TRA2B_HUMAN
ID TRA2B_HUMAN Reviewed; 288 AA.
AC P62995; B4DVK2; D3DNU3; 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 178.
DE RecName: Full=Transformer-2 protein homolog beta {ECO:0000305};
DE Short=TRA-2 beta;
DE Short=TRA2-beta;
DE Short=hTRA2-beta;
DE AltName: Full=Splicing factor, arginine/serine-rich 10;
DE AltName: Full=Transformer-2 protein homolog B;
GN Name=TRA2B {ECO:0000312|HGNC:HGNC:10781}; Synonyms=SFRS10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=9212162; DOI=10.1089/dna.1997.16.679;
RA Beil B., Screaton G., Stamm S.;
RT "Molecular cloning of htra2-beta-1 and htra2-beta-2, two human homologs of
RT tra-2 generated by alternative splicing.";
RL DNA Cell Biol. 16:679-690(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RX PubMed=9790768; DOI=10.1006/geno.1998.5471;
RA Nayler O., Cap C., Stamm S.;
RT "Human transformer-2-beta gene (SFRS10): complete nucleotide sequence,
RT chromosomal localization, and generation of a tissue-specific isoform.";
RL Genomics 53:191-202(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Dauwalder B., Manzanares F.A., Mattox W.;
RT "The human transformer-2 beta gene is a functional homologue of the D.
RT melanogaster sex determination factor transformer-2.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, Placenta, and Skin;
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 [7]
RP PROTEIN SEQUENCE OF 141-156; 160-173; 179-187; 189-210 AND 229-251,
RP METHYLATION AT ARG-241, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RC TISSUE=Cervix carcinoma;
RX 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 [9]
RP IDENTIFICATION IN A MRNA EXONIC SPLICING ENHANCER (ESE) COMPLEX WITH
RP SNRNP70; SNRPA1 AND SRRM1.
RX PubMed=10339552; DOI=10.1073/pnas.96.11.6125;
RA Eldridge A.G., Li Y., Sharp P.A., Blencowe B.J.;
RT "The SRm160/300 splicing coactivator is required for exon-enhancer
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6125-6130(1999).
RN [10]
RP INTERACTION WITH RBMY1A1.
RX PubMed=10749975; DOI=10.1093/hmg/9.5.685;
RA Venables J.P., Elliott D.J., Makarova O.V., Makarov E.M., Cooke H.J.,
RA Eperon E.C.;
RT "RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins
RT interact with Tra2beta and affect splicing.";
RL Hum. Mol. Genet. 9:685-694(2000).
RN [11]
RP FUNCTION, INTERACTION WITH RBMX, AND RNA-BINDING.
RX PubMed=12165565; DOI=10.1093/hmg/11.17.2037;
RA Hofmann Y., Wirth B.;
RT "hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via
RT direct interaction with Htra2-beta1.";
RL Hum. Mol. Genet. 11:2037-2049(2002).
RN [12]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=12761049; DOI=10.1093/hmg/ddg136;
RA Nasim M.T., Chernova T.K., Chowdhury H.M., Yue B.G., Eperon I.C.;
RT "HnRNP G and Tra2beta: opposite effects on splicing matched by antagonism
RT in RNA binding.";
RL Hum. Mol. Genet. 12:1337-1348(2003).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [14]
RP FUNCTION.
RX PubMed=15009664; DOI=10.1046/j.1471-4159.2003.02232.x;
RA Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.;
RT "Tau exon 10, whose missplicing causes frontotemporal dementia, is
RT regulated by an intricate interplay of cis elements and trans factors.";
RL J. Neurochem. 88:1078-1090(2004).
RN [15]
RP INTERACTION WITH CPSF6.
RX PubMed=15169763; DOI=10.1074/jbc.m403927200;
RA Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M.;
RT "Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im
RT mediate RNA binding, protein-protein interactions, and subcellular
RT localization.";
RL J. Biol. Chem. 279:35788-35797(2004).
RN [16]
RP INTERACTION WITH RNPS1.
RX PubMed=14729963; DOI=10.1128/mcb.24.3.1174-1187.2004;
RA Sakashita E., Tatsumi S., Werner D., Endo H., Mayeda A.;
RT "Human RNPS1 and its associated factors: a versatile alternative pre-mRNA
RT splicing regulator in vivo.";
RL Mol. Cell. Biol. 24:1174-1187(2004).
RN [17]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-241, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=15782174; DOI=10.1038/nmeth715;
RA Ong S.E., Mittler G., Mann M.;
RT "Identifying and quantifying in vivo methylation sites by heavy methyl
RT SILAC.";
RL Nat. Methods 1:119-126(2004).
RN [18]
RP INTERACTION WITH SFRS13A.
RX PubMed=14765198; DOI=10.1038/nature02288;
RA Shin C., Feng Y., Manley J.L.;
RT "Dephosphorylated SRp38 acts as a splicing repressor in response to heat
RT shock.";
RL Nature 427:553-558(2004).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND THR-201, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [21]
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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2; SER-14; SER-95; SER-97; SER-99; THR-103; THR-201 AND
RP THR-203, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2; SER-4; SER-14 AND THR-201, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-14; SER-83; SER-85;
RP SER-87; THR-201; SER-215 AND SER-237, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-241, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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 [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-197, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [29]
RP STRUCTURE BY NMR OF 109-191.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA recognition motif in arginine/serine-rich
RT splicing factor 10.";
RL Submitted (NOV-2005) to the PDB data bank.
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. {ECO:0000269|PubMed:12165565,
CC ECO:0000269|PubMed:12761049, ECO:0000269|PubMed:15009664,
CC ECO:0000269|PubMed:9546399}.
CC -!- SUBUNIT: Found in a pre-mRNA exonic splicing enhancer (ESE) complex
CC with TRA2B/SFRS10, SNRNP70, SNRPA1 and SRRM1 (PubMed:10339552). Binds
CC to A3 enhancer proteins SFRS4, SFRS5, SFRS6 and SFRS9. Interacts with
CC CPSF6, RBMY1A1, RBMX, RNPS1 and phosphorylated SFRS13A
CC (PubMed:10749975, PubMed:12165565, PubMed:14729963, PubMed:14765198,
CC PubMed:15169763, PubMed:19282290). Interacts with SAFB/SAFB1 (By
CC similarity). Interacts with ILDR1 (via C-terminus) and ILDR2 (By
CC similarity). {ECO:0000250|UniProtKB:P62996,
CC ECO:0000250|UniProtKB:P62997, ECO:0000269|PubMed:10339552,
CC ECO:0000269|PubMed:10749975, ECO:0000269|PubMed:12165565,
CC ECO:0000269|PubMed:14729963, ECO:0000269|PubMed:14765198,
CC ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:19282290}.
CC -!- INTERACTION:
CC P62995; P49759-3: CLK1; NbExp=5; IntAct=EBI-725485, EBI-11981867;
CC P62995; P49761: CLK3; NbExp=8; IntAct=EBI-725485, EBI-745579;
CC P62995; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-725485, EBI-6255981;
CC P62995; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-725485, EBI-746778;
CC P62995; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-725485, EBI-2858213;
CC P62995; Q9Y5E9: PCDHB14; NbExp=3; IntAct=EBI-725485, EBI-10329013;
CC P62995; P38159: RBMX; NbExp=4; IntAct=EBI-725485, EBI-743526;
CC P62995; Q15415: RBMY1J; NbExp=3; IntAct=EBI-725485, EBI-8642021;
CC P62995; P78362: SRPK2; NbExp=5; IntAct=EBI-725485, EBI-593303;
CC P62995; Q07955: SRSF1; NbExp=3; IntAct=EBI-725485, EBI-398920;
CC P62995; Q08170: SRSF4; NbExp=4; IntAct=EBI-725485, EBI-722621;
CC P62995; Q9BRL6-2: SRSF8; NbExp=3; IntAct=EBI-725485, EBI-10976394;
CC P62995; Q13242: SRSF9; NbExp=3; IntAct=EBI-725485, EBI-2949710;
CC P62995; P62995: TRA2B; NbExp=3; IntAct=EBI-725485, EBI-725485;
CC P62995; Q01081: U2AF1; NbExp=3; IntAct=EBI-725485, EBI-632461;
CC P62995; Q96MU7: YTHDC1; NbExp=4; IntAct=EBI-725485, EBI-2849854;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9212162,
CC ECO:0000269|PubMed:9546399}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=HTRA2-beta1;
CC IsoId=P62995-1, Q15815-1;
CC Sequence=Displayed;
CC Name=2; Synonyms=HTRA2-beta2;
CC IsoId=P62995-2, Q15815-2;
CC Sequence=VSP_005898, VSP_005899;
CC Name=3; Synonyms=HTRA2-beta3;
CC IsoId=P62995-3, Q15815-3;
CC Sequence=VSP_005896;
CC -!- TISSUE SPECIFICITY: Highest expression in heart, skeletal muscle and
CC pancreas. Less abundant in kidney, placenta and brain. Lowest
CC expression in kidney and liver. {ECO:0000269|PubMed:9790768}.
CC -!- PTM: Phosphorylated in the RS domains. {ECO:0000269|PubMed:9546399}.
CC -!- PTM: Dimethylation at Arg-241 is probably asymmetric.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; U61267; AAC28242.1; -; mRNA.
DR EMBL; U87836; AAB69763.1; -; mRNA.
DR EMBL; AF057159; AAD19277.1; -; Genomic_DNA.
DR EMBL; AF057159; AAD19278.1; -; Genomic_DNA.
DR EMBL; AF057159; AAD19279.1; -; Genomic_DNA.
DR EMBL; U68063; AAB08701.1; -; mRNA.
DR EMBL; AK301118; BAG62714.1; -; mRNA.
DR EMBL; CH471052; EAW78204.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78205.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78208.1; -; Genomic_DNA.
DR EMBL; BC000160; AAH00160.1; -; mRNA.
DR EMBL; BC000451; AAH00451.1; -; mRNA.
DR EMBL; BC005898; AAH05898.1; -; mRNA.
DR CCDS; CCDS33905.1; -.
DR CCDS; CCDS58872.1; -. [P62995-3]
DR RefSeq; NP_001230808.1; NM_001243879.1. [P62995-3]
DR RefSeq; NP_004584.1; NM_004593.2. [P62995-1]
DR RefSeq; XP_005247760.1; XM_005247703.1. [P62995-3]
DR RefSeq; XP_011511374.1; XM_011513072.2.
DR RefSeq; XP_016862522.1; XM_017007033.1.
DR PDB; 2CQC; NMR; -; A=110-191.
DR PDB; 2KXN; NMR; -; B=106-200.
DR PDB; 2RRA; NMR; -; A=109-201.
DR PDB; 2RRB; NMR; -; A=111-201.
DR PDBsum; 2CQC; -.
DR PDBsum; 2KXN; -.
DR PDBsum; 2RRA; -.
DR PDBsum; 2RRB; -.
DR AlphaFoldDB; P62995; -.
DR BMRB; P62995; -.
DR SMR; P62995; -.
DR BioGRID; 112332; 387.
DR CORUM; P62995; -.
DR DIP; DIP-42278N; -.
DR IntAct; P62995; 70.
DR MINT; P62995; -.
DR STRING; 9606.ENSP00000416959; -.
DR GlyGen; P62995; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62995; -.
DR PhosphoSitePlus; P62995; -.
DR SwissPalm; P62995; -.
DR BioMuta; TRA2B; -.
DR DMDM; 51703330; -.
DR EPD; P62995; -.
DR jPOST; P62995; -.
DR MassIVE; P62995; -.
DR MaxQB; P62995; -.
DR PaxDb; P62995; -.
DR PeptideAtlas; P62995; -.
DR PRIDE; P62995; -.
DR ProteomicsDB; 57464; -.
DR ProteomicsDB; 57465; -. [P62995-2]
DR ProteomicsDB; 57466; -. [P62995-3]
DR Antibodypedia; 3190; 176 antibodies from 26 providers.
DR DNASU; 6434; -.
DR Ensembl; ENST00000382191.4; ENSP00000371626.4; ENSG00000136527.19. [P62995-3]
DR Ensembl; ENST00000453386.7; ENSP00000416959.2; ENSG00000136527.19. [P62995-1]
DR Ensembl; ENST00000456380.5; ENSP00000416887.1; ENSG00000136527.19. [P62995-2]
DR GeneID; 6434; -.
DR KEGG; hsa:6434; -.
DR MANE-Select; ENST00000453386.7; ENSP00000416959.2; NM_004593.3; NP_004584.1.
DR UCSC; uc003fpv.4; human.
DR CTD; 6434; -.
DR DisGeNET; 6434; -.
DR GeneCards; TRA2B; -.
DR HGNC; HGNC:10781; TRA2B.
DR HPA; ENSG00000136527; Low tissue specificity.
DR MIM; 602719; gene.
DR neXtProt; NX_P62995; -.
DR OpenTargets; ENSG00000136527; -.
DR PharmGKB; PA35697; -.
DR VEuPathDB; HostDB:ENSG00000136527; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00950000183009; -.
DR HOGENOM; CLU_050438_3_0_1; -.
DR InParanoid; P62995; -.
DR OMA; FGFVNMV; -.
DR OrthoDB; 1524134at2759; -.
DR PhylomeDB; P62995; -.
DR TreeFam; TF106265; -.
DR PathwayCommons; P62995; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle.
DR SignaLink; P62995; -.
DR SIGNOR; P62995; -.
DR BioGRID-ORCS; 6434; 415 hits in 1097 CRISPR screens.
DR ChiTaRS; TRA2B; human.
DR EvolutionaryTrace; P62995; -.
DR GeneWiki; TRA2B; -.
DR GenomeRNAi; 6434; -.
DR Pharos; P62995; Tbio.
DR PRO; PR:P62995; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P62995; protein.
DR Bgee; ENSG00000136527; Expressed in germinal epithelium of ovary and 213 other tissues.
DR ExpressionAtlas; P62995; baseline and differential.
DR Genevisible; P62995; HS.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IMP:CAFA.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0036002; F:pre-mRNA binding; IDA:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IMP:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IMP:CAFA.
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; IDA:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS: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 3D-structure; Acetylation; Activator; Alternative splicing;
KW Direct protein sequencing; 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:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378"
FT CHAIN 2..288
FT /note="Transformer-2 protein homolog beta"
FT /id="PRO_0000081983"
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:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
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:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
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:0000269|Ref.7, ECO:0007744|PubMed:15782174"
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:0007744|PubMed:28112733"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_005896"
FT VAR_SEQ 13..38
FT /note="ESRSASRSGSAHGSGKSARHTPARSR -> VNVEEGKCGSRHLTSFINEYLK
FT LRNK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9212162"
FT /id="VSP_005898"
FT VAR_SEQ 39..288
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9212162"
FT /id="VSP_005899"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2CQC"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:2CQC"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:2CQC"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:2CQC"
FT STRAND 153..168
FT /evidence="ECO:0007829|PDB:2CQC"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:2CQC"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:2CQC"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:2CQC"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:2KXN"
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
