ID TRA2A_HUMAN Reviewed; 282 AA. AC Q13595; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 05-OCT-2010, entry version 104. DE RecName: Full=Transformer-2 protein homolog alpha; DE Short=TRA-2 alpha; DE Short=TRA2-alpha; DE AltName: Full=Transformer-2 protein homolog A; GN Name=TRA2A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=96392356; PubMed=8799144; DOI=10.1073/pnas.93.17.9004; RA Dauwalder B., Amaya-Manzanares F., Mattox W.; RT "A human homologue of the Drosophila sex determination factor RT transformer-2 has conserved splicing regulatory functions."; RL Proc. Natl. Acad. Sci. U.S.A. 93:9004-9009(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Uterus; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RC TISSUE=Cervix carcinoma; RX MEDLINE=98206475; PubMed=9546399; DOI=10.1016/S0092-8674(00)81153-8; RA Tacke R., Tohyama M., Ogawa S., Manley J.L.; RT "Human Tra2 proteins are sequence-specific activators of pre-mRNA RT splicing."; RL Cell 93:139-148(1998). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS RP SPECTROMETRY. RC TISSUE=Hepatoma; RX PubMed=16097034; DOI=10.1002/pmic.200401217; RA Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., RA Demol H., Martens L., Goethals M., Vandekerckhove J.; RT "Global phosphoproteome analysis on human HepG2 hepatocytes using RT reversed-phase diagonal LC."; RL Proteomics 5:3589-3599(2005). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-14; SER-16; RP SER-18; SER-84; SER-86; THR-88; SER-96; SER-98; SER-100 AND THR-204, RP AND MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260 AND SER-262, AND RP MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-264 AND TYR-265, AND RP MASS SPECTROMETRY. RC TISSUE=Lung carcinoma; RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; RT "Global survey of phosphotyrosine signaling identifies oncogenic RT kinases in lung cancer."; RL Cell 131:1190-1203(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260 AND SER-262, AND RP MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa RT cells and high confident phosphopeptide identification by cross- RT validation of MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260 AND SER-262, AND RP MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=17287340; DOI=10.1073/pnas.0611217104; RA Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; RT "Global proteomic profiling of phosphopeptides using electron transfer RT dissociation tandem mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-86; THR-88; RP THR-202; THR-204; SER-215; SER-260 AND SER-262, AND MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-14; THR-202; RP THR-204; SER-260 AND SER-262, AND MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS RP SPECTROMETRY. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260 AND SER-262, AND RP MASS SPECTROMETRY. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). CC -!- FUNCTION: Sequence-specific RNA-binding protein which participates CC in the control of pre-mRNA splicing. CC -!- SUBUNIT: Binds to A3 enhancer proteins SRp75, SRp55, SRp40 and CC SRp30. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q13595-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q13595-2; Sequence=VSP_005893, VSP_005894, VSP_005895; CC -!- PTM: Phosphorylated in the RS domains. CC -!- SIMILARITY: Belongs to the splicing factor SR family. CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U53209; AAC50658.1; -; mRNA. DR EMBL; BC017094; AAH17094.1; -; mRNA. DR IPI; IPI00013891; -. DR IPI; IPI00220447; -. DR RefSeq; NP_037425.1; -. DR UniGene; Hs.445652; -. DR ProteinModelPortal; Q13595; -. DR SMR; Q13595; 109-192. DR IntAct; Q13595; 2. DR MINT; MINT-1683046; -. DR STRING; Q13595; -. DR PhosphoSite; Q13595; -. DR PRIDE; Q13595; -. DR Ensembl; ENST00000297071; ENSP00000297071; ENSG00000164548. DR GeneID; 29896; -. DR KEGG; hsa:29896; -. DR UCSC; uc003swi.1; human. DR CTD; 29896; -. DR GeneCards; GC07M023544; -. DR H-InvDB; HIX0006522; -. DR HGNC; HGNC:16645; TRA2A. DR MIM; 602718; gene. DR eggNOG; prNOG20031; -. DR HOGENOM; HBG756718; -. DR HOVERGEN; HBG102125; -. DR InParanoid; Q13595; -. DR OMA; RYEEYDY; -. DR OrthoDB; EOG9VT8GT; -. DR PhylomeDB; Q13595; -. DR NextBio; 52459; -. DR ArrayExpress; Q13595; -. DR Bgee; Q13595; -. DR Genevestigator; Q13595; -. DR GermOnline; ENSG00000164548; Homo sapiens. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; IDA:UniProtKB. DR InterPro; IPR012677; a_b_plait_nuc-bd. DR InterPro; IPR000504; RRM_RNP1. DR Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1. DR Pfam; PF00076; RRM_1; 1. DR SMART; SM00360; RRM; 1. DR PROSITE; PS50102; RRM; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; mRNA processing; KW mRNA splicing; Nucleus; Phosphoprotein; RNA-binding. FT CHAIN 1 282 Transformer-2 protein homolog alpha. FT /FTId=PRO_0000081981. FT DOMAIN 119 197 RRM. FT REGION 198 225 Linker. FT COMPBIAS 30 112 Arg/Ser-rich (RS1 domain). FT COMPBIAS 226 282 Arg/Ser-rich (RS2 domain). FT MOD_RES 2 2 Phosphoserine. FT MOD_RES 14 14 Phosphoserine. FT MOD_RES 16 16 Phosphoserine. FT MOD_RES 18 18 Phosphoserine. FT MOD_RES 84 84 Phosphoserine. FT MOD_RES 86 86 Phosphoserine. FT MOD_RES 88 88 Phosphothreonine. FT MOD_RES 96 96 Phosphoserine. FT MOD_RES 98 98 Phosphoserine. FT MOD_RES 100 100 Phosphoserine. FT MOD_RES 202 202 Phosphothreonine. FT MOD_RES 204 204 Phosphothreonine. FT MOD_RES 215 215 Phosphoserine. FT MOD_RES 236 236 Phosphoserine (By similarity). FT MOD_RES 260 260 Phosphoserine. FT MOD_RES 262 262 Phosphoserine. FT MOD_RES 264 264 Phosphotyrosine. FT MOD_RES 265 265 Phosphotyrosine. FT VAR_SEQ 1 101 Missing (in isoform Short). FT /FTId=VSP_005893. FT VAR_SEQ 214 214 H -> Q (in isoform Short). FT /FTId=VSP_005894. FT VAR_SEQ 215 282 Missing (in isoform Short). FT /FTId=VSP_005895. SQ SEQUENCE 282 AA; 32689 MW; EDB5ABE7BEA023FD CRC64; MSDVEENNFE GRESRSQSKS PTGTPARVKS ESRSGSRSPS RVSKHSESHS RSRSKSRSRS RRHSHRRYTR SRSHSHSHRR RSRSRSYTPE YRRRRSRSHS PMSNRRRHTG SRANPDPNTC LGVFGLSLYT TERDLREVFS RYGPLSGVNV VYDQRTGRSR GFAFVYFERI DDSKEAMERA NGMELDGRRI RVDYSITKRA HTPTPGIYMG RPTHSGGGGG GGGGGGGGGG GRRRDSYYDR GYDRGYDRYE DYDYRYRRRS PSPYYSRYRS RSRSRSYSPR RY //