0000250|UniProtKB:Q13595}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; BC057448; AAH57448.1; -; mRNA.
DR AlphaFoldDB; Q6PFR5; -.
DR SMR; Q6PFR5; -.
DR IntAct; Q6PFR5; 5.
DR STRING; 10090.ENSMUSP00000031841; -.
DR iPTMnet; Q6PFR5; -.
DR PhosphoSitePlus; Q6PFR5; -.
DR EPD; Q6PFR5; -.
DR jPOST; Q6PFR5; -.
DR MaxQB; Q6PFR5; -.
DR PaxDb; Q6PFR5; -.
DR PeptideAtlas; Q6PFR5; -.
DR PRIDE; Q6PFR5; -.
DR ProteomicsDB; 258842; -.
DR UCSC; uc009bwm.1; mouse.
DR MGI; MGI:1933972; Tra2a.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; Q6PFR5; -.
DR PhylomeDB; Q6PFR5; -.
DR ChiTaRS; Tra2a; mouse.
DR PRO; PR:Q6PFR5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6PFR5; protein.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; ISS:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISO:MGI.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IDA:MGI.
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; Isopeptide bond; Methylation; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT CHAIN 2..281
FT /note="Transformer-2 protein homolog alpha"
FT /id="PRO_0000081982"
FT DOMAIN 117..195
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..223
FT /note="Linker"
FT REGION 199..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..86
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT MOD_RES 202
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT MOD_RES 233
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
FT CROSSLNK 196
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13595"
SQ SEQUENCE 281 AA; 32316 MW; 8074C89D4494D7F0 CRC64;
MSDVEENNFE GRESRSQSKS PTGTPARVKS ESRSGSRSPS RVSKHSESHS RSRSKSRSRS
RRHSHRRYTR SRSHSHRRRS RSRSYTPEYR RRRSRSHSPM SNRRRHTGSR ANPDPNTCLG
VFGLSLYTTE RDLREVFSRY GPLSGVNVVY DQRTGRSRGF AFVYFERIDD SKEAMERANG
MELDGRRIRV DYSITKRAHT PTPGIYMGRP THSGGGGGGG GGGGGGGGGG GGRRRDSYYD
RGYDRGYDRY EDYDYRRRSP SPYYSRYRSR SRSRSYSPRR Y
